|
Name |
Accession |
Description |
Interval |
E-value |
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
9-332 |
0e+00 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 719.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 9 QQPLLQAIDLKKYYPVKKGLFAPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLK 88
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 89 HDPQAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQ 168
Cdd:PRK11308 82 ADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 169 RIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQ 248
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 249 IFTHPRHPYTQALLSATPRLNPDDRRERIKLTGELPSPLNPPPGCAFNARCSRRFGPCTQLQPQLKDYGGQLVACFAVDQ 328
Cdd:PRK11308 242 IFNNPRHPYTQALLSATPRLNPDDRRERIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDYDGRLVACFAVEQ 321
|
....
gi 527035742 329 DENG 332
Cdd:PRK11308 322 DENP 325
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
6-330 |
0e+00 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 594.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 6 ATTQQPLLQAIDLKKYYPVKKGLFA-PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQ 84
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFPVRGGLFGrTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 85 DLLKHDPQAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSG 164
Cdd:COG4608 81 DITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 165 GQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 244
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 245 TKEQIFTHPRHPYTQALLSATPRLNPDDRRERIKLTGELPSPLNPPPGCAFNARCSRRFGPCTQLQPQLKDYG-GQLVAC 323
Cdd:COG4608 241 PRDELYARPLHPYTQALLSAVPVPDPERRRERIVLEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLREVGpGHQVAC 320
|
....*..
gi 527035742 324 FAVDQDE 330
Cdd:COG4608 321 HLAEEGS 327
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-330 |
2.70e-169 |
|
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: 473.39 E-value: 2.70e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 12 LLQAIDLKKYYPVKKGLfaperlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLT-MIEVP--TGGELYYQGQDLLK 88
Cdd:COG0444 1 LLEVRNLKVYFPTRRGV------VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILgLLPPPgiTSGEILFDGEDLLK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 89 HDPQA-QKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLK--TEHYDRYPHMFSGG 165
Cdd:COG0444 75 LSEKElRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPdpERRLDRYPHELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 166 QRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGT 245
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 246 KEQIFTHPRHPYTQALLSATPRLNPdDRRERIKLTGELPSPLNPPPGCAFNARCSRRFGPCTQLQPQLKDYG-GQLVACF 324
Cdd:COG0444 235 VEELFENPRHPYTRALLSSIPRLDP-DGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGpGHRVACH 313
|
....*.
gi 527035742 325 AVDQDE 330
Cdd:COG0444 314 LYEEEA 319
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-271 |
8.34e-146 |
|
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: 421.23 E-value: 8.34e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 6 ATTQQPLLQAIDLKKYYPVKKGlfapeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQD 85
Cdd:COG1123 254 AAAAEPLLEVRNLSKRYPVRGK-----GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 86 LLKHDPQAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGG 165
Cdd:COG1123 329 LTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 166 QRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGT 245
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGP 488
|
250 260
....*....|....*....|....*.
gi 527035742 246 KEQIFTHPRHPYTQALLSATPRLNPD 271
Cdd:COG1123 489 TEEVFANPQHPYTRALLAAVPSLDPA 514
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-268 |
5.51e-138 |
|
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: 401.76 E-value: 5.51e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 6 ATTQQPLLQAIDLKKYYPVKKGLF-APERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGR-LLTMIevPTGGELYYQG 83
Cdd:COG4172 269 PPDAPPLLEARDLKVWFPIKRGLFrRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLaLLRLI--PSEGEIRFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 84 QDLLKHDPQAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINS-NLNKEQRREKALAMMAKVGLKTEHYDRYPHMF 162
Cdd:COG4172 347 QDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLDPAARHRYPHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 163 SGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVE 242
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
250 260
....*....|....*....|....*.
gi 527035742 243 KGTKEQIFTHPRHPYTQALLSATPRL 268
Cdd:COG4172 507 QGPTEQVFDAPQHPYTRALLAAAPLL 532
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-327 |
4.46e-134 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 384.44 E-value: 4.46e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 5 QATTQQPLLQAIDLKKYYPVKKG---LFAPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYY 81
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDIKDGkqwFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 82 QGQDLLKHDPQAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLI-NSNLNKEQRREKALAMMAKVGLKTEHYDRYPH 160
Cdd:PRK15079 81 LGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 161 MFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRC 240
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 241 VEKGTKEQIFTHPRHPYTQALLSATPRlnPDDRRERIK----LTGELPSPLNPPPGCAFNARCSRRFGPCTQLQPQLKDY 316
Cdd:PRK15079 241 VELGTYDEVYHNPLHPYTKALMSAVPI--PDPDLERNKtiqlLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLEGS 318
|
330
....*....|.
gi 527035742 317 GGQLVACFAVD 327
Cdd:PRK15079 319 FRHAVSCLKVD 329
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-244 |
9.47e-121 |
|
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: 346.80 E-value: 9.47e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 12 LLQAIDLKKYYPVKKGLfaperlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDP 91
Cdd:cd03257 1 LLEVKNLSVSFPTGGGS------VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 92 QAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINSNLNK-EQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRI 170
Cdd:cd03257 75 RLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKkEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527035742 171 AIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 244
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
11-264 |
1.15e-114 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 332.96 E-value: 1.15e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 11 PLLQAIDLKKYYPVKKGLFAPERlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHD 90
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGLFRRQQ-FEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 91 pqaQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRI 170
Cdd:COG4167 82 ---YKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 171 AIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIF 250
Cdd:COG4167 159 ALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVF 238
|
250
....*....|....
gi 527035742 251 THPRHPYTQALLSA 264
Cdd:COG4167 239 ANPQHEVTKRLIES 252
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-268 |
3.25e-108 |
|
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: 315.59 E-value: 3.25e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 12 LLQAIDLKKYYPVKKglfapeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDP 91
Cdd:COG1124 1 MLEVRNLSVSYGQGG------RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 92 QAqklRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINSNLNKEQRREKALAmmaKVGLKTEHYDRYPHMFSGGQRQRIA 171
Cdd:COG1124 75 KA---FRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREERIAELLE---QVGLPPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 172 IARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFT 251
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
250
....*....|....*..
gi 527035742 252 HPRHPYTQALLSATPRL 268
Cdd:COG1124 229 GPKHPYTRELLAASLAF 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-271 |
6.30e-96 |
|
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: 294.28 E-value: 6.30e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 8 TQQPLLQAIDLKKYYPvkkglfAPERLVKALDGVSFTLERGKTLAVVGESGCGKS----TLGRLLTMIEVPTGGELYYQG 83
Cdd:COG4172 2 MSMPLLSVEDLSVAFG------QGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 84 QDLLKHDPQA-QKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLK--TEHYDRYPH 160
Cdd:COG4172 76 QDLLGLSERElRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPdpERRLDAYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 161 MFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRC 240
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
250 260 270
....*....|....*....|....*....|.
gi 527035742 241 VEKGTKEQIFTHPRHPYTQALLSATPRLNPD 271
Cdd:COG4172 236 VEQGPTAELFAAPQHPYTRKLLAAEPRGDPR 266
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-285 |
1.33e-91 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 285.60 E-value: 1.33e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 10 QPLLQAIDLKKYYPVKKGLFAP-ERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQ--DL 86
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSGLLNRvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQriDT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 87 LKhDPQAQKLRRQkIQIVFQNPYGSLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQ 166
Cdd:PRK10261 391 LS-PGKLQALRRD-IQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQ 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 167 RQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTK 246
Cdd:PRK10261 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPR 548
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 527035742 247 EQIFTHPRHPYTQALLSATPRLNPDDRR-ERIKLTGELPS 285
Cdd:PRK10261 549 RAVFENPQHPYTRKLMAAVPVADPSRQRpQRVLLSDDLPS 588
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-324 |
6.80e-82 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 251.57 E-value: 6.80e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 1 MSTQQATTQQPLLQAIDLKKYYPVkkglfaPERLVKALDGVSFTLERGKTLAVVGESGCGKS-TLGRLLTMIEVP--TGG 77
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTFST------PDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 78 ELYYQGQDLLKHdPQAQ--KLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKtEHY 155
Cdd:PRK09473 75 SATFNGREILNL-PEKElnKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMP-EAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 156 DR---YPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEV 232
Cdd:PRK09473 153 KRmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 233 MVMYLGRCVEKGTKEQIFTHPRHPYTQALLSATPRLNPDDrRERIKLTGELPSPLNPPPGCAFNARCSRRFGPCtQLQPQ 312
Cdd:PRK09473 233 LVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPRLDAEG-ESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEIC-SSAPP 310
|
330
....*....|...
gi 527035742 313 LKDYG-GQLVACF 324
Cdd:PRK09473 311 LEEFGpGRLRACF 323
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-265 |
1.81e-78 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 249.24 E-value: 1.81e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 9 QQPLLQAIDLKKYYPVKKGLFApeRLV---KALDGVSFTLERGKTLAVVGESGCGKSTLG-RLLTMIevPTGGELYYQGQ 84
Cdd:PRK15134 272 ASPLLDVEQLQVAFPIRKGILK--RTVdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGlALLRLI--NSQGEIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 85 DLLKHDPQAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINS-NLNKEQRREKALAMMAKVGLKTEHYDRYPHMFS 163
Cdd:PRK15134 348 PLHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 164 GGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEK 243
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQ 507
|
250 260
....*....|....*....|..
gi 527035742 244 GTKEQIFTHPRHPYTQALLSAT 265
Cdd:PRK15134 508 GDCERVFAAPQQEYTRQLLALS 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-287 |
3.59e-77 |
|
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: 245.20 E-value: 3.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 10 QPLLQAIDLKKYYPvkkglfapERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTG---GELYYQGQDL 86
Cdd:COG1123 2 TPLLEVRDLSVRYP--------GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 87 LKHDPQaqkLRRQKIQIVFQNPYGSLNPRKkVGQILEEPLLiNSNLNKEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQ 166
Cdd:COG1123 74 LELSEA---LRGRRIGMVFQDPMTQLNPVT-VGDQIAEALE-NLGLSRAEARARVLELLEAVGLE-RRLDRYPHQLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 167 RQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTK 246
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPP 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 527035742 247 EQIFTHPRhpytqaLLSATPRLNPddRRERIKLTGELPSPL 287
Cdd:COG1123 228 EEILAAPQ------ALAAVPRLGA--ARGRAAPAAAAAEPL 260
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
12-264 |
7.98e-77 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 236.61 E-value: 7.98e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 12 LLQAIDLKKYYPVKKGLFAPERlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDp 91
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRRQT-VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 92 qaQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIA 171
Cdd:PRK15112 82 --YSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 172 IARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFT 251
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
250
....*....|...
gi 527035742 252 HPRHPYTQALLSA 264
Cdd:PRK15112 240 SPLHELTKRLIAG 252
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-275 |
3.20e-76 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 235.08 E-value: 3.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 12 LLQAIDLKKYYPvKKGLFAPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDP 91
Cdd:TIGR02769 2 LLEVRDVTHTYR-TGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 92 QAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIA 171
Cdd:TIGR02769 81 KQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 172 IARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFT 251
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLS 240
|
250 260
....*....|....*....|....
gi 527035742 252 HpRHPYTQALLSATPRLNPDDRRE 275
Cdd:TIGR02769 241 F-KHPAGRNLQSAVLPEHPVRRSI 263
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
9-264 |
1.66e-72 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 225.46 E-value: 1.66e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 9 QQPLLQAIDLKKYYPVKKGLfaperlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLK 88
Cdd:COG4107 5 EQPLLSVRGLSKRYGPGCGT------VVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDRDGGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 89 HD----PQAQK--LRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMF 162
Cdd:COG4107 79 RDlfalSEAERrrLRRTDWGMVYQNPRDGLRMDVSAGGNIAERLMAAGERHYGDIRARALEWLERVEIPLERIDDLPRTF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 163 SGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVE 242
Cdd:COG4107 159 SGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVE 238
|
250 260
....*....|....*....|..
gi 527035742 243 KGTKEQIFTHPRHPYTQALLSA 264
Cdd:COG4107 239 SGLTDQVLEDPQHPYTQLLVSS 260
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-279 |
2.09e-71 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 222.64 E-value: 2.09e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 11 PLLQAIDLKKYYPvKKGLFAPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHD 90
Cdd:PRK10419 2 TLLNVSGLSHHYA-HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 91 PQAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRI 170
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 171 AIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEkgtkEQIF 250
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE----TQPV 236
|
250 260 270
....*....|....*....|....*....|..
gi 527035742 251 THP---RHPYTQALLSATPRLNPDDRRERIKL 279
Cdd:PRK10419 237 GDKltfSSPAGRVLQNAVLPAFPVRRRTTEKV 268
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
36-323 |
4.08e-68 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 216.15 E-value: 4.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLG-RLLTMIEVP---TGGELYYQGQDLLK-HDPQAQKLRRQKIQIVFQNPYG 110
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSlAIMGLIDYPgrvMAEKLEFNGQDLQRiSEKERRNLVGAEVAMIFQDPMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 111 SLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLK--TEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEP 188
Cdd:PRK11022 101 SLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 189 VSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQALLSATPRL 268
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRALPEF 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 527035742 269 NPDDRRERiKLTGELPSPLNPPPGCAFNARCSRRFGPCTQLQPQLKDYGGQLVAC 323
Cdd:PRK11022 261 AQDKARLA-SLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLAGRQSKC 314
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-278 |
7.06e-68 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 216.10 E-value: 7.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 17 DLKKYYPVKKGLfaperlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqkL 96
Cdd:COG1135 6 NLSKTFPTKGGP------VTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERE--L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 97 R--RQKIQIVFQNPygSLNPRKKVGQILEEPLLInSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIAR 174
Cdd:COG1135 78 RaaRRKIGMIFQHF--NLLSSRTVAENVALPLEI-AGVPKAEIRKRVAELLELVGL-SDKADAYPSQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 175 GLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPR 254
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQ 233
|
250 260
....*....|....*....|....*
gi 527035742 255 HPYTQALLSATPRLN-PDDRRERIK 278
Cdd:COG1135 234 SELTRRFLPTVLNDElPEELLARLR 258
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
17-254 |
1.03e-63 |
|
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: 201.66 E-value: 1.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 17 DLKKYYPVKKGLfaperlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQKL 96
Cdd:cd03258 6 NVSKVFGDTGGK------VTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 97 RRQKIQIVFQNpYGSLNPRKKVGQIlEEPLLInSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGL 176
Cdd:cd03258 80 ARRRIGMIFQH-FNLLSSRTVFENV-ALPLEI-AGVPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527035742 177 MLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPR 254
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
12-263 |
2.51e-62 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 198.29 E-value: 2.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 12 LLQAIDLKKYYpvkkGLFaperlvKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDP 91
Cdd:COG1126 1 MIEIENLHKSF----GDL------EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 92 QAQKLRRqKIQIVFQNPygSLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQRIA 171
Cdd:COG1126 71 DINKLRR-KVGMVFQQF--NLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLA-DKADAYPAQLSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 172 IARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFT 251
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFE 225
|
250
....*....|..
gi 527035742 252 HPRHPYTQALLS 263
Cdd:COG1126 226 NPQHERTRAFLS 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
39-271 |
1.41e-61 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 204.94 E-value: 1.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 39 DGVSFTLERGKTLAVVGESGCGKS----TLGRLL-TMIEVPTGGELYYQGQDLLKHDPQA-QKLRRQKIQIVFQNPYGSL 112
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESLLHASEQTlRGVRGNKIAMIFQEPMVSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 113 NPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLK--TEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVS 190
Cdd:PRK15134 106 NPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 191 ALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQALLSATPRLNP 270
Cdd:PRK15134 186 ALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLNSEPSGDP 265
|
.
gi 527035742 271 D 271
Cdd:PRK15134 266 V 266
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
17-281 |
2.30e-61 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 199.26 E-value: 2.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 17 DLKKYYPVKKglfapeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQKL 96
Cdd:PRK11153 6 NISKVFPQGG------RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 97 RRQKIQIVFQNpYGSLNPRKKVGQI-LeePLLInSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARG 175
Cdd:PRK11153 80 ARRQIGMIFQH-FNLLSSRTVFDNVaL--PLEL-AGTPKAEIKARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 176 LMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRH 255
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKH 234
|
250 260
....*....|....*....|....*..
gi 527035742 256 PYTQALLSATPRLN-PDDRRERIKLTG 281
Cdd:PRK11153 235 PLTREFIQSTLHLDlPEDYLARLQAEP 261
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
35-268 |
1.35e-60 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 204.32 E-value: 1.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKS-TLGRLLTMIEvPTGGELYYQGQDLLKH-----------DPQAQKLRRQKIQ 102
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLE-QAGGLVQCDKMLLRRRsrqvielseqsAAQMRHVRGADMA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 103 IVFQNPYGSLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKTEH--YDRYPHMFSGGQRQRIAIARGLMLDP 180
Cdd:PRK10261 108 MIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtiLSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 181 DVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQA 260
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRA 267
|
....*...
gi 527035742 261 LLSATPRL 268
Cdd:PRK10261 268 LLAAVPQL 275
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
13-239 |
5.35e-60 |
|
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: 191.55 E-value: 5.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 13 LQAIDLKKYYPvkkglfAPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQ 92
Cdd:cd03255 1 IELKNLSKTYG------GGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 93 AQ-KLRRQKIQIVFQNPYgsLNPRKKVGQILEEPLLINSNLNKEqRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQRIA 171
Cdd:cd03255 75 ELaAFRRRHIGFVFQSFN--LLPDLTALENVELPLLLAGVPKKE-RRERAEELLERVGLG-DRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527035742 172 IARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHiADEVMVMYLGR 239
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGK 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
8-262 |
7.14e-60 |
|
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: 192.12 E-value: 7.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 8 TQQPLLQAIDLKKYYpvkkGlfapERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLL 87
Cdd:COG1127 1 MSEPMIEVRNLTKSF----G----DRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 88 KHDPQAQKLRRQKIQIVFQNP--YGSLNprkkVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKtEHYDRYPHMFSGG 165
Cdd:COG1127 71 GLSEKELYELRRRIGMLFQGGalFDSLT----VFENVAFPLREHTDLSEAEIRELVLEKLELVGLP-GAADKMPSELSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 166 QRQRIAIARGLMLDPDVVIADEPVSALD-VSVRAqVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 244
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDpITSAV-IDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
250
....*....|....*...
gi 527035742 245 TKEQIFTHPrHPYTQALL 262
Cdd:COG1127 225 TPEELLASD-DPWVRQFL 241
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-242 |
8.96e-60 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 191.41 E-value: 8.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 10 QPLLQAIDLKKYYPVKKGLfaperlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDL--L 87
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGE------VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIssL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 88 KhDPQAQKLRRQKIQIVFQNPYgsLNPRKKVGQILEEPLLInSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQR 167
Cdd:COG1136 76 S-ERELARLRRRHIGFVFQFFN--LLPELTALENVALPLLL-AGVSRKERRERARELLERVGL-GDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527035742 168 QRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHiADEVMVMYLGRCVE 242
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
38-257 |
1.33e-58 |
|
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: 188.86 E-value: 1.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQKLRRQKIQIVFQNP--YGSLNpr 115
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQSGalFDSLT-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 116 kkVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKTEHyDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVS 195
Cdd:cd03261 94 --VFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527035742 196 VRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPrHPY 257
Cdd:cd03261 171 ASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPL 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-264 |
1.74e-57 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 186.67 E-value: 1.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 8 TQQPLLQAIDLKKYYPVKKGLfaperlvkalDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLL 87
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGC----------RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 88 KHD------PQAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKTEHYDRYPHM 161
Cdd:PRK11701 72 LRDlyalseAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAARIDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 162 FSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCV 241
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
250 260
....*....|....*....|...
gi 527035742 242 EKGTKEQIFTHPRHPYTQALLSA 264
Cdd:PRK11701 232 ESGLTDQVLDDPQHPYTQLLVSS 254
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
31-323 |
2.01e-57 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 188.96 E-value: 2.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVP----TGGELYYQGQDLLKHDPQAQ-KLRRQKIQIVF 105
Cdd:COG4170 16 PQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERrKIIGREIAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 106 QNPYGSLNPRKKVGQILEEPLLiNSNLN------KEQRREKALAMMAKVGLKtEHYD---RYPHMFSGGQRQRIAIARGL 176
Cdd:COG4170 96 QEPSSCLDPSAKIGDQLIEAIP-SWTFKgkwwqrFKWRKKRAIELLHRVGIK-DHKDimnSYPHELTEGECQKVMIAMAI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 177 MLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHP 256
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHP 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 257 YTQALLSATPRLNPD--DRRERIKLTGELPSPLNPPPGCAFNARCSRRFGPCTQlQPQLKDYGGQLVAC 323
Cdd:COG4170 254 YTKALLRSMPDFRQPlpHKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVE-TPRLRKIKGHEFAC 321
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
35-254 |
2.15e-56 |
|
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: 182.92 E-value: 2.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqklRRQKIQIVFQNPYGSLnp 114
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE---LRRKVGLVFQNPDDQL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 rkkVGQILEEPL---LINSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSA 191
Cdd:COG1122 89 ---FAPTVEEDVafgPENLGLPREEIRERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527035742 192 LDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPR 254
Cdd:COG1122 165 LDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
7-235 |
1.33e-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: 176.82 E-value: 1.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 7 TTQQPLLQAIDLKKYYPVKKGLfaperlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDL 86
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGG------VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 87 LKHDPqaqklrrqKIQIVFQNPygSLNPRKKVGQILEEPLLInSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQ 166
Cdd:COG1116 76 TGPGP--------DRGVVFQEP--ALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGL-AGFEDAYPHQLSGGM 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527035742 167 RQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSvvE--HIADEVMVM 235
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVD--EavFLADRVVVL 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
24-235 |
3.03e-52 |
|
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: 171.89 E-value: 3.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 24 VKKGLFAPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQaqklrrqkIQI 103
Cdd:cd03293 6 VSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD--------RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 104 VFQNPygSLNPRKKVGQILEEPLLINsNLNKEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQRIAIARGLMLDPDVV 183
Cdd:cd03293 78 VFQQD--ALLPWLTVLDNVALGLELQ-GVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 527035742 184 IADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVM 235
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
14-270 |
1.10e-51 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 172.06 E-value: 1.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 14 QAIDLKKYYPVKKGLFAPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQA 93
Cdd:cd03294 16 KAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 94 -QKLRRQKIQIVFQNpYGsLNPRKKVGQILEEPLLInSNLNKEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQRIAI 172
Cdd:cd03294 96 lRELRRKKISMVFQS-FA-LLPHRTVLENVAFGLEV-QGVPRAEREERAAEALELVGLE-GWEHKYPDELSGGMQQRVGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 173 ARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTH 252
Cdd:cd03294 172 ARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
250
....*....|....*...
gi 527035742 253 PRHPYTQALLSATPRLNP 270
Cdd:cd03294 252 PANDYVREFFRGVDRAKV 269
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
31-239 |
7.22e-51 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 168.03 E-value: 7.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPqaqKLRRQKIQIVFQNPYG 110
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSL---KELRRKVGLVFQNPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 111 SLnprkkVGQILEEPL---LINSNLNKEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADE 187
Cdd:cd03225 87 QF-----FGPTVEEEVafgLENLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 527035742 188 PVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
36-253 |
1.35e-50 |
|
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: 168.25 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLT-MIEvPTGGELYYQGQDLLKHDPQaqKLRRqKIQIVFQNPygSLNP 114
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINrLIE-PTSGEIFIDGEDIREQDPV--ELRR-KIGYVIQQI--GLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 RKKVGQ-ILEEPLLINsnLNKEQRREKALAMMAKVGLKTEHY-DRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSAL 192
Cdd:cd03295 89 HMTVEEnIALVPKLLK--WPKEKIRERADELLALVGLDPAEFaDRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527035742 193 DVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHP 253
Cdd:cd03295 167 DPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
35-292 |
1.91e-50 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 171.43 E-value: 1.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLgrlLTMI---EVPTGGELYYQGQDLLKHDPQaqklRRQkIQIVFQNpYgS 111
Cdd:COG3842 18 VTALDDVSLSIEPGEFVALLGPSGCGKTTL---LRMIagfETPDSGRILLDGRDVTGLPPE----KRN-VGMVFQD-Y-A 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 112 LNPRKKVGQILEEPLLInSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSA 191
Cdd:COG3842 88 LFPHLTVAENVAFGLRM-RGVPKAEIRARVAELLELVGL-EGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 192 LDVSVRAQVLNLMMDLQQDMGLSYVFISHD----LSvvehIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTqA------- 260
Cdd:COG3842 166 LDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRIAVMNDGRIEQVGTPEEIYERPATRFV-Adfigean 240
|
250 260 270
....*....|....*....|....*....|....*
gi 527035742 261 LLSATPRlnpDDRRERIKLTG---ELPSPLNPPPG 292
Cdd:COG3842 241 LLPGTVL---GDEGGGVRTGGrtlEVPADAGLAAG 272
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
35-239 |
7.02e-50 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 164.28 E-value: 7.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQKLRRqKIQIVFQNPygSLNP 114
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR-RIGMVFQDF--ALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 RKKVGQILEEPLlinsnlnkeqrrekalammakvglktehydryphmfSGGQRQRIAIARGLMLDPDVVIADEPVSALDV 194
Cdd:cd03229 90 HLTVLENIALGL------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 527035742 195 SVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:cd03229 134 ITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
13-249 |
2.26e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.85 E-value: 2.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 13 LQAIDLKKYYPVKKglfaperlvkALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQ 92
Cdd:COG1131 1 IEVRGLTKRYGDKT----------ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 93 AqklrRQKIQIVFQNPygSLNPRKKVGQILEeplLINS--NLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRI 170
Cdd:COG1131 71 V----RRRIGYVPQEP--ALYPDLTVRENLR---FFARlyGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 171 AIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 249
Cdd:COG1131 141 GLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
35-244 |
3.45e-49 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 163.84 E-value: 3.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPqaqklRRQKIQIVFQNPygSLNP 114
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP-----ERRNIGMVFQDY--ALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 RKKVGQILEEPLLINsNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDV 194
Cdd:cd03259 86 HLTVAENIAFGLKLR-GVPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 527035742 195 SVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 244
Cdd:cd03259 164 KLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
13-239 |
7.18e-49 |
|
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: 163.08 E-value: 7.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 13 LQAIDLKKYYpvkkGLFaperlvKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQ 92
Cdd:cd03262 1 IEIKNLHKSF----GDF------HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 93 AQKLRrQKIQIVFQNPYgsLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQRIAI 172
Cdd:cd03262 71 INELR-QKVGMVFQQFN--LFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527035742 173 ARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
10-264 |
8.24e-49 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 164.23 E-value: 8.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 10 QPLLQAIDLKKYYPVKKGLFaperlvkaldGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKH 89
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCR----------DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 90 D------PQAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFS 163
Cdd:TIGR02323 71 ElyqlseAERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDPTRIDDLPRAFS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 164 GGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEK 243
Cdd:TIGR02323 151 GGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVES 230
|
250 260
....*....|....*....|.
gi 527035742 244 GTKEQIFTHPRHPYTQALLSA 264
Cdd:TIGR02323 231 GLTDQVLDDPQHPYTQLLVSS 251
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
36-257 |
3.83e-48 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 164.11 E-value: 3.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLT-MIEvPTGGELYYQGQDLLKHDPQaqKLRRQkIQIVFQNpyGSLNP 114
Cdd:COG1125 16 VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINrLIE-PTSGRILIDGEDIRDLDPV--ELRRR-IGYVIQQ--IGLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 RKKVGQ-ILEEPLLINSNlnKEQRREKALAMMAKVGLKTEHY-DRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSAL 192
Cdd:COG1125 90 HMTVAEnIATVPRLLGWD--KERIRARVDELLELVGLDPEEYrDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527035742 193 DVSVRAQVLNLMMDLQQDMGLSYVFISHDLSvvE--HIADEVMVMYLGRCVEKGTKEQIFTHPRHPY 257
Cdd:COG1125 168 DPITREQLQDELLRLQRELGKTIVFVTHDID--EalKLGDRIAVMREGRIVQYDTPEEILANPANDF 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
36-294 |
5.47e-48 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 164.55 E-value: 5.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPqaqkLRRQKIQIVFQNP------- 108
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLP----PRERRVGFVFQHYalfphmt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 109 ------YGslnPRKKvgqileepllinsNLNKEQRREKALAMMAKVGLktEHY-DRYPHMFSGGQRQRIAIARGLMLDPD 181
Cdd:COG1118 92 vaeniaFG---LRVR-------------PPSKAEIRARVEELLELVQL--EGLaDRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 182 VVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQAL 261
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARF 233
|
250 260 270
....*....|....*....|....*....|....
gi 527035742 262 LSATPRLNPDDRRERIKLTG-ELPSPLNPPPGCA 294
Cdd:COG1118 234 LGCVNVLRGRVIGGQLEADGlTLPVAEPLPDGPA 267
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
37-253 |
6.22e-48 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 161.33 E-value: 6.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDL-LKHDPQAQKLR--RQKIQIVFQNpYgSLN 113
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdFSQKPSEKAIRllRQKVGMVFQQ-Y-NLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 114 PRKKVGQ-ILEEPLLInSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSAL 192
Cdd:COG4161 95 PHLTVMEnLIEAPCKV-LGLSKEQAREKAMKLLARLRL-TDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527035742 193 DVSVRAQVLNLMMDLQQdMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEqIFTHP 253
Cdd:COG4161 173 DPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQP 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
36-253 |
1.04e-47 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 160.95 E-value: 1.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDL-LKHDPQAQKLR--RQKIQIVFQNpYgSL 112
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdFSKTPSDKAIRelRRNVGMVFQQ-Y-NL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 113 NPRKKVGQIL-EEPLLInSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSA 191
Cdd:PRK11124 94 WPHLTVQQNLiEAPCRV-LGLSKDQALARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527035742 192 LDVSVRAQVLNLMMDLQQdMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQiFTHP 253
Cdd:PRK11124 172 LDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQP 231
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
36-253 |
1.23e-47 |
|
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: 161.85 E-value: 1.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQKLRRQKIQIVFQNP-Ygslnp 114
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPeH----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 rkkvgQILEEPLL-------INSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADE 187
Cdd:TIGR04521 94 -----QLFEETVYkdiafgpKNLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527035742 188 PVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHP 253
Cdd:TIGR04521 169 PTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
37-253 |
4.73e-47 |
|
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: 158.94 E-value: 4.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQaqklRRQkIQIVFQNpYgSLNPRK 116
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH----KRP-VNTVFQN-Y-ALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 KVGQILEEPLLInSNLNKEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSV 196
Cdd:cd03300 88 TVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 527035742 197 RAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHP 253
Cdd:cd03300 166 RKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
12-242 |
7.78e-46 |
|
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: 155.20 E-value: 7.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 12 LLQAIDLKKYYPVKKglfapeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDP 91
Cdd:TIGR02211 1 LLKCENLGKRYQEGK------LDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 92 QAQ-KLRRQKIQIVFQnpYGSLNPRKKVGQILEEPLLInSNLNKEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQRI 170
Cdd:TIGR02211 75 NERaKLRNKKLGFIYQ--FHHLLPDFTALENVAMPLLI-GKKSVKEAKERAYEMLEKVGLE-HRINHRPSELSGGERQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527035742 171 AIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIaDEVMVMYLGRCVE 242
Cdd:TIGR02211 151 AIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
31-323 |
3.49e-45 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 156.89 E-value: 3.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVP----TGGELYYQGQDLLKHDP-QAQKLRRQKIQIVF 105
Cdd:PRK15093 16 SDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPrERRKLVGHNVSMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 106 QNPYGSLNPRKKVGQILEEPllINSNLNKEQ-------RREKALAMMAKVGLKtEHYD---RYPHMFSGGQRQRIAIARG 175
Cdd:PRK15093 96 QEPQSCLDPSERVGRQLMQN--IPGWTYKGRwwqrfgwRKRRAIELLHRVGIK-DHKDamrSFPYELTEGECQKVMIAIA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 176 LMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRH 255
Cdd:PRK15093 173 LANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHH 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 256 PYTQALLSATPRL-NPDDRRERIK-LTGELPSPLNPPPGCAFNARCSRRFGPCTQlQPQLKDYGGQLVAC 323
Cdd:PRK15093 253 PYTQALIRAIPDFgSAMPHKSRLNtLPGAIPLLEHLPIGCRLGPRCPYAQRECIE-TPRLTGAKNHLYAC 321
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
28-264 |
5.88e-45 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 154.09 E-value: 5.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 28 LFAPERLVkalDGVSFTLERGKTLAVVGESGCGKS-TLGRLLTMIevPTGGElYYQGQDLLKHDPQA-QKLRRQKIQIVF 105
Cdd:PRK10418 12 LQAAQPLV---HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGIL--PAGVR-QTAGRVLLDGKPVApCALRGRKIATIM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 106 QNPYGSLNPRKKVGQILEEPLLInsnLNKEQRREKALAMMAKVGLKTEH--YDRYPHMFSGGQRQRIAIARGLMLDPDVV 183
Cdd:PRK10418 86 QNPRSAFNPLHTMHTHARETCLA---LGKPADDATLTAALEAVGLENAArvLKLYPFEMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 184 IADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQALLS 263
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
.
gi 527035742 264 A 264
Cdd:PRK10418 243 A 243
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
36-249 |
1.94e-44 |
|
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: 151.95 E-value: 1.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLT-MIE----VPTGGELYYQGQDLLKHDPQAQKLRRQkIQIVFQNPyg 110
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrLNDlipgAPDEGEVLLDGKDIYDLDVDVLELRRR-VGMVFQKP-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 111 slNP-RKKVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKTEHYDR-YPHMFSGGQRQRIAIARGLMLDPDVVIADEP 188
Cdd:cd03260 91 --NPfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527035742 189 VSALDVSVRAQVLNLMMDLQQDMGLsyVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 249
Cdd:cd03260 169 TSALDPISTAKIEELIAELKKEYTI--VIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
38-239 |
2.12e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 151.12 E-value: 2.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqkLRRQkIQIVFQNPY---GSlnp 114
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE--WRRQ-VAYVPQEPAlwgGT--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 rkkVGQILEEPLLINsnlNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDV 194
Cdd:COG4619 90 ---VRDNLPFPFQLR---ERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 527035742 195 SVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:COG4619 164 ENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
31-249 |
3.24e-44 |
|
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: 161.16 E-value: 3.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqkLRRQkIQIVFQNPY- 109
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS--LRRQ-IGVVLQDVFl 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 110 --GSlnprkkvgqILEEPLLINSNLNKEQRRE-----------KALAMmakvGLKTEHYDRYpHMFSGGQRQRIAIARGL 176
Cdd:COG2274 561 fsGT---------IRENITLGDPDATDEEIIEaarlaglhdfiEALPM----GYDTVVGEGG-SNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527035742 177 MLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLsyVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 249
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLLKGRTV--IIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
38-188 |
8.88e-44 |
|
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: 147.79 E-value: 8.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPqaqKLRRQKIQIVFQNPygSLNPRKK 117
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER---KSLRKEIGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527035742 118 VGQILEEPLLI--NSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEP 188
Cdd:pfam00005 76 VRENLRLGLLLkgLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
36-257 |
9.44e-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: 150.57 E-value: 9.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQaqklRRQkIQIVFQN--PYGSLN 113
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ----ERN-VGFVFQHyaLFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 114 PRKKVGQILEEPLlINSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALD 193
Cdd:cd03296 91 VFDNVAFGLRVKP-RSERPPEAEIRAKVHELLKLVQL-DWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527035742 194 VSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPY 257
Cdd:cd03296 169 AKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
37-268 |
1.57e-43 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 149.95 E-value: 1.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPqaqklRRQKIQIVFQN--PYGSLNP 114
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHA-----RDRKIGFVFQHyaLFKHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 RKKVGQILEepLLINSNLNKEQRREKALAMMAKVGLKtehyDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDV 194
Cdd:TIGR00968 90 RDNIAFGLE--IRKHPKAKIKARVEELLELVQLEGLG----DRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527035742 195 SVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQALLSATPRL 268
Cdd:TIGR00968 164 KVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-249 |
3.92e-43 |
|
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: 148.85 E-value: 3.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 12 LLQAIDLKKYYpvkkglfapeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDP 91
Cdd:COG4555 1 MIEVENLSKKY----------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 92 QAqklrRQKIQIVFQNPYgsLNPRKKVGQILEEPLLINsNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIA 171
Cdd:COG4555 71 EA----RRQIGVLPDERG--LYDRLTVRENIRYFAELY-GLFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527035742 172 IARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 249
Cdd:COG4555 143 LARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
35-246 |
1.09e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 147.12 E-value: 1.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDL--LKHDpQAQKLRRqKIQIVFQNpyGSL 112
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrLKRR-EIPYLRR-RIGVVFQD--FRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 113 NPRKKVGQILEEPLLInSNLNKEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSAL 192
Cdd:COG2884 91 LPDRTVYENVALPLRV-TGKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 527035742 193 DVSVRAQVLNLMMDLQQdMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTK 246
Cdd:COG2884 169 DPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
35-254 |
1.14e-42 |
|
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: 147.58 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPqaQKLRRQKIQIVFQNP--YGSL 112
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP--HEIARLGIGRTFQIPrlFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 113 ----NPRKKVGQILEEPLLINSNLNKEQR-REKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADE 187
Cdd:cd03219 91 tvleNVMVAAQARTGSGLLLARARREEREaRERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527035742 188 PVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPR 254
Cdd:cd03219 170 PAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
6-242 |
2.03e-42 |
|
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: 146.81 E-value: 2.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 6 ATTQQPLLQAIDLKKYYPvkkglfAPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQD 85
Cdd:COG4181 2 SSSSAPIIELRGLTKTVG------TGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 86 L--LKHDPQAQkLRRQKIQIVFQN----PygSLNPRKKVGQILEEpllinsnLNKEQRREKALAMMAKVGLKtEHYDRYP 159
Cdd:COG4181 76 LfaLDEDARAR-LRARHVGFVFQSfqllP--TLTALENVMLPLEL-------AGRRDARARARALLERVGLG-HRLDHYP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 160 HMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHiADEVMVMYLGR 239
Cdd:COG4181 145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGR 223
|
...
gi 527035742 240 CVE 242
Cdd:COG4181 224 LVE 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
31-239 |
2.55e-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: 144.45 E-value: 2.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqklRRQKIQIVFQNPY- 109
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES---LRKNIAYVPQDPFl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 110 --GSlnprkkvgqILEepllinsNLnkeqrrekalammakvglktehydryphmFSGGQRQRIAIARGLMLDPDVVIADE 187
Cdd:cd03228 88 fsGT---------IRE-------NI-----------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 527035742 188 PVSALDVSVRAQVLNLMMDLQQDMGLsyVFISHDLSVVEHiADEVMVMYLGR 239
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTV--IVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
35-257 |
7.66e-42 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 148.68 E-value: 7.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQaqklRRqKIQIVFQNPygSLNP 114
Cdd:COG3839 16 VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK----DR-NIAMVFQSY--ALYP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 RKKVGQILEEPLLInSNLNKEQRREKALAMMAKVGLktEHY-DRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALD 193
Cdd:COG3839 89 HMTVYENIAFPLKL-RKVPKAEIDRRVREAAELLGL--EDLlDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527035742 194 VSVRAQVLNLMMDLQQDMGLSYVFISHDLsvVE--HIADEVMVMYLGRCVEKGTKEQIFTHPRHPY 257
Cdd:COG3839 166 AKLRVEMRAEIKRLHRRLGTTTIYVTHDQ--VEamTLADRIAVMNDGRIQQVGTPEELYDRPANLF 229
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
35-241 |
8.97e-42 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 145.58 E-value: 8.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQA-QKLRRQkIQIVFQNPYgsLN 113
Cdd:COG3638 16 TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlRRLRRR-IGMIFQQFN--LV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 114 PRKKV---------GQIleePLL--INSNLNKEQRrEKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDV 182
Cdd:COG3638 93 PRLSVltnvlagrlGRT---STWrsLLGLFPPEDR-ERALEALERVGL-ADKAYQRADQLSGGQQQRVAIARALVQEPKL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 183 VIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCV 241
Cdd:COG3638 168 ILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
36-239 |
1.80e-41 |
|
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: 142.00 E-value: 1.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqklRRQKIQIVFQnpygslnpr 115
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE---LRRRIGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 116 kkvgqileepllinsnlnkeqrrekalammakvglktehydryphmFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVS 195
Cdd:cd00267 81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 527035742 196 VRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:cd00267 115 SRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
12-252 |
2.71e-41 |
|
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: 144.36 E-value: 2.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 12 LLQAIDLKKYYPVKKglfaperlvKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKhdP 91
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---------QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITK--L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 92 QAQKLR--RQKIQIVFQNpYgSLNPRKKVGQILEEPLL-----INSNLN--KEQRREKALAMMAKVGLKTEHYDRYPHMf 162
Cdd:TIGR02315 70 RGKKLRklRRRIGMIFQH-Y-NLIERLTVLENVLHGRLgykptWRSLLGrfSEEDKERALSALERVGLADKAYQRADQL- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 163 SGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVE 242
Cdd:TIGR02315 147 SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVF 226
|
250
....*....|
gi 527035742 243 KGTKEQIFTH 252
Cdd:TIGR02315 227 DGAPSELDDE 236
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-239 |
5.00e-41 |
|
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: 141.38 E-value: 5.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 13 LQAIDLKKYYPVKKglfaperlvkALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQ 92
Cdd:cd03230 1 IEVRNLSKRYGKKT----------ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 93 AqklrRQKIQIVFQNPygSLNPRKKVGQILEepllinsnlnkeqrrekalammakvglktehydryphmFSGGQRQRIAI 172
Cdd:cd03230 71 V----KRRIGYLPEEP--SLYENLTVRENLK--------------------------------------LSGGMKQRLAL 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527035742 173 ARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:cd03230 107 AQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
37-251 |
1.20e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 143.21 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDpqaQKLRRQKIQIVFQNPYGSLnprk 116
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN---LKEIRKKIGIIFQNPDNQF---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 kVGQILEEPL---LINSNLNKEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALD 193
Cdd:PRK13632 97 -IGATVEDDIafgLENKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 194 VSVRAQVLNLMMDLQQDMGLSYVFISHDLSvvEHI-ADEVMVMYLGRCVEKGTKEQIFT 251
Cdd:PRK13632 175 PKGKREIKKIMVDLRKTRKKTLISITHDMD--EAIlADKVIVFSEGKLIAQGKPKEILN 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-241 |
1.28e-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: 139.87 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 13 LQAIDLKKYYPVkkglfaperlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQ 92
Cdd:cd03216 1 LELRGITKRFGG----------VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 93 AQklRRQKIQIVFQnpygslnprkkvgqileepllinsnlnkeqrrekalammakvglktehydryphmFSGGQRQRIAI 172
Cdd:cd03216 71 DA--RRAGIAMVYQ-------------------------------------------------------LSVGERQMVEI 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 173 ARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCV 241
Cdd:cd03216 94 ARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
35-249 |
1.90e-40 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 141.94 E-value: 1.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQKLRRQKIQIVFQNPygSLNP 114
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIGMIFQQF--NLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 RKKVGQ-ILEEPL----LINS--NLNKEQRREKALAMMAKVGLKTEHYDRYPHMfSGGQRQRIAIARGLMLDPDVVIADE 187
Cdd:cd03256 92 RLSVLEnVLSGRLgrrsTWRSlfGLFPKEEKQRALAALERVGLLDKAYQRADQL-SGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527035742 188 PVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 249
Cdd:cd03256 171 PVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
38-263 |
2.80e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 141.81 E-value: 2.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGG-----ELYYQGQDLLKHDPQAQKLRRQKIQIVFQNpyGSL 112
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARSLSQQKGLIRQLRQHVGFVFQN--FNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 113 NPRKKVGQ-ILEEPLLINSNlNKEQRREKALAMMAKVGLKTEHyDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSA 191
Cdd:PRK11264 97 FPHRTVLEnIIEGPVIVKGE-PKEEATARARELLAKVGLAGKE-TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527035742 192 LDVSVRAQVLNLMMDLQQDMgLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQALLS 263
Cdd:PRK11264 175 LDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-264 |
3.93e-40 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 141.48 E-value: 3.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 6 ATTQQPLLQAIDLKKYYPVkkglfaperlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQD 85
Cdd:COG4598 2 TDTAPPALEVRDLHKSFGD----------LEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 86 L-LKHDP----------QAQKLRRQkIQIVFQNpyGSLNPRKKVGQ-ILEEPLLINsNLNKEQRREKALAMMAKVGLkTE 153
Cdd:COG4598 72 IrLKPDRdgelvpadrrQLQRIRTR-LGMVFQS--FNLWSHMTVLEnVIEAPVHVL-GRPKAEAIERAEALLAKVGL-AD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 154 HYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVM 233
Cdd:COG4598 147 KRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVV 225
|
250 260 270
....*....|....*....|....*....|.
gi 527035742 234 VMYLGRCVEKGTKEQIFTHPRHPYTQALLSA 264
Cdd:COG4598 226 FLHQGRIEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
36-265 |
1.60e-39 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 140.10 E-value: 1.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDL-LKHDPQAQ---------KLRRQKIQIVF 105
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInLVRDKDGQlkvadknqlRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 106 QNpYGSLNPRKKVGQILEEPLLInSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIA 185
Cdd:PRK10619 99 QH-FNLWSHMTVLENVMEAPIQV-LGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 186 DEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQALLSAT 265
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLKGS 255
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-242 |
5.89e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 144.01 E-value: 5.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 10 QPLLQAIDLKKYYPvkkGlfaperlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKH 89
Cdd:COG1129 2 EPLLEMRGISKSFG---G-------VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 90 DP-QAQKLRrqkIQIVFQnpygslnprkkvgqileEPLLINS-----N--LNKEQRR----------EKALAMMAKVGLk 151
Cdd:COG1129 72 SPrDAQAAG---IAIIHQ-----------------ELNLVPNlsvaeNifLGREPRRgglidwramrRRARELLARLGL- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 152 teHYDryPHM----FSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEH 227
Cdd:COG1129 131 --DID--PDTpvgdLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFE 205
|
250
....*....|....*
gi 527035742 228 IADEVMVMYLGRCVE 242
Cdd:COG1129 206 IADRVTVLRDGRLVG 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-254 |
7.75e-39 |
|
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: 138.25 E-value: 7.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 10 QPLLQAIDLKKYYpvkKGLfaperlvKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKH 89
Cdd:COG0411 2 DPLLEVRGLTKRF---GGL-------VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 90 DPQaqKLRRQKIQIVFQNP--YGSL----N-----PRKKVGQILEEPLLINSNLNKEQR-REKALAMMAKVGLkTEHYDR 157
Cdd:COG0411 72 PPH--RIARLGIARTFQNPrlFPELtvleNvlvaaHARLGRGLLAALLRLPRARREEREaRERAEELLERVGL-ADRADE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 158 YPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYL 237
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF 228
|
250
....*....|....*..
gi 527035742 238 GRCVEKGTKEQIFTHPR 254
Cdd:COG0411 229 GRVIAEGTPAEVRADPR 245
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
36-250 |
9.29e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 139.03 E-value: 9.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQKLRRqKIQIVFQNP-Ygslnp 114
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRK-KVGLVFQYPeY----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 rkkvgQILEEPL-------LINSNLNKEQRREKALAMMAKVGLKTEHY-DRYPHMFSGGQRQRIAIARGLMLDPDVVIAD 186
Cdd:PRK13637 95 -----QLFEETIekdiafgPINLGLSEEEIENRVKRAMNIVGLDYEDYkDKSPFELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527035742 187 EPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIF 250
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
37-252 |
2.19e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 137.84 E-value: 2.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlkhDPQAQKLRRQKIQIVFQNPYGSLnprk 116
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL---SEETVWDVRRQVGMVFQNPDNQF---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 kVGQILEEPL---LINSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALD 193
Cdd:PRK13635 95 -VGATVQDDVafgLENIGVPREEMVERVDQALRQVGM-EDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 194 VSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFTH 252
Cdd:PRK13635 173 PRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
38-262 |
3.24e-38 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 135.99 E-value: 3.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLkhDPQAQ-KLRRQKIQIVFQNPYgsLNPRK 116
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN--DPKVDeRLIRQEAGMVFQQFY--LFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 KVgqiLEE----PLLINSnLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSAL 192
Cdd:PRK09493 93 TA---LENvmfgPLRVRG-ASKEEAEKQARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 193 DVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQALL 262
Cdd:PRK09493 168 DPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
38-251 |
3.38e-38 |
|
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: 136.33 E-value: 3.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqklRRQKIQIVFQNPYGSLN---- 113
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE---LARRIAYVPQEPPAPFGltvr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 114 --------PRKKVGQILeepllinsnlnKEQRREKALAMMAKVGLktEHY-DRYPHMFSGGQRQRIAIARGLMLDPDVVI 184
Cdd:COG1120 94 elvalgryPHLGLFGRP-----------SAEDREAVEEALERTGL--EHLaDRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527035742 185 ADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFT 251
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
35-244 |
3.48e-38 |
|
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: 135.07 E-value: 3.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPqaqklRRQKIQIVFQNpYgSLNP 114
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP-----KDRDIAMVFQN-Y-ALYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 RKKVGQILEEPLlinsNLNKEQRRE--KALAMMAKVgLKTEHY-DRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSA 191
Cdd:cd03301 86 HMTVYDNIAFGL----KLRKVPKDEidERVREVAEL-LQIEHLlDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 527035742 192 LDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 244
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
37-252 |
5.08e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 136.42 E-value: 5.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlkhDPQAQKLRRQKIQIVFQNPYGSLnprk 116
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEKLRKHIGIVFQNPDNQF---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 kVGQILEEPL---LINSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALD 193
Cdd:PRK13648 97 -VGSIVKYDVafgLENHAVPYDEMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 194 VSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFTH 252
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
41-239 |
3.12e-37 |
|
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: 132.80 E-value: 3.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 41 VSFTLErGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLkhDPQaQKL----RRQKIQIVFQNpyGSLNPRK 116
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLF--DSR-KKInlppQQRKIGLVFQQ--YALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 KVGQILEEPLLINSNLNKEQRREKALAMMAKVGLKtehyDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSV 196
Cdd:cd03297 91 NVRENLAFGLKRKRNREDRISVDELLDLLGLDHLL----NRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 527035742 197 RAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-263 |
3.14e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 134.01 E-value: 3.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 3 TQQATTQQPLLQAIDLKKYYpvkkGLFaperlvKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLT-MIE-VP---TGG 77
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYY----GDK------QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNrMNDlIPgarVEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 78 ELYYQGQDLLKHDPQAQKLRRqKIQIVFQNP------------YGslnPRkkvgqileepllINSNLNK---EQRREKAL 142
Cdd:COG1117 72 EILLDGEDIYDPDVDVVELRR-RVGMVFQKPnpfpksiydnvaYG---LR------------LHGIKSKselDEIVEESL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 143 AmmaKVGLKTEHYDR---YPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALD-VSVrAQVLNLMMDLQQDMglSYVFI 218
Cdd:COG1117 136 R---KAALWDEVKDRlkkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpIST-AKIEELILELKKDY--TIVIV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 527035742 219 SHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQALLS 263
Cdd:COG1117 210 THNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYIT 254
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
38-253 |
3.42e-37 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 133.23 E-value: 3.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQaqklrRQKIQIVFQNPYgsLNPRKK 117
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISYVPQNYA--LFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 118 VGQILEEPLlINSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVR 197
Cdd:cd03299 88 VYKNIAYGL-KKRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 527035742 198 AQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHP 253
Cdd:cd03299 166 EKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
42-264 |
1.33e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 131.42 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 42 SFTLERGKTLAVVGESGCGKSTLgrlLTMI---EVPTGGELYYQGQDLLKHDPqAQKlrrqKIQIVFQ--NPYGSLNPRK 116
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTL---LNLIagfLPPDSGRILWNGQDLTALPP-AER----PVSMLFQenNLFPHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 KVGqileepLLINSN--LNKEQRrEKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDV 194
Cdd:COG3840 91 NIG------LGLRPGlkLTAEQR-AQVEQALERVGL-AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 195 SVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQALLSA 264
Cdd:COG3840 163 ALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
31-248 |
1.69e-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: 138.36 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqklRRQKIQIVFQNPY- 109
Cdd:COG4987 344 PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD---LRRRIAVVPQRPHl 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 110 --GSlnprkkvgqILEEPLLINSNLNKEQrrekALAMMAKVGLkTEHYDRYPH-----------MFSGGQRQRIAIARGL 176
Cdd:COG4987 421 fdTT---------LRENLRLARPDATDEE----LWAALERVGL-GDWLAALPDgldtwlgeggrRLSGGERRRLALARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527035742 177 MLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLsyVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQ 248
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV--LLITHRLAGLER-MDRILVLEDGRIVEQGTHEE 555
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
10-224 |
1.88e-36 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 131.48 E-value: 1.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 10 QPLLQAIDLKKYYpvKKGLFAPErlvkALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKH 89
Cdd:PRK11629 3 KILLQCDNLCKRY--QEGSVQTD----VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 90 DPQAQ-KLRRQKIQIVFQnpYGSLNPRKKVGQILEEPLLInSNLNKEQRREKALAMMAKVGLKTEHYDRyPHMFSGGQRQ 168
Cdd:PRK11629 77 SSAAKaELRNQKLGFIYQ--FHHLLPDFTALENVAMPLLI-GKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 527035742 169 RIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSV 224
Cdd:PRK11629 153 RVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQL 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
38-244 |
2.81e-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: 129.09 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPqaqKLRRQKIQIVFQnpygslnprkk 117
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSP---KELARKIAYVPQ----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 118 vgqileepllinsnlnkeqrrekalaMMAKVGLktEHY-DRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSV 196
Cdd:cd03214 81 --------------------------ALELLGL--AHLaDRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 527035742 197 RAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 244
Cdd:cd03214 133 QIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
53-262 |
4.37e-36 |
|
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: 133.00 E-value: 4.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 53 VVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQaqklrRQKIQIVFQNpYgSLNPRKKVGQILEEPLLINSnL 132
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH-----LRHINMVFQS-Y-ALFPHMTVEENVAFGLKMRK-V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 133 NKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMG 212
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 527035742 213 LSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQALL 262
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
38-253 |
5.05e-36 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 133.31 E-value: 5.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQaqklrRQKIQIVFQNpYgSLNPRKK 117
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-----QRDICMVFQS-Y-ALFPHMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 118 VGQILEEPLLInSNLNKEQRREK---ALAMMAKVGLKtehyDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDV 194
Cdd:PRK11432 95 LGENVGYGLKM-LGVPKEERKQRvkeALELVDLAGFE----DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 195 SVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHP 253
Cdd:PRK11432 170 NLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
10-249 |
1.42e-35 |
|
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: 134.93 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 10 QPLLQAIDLKK-YYPVKKGLfaperlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQ-GQ--- 84
Cdd:TIGR03269 277 EPIIKVRNVSKrYISVDRGV------VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDewv 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 85 DLLKHDPQAQKLRRQKIQIVFQNpYGsLNPRKKVGQILEEPllINSNLNKEQRREKALAMMAKVGLKTEH----YDRYPH 160
Cdd:TIGR03269 351 DMTKPGPDGRGRAKRYIGILHQE-YD-LYPHRTVLDNLTEA--IGLELPDELARMKAVITLKMVGFDEEKaeeiLDKYPD 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 161 MFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRC 240
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
....*....
gi 527035742 241 VEKGTKEQI 249
Cdd:TIGR03269 507 VKIGDPEEI 515
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
12-253 |
4.09e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 129.04 E-value: 4.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 12 LLQAIDLKKYYPvkKGlfaperlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlKHDP 91
Cdd:PRK13639 1 ILETRDLKYSYP--DG-------TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 92 QAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLliNSNLNKEQRREKALAMMAKVGLktEHYDRY-PHMFSGGQRQRI 170
Cdd:PRK13639 71 KSLLEVRKTVGIVFQNPDDQLFAPTVEEDVAFGPL--NLGLSKEEVEKRVKEALKAVGM--EGFENKpPHHLSGGQKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 171 AIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIF 250
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
...
gi 527035742 251 THP 253
Cdd:PRK13639 226 SDI 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
37-250 |
6.38e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 128.67 E-value: 6.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLkhDPQAQKLRRQKIQIVFQNPYGSLnprk 116
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS--DEENLWDIRNKAGMVFQNPDNQI---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 kVGQILEEPLLI---NSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALD 193
Cdd:PRK13633 99 -VATIVEEDVAFgpeNLGIPPEEIRERVDESLKKVGM-YEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 527035742 194 VSVRAQVLNLMMDLQQDMGLSYVFISHDL-SVVEhiADEVMVMYLGRCVEKGTKEQIF 250
Cdd:PRK13633 177 PSGRREVVNTIKELNKKYGITIILITHYMeEAVE--ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
37-248 |
9.26e-35 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 133.34 E-value: 9.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqklRRQKIQIVFQNPY---GSLn 113
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS---WRRQIAWVPQNPYlfaGTI- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 114 prkkvgqilEEPLLI-NSNLNKEQRREkALAmmaKVGLkTEHYDRYPH-----------MFSGGQRQRIAIARGLMLDPD 181
Cdd:COG4988 428 ---------RENLRLgRPDASDEELEA-ALE---AAGL-DEFVAALPDgldtplgeggrGLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527035742 182 VVIADEPVSALDVSVRAQVLNLMMDLQQdmGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQ 248
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
32-249 |
1.25e-34 |
|
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: 125.95 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 32 ERLVK------ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKhdpQAQKLRRqKIQIVF 105
Cdd:cd03265 4 ENLVKkygdfeAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR---EPREVRR-RIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 106 QNPygslnprkKVGQILE--EPLLINS---NLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDP 180
Cdd:cd03265 80 QDL--------SVDDELTgwENLYIHArlyGVPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 181 DVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 249
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
42-262 |
1.72e-34 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 130.15 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 42 SFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLK-HDPQAQKLRRQKIQIVFQN----PYGSLNPRK 116
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKiSDAELREVRRKKIAMVFQSfalmPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 KVGQILeepllinSNLNKEQRREKALAMMAKVGLktEHYDR-YPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVS 195
Cdd:PRK10070 128 AFGMEL-------AGINAEERREKALDALRQVGL--ENYAHsYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527035742 196 VRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQALL 262
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-259 |
2.14e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 126.57 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMI-----EVPTGGELYYQGQDLLKHDpqAQKLRRqKIQIVFQ--N 107
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD--VIELRR-RVQMVFQipN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 108 PYGSLNPRKKVGQILEEPLLINSNLNKEQRREKALAmmaKVGLKTEHYDRY---PHMFSGGQRQRIAIARGLMLDPDVVI 184
Cdd:PRK14247 93 PIPNLSIFENVALGLKLNRLVKSKKELQERVRWALE---KAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527035742 185 ADEPVSALDVSVRAQVLNLMMDLQQDMGLsyVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQ 259
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDMTI--VLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTE 242
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
35-253 |
2.23e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 127.23 E-value: 2.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDpqaQKLRRQKIQIVFQNPYGSLNP 114
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN---IREVRKFVGLVFQNPDDQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 RKKVGQILEEPllINSNLNKE---QRREKALAMmakVGLKtEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSA 191
Cdd:PRK13652 94 PTVEQDIAFGP--INLGLDEEtvaHRVSSALHM---LGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527035742 192 LDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHP 253
Cdd:PRK13652 168 LDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
36-253 |
4.52e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 126.67 E-value: 4.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYqGQDLLKHDPQAQKLR--RQKIQIVFQNPYGsln 113
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKLKplRKKVGIVFQFPEH--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 114 prkkvgQILEEPLL-------INSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIAD 186
Cdd:PRK13634 97 ------QLFEETVEkdicfgpMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527035742 187 EPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHP 253
Cdd:PRK13634 171 EPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
36-250 |
8.09e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 125.66 E-value: 8.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELyyQGQDL-LKHDPQAQKLR--RQKIQIVFQNPYGSL 112
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTV--TVDDItITHKTKDKYIRpvRKRIGMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 113 NPRKKVGQILEEPLliNSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSAL 192
Cdd:PRK13646 99 FEDTVEREIIFGPK--NFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 527035742 193 DVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIF 250
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
29-248 |
1.34e-33 |
|
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: 123.88 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 29 FAPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDpqaQKLRRQKIQIVFQNP 108
Cdd:cd03253 10 YDPGRPV--LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLRRAIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 109 ------------YGslnprkkvgqileeplliNSNLNKEQRREKALAmmAKVGLKTEhydRYPH-----------MFSGG 165
Cdd:cd03253 85 vlfndtigynirYG------------------RPDATDEEVIEAAKA--AQIHDKIM---RFPDgydtivgerglKLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 166 QRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQdmGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGT 245
Cdd:cd03253 142 EKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
...
gi 527035742 246 KEQ 248
Cdd:cd03253 219 HEE 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-258 |
1.36e-33 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 127.26 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 3 TQQATTqqPLLQAIDLKKYYPVKKglfaperlvkALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQ 82
Cdd:PRK11607 12 TRKALT--PLLEIRNLTKSFDGQH----------AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 83 GQDLlKHDPQAQKlrrqKIQIVFQNpYgSLNPRKKVGQILEEPLLiNSNLNKEQRREKALAMMAKVGLKtEHYDRYPHMF 162
Cdd:PRK11607 80 GVDL-SHVPPYQR----PINMMFQS-Y-ALFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 163 SGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVE 242
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
|
250
....*....|....*.
gi 527035742 243 KGTKEQIFTHPRHPYT 258
Cdd:PRK11607 231 IGEPEEIYEHPTTRYS 246
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
35-235 |
2.06e-33 |
|
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: 122.93 E-value: 2.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLgrlLTMI---EVPTGGELYYQGQ----DLLKHDP-QAQKLRRQKIQIVFQ 106
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTL---LKCIygnYLPDSGSILVRHDggwvDLAQASPrEILALRRRTIGYVSQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 107 npygSLN--PRKKVGQILEEPLLiNSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVI 184
Cdd:COG4778 101 ----FLRviPRVSALDVVAEPLL-ERGVDREEARARARELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 527035742 185 ADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVM 235
Cdd:COG4778 176 LDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDV 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
36-248 |
2.21e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 129.51 E-value: 2.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLT-MIEvPTGGELYYQGQDLLKHDPQAqkLRRQkIQIVFQNPY---GS 111
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLrFYD-PTSGRILIDGVDIRDLTLES--LRRQ-IGVVPQDTFlfsGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 112 lnprkkvgqILEepllinsNL---NKEQRREKALAMMAKVGLkTEHYDRYPH-----------MFSGGQRQRIAIARGLM 177
Cdd:COG1132 430 ---------IRE-------NIrygRPDATDEEVEEAAKAAQA-HEFIEALPDgydtvvgergvNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527035742 178 LDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLsyVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQ 248
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGRTT--IVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEE 560
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
37-250 |
2.63e-33 |
|
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: 122.72 E-value: 2.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDpqaQKLRRQKIQIVFQNPYgsLNPrk 116
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLRSMIGVVLQDTF--LFS-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 kvGQILEEpLLINSNLNKEQRREKALA--------MMAKVGLKTEHYDRyPHMFSGGQRQRIAIARGLMLDPDVVIADEP 188
Cdd:cd03254 91 --GTIMEN-IRLGRPNATDEEVIEAAKeagahdfiMKLPNGYDTVLGEN-GGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527035742 189 VSALDVSVRAQVLNLMMDLQQdmGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIF 250
Cdd:cd03254 167 TSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
37-253 |
2.99e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 123.28 E-value: 2.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQdllkhdPQAQKLRR-----QKIQIVFQNP--- 108
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK------PPRRARRRigyvpQRAEVDWDFPitv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 109 --------YGSLNPRKKVGQileepllinsnlnkeQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDP 180
Cdd:COG1121 95 rdvvlmgrYGRRGLFRRPSR---------------ADREAVDEALERVGL-EDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527035742 181 DVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMyLGRCVEKGTKEQIFTHP 253
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPE 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
38-221 |
1.08e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 120.66 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLgrLLTMI-----EVPTGGELYYQGQDLLKHDPQAqklRRqkIQIVFQNPYgsL 112
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTL--LAAIAgtlspAFSASGEVLLNGRRLTALPAEQ---RR--IGILFQDDL--L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 113 NPRKKVGQILeePLLINSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSAL 192
Cdd:COG4136 88 FPHLSVGENL--AFALPPTIGRAQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180
....*....|....*....|....*....
gi 527035742 193 DVSVRAQVLNLMMDLQQDMGLSYVFISHD 221
Cdd:COG4136 165 DAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
32-235 |
1.12e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 120.44 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 32 ERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlkhdpqAQKLRRQKIQIVFQNPYGS 111
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI------KAKERRKSIGYVMQDVDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 112 LnprkkVGQILEEPLLInSNLNKEQRREKALAMMAKVGLKTEHyDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSA 191
Cdd:cd03226 84 L-----FTDSVREELLL-GLKELDAGNEQAETVLKDLDLYALK-ERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 527035742 192 LDVSVRAQVLNLMMDLqQDMGLSYVFISHDLSVVEHIADEVMVM 235
Cdd:cd03226 157 LDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
37-257 |
1.12e-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: 124.45 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDgVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKhdpQAQKL----RRQKIQIVFQNpyGSL 112
Cdd:TIGR02142 13 SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFD---SRKGIflppEKRRIGYVFQE--ARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 113 NPRKKVGQILEEPLlinSNLNKEQRREKALAMMAKVGLktEHY-DRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSA 191
Cdd:TIGR02142 87 FPHLSVRGNLRYGM---KRARPSERRISFERVIELLGI--GHLlGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527035742 192 LDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPY 257
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
35-239 |
1.27e-32 |
|
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: 120.59 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQKLRRQKIQIVFQNpyGSLNP 114
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 RKKVGQILEEPLLINSNLNKEQRReKALAMMAKVGLKTEHyDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDV 194
Cdd:cd03292 92 DRNVYENVAFALEVTGVPPREIRK-RVPAALELVGLSHKH-RALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 527035742 195 SVRAQVLNLMMDLQQdMGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:cd03292 170 DTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-253 |
5.33e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 122.75 E-value: 5.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 1 MSTQQATTQQPLLQAIDLKKYYPVKKglfaperlvkALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELY 80
Cdd:PRK09452 3 KLNKQPSSLSPLVELRGISKSFDGKE----------VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 81 YQGQDLLKHDPQaqklRRQkIQIVFQNpYgSLNPR-------------KKVgqileepllinSNLNKEQRREKALAMmak 147
Cdd:PRK09452 73 LDGQDITHVPAE----NRH-VNTVFQS-Y-ALFPHmtvfenvafglrmQKT-----------PAAEITPRVMEALRM--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 148 VGLKtEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEH 227
Cdd:PRK09452 132 VQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALT 210
|
250 260
....*....|....*....|....*.
gi 527035742 228 IADEVMVMYLGRCVEKGTKEQIFTHP 253
Cdd:PRK09452 211 MSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
36-253 |
5.47e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 121.09 E-value: 5.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDL-LKHDPQAQKLRRQKIQIVFQNPYGSLNP 114
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRKKVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 RKKVGQILEEPLliNSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDV 194
Cdd:PRK13641 101 NTVLKDVEFGPK--NFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 195 SVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHP 253
Cdd:PRK13641 179 EGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
11-221 |
6.48e-32 |
|
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: 118.35 E-value: 6.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 11 PLLQAIDLKKYYPvkkglfapERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHD 90
Cdd:COG4133 1 MMLEAENLSCRRG--------ERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 91 PQAqklrRQKIQIVFQNP--YGSLNPRkkvgQILEeplLINSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQ 168
Cdd:COG4133 71 EDY----RRRLAYLGHADglKPELTVR----ENLR---FWAALYGLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 527035742 169 RIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHD 221
Cdd:COG4133 139 RVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
37-235 |
8.73e-32 |
|
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: 118.65 E-value: 8.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQ----DLLKHDP-QAQKLRRQKIQIVFQnpYGS 111
Cdd:TIGR02324 23 VLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEgawvDLAQASPrEVLEVRRKTIGYVSQ--FLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 112 LNPRKKVGQILEEPLLINSnLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSA 191
Cdd:TIGR02324 101 VIPRVSALEVVAEPLLERG-VPREAARARARELLARLNIPERLWHLPPATFSGGEQQRVNIARGFIADYPILLLDEPTAS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 527035742 192 LDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVM 235
Cdd:TIGR02324 180 LDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRVMDV 222
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
35-253 |
9.61e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 121.11 E-value: 9.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGEL----YYQGQDLLKHDP----------QAQKLRRqK 100
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELitnpyskkikNFKELRR-R 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 101 IQIVFQNPYGSLNPRKKVGQILEEPllINSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDP 180
Cdd:PRK13631 118 VSMVFQFPEYQLFKDTIEKDIMFGP--VALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527035742 181 DVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHP 253
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
42-244 |
1.36e-31 |
|
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: 117.98 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 42 SFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQaqklrRQKIQIVFQ--NPYGSLNPRKKVG 119
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-----DRPVSMLFQenNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 120 QILEEPLLINsnlnkEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQ 199
Cdd:cd03298 93 LGLSPGLKLT-----AEDRQAIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 527035742 200 VLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 244
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
38-255 |
1.92e-31 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 117.95 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQklrrqkiqIVFQNpYgSLNPRKK 117
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQN-Y-SLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 118 VGQ-ILEEPLLINSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSV 196
Cdd:TIGR01184 71 VREnIALAVDRVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 197 RAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI-FTHPRH 255
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-239 |
2.42e-31 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 117.22 E-value: 2.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 13 LQAIDLKKYYPvkkglfapERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQ 92
Cdd:cd03263 1 LQIRNLTKTYK--------KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 93 AqklrRQKIQIVFQNP--YGSLNPRkkvgqileEPLLINS---NLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQR 167
Cdd:cd03263 73 A----RQSLGYCPQFDalFDELTVR--------EHLRFYArlkGLPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527035742 168 QRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQdmGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:cd03263 140 RKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
11-224 |
7.67e-31 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 122.91 E-value: 7.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 11 PLLQAIDLKKYYPvkkglfAPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHD 90
Cdd:PRK10535 3 ALLELKDIRRSYP------SGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 91 PQA-QKLRRQKIQIVFQNPYgsLNPRKKVGQILEEPLlINSNLNKEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQR 169
Cdd:PRK10535 77 ADAlAQLRREHFGFIFQRYH--LLSHLTAAQNVEVPA-VYAGLERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 527035742 170 IAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLqQDMGLSYVFISHDLSV 224
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQV 206
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
35-248 |
8.07e-31 |
|
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: 116.48 E-value: 8.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlkHDPQAQKLRRQkIQIVFQnpygslnp 114
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI--RDLNLRWLRSQ-IGLVSQ-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 rkkvgqileEPLL----INSNLnKEQRREKALAMMAKVGLKTEHYD---RYPHMF-----------SGGQRQRIAIARGL 176
Cdd:cd03249 85 ---------EPVLfdgtIAENI-RYGKPDATDEEVEEAAKKANIHDfimSLPDGYdtlvgergsqlSGGQKQRIAIARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527035742 177 MLDPDVVIADEPVSALDVSVRAQV---LNLMMdlqqdMGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQ 248
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVqeaLDRAM-----KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
38-270 |
8.53e-31 |
|
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: 119.33 E-value: 8.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTG--GELYYQGQDLLKHDPQAQKLrrqkiQIVFQNPygSLNPR 115
Cdd:TIGR03258 21 LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGltGRIAIADRDLTHAPPHKRGL-----ALLFQNY--ALFPH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 116 KKVGQILEEPLlinsnlnKEQRREKAL-AMMAKVGLKT----EHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVS 190
Cdd:TIGR03258 94 LKVEDNVAFGL-------RAQKMPKADiAERVADALKLvglgDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 191 ALDVSVRAQVLNLMMDLQQDM-GLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQALLSATPRLN 269
Cdd:TIGR03258 167 ALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANILP 246
|
.
gi 527035742 270 P 270
Cdd:TIGR03258 247 A 247
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
31-253 |
1.57e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 116.82 E-value: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQKLRRQKIQIVFQNPYG 110
Cdd:PRK13640 16 PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIREKVGIVFQNPDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 111 SLnprkkVGQILEEPL---LINSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADE 187
Cdd:PRK13640 96 QF-----VGATVGDDVafgLENRAVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527035742 188 PVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFTHP 253
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
31-248 |
2.21e-30 |
|
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: 115.41 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlkHDPQAQKLRRQkIQIVFQNPYg 110
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV--RDYTLASLRRQ-IGLVSQDVF- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 111 SLNprkkvGQILEEPLLINSNLNKEQRREKALAMMA-------KVGLKTEHYDRYPHMfSGGQRQRIAIARGLMLDPDVV 183
Cdd:cd03251 87 LFN-----DTVAENIAYGRPGATREEVEEAARAANAhefimelPEGYDTVIGERGVKL-SGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527035742 184 IADEPVSALDVSVRAQVLNLMMDLQQDMgLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQ 248
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNR-TTFV-IAHRLSTIEN-ADRIVVLEDGKIVERGTHEE 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
31-244 |
3.44e-30 |
|
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: 113.18 E-value: 3.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKhdpqAQKLRRQKIQIVFQNPYg 110
Cdd:cd03247 11 PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD----LEKALSSLISVLNQRPY- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 111 slnprkkvgqileeplLINSNLnkeqrrekalamMAKVGLKtehydryphmFSGGQRQRIAIARGLMLDPDVVIADEPVS 190
Cdd:cd03247 86 ----------------LFDTTL------------RNNLGRR----------FSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 527035742 191 ALDVSVRAQVLNLMMDLQQDMGLsyVFISHDLSVVEHiADEVMVMYLGRCVEKG 244
Cdd:cd03247 128 GLDPITERQLLSLIFEVLKDKTL--IWITHHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
37-242 |
3.79e-30 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 115.34 E-value: 3.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKhdPQAQKlrrqkiQIVFQNpyGSLNPRK 116
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADR------GVVFQK--DALLPWL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 KVGQILEEPLLINSnLNKEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSV 196
Cdd:COG4525 92 NVLDNVAFGLRLRG-VPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 527035742 197 RAQVLNLMMDLQQDMGLSYVFISHDlsvVEH---IADEVMVM--YLGRCVE 242
Cdd:COG4525 170 REQMQELLLDVWQRTGKGVFLITHS---VEEalfLATRLVVMspGPGRIVE 217
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
37-248 |
6.33e-30 |
|
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: 120.06 E-value: 6.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqkLRRQkIQIVFQNpyGSLNPrk 116
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQA--VRRQ-LGVVLQN--GRLMS-- 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 kvGQILEEpLLINSNLNKEQRREkALAMmakVGLKtEHYDRYPhM------------FSGGQRQRIAIARGLMLDPDVVI 184
Cdd:TIGR03797 541 --GSIFEN-IAGGAPLTLDEAWE-AARM---AGLA-EDIRAMP-MgmhtvisegggtLSGGQRQRLLIARALVRKPRILL 611
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527035742 185 ADEPVSALDVSVRAQVLNLMMDLQqdmgLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQ 248
Cdd:TIGR03797 612 FDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDE 670
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
38-250 |
8.67e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 114.83 E-value: 8.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGqDLLKHDPQAQKlrRQKIQIVFQNPYGSLnprkk 117
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEENVWDI--RHKIGMVFQNPDNQF----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 118 VGQILEEPL---LINSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDV 194
Cdd:PRK13650 95 VGATVEDDVafgLENKGIPHEEMKERVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 527035742 195 SVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEhIADEVMVMYLGRCVEKGTKEQIF 250
Cdd:PRK13650 174 EGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELF 228
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
31-252 |
1.08e-29 |
|
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: 119.05 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlkHDPQAQKLRRQkIQIVFQN--- 107
Cdd:TIGR02203 341 PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL--ADYTLASLRRQ-VALVSQDvvl 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 108 ---------PYGSLnprkkvGQILEEpllinsnlnkeqRREKALAMmakvGLKTEHYDRYPHMF-----------SGGQR 167
Cdd:TIGR02203 418 fndtianniAYGRT------EQADRA------------EIERALAA----AYAQDFVDKLPLGLdtpigengvllSGGQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 168 QRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQdmGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKE 247
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHN 552
|
....*
gi 527035742 248 QIFTH 252
Cdd:TIGR02203 553 ELLAR 557
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
37-253 |
1.79e-29 |
|
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: 115.58 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDgVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHdpqAQKL-----RRQkIQIVFQNPygS 111
Cdd:COG4148 15 TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDS---ARGIflpphRRR-IGYVFQEA--R 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 112 LNPRKKVGQileepllinsNLN-------KEQRREKALAMMAKVGLktEHY-DRYPHMFSGGQRQRIAIARGLMLDPDVV 183
Cdd:COG4148 88 LFPHLSVRG----------NLLygrkrapRAERRISFDEVVELLGI--GHLlDRRPATLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 184 IADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHP 253
Cdd:COG4148 156 LMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
36-252 |
3.16e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 113.30 E-value: 3.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQ-KLRRQKIQIVFQNPYGslnp 114
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDiKQIRKKVGLVFQFPES---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 rkkvgQILEEPLLI-------NSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADE 187
Cdd:PRK13649 97 -----QLFEETVLKdvafgpqNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527035742 188 PVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTH 252
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
37-249 |
4.03e-29 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 112.19 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqkLRRQkiqivfqnpygslnprk 116
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW--LRRQ----------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 kVGQILEEPLLINSNLNKE----------QRREKALAMMAKVGLKTEHYDRYPHM-------FSGGQRQRIAIARGLMLD 179
Cdd:cd03252 78 -VGVVLQENVLFNRSIRDNialadpgmsmERVIEAAKLAGAHDFISELPEGYDTIvgeqgagLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 180 PDVVIADEPVSALDVSVRAQVLNLMMDLQQdmGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 249
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
37-243 |
4.20e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 112.49 E-value: 4.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlkHDPQAQKlrrqkiQIVFQNPygSLNPRK 116
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV--EGPGAER------GVVFQNE--GLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 KVGQILEEPLLInSNLNKEQRREKALAMMAKVGLKTEHyDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSV 196
Cdd:PRK11248 86 NVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 527035742 197 RAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMY--LGRCVEK 243
Cdd:PRK11248 164 REQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVER 212
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
241-325 |
1.20e-28 |
|
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: 105.91 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 241 VEKGTKEQIFTHPRHPYTQALLSATPRLNpDDRRERIKLTGELPSPLNPPPGCAFNARCSRRFGPCTQLQPQLKDY-GGQ 319
Cdd:TIGR01727 3 VETGPAEEIFKNPLHPYTKALLSAIPTIK-KRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVEIaEGH 81
|
....*.
gi 527035742 320 LVACFA 325
Cdd:TIGR01727 82 RVACHL 87
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
32-239 |
1.26e-28 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 111.31 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 32 ERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELyyqgqdLLKHDPQAQKlrRQKIQIVFQNpyGS 111
Cdd:PRK11247 24 ERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAGTAPLAEA--REDTRLMFQD--AR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 112 LNPRKKVgqileeplLINSNLN-KEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVS 190
Cdd:PRK11247 92 LLPWKKV--------IDNVGLGlKGQWRDAALQALAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 527035742 191 ALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
37-235 |
1.42e-28 |
|
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: 109.93 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQdllkhdPQAQKLRR-----QKIQIVFQNP--- 108
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK------PLEKERKRigyvpQRRSIDRDFPisv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 109 --------YGSLNPRKKVGQileepllinsnlnkeQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDP 180
Cdd:cd03235 88 rdvvlmglYGHKGLFRRLSK---------------ADKAKVDEALERVGL-SELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 527035742 181 DVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVM 235
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
31-250 |
1.59e-28 |
|
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: 115.57 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERL-VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQaqKLRRQkIQIVFQNP- 108
Cdd:TIGR02204 348 PARPdQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPA--ELRAR-MALVPQDPv 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 109 --YGSLNPRKKVGqileeplliNSNLNKEQRREKALAMMAK--VGLKTEHYDRY----PHMFSGGQRQRIAIARGLMLDP 180
Cdd:TIGR02204 425 lfAASVMENIRYG---------RPDATDEEVEAAARAAHAHefISALPEGYDTYlgerGVTLSGGQRQRIAIARAILKDA 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 181 DVVIADEPVSALDVSVRAQVLNLMMDLQQdmGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIF 250
Cdd:TIGR02204 496 PILLLDEATSALDAESEQLVQQALETLMK--GRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAELI 562
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
36-253 |
1.97e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 112.87 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLK-HdpqaqkLRRQKIQIVFQN------- 107
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlH------ARDRKVGFVFQHyalfrhm 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 108 ------PYG-SLNPRKkvgqilEEPllinsnlNKEQRREKALAMMAKVGLktEHY-DRYPHMFSGGQRQRIAIARGLMLD 179
Cdd:PRK10851 90 tvfdniAFGlTVLPRR------ERP-------NAAAIKAKVTQLLEMVQL--AHLaDRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527035742 180 PDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHP 253
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
36-244 |
2.15e-28 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 109.20 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTlAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKhdpQAQKLRRqKIQIVFQNPygSLNPR 115
Cdd:cd03264 14 RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK---QPQKLRR-RIGYLPQEF--GVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 116 KKVGQILEEpLLINSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVS 195
Cdd:cd03264 87 FTVREFLDY-IAWLKGIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 527035742 196 VRAQVLNLMMDLQQDMglSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 244
Cdd:cd03264 165 ERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
37-250 |
2.36e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.09 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQKLRrQKIQIVFQNPYGSLNPRK 116
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLR-ESVGMVFQDPDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 KVGQILEEPLliNSNLNKEQRREKALAMMAKVGLktEHYDRYP-HMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVS 195
Cdd:PRK13636 100 VYQDVSFGAV--NLKLPEDEVRKRVDNALKRTGI--EHLKDKPtHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 527035742 196 VRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIF 250
Cdd:PRK13636 176 GVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-263 |
2.69e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 110.32 E-value: 2.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTL----GRLLTMIEVP-TGGELYYQGQDLLKHDPQAQKLRRqKIQIVFQ--NPYG 110
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLlrtfNRLLELNEEArVEGEVRLFGRNIYSPDVDPIEVRR-EVGMVFQypNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 111 SLNPRKKVGQILEEPLLINSNLNKEQRREKALAmmaKVGLKTEHYDR---YPHMFSGGQRQRIAIARGLMLDPDVVIADE 187
Cdd:PRK14267 99 HLTIYDNVAIGVKLNGLVKSKKELDERVEWALK---KAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527035742 188 PVSALDVSVRAQVLNLMMDLQQDmgLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQALLS 263
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVT 249
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
36-252 |
2.92e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 111.25 E-value: 2.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTlgrlltMIEVPTGGELYYQGQDL---------LKHDPQAQKLRRQkIQIVFQ 106
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKST------MIQLTNGLIISETGQTIvgdyaipanLKKIKEVKRLRKE-IGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 107 NPYGSLNPRKKVGQILEEPllINSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIAD 186
Cdd:PRK13645 98 FPEYQLFQETIEKDIAFGP--VNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527035742 187 EPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTH 252
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
31-251 |
2.98e-28 |
|
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: 115.35 E-value: 2.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqkLRRQkIQIVFQNP-- 108
Cdd:TIGR03375 474 PGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAD--LRRN-IGYVPQDPrl 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 109 -YGSLnprkkvgqilEEPLLINSNLNKEQRREKAlAMMAKVG-LKTEHYDRYPHM-------FSGGQRQRIAIARGLMLD 179
Cdd:TIGR03375 551 fYGTL----------RDNIALGAPYADDEEILRA-AELAGVTeFVRRHPDGLDMQigergrsLSGGQRQAVALARALLRD 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527035742 180 PDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLsyVFISHDLSVVEhIADEVMVMYLGRCVEKGTKEQIFT 251
Cdd:TIGR03375 620 PPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTL--VLVTHRTSLLD-LVDRIIVMDNGRIVADGPKDQVLE 688
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
36-239 |
2.39e-27 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 105.59 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqkLRRQKIQIVfqnpygslnP- 114
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD--AIRAGIAYV---------Pe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 -RKKVGQILEEPLLINSNLnkeqrrekalammakvglktehydryPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALD 193
Cdd:cd03215 83 dRKREGLVLDLSVAENIAL--------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 527035742 194 VSVRAQVLNLMMDLqQDMGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:cd03215 137 VGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
42-263 |
4.10e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 106.59 E-value: 4.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 42 SFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQaqklrRQKIQIVFQ--NPYGSLNPRKKVG 119
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-----RRPVSMLFQenNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 120 QILEEPLlinsNLNKEQRREKAlAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQ 199
Cdd:PRK10771 94 LGLNPGL----KLNAAQREKLH-AIARQMGI-EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527035742 200 VLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTkeqifthprhpyTQALLS 263
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP------------TDELLS 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-259 |
4.75e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 107.06 E-value: 4.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMI------EVPTGGELYYQGQDLLKHDpqAQKLRRQkIQIVFQNPygS 111
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQID--AIKLRKE-VGMVFQQP--N 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 112 LNPRKKVGQILEEPLliNSNLNKEQRREKALA--MMAKVGLKTEHYDRY---PHMFSGGQRQRIAIARGLMLDPDVVIAD 186
Cdd:PRK14246 101 PFPHLSIYDNIAYPL--KSHGIKEKREIKKIVeeCLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527035742 187 EPVSALDVSVRAQVLNLMMDLQQDMGLsyVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQ 259
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAI--VIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
37-282 |
6.22e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 111.21 E-value: 6.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlkHDPQAQKLRRQkIQIVFQNPyGSLNprk 116
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI--RTVTRASLRRN-IAVVFQDA-GLFN--- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 kvgQILEEPLLI------NSNLNKEQRREKALAMMAK--VGLKTEHYDRyPHMFSGGQRQRIAIARGLMLDPDVVIADEP 188
Cdd:PRK13657 423 ---RSIEDNIRVgrpdatDEEMRAAAERAQAHDFIERkpDGYDTVVGER-GRQLSGGERQRLAIARALLKDPPILILDEA 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 189 VSALDVSVRAQVLNLMMDLQQdmGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFTHPRHPYtqALLSATPRL 268
Cdd:PRK13657 499 TSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVARGGRFA--ALLRAQGML 573
|
250
....*....|....
gi 527035742 269 NPDDRRERIKLTGE 282
Cdd:PRK13657 574 QEDERRKQPAAEGA 587
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
42-239 |
7.64e-27 |
|
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: 105.33 E-value: 7.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 42 SFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQaqklrRQKIQIVFQ--NPYGSLNPRKKVG 119
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY-----QRPVSMLFQenNLFAHLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 120 QILEEPLlinsNLNKEQRrEKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQ 199
Cdd:TIGR01277 93 LGLHPGL----KLNAEQQ-EKVVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 527035742 200 VLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:TIGR01277 167 MLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-253 |
9.19e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 110.97 E-value: 9.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 22 YPVKkglfaPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDpqaQKLRRQKI 101
Cdd:TIGR00958 488 YPNR-----PDVPV--LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD---HHYLHRQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 102 QIVFQNP--YGslnprkkvGQILEEpllINSNLNKEQRRE-KALAMMAKV---------GLKTEHYDRYPHMfSGGQRQR 169
Cdd:TIGR00958 558 ALVGQEPvlFS--------GSVREN---IAYGLTDTPDEEiMAAAKAANAhdfimefpnGYDTEVGEKGSQL-SGGQKQR 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 170 IAIARGLMLDPDVVIADEPVSALDVSVRAQvlnlmmdLQQDM---GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTK 246
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALDAECEQL-------LQESRsraSRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTH 697
|
....*..
gi 527035742 247 EQIFTHP 253
Cdd:TIGR00958 698 KQLMEDQ 704
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
31-244 |
9.54e-27 |
|
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: 104.98 E-value: 9.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqklRRQKIQIVFQNP-- 108
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD---LRRNIGYVPQDVtl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 109 -YGSlnprkkvgqiLEEPLLINSNLNKEQRREKAlAMMAKVglkTEHYDRYPHMF-----------SGGQRQRIAIARGL 176
Cdd:cd03245 90 fYGT----------LRDNITLGAPLADDERILRA-AELAGV---TDFVNKHPNGLdlqigergrglSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527035742 177 MLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLsyVFISHDLSVVEhIADEVMVMYLGRCVEKG 244
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTL--IIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-221 |
1.14e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 105.25 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 32 ERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQ-KLRRQKIQIVFQN--- 107
Cdd:PRK10584 20 EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaKLRAKHVGFVFQSfml 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 108 -PygSLNPRKKVgqilEEPLLINSNlNKEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIAD 186
Cdd:PRK10584 100 iP--TLNALENV----ELPALLRGE-SSRQSRNGAKALLEQLGLG-KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190
....*....|....*....|....*....|....*
gi 527035742 187 EPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHD 221
Cdd:PRK10584 172 EPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
13-253 |
1.42e-26 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 107.62 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 13 LQAIDLKKYYPVKkglfaperlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPq 92
Cdd:PRK11650 4 LKLQAVRKSYDGK---------TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 93 aqklRRQKIQIVFQNpYgSLNPRKKVGQILEEPLLiNSNLNKEQRREKaLAMMAKVgLKTEHY-DRYPHMFSGGQRQRIA 171
Cdd:PRK11650 74 ----ADRDIAMVFQN-Y-ALYPHMSVRENMAYGLK-IRGMPKAEIEER-VAEAARI-LELEPLlDRKPRELSGGQRQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 172 IARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLsvVEH--IADEVMVMYLGRcVEK-GTKEQ 248
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQ--VEAmtLADRVVVMNGGV-AEQiGTPVE 221
|
....*
gi 527035742 249 IFTHP 253
Cdd:PRK11650 222 VYEKP 226
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
38-247 |
1.56e-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: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEV--PTGGELYYQGQDLLKHDPQAqklRRQK-IQIVFQNPygslnP 114
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDE---RARAgIFLAFQYP-----V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 R---KKVGQILEepLLINSNLNKEQR----REKALAMMAKVGLKTEHYDRYPHM-FSGGQRQRIAIARGLMLDPDVVIAD 186
Cdd:COG0396 88 EipgVSVSNFLR--TALNARRGEELSarefLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527035742 187 EPVSALDV-SVR--AQVLNLMMDlqQDMGLsyVFISHDLSVVEHI-ADEVMVMYLGRCVEKGTKE 247
Cdd:COG0396 166 ETDSGLDIdALRivAEGVNKLRS--PDRGI--LIITHYQRILDYIkPDFVHVLVDGRIVKSGGKE 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
36-247 |
2.36e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.59 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlkhDPQAQKLRRQKIQIVFQNPYGSLNPR 115
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV---NAENEKWVRSKVGLVFQDPDDQVFSS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 116 KKVGQILEEPllINSNLNKEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVS 195
Cdd:PRK13647 96 TVWDDVAFGP--VNMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 527035742 196 VRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKE 247
Cdd:PRK13647 173 GQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
38-249 |
3.00e-26 |
|
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: 109.45 E-value: 3.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqkLRRQkiqivfqnpygslnprkk 117
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAW--LRRQ------------------ 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 118 VGQILEEPLLI------NSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMF-----------SGGQRQRIAIARGLMLDP 180
Cdd:TIGR01846 533 MGVVLQENVLFsrsirdNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYntevgekganlSGGQRQRIAIARALVGNP 612
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 181 DVVIADEPVSALDVSVRAQVLNLMMDLQQdmGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 249
Cdd:TIGR01846 613 RILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEEL 678
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
31-252 |
5.61e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 108.18 E-value: 5.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlkHDPQAQKLRRQkIQIVFQNPYg 110
Cdd:PRK11176 352 PGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL--RDYTLASLRNQ-VALVSQNVH- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 111 slnprkkvgqileeplLINSNL-------NKEQRREKALAMMAKVGLKTEHYDRYPH-----------MFSGGQRQRIAI 172
Cdd:PRK11176 428 ----------------LFNDTIanniayaRTEQYSREQIEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAI 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 173 ARGLMLDPDVVIADEPVSALDV-SVRAqVLNLMMDLQQDMglSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFT 251
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTeSERA-IQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567
|
.
gi 527035742 252 H 252
Cdd:PRK11176 568 Q 568
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
37-253 |
5.75e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 104.68 E-value: 5.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDllKHDPQAQKLRRQKIQIVFQNPYGSLnprk 116
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKLQGIRKLVGIVFQNPETQF---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 kVGQILEEPLLI---NSNLNKEQRREKALAMMAKVGLKTEHYdRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALD 193
Cdd:PRK13644 91 -VGRTVEEDLAFgpeNLCLPPIEIRKRVDRALAEIGLEKYRH-RSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 194 VSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVeHIADEVMVMYLGRCVEKGTKEQIFTHP 253
Cdd:PRK13644 169 PDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
38-239 |
9.70e-26 |
|
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: 101.14 E-value: 9.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlkhdpqaqklrrqkiqivfqNPYGSLNPRKK 117
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI--------------------SQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 118 VGQILEEPLL----INSNLnkeqrrekalammakvglktehydryphmFSGGQRQRIAIARGLMLDPDVVIADEPVSALD 193
Cdd:cd03246 78 VGYLPQDDELfsgsIAENI-----------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 527035742 194 VSVRAQVLNLMMDLQQdMGLSYVFISHDLSVVEhIADEVMVMYLGR 239
Cdd:cd03246 129 VEGERALNQAIAALKA-AGATRIVIAHRPETLA-SADRILVLEDGR 172
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
12-244 |
1.23e-25 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 102.06 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 12 LLQAIDLKKYYPVKKglfapeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLkHDP 91
Cdd:cd03266 1 MITADALTKRFRDVK------KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV-KEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 92 QAQklrRQKIQIVFQNPygSLNPRKKVgqilEEPLLINSNLNKEQRRE--KALAMMAKVgLKTEHY-DRYPHMFSGGQRQ 168
Cdd:cd03266 74 AEA---RRRLGFVSDST--GLYDRLTA----RENLEYFAGLYGLKGDEltARLEELADR-LGMEELlDRRVGGFSTGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527035742 169 RIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLqQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 244
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
29-250 |
2.24e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.86 E-value: 2.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 29 FAPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDpqAQKLRRqKIQIVFQNP 108
Cdd:PRK13642 14 YEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEN--VWNLRR-KIGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 109 YGSLnprkkVGQILEEPL---LINSNLNKEQ---RREKALAMMAKVGLKTehydRYPHMFSGGQRQRIAIARGLMLDPDV 182
Cdd:PRK13642 91 DNQF-----VGATVEDDVafgMENQGIPREEmikRVDEALLAVNMLDFKT----REPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527035742 183 VIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIF 250
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
36-235 |
2.41e-25 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 106.22 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqklRRQKIQIVFQNPYgsLNPr 115
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS---WRDQIAWVPQHPF--LFA- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 116 kkvGQILEEPLLinsnlnkeQRREKALAMMAKV---------------GLKTEhYDRYPHMFSGGQRQRIAIARGLMLDP 180
Cdd:TIGR02857 410 ---GTIAENIRL--------ARPDASDAEIREAleragldefvaalpqGLDTP-IGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 527035742 181 DVVIADEPVSALDVSVRAQVLNLMMDLQQdmGLSYVFISHDLSVVEhIADEVMVM 235
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAA-LADRIVVL 529
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
37-222 |
3.34e-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: 105.91 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDpqaQKLRRQKIQIVFQNPYgslnprk 116
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD---QDEVRRRVSVCAQDAH------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 KVGQILEEPLLINsnlNKEQRREKALAMMAKVGLKtEHYDRYPH-----------MFSGGQRQRIAIARGLMLDPDVVIA 185
Cdd:TIGR02868 420 LFDTTVRENLRLA---RPDATDEELWAALERVGLA-DWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*..
gi 527035742 186 DEPVSALDVSVRAQVLNLMmdLQQDMGLSYVFISHDL 222
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
36-244 |
4.44e-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: 100.37 E-value: 4.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDllkhdpqaqklrrqkiqivFQNPYgslNPR 115
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS-------------------YQKNI---EAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 116 KKVGQILEEPLLINSNLNKEQRREKALAMMAK----------VGLKtEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIA 185
Cdd:cd03268 72 RRIGALIEAPGFYPNLTARENLRLLARLLGIRkkridevldvVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 186 DEPVSALDVSVRAQVLNLMMDLqQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 244
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
38-251 |
5.47e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.39 E-value: 5.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQKLRR----QKIQIVFqnPYgsln 113
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRavlpQHSSLSF--PF---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 114 prkKVGQILEEPLLINSNLNKEQRREkALAMMAKVGLktEHY-DRYPHMFSGGQRQRIAIARGLM------LDPDVVIAD 186
Cdd:PRK13548 92 ---TVEEVVAMGRAPHGLSRAEDDAL-VAAALAQVDL--AHLaGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527035742 187 EPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFT 251
Cdd:PRK13548 166 EPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
36-239 |
6.62e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 100.33 E-value: 6.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQKLRRQKIQIVFQNPYGSLNpr 115
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 116 KKVGQILEEPLLInSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVS 195
Cdd:PRK10908 94 RTVYDNVAIPLII-AGASGDDIRRRVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 527035742 196 VRAQVLNLMMDLQQdMGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:PRK10908 172 LSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-241 |
1.42e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.95 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 8 TQQPLLQAIDLKKYYPvkkGlfaperlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLL 87
Cdd:COG3845 1 MMPPALELRGITKRFG---G-------VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 88 KHDPQAQklRRQKIQIVFQNPygSLNPRKKVGQ--ILEEPLLINSNLNKEQRREKALAMMAKVGLKTEhYDRYPHMFSGG 165
Cdd:COG3845 71 IRSPRDA--IALGIGMVHQHF--MLVPNLTVAEniVLGLEPTKGGRLDRKAARARIRELSERYGLDVD-PDAKVEDLSVG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527035742 166 QRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCV 241
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
31-248 |
2.14e-24 |
|
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: 103.75 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDlLKHDPQAQkLRRQkIQIVFQnpyg 110
Cdd:COG5265 369 PERPI--LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQD-IRDVTQAS-LRAA-IGIVPQ---- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 111 slnprkkvgqileEPLLINSNL-----------NKEQRREKA-LAMM------------AKV---GLKtehydryphmFS 163
Cdd:COG5265 440 -------------DTVLFNDTIayniaygrpdaSEEEVEAAArAAQIhdfieslpdgydTRVgerGLK----------LS 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 164 GGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQdmGLSYVFISHDLSVVEHiADEVMVMYLGRCVEK 243
Cdd:COG5265 497 GGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVER 573
|
....*
gi 527035742 244 GTKEQ 248
Cdd:COG5265 574 GTHAE 578
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
13-244 |
2.46e-24 |
|
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: 98.51 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 13 LQAIDLKKYYpvkkglfapeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGqdllkhdpq 92
Cdd:cd03269 1 LEVENVTKRF----------GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG--------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 93 aqklrrQKIQIVFQNPYG------SLNPRKKVGQILeepLLINS--NLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSG 164
Cdd:cd03269 62 ------KPLDIAARNRIGylpeerGLYPKMKVIDQL---VYLAQlkGLKKEEARRRIDEWLERLEL-SEYANKRVEELSK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 165 GQRQRIAIARGLMLDPDVVIADEPVSALDVsVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 244
Cdd:cd03269 132 GNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
10-263 |
3.00e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.46 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 10 QPLLQAIDLKKYYPVKKglfaperlvkALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMI-----EVPTGGELYYQGQ 84
Cdd:PRK14239 3 EPILQVSDLSVYYNKKK----------ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 85 DLlkHDPQAQKLR-RQKIQIVFQNP------------YG----SLNPRKKVGQILEEPLLINSNLN--KEQRREKALAMm 145
Cdd:PRK14239 73 NI--YSPRTDTVDlRKEIGMVFQQPnpfpmsiyenvvYGlrlkGIKDKQVLDEAVEKSLKGASIWDevKDRLHDSALGL- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 146 akvglktehydryphmfSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLsyVFISHDLSVV 225
Cdd:PRK14239 150 -----------------SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQA 210
|
250 260 270
....*....|....*....|....*....|....*...
gi 527035742 226 EHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQALLS 263
Cdd:PRK14239 211 SRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYIS 248
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
36-250 |
5.33e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.42 E-value: 5.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYqGQDLLKHDPQAQKLR--RQKIQIVFQNPYGSLN 113
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEIKpvRKKVGVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 114 PRKKVGQILEEPLliNSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALD 193
Cdd:PRK13643 99 EETVLKDVAFGPQ--NFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 527035742 194 VSVRAQVLNLMMDLQQdMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIF 250
Cdd:PRK13643 177 PKARIEMMQLFESIHQ-SGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
37-249 |
8.44e-24 |
|
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: 97.12 E-value: 8.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQaQKLRRqKIQIVFQNP--YGSLNp 114
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH-ERARA-GIGYVPEGRriFPELT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 rkkvgqiLEEPLLINSNLNKEQRREKALAMMakvglktehYDRYP-----------HMfSGGQRQRIAIARGLMLDPDVV 183
Cdd:cd03224 92 -------VEENLLLGAYARRRAKRKARLERV---------YELFPrlkerrkqlagTL-SGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527035742 184 IADEPVSALDVSVRAQVLNLMMDLqQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 249
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
36-235 |
1.03e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.09 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQklrRQKIQIVFQNPygSLnpr 115
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY---RQQVSYCAQTP--TL--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 116 kkVGQILEEPLLINSNLNKEQRREKALAM-MAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDV 194
Cdd:PRK10247 93 --FGDTVYDNLIFPWQIRNQQPDPAIFLDdLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 527035742 195 SVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHiADEVMVM 235
Cdd:PRK10247 171 SNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
36-244 |
1.25e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 98.62 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlKHDPQAQKLRRQKIQIVFQNPYGSL--- 112
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDE-KNKKKTKEKEKVLEKLVIQKTRFKKikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 113 --NPRKKVG--------QILEEPLL-------INSNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARG 175
Cdd:PRK13651 100 ikEIRRRVGvvfqfaeyQLFEQTIEkdiifgpVSMGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 176 LMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQdMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 244
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-259 |
1.75e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.41 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMI-----EVPTGGELYYQGQDLLKHDPQAQKLRRQkIQIVFQNP-- 108
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNLNRLRRQ-VSMVHPKPnl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 109 ----------YG----SLNPRKKVGQILEEPLLiNSNLNKEQRREkalamMAKVGLKtehydryphmFSGGQRQRIAIAR 174
Cdd:PRK14258 100 fpmsvydnvaYGvkivGWRPKLEIDDIVESALK-DADLWDEIKHK-----IHKSALD----------LSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 175 GLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMY-----LGRCVEKGTKEQI 249
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKI 243
|
250
....*....|
gi 527035742 250 FTHPRHPYTQ 259
Cdd:PRK14258 244 FNSPHDSRTR 253
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
38-251 |
3.65e-23 |
|
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: 96.31 E-value: 3.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPT-GGELYYQGQDLLKHDPQaqKLRRqKIQIV---FQNPYgsln 113
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTyGNDVRLFGERRGGEDVW--ELRK-RIGLVspaLQLRF---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 114 prkKVGQILEEPLL--------INSNLNKEQRrEKALAMMAKVGLktEHY-DRYPHMFSGGQRQRIAIARGLMLDPDVVI 184
Cdd:COG1119 92 ---PRDETVLDVVLsgffdsigLYREPTDEQR-ERARELLELLGL--AHLaDRPFGTLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527035742 185 ADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLS-VVEHIaDEVMVMYLGRCVEKGTKEQIFT 251
Cdd:COG1119 166 LDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGI-THVLLLKDGRVVAAGPKEEVLT 232
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
36-249 |
4.15e-23 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 100.20 E-value: 4.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQklrRQKIQIVFQNPYgslnpr 115
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL---RQFINYLPQEPY------ 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 116 KKVGQILEEpLLINSNLNKEQRREKALAMMAKV---------GLKTEhYDRYPHMFSGGQRQRIAIARGLMLDPDVVIAD 186
Cdd:TIGR01193 559 IFSGSILEN-LLLGAKENVSQDEIWAACEIAEIkddienmplGYQTE-LSEEGSSISGGQKQRIALARALLTDSKVLILD 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527035742 187 EPVSALDVSVRAQVLNLMMDLQQDmglSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 249
Cdd:TIGR01193 637 ESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
38-252 |
6.21e-23 |
|
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: 99.34 E-value: 6.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQaqKLRR------QKIQIvFQnpygs 111
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRE--TFGKhigylpQDVEL-FP----- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 112 lnprkkvGQILEEPLLINSNLNKEQRREKA-LAMMAKVGLKTEH-YDRY----PHMFSGGQRQRIAIARGLMLDPDVVIA 185
Cdd:TIGR01842 406 -------GTVAENIARFGENADPEKIIEAAkLAGVHELILRLPDgYDTVigpgGATLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527035742 186 DEPVSALDVSVRAQVLNLMMDLQQdMGLSYVFISHDLSVVEhIADEVMVMYLGRCVEKGTKEQIFTH 252
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALKA-RGITVVVITHRPSLLG-CVDKILVLQDGRIARFGERDEVLAK 543
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
35-249 |
9.46e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.95 E-value: 9.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDpqaqklrRQKIqivfqnpyG---- 110
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED-------RRRI--------Gylpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 111 --SLNPRKKVG-QI-----LEepllinsNLNKEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQRIAIARGLMLDPDV 182
Cdd:COG4152 79 erGLYPKMKVGeQLvylarLK-------GLSKAEAKRRADEWLERLGLG-DRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527035742 183 VIADEPVSALD-VSVraqvlNLMMDL---QQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 249
Cdd:COG4152 151 LILDEPFSGLDpVNV-----ELLKDVireLAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-252 |
1.13e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 96.31 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 17 DLKKYYPVK----------KGLFAPE-RLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGqd 85
Cdd:COG4586 6 NLSKTYRVYekepglkgalKGLFRREyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 86 llkHDPQAQKLR-RQKIQIVFqnpygslnprkkvGQ----ILEEPLLINSNLNKE------QRREKALAMMAKVgLKTEH 154
Cdd:COG4586 84 ---YVPFKRRKEfARRIGVVF-------------GQrsqlWWDLPAIDSFRLLKAiyripdAEYKKRLDELVEL-LDLGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 155 YDRYP-HMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVM 233
Cdd:COG4586 147 LLDTPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVI 226
|
250
....*....|....*....
gi 527035742 234 VMYLGRCVEKGTKEQIFTH 252
Cdd:COG4586 227 VIDHGRIIYDGSLEELKER 245
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
38-251 |
1.26e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.08 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQaqKLRRQkIQIVFQNPygsLNPRK- 116
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR--QLARR-LALLPQHH---LTPEGi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 KVGQILE---EPLLinsNL------NKEQRREKAlamMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADE 187
Cdd:PRK11231 92 TVRELVAygrSPWL---SLwgrlsaEDNARVNQA---MEQTRI-NHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527035742 188 PVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFT 251
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-241 |
1.45e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.78 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 17 DLKKYYPVKKGLFAPERL-VKAL------DGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKH 89
Cdd:COG1129 240 ELEDLFPKRAAAPGEVVLeVEGLsvggvvRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 90 DP-QAQKLRrqkiqIVF--QNpygslnpRKKVGQILEEPLLIN---SNLNK-------EQRREKALA--MMAKVGLKTEH 154
Cdd:COG1129 320 SPrDAIRAG-----IAYvpED-------RKGEGLVLDLSIRENitlASLDRlsrggllDRRRERALAeeYIKRLRIKTPS 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 155 YDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMV 234
Cdd:COG1129 388 PEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILV 466
|
....*..
gi 527035742 235 MYLGRCV 241
Cdd:COG1129 467 MREGRIV 473
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
241-306 |
2.12e-22 |
|
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: 88.61 E-value: 2.12e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527035742 241 VEKGTKEQIFTHPRHPYTQALLSATPRLNPDDRReRIKLTGELPSPLNPPPGCAFNARCSRRFGPC 306
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRP-LYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
26-239 |
3.05e-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: 93.55 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 26 KGLFAPE-RLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGqdllkHDPQAQKLR-RQKIQI 103
Cdd:cd03267 24 KSLFKRKyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----LVPWKRRKKfLRRIGV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 104 VFqnpygslnprkkvGQ----ILEEPLLINSNLNKE---------QRREKALAMMAKVGlktEHYDRYPHMFSGGQRQRI 170
Cdd:cd03267 99 VF-------------GQktqlWWDLPVIDSFYLLAAiydlpparfKKRLDELSELLDLE---ELLDTPVRQLSLGQRMRA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 171 AIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
39-292 |
3.47e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 94.06 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 39 DGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQKLRRQKIQIVFQNpyGSLNPRKKV 118
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQS--GALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 119 GQILEEPLLINSNLNKEQRREKALAMMAKVGLKTEHyDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRA 198
Cdd:PRK11831 102 FDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAA-KLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 199 QVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIfthprhpytqallsatpRLNPDDR-RERI 277
Cdd:PRK11831 181 VLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL-----------------QANPDPRvRQFL 243
|
250
....*....|....*
gi 527035742 278 KLTGELPSPLNPPPG 292
Cdd:PRK11831 244 DGIADGPVPFRYPAG 258
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
38-250 |
3.51e-22 |
|
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: 97.13 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqkLRR------QKIQI----VFQN 107
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE--LGRhigylpQDVELfdgtIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 108 --PYGSLNPRKKVgqileepllinsnlnkeqrrekALAMMAKVglkteH---------YDRYP----HMFSGGQRQRIAI 172
Cdd:COG4618 426 iaRFGDADPEKVV----------------------AAAKLAGV-----HemilrlpdgYDTRIgeggARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527035742 173 ARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIF 250
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVL 554
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
31-239 |
3.83e-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: 92.92 E-value: 3.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDpqaQKLRRQKIQIVFQNPY- 109
Cdd:cd03248 25 PDTLV--LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE---HKYLHSKVSLVGQEPVl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 110 --GSLN-------PRKKVGQILEEPLLINSNLNkeqrrekaLAMMAKvGLKTEhYDRYPHMFSGGQRQRIAIARGLMLDP 180
Cdd:cd03248 100 faRSLQdniayglQSCSFECVKEAAQKAHAHSF--------ISELAS-GYDTE-VGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 181 DVVIADEPVSALDVSVRAQVLNLMMDLQQDMglSYVFISHDLSVVEHiADEVMVMYLGR 239
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
35-239 |
8.67e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 95.77 E-value: 8.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIeVPTG---GELYYQGQDLlkhdpQAQKLR---RQKIQIVFQNP 108
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEEL-----QASNIRdteRAGIAIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 109 ygSLNPRKKVGQ--ILEEPLLINSNLNKEQRREKALAMMAKVGLKTEHYDRYPHmFSGGQRQRIAIARGLMLDPDVVIAD 186
Cdd:PRK13549 92 --ALVKELSVLEniFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGN-LGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 527035742 187 EPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-263 |
8.68e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.92 E-value: 8.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 3 TQQATTQQPLLQAIDLKKYYpvkkGLFAperlvkALDGVSFTLERGKTLAVVGESGCGKSTL----GRLLTMIE-VPTGG 77
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYY----GSFL------AVKNVWLDIPKNQITAFIGPSGCGKSTIlrcfNRLNDLIPgFRVEG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 78 ELYYQGQDLLKHDPQAQKLRRqKIQIVFQNPygslNPRKK--VGQILEEPLLINSNLNKEQRREKALAMMAkvgLKTEHY 155
Cdd:PRK14243 71 KVTFHGKNLYAPDVDPVEVRR-RIGMVFQKP----NPFPKsiYDNIAYGARINGYKGDMDELVERSLRQAA---LWDEVK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 156 DRYPH---MFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMglSYVFISHDLSVVEHIADev 232
Cdd:PRK14243 143 DKLKQsglSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSD-- 218
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 527035742 233 MVMYL-----------GRCVEKGTKEQIFTHPRHPYTQALLS 263
Cdd:PRK14243 219 MTAFFnveltegggryGYLVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-284 |
1.09e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 95.50 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 7 TTQQPLLQAIDLKKYYPVkkglfaperlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDL 86
Cdd:PRK15439 6 TTAPPLLCARSISKQYSG----------VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 87 LKHDP-QAQKLrrqKIQIVFQNPYgsLNPRKKVgqiLEEPLLinsNLNKEQRREKALAmmAKVGLKTEHYDryPHMFSG- 164
Cdd:PRK15439 76 ARLTPaKAHQL---GIYLVPQEPL--LFPNLSV---KENILF---GLPKRQASMQKMK--QLLAALGCQLD--LDSSAGs 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 165 ---GQRQRIAIARGLMLDPDVVIADEPVSALdvsVRAQVLNLMMDLQ--QDMGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:PRK15439 141 levADRQIVEILRGLMRDSRILILDEPTASL---TPAETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGT 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 527035742 240 CVEKGTKEQIfthprhpYTQALLSA-TPRLNPDDRRERIKLTGELP 284
Cdd:PRK15439 218 IALSGKTADL-------STDDIIQAiTPAAREKSLSASQKLWLELP 256
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
11-244 |
2.04e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.85 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 11 PLLQAIDLKKYYPVkkglfaperlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHD 90
Cdd:PRK09700 4 PYISMAGIGKSFGP----------VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 91 PQ-AQKLrrqKIQIVFQ------------NPYGSLNPRKKVGQIleePLlinsnLNKEQRREKALAMMAKVGLKTEhYDR 157
Cdd:PRK09700 74 HKlAAQL---GIGIIYQelsvideltvleNLYIGRHLTKKVCGV---NI-----IDWREMRVRAAMMLLRVGLKVD-LDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 158 YPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYL 237
Cdd:PRK09700 142 KVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKD 220
|
....*..
gi 527035742 238 GRCVEKG 244
Cdd:PRK09700 221 GSSVCSG 227
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
38-248 |
2.39e-21 |
|
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: 95.01 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDL--LKHDPQAQKLR--RQKIQIvFQnpygsln 113
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPReeIPREVLANSVAmvDQDIFL-FE------- 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 114 prkkvGQILEEPLLINSNLNKEQRREKAL------AMMAKVGlktehydRYPHM-------FSGGQRQRIAIARGLMLDP 180
Cdd:TIGR03796 567 -----GTVRDNLTLWDPTIPDADLVRACKdaaihdVITSRPG-------GYDAElaegganLSGGQRQRLEIARALVRNP 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 181 DVVIADEPVSALDVSVRAQVL-NLmmdlqQDMGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQ 248
Cdd:TIGR03796 635 SILILDEATSALDPETEKIIDdNL-----RRRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEE 697
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
41-269 |
2.79e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.17 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 41 VSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQdLLKHDPQAQKlrrqKIQIVFQNpYgSLNPRKKVGQ 120
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-RMNDVPPAER----GVGMVFQS-Y-ALYPHLSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 121 ILEEPL-LINSNLNKEQRREKALAMMakvgLKTEHY-DRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRA 198
Cdd:PRK11000 95 NMSFGLkLAGAKKEEINQRVNQVAEV----LQLAHLlDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527035742 199 QVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPRHPYTQALLsATPRLN 269
Cdd:PRK11000 171 QMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFI-GSPKMN 240
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
35-242 |
3.02e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 94.09 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIeVPTG---GELYYQGQDLlkhdpQAQKLR---RQKIQIVFQN- 107
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyeGEILFDGEVC-----RFKDIRdseALGIVIIHQEl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 108 ---PYGSL-------NPRKKVGQIleepllinsnlNKEQRREKALAMMAKVGLKtEHydryPHMFSG----GQRQRIAIA 173
Cdd:NF040905 88 aliPYLSIaeniflgNERAKRGVI-----------DWNETNRRARELLAKVGLD-ES----PDTLVTdigvGKQQLVEIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 174 RGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVE 242
Cdd:NF040905 152 KALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
38-247 |
6.15e-21 |
|
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: 88.74 E-value: 6.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIE--VPTGGELYYQGQDLLKHDPQAQKlrRQKIQIVFQNPYgslnpr 115
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERA--RLGIFLAFQYPP------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 116 kkvgqilEEPllinsnlnkeqrrekalammakvGLKTEHYDRYPHM-FSGGQRQRIAIARGLMLDPDVVIADEPVSALDV 194
Cdd:cd03217 88 -------EIP-----------------------GVKNADFLRYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 527035742 195 SVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHI-ADEVMVMYLGRCVEKGTKE 247
Cdd:cd03217 138 DALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKE 190
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-258 |
1.31e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.77 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMI-----------EVPTGGELYYQGQDLLKHdpqaqklrRQKIQIVFQ 106
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsgyrysgDVLLGGRSIFNYRDVLEF--------RRRVGMLFQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 107 NPygslNPRkkvgqileePLLINSNL----------NKEQRREKALAMMAKVGLKTEHYDRY---PHMFSGGQRQRIAIA 173
Cdd:PRK14271 109 RP----NPF---------PMSIMDNVlagvrahklvPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 174 RGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmgLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHP 253
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
....*
gi 527035742 254 RHPYT 258
Cdd:PRK14271 254 KHAET 258
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
37-249 |
1.83e-20 |
|
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: 88.35 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQaQKLRR------QKIQIVfqnpyg 110
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPH-ERARAgiayvpQGREIF------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 111 slnPRKKVgqilEEPLLINsnLNKEQRREKALammakvglKTEHYDRYPHMF----------SGGQRQRIAIARGLMLDP 180
Cdd:TIGR03410 88 ---PRLTV----EENLLTG--LAALPRRSRKI--------PDEIYELFPVLKemlgrrggdlSGGQQQQLAIARALVTRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 181 DVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 249
Cdd:TIGR03410 151 KLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
9-254 |
2.95e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.51 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 9 QQPLLQAIDLKKYYpvkKGLFAperlvkaLDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLK 88
Cdd:PRK11300 2 SQPLLSVSGLMMRF---GGLLA-------VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 89 HdpQAQKLRRQKIQIVFQNpygsLNPRKKVGQIleEPLLI------NSNL------NKEQRR------EKALAMMAKVGL 150
Cdd:PRK11300 72 L--PGHQIARMGVVRTFQH----VRLFREMTVI--ENLLVaqhqqlKTGLfsgllkTPAFRRaesealDRAATWLERVGL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 151 kTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIAD 230
Cdd:PRK11300 144 -LEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISD 222
|
250 260
....*....|....*....|....
gi 527035742 231 EVMVMYLGRCVEKGTKEQIFTHPR 254
Cdd:PRK11300 223 RIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
35-254 |
3.56e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.29 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlkHDPQAQKLRRQkIQIVFQNPYGSLNP 114
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV--EALSARAASRR-VASVPQDTSLSFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 RkkVGQILE---EPLLINSNLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSA 191
Cdd:PRK09536 93 D--VRQVVEmgrTPHRSRFDTWTETDRAAVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527035742 192 LDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPR 254
Cdd:PRK09536 170 LDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADT 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
35-258 |
5.91e-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: 90.27 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEvPTG---GELYYQGQDLlkhdpQAQKLR---RQKIQIVFQNP 108
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPL-----KASNIRdteRAGIVIIHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 109 ygSLNPRKKVgqiLEEPLLINS--------NLNKEQRREKALamMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDP 180
Cdd:TIGR02633 88 --TLVPELSV---AENIFLGNEitlpggrmAYNAMYLRAKNL--LRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 181 DVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCV-----EKGTKEQIFT---- 251
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVatkdmSTMSEDDIITmmvg 239
|
250
....*....|...
gi 527035742 252 ------HPRHPYT 258
Cdd:TIGR02633 240 reitslYPHEPHE 252
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-248 |
6.44e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 90.27 E-value: 6.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 2 STQQATTQQPLLQAIDLKKYYPvkkglfapERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYY 81
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYP--------DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 82 QGQDLLKHDPQAqkLRRQkIQIVFQNPY---GSLnprkkvgqilEEPLLINsnlNKEQRREKALAMMAKVGLKTEHYDRY 158
Cdd:PRK11160 400 NGQPIADYSEAA--LRQA-ISVVSQRVHlfsATL----------RDNLLLA---APNASDEALIEVLQQVGLEKLLEDDK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 159 P---------HMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLsyVFISHDLSVVEHIa 229
Cdd:PRK11160 464 GlnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTV--LMITHRLTGLEQF- 540
|
250
....*....|....*....
gi 527035742 230 DEVMVMYLGRCVEKGTKEQ 248
Cdd:PRK11160 541 DRICVMDNGQIIEQGTHQE 559
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
31-253 |
1.44e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 89.39 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlkHDPQAQKLRRqKIQIVFQNPYg 110
Cdd:PRK10789 324 PQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL--TKLQLDSWRS-RLAVVSQTPF- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 111 sLNPRKKVGQI-LEEPllinsnlNKEQRREKALAMMAKV---------GLKTEHYDRyPHMFSGGQRQRIAIARGLMLDP 180
Cdd:PRK10789 400 -LFSDTVANNIaLGRP-------DATQQEIEHVARLASVhddilrlpqGYDTEVGER-GVMLSGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527035742 181 DVVIADEPVSALDVSVRAQVLNlmmDLQQDMGLSYVFIS-HDLSVVEHiADEVMVMYLGRCVEKGTKEQIFTHP 253
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILH---NLRQWGEGRTVIISaHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-249 |
1.48e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.32 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 26 KGLFAP-ERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPqaQKLRRQKIQIV 104
Cdd:COG3845 261 ENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSP--RERRRLGVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 105 fqnpygslnP--RKKVGQILEEPLLINS--------------NLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQ 168
Cdd:COG3845 339 ---------PedRLGRGLVPDMSVAENLilgryrrppfsrggFLDRKAIRAFAEELIEEFDVRTPGPDTPARSLSGGNQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 169 RIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLqQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCV-----EK 243
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVgevpaAE 488
|
....*.
gi 527035742 244 GTKEQI 249
Cdd:COG3845 489 ATREEI 494
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
35-254 |
2.86e-19 |
|
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: 85.03 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPqAQKLRR------QKIQI----- 103
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP-HRIARLgigyvpEGRRIfpslt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 104 VFQN---PYGSLNPRKKVGQILEE-----PLLinsnlnKEQRREKALAMmakvglktehydryphmfSGGQRQRIAIARG 175
Cdd:COG0410 95 VEENlllGAYARRDRAEVRADLERvyelfPRL------KERRRQRAGTL------------------SGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 176 LMLDPDVVIADEPVSALDVSVRAQVLNLMMDLqQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPR 254
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
38-251 |
4.17e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 85.13 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTL----GRLLTMievpTGGELYYQGQDLLKHDPQ--AQKLrrqkiQIVFQNPygS 111
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLlsmiSRLLPP----DSGEVLVDGLDVATTPSRelAKRL-----AILRQEN--H 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 112 LNPRKKVGQileeplLIN--------SNLNKEQRR--EKALAMMAKVGLKtehyDRYPHMFSGGQRQRIAIARGLMLDPD 181
Cdd:COG4604 86 INSRLTVRE------LVAfgrfpyskGRLTAEDREiiDEAIAYLDLEDLA----DRYLDELSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 182 VVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFT 251
Cdd:COG4604 156 YVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIIT 225
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
36-248 |
8.95e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 84.29 E-value: 8.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIevPTGGELYYQGQDLLKHDPQ-----AQKLRRQKIQI--VFQ-- 106
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--ITGDKSAGSHIELLGRTVQregrlARDIRKSRANTgyIFQqf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 107 NPYGSLNPRKKV--GQILEEPLLINS-NLNKEQRREKALAMMAKVGLKTEHYDRYPHMfSGGQRQRIAIARGLMLDPDVV 183
Cdd:PRK09984 96 NLVNRLSVLENVliGALGSTPFWRTCfSWFTREQKQRALQALTRVGMVHFAHQRVSTL-SGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527035742 184 IADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQ 248
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
48-251 |
1.25e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.27 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 48 GKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHdpqAQKLRRQKIQIVFQNPY--GSLNPRKKV--GQILE 123
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHY---ASKEVARRIGLLAQNATtpGDITVQELVarGRYPH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 124 EPLLinSNLNKEQRREKALAMMAkVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNL 203
Cdd:PRK10253 110 QPLF--TRWRKEDEEAVTKAMQA-TGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 527035742 204 MMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFT 251
Cdd:PRK10253 186 LSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-249 |
1.31e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 86.44 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 3 TQQATTQQPL-LQAIDLKKYYPVKKGLFAPerlvkaldgVSFTLERGKTLAVVGESGCGKSTL-GRLLTMIevPTGGELY 80
Cdd:PRK11174 339 EKELASNDPVtIEAEDLEILSPDGKTLAGP---------LNFTLPAGQRIALVGPSGAGKTSLlNALLGFL--PYQGSLK 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 81 YQGQDLLKHDPQAQklrRQKIQIVFQNPygSLNPrkkvGQILEEPLLINSNLNKEQRR---EKA-----LAMMAKvGLKT 152
Cdd:PRK11174 408 INGIELRELDPESW---RKHLSWVGQNP--QLPH----GTLRDNVLLGNPDASDEQLQqalENAwvsefLPLLPQ-GLDT 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 153 EHYDRYPHMfSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVlnlMMDLQQDM-GLSYVFISHDLSVVEHIaDE 231
Cdd:PRK11174 478 PIGDQAAGL-SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV---MQALNAASrRQTTLMVTHQLEDLAQW-DQ 552
|
250
....*....|....*...
gi 527035742 232 VMVMYLGRCVEKGTKEQI 249
Cdd:PRK11174 553 IWVMQDGQIVQQGDYAEL 570
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
22-244 |
1.68e-18 |
|
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: 82.21 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 22 YPVKKGLFAPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLGRLLTM--IEVPTGGELYYQGQDLLKHdpqaqklrrq 99
Cdd:cd03213 11 VTVKSSPSKSGKQL--LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKR---------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 100 kiqivfqnpygslNPRKKVGQILEEPLLInsnlnKEQRREKALAMMAKV-GLktehydryphmfSGGQRQRIAIARGLML 178
Cdd:cd03213 79 -------------SFRKIIGYVPQDDILH-----PTLTVRETLMFAAKLrGL------------SGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527035742 179 DPDVVIADEPVSALDVSVRAQVLNLMMDLQQdMGLSYVFISHDLS-VVEHIADEVMVMYLGRCVEKG 244
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
38-250 |
4.77e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.75 E-value: 4.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlKHDPQAQKLRRQKIQIVFQNP-----YGSL 112
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVATVFQDPeqqifYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 113 NPR-----KKVGqILEEPLlinsnlnkEQRREKALAMmakvgLKTEHYDRYP-HMFSGGQRQRIAIARGLMLDPDVVIAD 186
Cdd:PRK13638 96 DSDiafslRNLG-VPEAEI--------TRRVDEALTL-----VDAQHFRHQPiQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527035742 187 EPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIF 250
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
35-249 |
5.19e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 84.85 E-value: 5.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTL--------------GRLL---------TMIEVPT---------GGELYYQ 82
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLmhvlrgmdqyeptsGRIIyhvalcekcGYVERPSkvgepcpvcGGTLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 83 GQDLLKHDPQAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEplLINSNLNKEQRREKALAMMAKVGLktEHydRYPHM- 161
Cdd:TIGR03269 93 EVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEA--LEEIGYEGKEAVGRAVDLIEMVQL--SH--RITHIa 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 162 --FSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:TIGR03269 167 rdLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGE 246
|
250
....*....|
gi 527035742 240 CVEKGTKEQI 249
Cdd:TIGR03269 247 IKEEGTPDEV 256
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
38-239 |
6.56e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.28 E-value: 6.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQaQKLRRQkiqIVfqnpYGSLNpRKK 117
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQ-DGLANG---IV----YISED-RKR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 118 VGQILEEPLlinsnlnKEQRREKALAMMAKVGLKTEHYD--------------RYPHM------FSGGQRQRIAIARGLM 177
Cdd:PRK10762 339 DGLVLGMSV-------KENMSLTALRYFSRAGGSLKHADeqqavsdfirlfniKTPSMeqaiglLSGGNQQKVAIARGLM 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527035742 178 LDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:PRK10762 412 TRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
37-225 |
7.65e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 80.36 E-value: 7.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQKLR-------RQKIQIVFQNPY 109
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPdslpltvRDLVAMGRWARR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 110 GSLNPrkkvgqileepllinsnLNKEQRREKALAMMAkVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPV 189
Cdd:NF040873 87 GLWRR-----------------LTRDDRAAVDDALER-VGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 527035742 190 SALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVV 225
Cdd:NF040873 148 TGLDAESRERIIALLAEEHAR-GATVVVVTHDLELV 182
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
38-230 |
9.84e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.96 E-value: 9.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQD---LLKHDPQAQKLRRqkiqiVFQNPYGSLNP 114
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLrigYLPQEPPLDDDLT-----VLDTVLDGDAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 RKKVGQILEEPLLINSNLNKEQRRE-----------------KALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLM 177
Cdd:COG0488 89 LRALEAELEELEAKLAEPDEDLERLaelqeefealggweaeaRAEEILSGLGFPEEDLDRPVSELSGGWRRRVALARALL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527035742 178 LDPDVVIADEPVSALDV-SVR--AQVLNlmmdlqqdmglSY----VFISHD---L-SVVEHIAD 230
Cdd:COG0488 169 SEPDLLLLDEPTNHLDLeSIEwlEEFLK-----------NYpgtvLVVSHDryfLdRVATRILE 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-235 |
1.16e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.51 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 10 QPLLQAIDLKKYYPvkkGlfaperlVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKH 89
Cdd:PRK10762 2 QALLQLKGIDKAFP---G-------VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 90 DPQAQKlrRQKIQIVFQnpygSLNprkkvgqiLEEPLLINSN--LNKE-----------QRREKALAMMAKVGLKtEHYD 156
Cdd:PRK10762 72 GPKSSQ--EAGIGIIHQ----ELN--------LIPQLTIAENifLGREfvnrfgridwkKMYAEADKLLARLNLR-FSSD 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 157 RYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLqQDMGLSYVFISHDLSVVEHIADEVMVM 235
Cdd:PRK10762 137 KLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVF 214
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
37-245 |
1.63e-17 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 79.85 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGR-LLTMIEvPTGGELYYQGQDLlkhdpqaQKLRRQKIqivfqnpygslnpR 115
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLaLFRLVE-LSSGSILIDGVDI-------SKIGLHDL-------------R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 116 KKVGQILEEPLL----INSNLN-----KEQRREKALAmmaKVGLKtEHYDRYPHM-----------FSGGQRQRIAIARG 175
Cdd:cd03244 78 SRISIIPQDPVLfsgtIRSNLDpfgeySDEELWQALE---RVGLK-EFVESLPGGldtvveeggenLSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 176 LMLDPDVVIADEPVSALDVSVRAQVLNLMMdlQQDMGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGT 245
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
41-249 |
1.80e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.18 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 41 VSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPqAQKLRRQkiqIVFQNpygslNPRKKVGQ 120
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST-AQRLARG---LVYLP-----EDRQSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 121 ILEEPL------LINSNLNKEQRREKALAMM----AKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVS 190
Cdd:PRK15439 353 YLDAPLawnvcaLTHNRRGFWIKPARENAVLeryrRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 191 ALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 249
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
16-252 |
2.00e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.13 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 16 IDLKKYYPVKKGLFAPERL----VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGqdllkhdp 91
Cdd:COG1134 16 LYHEPSRSLKELLLRRRRTrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 92 qaqklrrqkiQIVF---------------QNPYgsLNprkkvGQILeepllinsNLNKEQRREKalamMAKV----GLKt 152
Cdd:COG1134 88 ----------RVSAllelgagfhpeltgrENIY--LN-----GRLL--------GLSRKEIDEK----FDEIvefaELG- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 153 EHYDRyP-HMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADE 231
Cdd:COG1134 138 DFIDQ-PvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDR 215
|
250 260
....*....|....*....|.
gi 527035742 232 VMVMYLGRCVEKGTKEQIFTH 252
Cdd:COG1134 216 AIWLEKGRLVMDGDPEEVIAA 236
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
38-247 |
2.92e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 80.07 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLL------TMIEvptgGELYYQGQDLLKHDPQAQKlrRQKIQIVFQNPYG- 110
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpayKILE----GDILFKGESILDLEPEERA--HLGIFLAFQYPIEi 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 111 -----------SLNPRKKVGQILE-EPL----LINSNLNKeqrrekalammakVGLKTEHYDRYPHM-FSGGQRQRIAIA 173
Cdd:CHL00131 97 pgvsnadflrlAYNSKRKFQGLPElDPLefleIINEKLKL-------------VGMDPSFLSRNVNEgFSGGEKKRNEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527035742 174 RGLMLDPDVVIADEPVSALDVS---VRAQVLNLMMDLQQdmglSYVFISHDLSVVEHIA-DEVMVMYLGRCVEKGTKE 247
Cdd:CHL00131 164 QMALLDSELAILDETDSGLDIDalkIIAEGINKLMTSEN----SIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDAE 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-253 |
6.18e-17 |
|
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: 78.74 E-value: 6.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 13 LQAIDLKKYYPVKKglfaperlvkALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDlLKHDPQ 92
Cdd:cd03218 1 LRAENLSKRYGKRK----------VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQD-ITKLPM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 93 AQKLRR------QKiQIVFQnpygSLNPRKKVGQILEEpllinSNLNKEQRREKALAMMAKVGLktEHY-DRYPHMFSGG 165
Cdd:cd03218 70 HKRARLgigylpQE-ASIFR----KLTVEENILAVLEI-----RGLSKKEREEKLEELLEEFHI--THLrKSKASSLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 166 QRQRIAIARGLMLDPDVVIADEPVSALD-VSVRaqvlnlmmDLQQ------DMGLSYVFISHDLSVVEHIADEVMVMYLG 238
Cdd:cd03218 138 ERRRVEIARALATNPKFLLLDEPFAGVDpIAVQ--------DIQKiikilkDRGIGVLITDHNVRETLSITDRAYIIYEG 209
|
250
....*....|....*
gi 527035742 239 RCVEKGTKEQIFTHP 253
Cdd:cd03218 210 KVLAEGTPEEIAANE 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-244 |
6.86e-17 |
|
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: 78.34 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 13 LQAIDLKKYYPVKKGLFAPERL------------VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELY 80
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKlgilgrkgevgeFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 81 YQGQDLLKHDPQaqklrrqkiqivfqnpyGSLNPR-------KKVGQILeepllinsNLNKEQRREK--ALAMMAKVGlk 151
Cdd:cd03220 81 VRGRVSSLLGLG-----------------GGFNPEltgreniYLNGRLL--------GLSRKEIDEKidEIIEFSELG-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 152 tEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADE 231
Cdd:cd03220 134 -DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDR 211
|
250
....*....|...
gi 527035742 232 VMVMYLGRCVEKG 244
Cdd:cd03220 212 ALVLEKGKIRFDG 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-239 |
2.94e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.18 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERL-VKALDG------VSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPqaqklrRQKIQ- 102
Cdd:PRK11288 255 EVRLrLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSP------RDAIRa 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 103 -IVfqnpygsLNP--RKKVGQI----LEEPLLINSN---------LNKEQRREKALAMMAKVGLKTEHYDRyPHMF-SGG 165
Cdd:PRK11288 329 gIM-------LCPedRKAEGIIpvhsVADNINISARrhhlragclINNRWEAENADRFIRSLNIKTPSREQ-LIMNlSGG 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527035742 166 QRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
38-232 |
3.11e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 75.99 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlkhDPQAQKLRRQKIQIVFQNPY-GSLNPRk 116
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL---DFQRDSIARGLLYLGHAPGIkTTLSVL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 kvgqileEPLLINSNLNKEQRREKALAMMAKVGLKtehyDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSV 196
Cdd:cd03231 92 -------ENLRFWHADHSDEQVEEALARVGLNGFE----DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 527035742 197 RAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEV 232
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
7-239 |
3.45e-16 |
|
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: 79.10 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 7 TTQQPLLQAIDLKKYYPVKkglfapeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLGR-LLTMIEVPTGGELYYQGQD 85
Cdd:TIGR02633 252 EIGDVILEARNLTCWDVIN-------PHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKP 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 86 LLKHDPQaqKLRRQKIQIVFQN-PYGSLNPRKKVGQILEEPLLIN----SNLNKEQRREKALAMMAKVGLKTEHYDRYPH 160
Cdd:TIGR02633 325 VDIRNPA--QAIRAGIAMVPEDrKRHGIVPILGVGKNITLSVLKSfcfkMRIDAAAELQIIGSAIQRLKVKTASPFLPIG 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 161 MFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
35-242 |
3.71e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.18 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQdllkhdpqaqklrrqkiQIVFQNPYGSLNp 114
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-----------------EMRFASTTAALA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 rKKVGQILEE----P-LLINSNL------------NKEQRREKALAMMAKVGLKTEhydryPHM----FSGGQRQRIAIA 173
Cdd:PRK11288 79 -AGVAIIYQElhlvPeMTVAENLylgqlphkggivNRRLLNYEAREQLEHLGVDID-----PDTplkyLSIGQRQMVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527035742 174 RGLMLDPDVVIADEPVSALdvSVR--AQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVE 242
Cdd:PRK11288 153 KALARNARVIAFDEPTSSL--SAReiEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
32-206 |
5.18e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.23 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 32 ERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQaqkLRRQKIQIVFQNP-YG 110
Cdd:PRK13538 13 ERIL--FSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE---YHQDLLYLGHQPGiKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 111 SLNPrkkvgqilEEPLLINSNLNKEQRREKALAMMAKVGLK-TEHydrYP-HMFSGGQRQRIAIARGLMLDPDVVIADEP 188
Cdd:PRK13538 88 ELTA--------LENLRFYQRLHGPGDDEALWEALAQVGLAgFED---VPvRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170
....*....|....*...
gi 527035742 189 VSALDVSVRAQVLNLMMD 206
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQ 174
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
52-265 |
8.63e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.22 E-value: 8.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 52 AVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDpqaQKL----RRQKIQIVFQNpyGSLNPRKKVgqileepll 127
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAE---KGIclppEKRRIGYVFQD--ARLFPHYKV--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 128 iNSNLN---KEQRREKALAMMAKVGLktEHY-DRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNL 203
Cdd:PRK11144 94 -RGNLRygmAKSMVAQFDKIVALLGI--EPLlDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527035742 204 MMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPR-HPYTQ-----ALLSAT 265
Cdd:PRK11144 171 LERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmRPWLPkeeqsSILKVT 238
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
42-220 |
1.24e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 73.34 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 42 SFTLERGKTLAVVGESGCGKSTLGRLLtmievptgGEL--YYQGQdllkhdpqAQKLRRQKIQIVFQNPY---GSLnprk 116
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRAL--------AGLwpWGSGR--------IGMPEGEDLLFLPQRPYlplGTL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 kvgqileepllinsnlnkeqrREkALAmmakvglktehydrYP--HMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDV 194
Cdd:cd03223 81 ---------------------RE-QLI--------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180
....*....|....*....|....*.
gi 527035742 195 svraQVLNLMMDLQQDMGLSYVFISH 220
Cdd:cd03223 125 ----ESEDRLYQLLKELGITVISVGH 146
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
24-235 |
1.45e-15 |
|
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: 74.67 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 24 VKKGLFAPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLgrLLTMI-EVPT-GGELYYQGQDLLKHDPQAQKLR-RQK 100
Cdd:cd03290 3 VTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSL--LLAILgEMQTlEGKVHWSNKNESEPSFEATRSRnRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 101 IQIVFQNPYgSLNPrkkvgqILEEPLLINSNLNKEQRRE--KALAMMAKVGL-----KTEHYDRYPHMfSGGQRQRIAIA 173
Cdd:cd03290 81 VAYAAQKPW-LLNA------TVEENITFGSPFNKQRYKAvtDACSLQPDIDLlpfgdQTEIGERGINL-SGGQRQRICVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527035742 174 RGLMLDPDVVIADEPVSALDVSVRAQVLNL-MMDLQQDMGLSYVFISHDLSVVEHiADEVMVM 235
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAM 214
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
37-239 |
1.68e-15 |
|
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: 74.04 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLgrLLTMI-EVP-TGGELYYQGQdlLKHDPQAQKLRRQKIQ--IVFQNPYgsl 112
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSL--LSALLgELEkLSGSVSVPGS--IAYVSQEPWIQNGTIRenILFGKPF--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 113 nprkkvgqileepllinsnlnKEQRREKA---------LAMMAKvGLKTEHYDRYPHMfSGGQRQRIAIARGLMLDPDVV 183
Cdd:cd03250 93 ---------------------DEERYEKVikacalepdLEILPD-GDLTEIGEKGINL-SGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527035742 184 IADEPVSALDVSVRAQ-----VLNLMMDlqqdmGLSYVFISHDLSVVEHiADEVMVMYLGR 239
Cdd:cd03250 150 LLDDPLSAVDAHVGRHifencILGLLLN-----NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
38-251 |
4.80e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 73.72 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLgrlLTMI--EVPTGGELYYQGQDLLKHDPQAQKLRR----QKIQIVFQNPygs 111
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTL---LARMagLLPGQGEILLNGRPLSDWSAAELARHRaylsQQQSPPFAMP--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 112 lnprkkVGQILEepLLINSNLNKEQRrEKALAMMA-KVGLKtehyDRYPHMF---SGGQRQRIAIARGLM-----LDPD- 181
Cdd:COG4138 86 ------VFQYLA--LHQPAGASSEAV-EQLLAQLAeALGLE----DKLSRPLtqlSGGEWQRVRLAAVLLqvwptINPEg 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527035742 182 -VVIADEPVSALDVSVRAQVLNLMMDLQQdMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFT 251
Cdd:COG4138 153 qLLLLDEPMNSLDVAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
42-236 |
5.48e-15 |
|
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: 73.55 E-value: 5.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 42 SFTLER------GKTLAVVGESGCGKSTLGRLLTMIEVPTGGEL-----------YYQGQDLLKHdpqAQKLRRQKIQIV 104
Cdd:cd03236 14 SFKLHRlpvpreGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNY---FTKLLEGDVKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 105 FQNPYGSLNPRKKVGQILEepllinsNLNKEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVI 184
Cdd:cd03236 91 VKPQYVDLIPKAVKGKVGE-------LLKKKDERGKLDELVDQLELR-HVLDRNIDQLSGGELQRVAIAAALARDADFYF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 527035742 185 ADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMY 236
Cdd:cd03236 163 FDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
44-236 |
5.54e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 75.59 E-value: 5.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 44 TLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGEL-----------YYQGQDLLKHdpqAQKLRRQKIQIVFQNPYGSL 112
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGTELQDY---FKKLANGEIKVAHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 113 NPRK---KVGQILEepllinsnlnKEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPV 189
Cdd:COG1245 172 IPKVfkgTVRELLE----------KVDERGKLDELAEKLGLE-NILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 527035742 190 SALDVSVRAQVLNLMMDLQQDMglSYVF-ISHDLSVVEHIADEVMVMY 236
Cdd:COG1245 241 SYLDIYQRLNVARLIRELAEEG--KYVLvVEHDLAILDYLADYVHILY 286
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
38-220 |
6.52e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 75.23 E-value: 6.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTL------------GRlltmIEVPTGGElyyqgqdllkhdpqaqklrrqkiqIVF 105
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLlraiaglwpygsGR----IARPAGAR------------------------VLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 106 --QNPY---GSLnpRkkvgQILEEPllinsNLNKEQRREKALAMMAKVGLktEHY-------DRYPHMFSGGQRQRIAIA 173
Cdd:COG4178 431 lpQRPYlplGTL--R----EALLYP-----ATAEAFSDAELREALEAVGL--GHLaerldeeADWDQVLSLGEQQRLAFA 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 527035742 174 RGLMLDPDVVIADEPVSALDVSVRAQVLNLmmdLQQDM-GLSYVFISH 220
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQL---LREELpGTTVISVGH 542
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-250 |
6.58e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.52 E-value: 6.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 7 TTQQPLLQaidlkkyypvkKGLFAPERLVKALDG---------------------VSFTLERGKT--------------L 51
Cdd:PRK10790 302 TTQQSMLQ-----------QAVVAGERVFELMDGprqqygnddrplqsgrididnVSFAYRDDNLvlqninlsvpsrgfV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 52 AVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDL--LKHdpqaQKLrRQKIQIVFQNPYgslnprkkvgqILEEPLLIN 129
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLssLSH----SVL-RQGVAMVQQDPV-----------VLADTFLAN 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 130 SNLNKEQRREKALAMMAKV-----------GLKTEHYDRyPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRA 198
Cdd:PRK10790 435 VTLGRDISEEQVWQALETVqlaelarslpdGLYTPLGEQ-GNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 527035742 199 QVLNLMMDLQQDMGLsyVFISHDLS-VVEhiADEVMVMYLGRCVEKGTKEQIF 250
Cdd:PRK10790 514 AIQQALAAVREHTTL--VVIAHRLStIVE--ADTILVLHRGQAVEQGTHQQLL 562
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
37-226 |
9.20e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 71.62 E-value: 9.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlkhdPQAQKLRRQKIQIVfqnpyGSLNPRK 116
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL----AEQRDEPHENILYL-----GHLPGLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 KVGQILEEPLLINSNLNKEQRreKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSV 196
Cdd:TIGR01189 86 PELSALENLHFWAAIHGGAQR--TIEDALAAVGL-TGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180 190
....*....|....*....|....*....|
gi 527035742 197 RAQVLNLMMDLQQDMGLSYVFISHDLSVVE 226
Cdd:TIGR01189 163 VALLAGLLRAHLARGGIVLLTTHQDLGLVE 192
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
38-249 |
9.47e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.90 E-value: 9.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqkLRRQKIQIVFQNPYGS-LNPRK 116
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA--FARKVAYLPQQLPAAEgMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 KV--GQILEEPLLINSNLNKEQRREKALAMmakVGLKTeHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDV 194
Cdd:PRK10575 105 LVaiGRYPWHGALGRFGAADREKVEEAISL---VGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 527035742 195 SVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 249
Cdd:PRK10575 181 AHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
9-235 |
9.79e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.45 E-value: 9.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 9 QQPLLQA-IDLKKYYPVKKGLFAPERL-------VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELY 80
Cdd:PTZ00265 364 RKPLVENnDDGKKLKDIKKIQFKNVRFhydtrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDII 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 81 YQGQDLLKHdpQAQKLRRQKIQIVFQNPYGSLNPRK----------KVGQILEEPLLINSNLNKEQRREKA--------- 141
Cdd:PTZ00265 444 INDSHNLKD--INLKWWRSKIGVVSQDPLLFSNSIKnnikyslyslKDLEALSNYYNEDGNDSQENKNKRNscrakcagd 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 142 LAMMAKVGLKTE------HY-------------------------DRYPHM-------FSGGQRQRIAIARGLMLDPDVV 183
Cdd:PTZ00265 522 LNDMSNTTDSNEliemrkNYqtikdsevvdvskkvlihdfvsalpDKYETLvgsnaskLSGGQKQRISIARAIIRNPKIL 601
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 527035742 184 IADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHiADEVMVM 235
Cdd:PTZ00265 602 ILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY-ANTIFVL 652
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
36-253 |
1.14e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.45 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQaqKLRRQKIQIVFQNPYGSLNPR 115
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ--KLYLDTTLPLTVNRFLRLRPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 116 KKVGQILeePLLinsnlnkeqRREKAlammakvglktEHYDRYP-HMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDV 194
Cdd:PRK09544 96 TKKEDIL--PAL---------KRVQA-----------GHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 195 SVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEkGTKEQIFTHP 253
Cdd:PRK09544 154 NGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCS-GTPEVVSLHP 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
35-251 |
1.16e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.58 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTL---------GRlltmievpTGGELYYQGQDLLKHDPQaqKLRRQKIQIVF 105
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELvqclfgaypGR--------WEGEIFIDGKPVKIRNPQ--QAIAQGIAMVP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 106 QNpygslnpRKKVGQILEEPLLIN------------SNLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIA 173
Cdd:PRK13549 345 ED-------RKRDGIVPVMGVGKNitlaaldrftggSRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 174 RGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQdMGLSYVFISHDLSVVEHIADEVMVMYLGRCveKG-------TK 246
Cdd:PRK13549 418 KCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKL--KGdlinhnlTQ 494
|
....*
gi 527035742 247 EQIFT 251
Cdd:PRK13549 495 EQVME 499
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-234 |
1.18e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.72 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 11 PLLQAIDLKKYYPvkkglfapERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGEL---------YY 81
Cdd:COG0488 314 KVLELEGLSKSYG--------DKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVklgetvkigYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 82 -QGQDllkhdpqaqklrrqkiqivfqnpygSLNPRKKVGQILEEpllinsnLNKEQRREKALAMMAKVGLKTEHYDRYPH 160
Cdd:COG0488 384 dQHQE-------------------------ELDPDKTVLDELRD-------GAPGGTEQEVRGYLGRFLFSGDDAFKPVG 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527035742 161 MFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDlqqdmglsY----VFISHDLSVVEHIADEVMV 234
Cdd:COG0488 432 VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD--------FpgtvLLVSHDRYFLDRVATRILE 501
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
37-251 |
2.58e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.84 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQG--------QDLLKHDPQAQKLRRQ----KIQIV 104
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGqptrqalqKNLVAYVPQSEEVDWSfpvlVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 105 FQNPYGSLNprkkvgqILEEPllinsnlnKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVI 184
Cdd:PRK15056 102 MMGRYGHMG-------WLRRA--------KKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527035742 185 ADEPVSALDVSVRAQVLNLMMDLqQDMGLSYVFISHDLSVVEHIADeVMVMYLGRCVEKGTKEQIFT 251
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFT 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
35-193 |
4.16e-14 |
|
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: 70.38 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTL-----GRLLTmiEVPTGGELYYQGQDLLKHdpqaqkLRRQKIQIVFQNPY 109
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLldaisGRVEG--GGTTSGQILFNGQPRKPD------QFQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 110 gsLNPRKKVGQILE-EPLLINSNLNKEQRREKalaMMAKVGLKTEHYDRYPHMF----SGGQRQRIAIARGLMLDPDVVI 184
Cdd:cd03234 92 --LLPGLTVRETLTyTAILRLPRKSSDAIRKK---RVEDVLLRDLALTRIGGNLvkgiSGGERRRVSIAVQLLWDPKVLI 166
|
....*....
gi 527035742 185 ADEPVSALD 193
Cdd:cd03234 167 LDEPTSGLD 175
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
44-236 |
4.21e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.92 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 44 TLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGEL-----------YYQG---QDLLKhdpqaqKLRRQKIQIVFQNPY 109
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkRFRGtelQNYFK------KLYNGEIKVVHKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 110 GSLNPRK---KVGQILEepllinsnlnKEQRREKALAMMAKVGLKtEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIAD 186
Cdd:PRK13409 169 VDLIPKVfkgKVRELLK----------KVDERGKLDEVVERLGLE-NILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 527035742 187 EPVSALDVSVRAQVLNLMMDLQQDmglSYVF-ISHDLSVVEHIADEVMVMY 236
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELAEG---KYVLvVEHDLAVLDYLADNVHIAY 285
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
35-222 |
9.06e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.11 E-value: 9.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTL-----GRLLtmievPTGGELYYQGQDLLKHdPQAQklRRQKIQIVFQNPY 109
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLlnaiaGSLP-----PDSGSILIDGKDVTKL-PEYK--RAKYIGRVFQDPM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 110 ----GSLnprkkvgQIlEEPLLINSN----------LNKEQR---REKaLAMM---------AKVGLktehydryphmFS 163
Cdd:COG1101 91 mgtaPSM-------TI-EENLALAYRrgkrrglrrgLTKKRRelfREL-LATLglglenrldTKVGL-----------LS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 164 GGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDL 222
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM 209
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
32-252 |
9.45e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.60 E-value: 9.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 32 ERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAqklrRQKIQIVFQnpYGS 111
Cdd:PRK13537 19 DKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA----RQRVGVVPQ--FDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 112 LNPRKKVgqilEEPLLINS---NLNKEQRREK--ALAMMAKVGLKTEHYDRyphMFSGGQRQRIAIARGLMLDPDVVIAD 186
Cdd:PRK13537 91 LDPDFTV----RENLLVFGryfGLSAAAARALvpPLLEFAKLENKADAKVG---ELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527035742 187 EPVSALDVSVRAQVLNLMMDLQQdMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTH 252
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
29-245 |
1.29e-13 |
|
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: 68.59 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 29 FAPErLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDpqAQKLRRqKIQIVFQNP 108
Cdd:cd03369 16 YAPD-LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP--LEDLRS-SLTIIPQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 109 Y---GSlnprkkvgqileepllINSNLNKEQRREKALAMMA-KV---GLKtehydryphmFSGGQRQRIAIARGLMLDPD 181
Cdd:cd03369 92 TlfsGT----------------IRSNLDPFDEYSDEEIYGAlRVsegGLN----------LSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527035742 182 VVIADEPVSALDVSVRAQVLNLMMDLQQDMGLsyVFISHDLSVVEHIaDEVMVMYLGRCVEKGT 245
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTNSTI--LTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
13-235 |
2.09e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 66.70 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 13 LQAIDLKKYYPVKKgLFaperlvkalDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELyyqgqdllkhdpq 92
Cdd:cd03221 1 IELENLSKTYGGKL-LL---------KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 93 aqklrrqkiqivfqnpygSLNPRKKVGQIleepllinsnlnkEQrrekalammakvglktehydryphmFSGGQRQRIAI 172
Cdd:cd03221 58 ------------------TWGSTVKIGYF-------------EQ-------------------------LSGGEKMRLAL 81
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527035742 173 ARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMglsyVFISHDLSVVEHIADEVMVM 235
Cdd:cd03221 82 AKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTV----ILVSHDRYFLDQVATKIIEL 140
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
43-249 |
3.37e-13 |
|
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: 67.95 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 43 FTLERGKTLAVVGESGCGKSTLGR-LLTMIEVPTG-----GELYYQGQDLLKHDPQAQKLRRQKIQIVFQNpygSLNPRK 116
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRaILGLIPPAKGtvkvaGASPGKGWRHIGYVPQRHEFAWDFPISVAHT---VMSGRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 KVGQILEEPllinsnlNKEQRREKALAMmAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSV 196
Cdd:TIGR03771 78 GHIGWLRRP-------CVADFAAVRDAL-RRVGL-TELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPT 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 527035742 197 RAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVmVMYLGRCVEKGTKEQI 249
Cdd:TIGR03771 149 QELLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQL 199
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-248 |
1.14e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.54 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 14 QAIDLKKYYPVKKGLFAPERLVKA-LDGVSFTLERGKTLAVVGESGCGKSTLGRLLtMIEVPTGgeLYYQGQDLLKHDPQ 92
Cdd:TIGR00955 16 QDGSWKQLVSRLRGCFCRERPRKHlLKNVSGVAKPGELLAVMGSSGAGKTTLMNAL-AFRSPKG--VKGSGSVLLNGMPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 93 AQKLRRQKIQIVFQNP--YGSLNPRkkvgqileEPLLINS------NLNKEQRREKALAMMAKVGL------KTEHYDRY 158
Cdd:TIGR00955 93 DAKEMRAISAYVQQDDlfIPTLTVR--------EHLMFQAhlrmprRVTKKEKRERVDEVLQALGLrkcantRIGVPGRV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 159 PHMfSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLG 238
Cdd:TIGR00955 165 KGL-SGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEG 243
|
250
....*....|
gi 527035742 239 RCVEKGTKEQ 248
Cdd:TIGR00955 244 RVAYLGSPDQ 253
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
11-254 |
1.36e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 66.21 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 11 PLLQAIDLKKYYpvKKglfapeRLVkaLDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlKHD 90
Cdd:COG1137 2 MTLEAENLVKSY--GK------RTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 91 PQAQKLRR------QKIQI-----VFQNPYGslnprkkvgqILEEpllinSNLNKEQRREKALAMMAKVGLkTEHYDRYP 159
Cdd:COG1137 71 PMHKRARLgigylpQEASIfrkltVEDNILA----------VLEL-----RKLSKKEREERLEELLEEFGI-THLRKSKA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 160 HMFSGGQRQRIAIARGLMLDPDVVIADEPVSALD-VSVraqvlnlmMDLQQ------DMGLSyVFIShDLSVVE--HIAD 230
Cdd:COG1137 135 YSLSGGERRRVEIARALATNPKFILLDEPFAGVDpIAV--------ADIQKiirhlkERGIG-VLIT-DHNVREtlGICD 204
|
250 260
....*....|....*....|....
gi 527035742 231 EVMVMYLGRCVEKGTKEQIFTHPR 254
Cdd:COG1137 205 RAYIISEGKVLAEGTPEEILNNPL 228
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
38-229 |
2.77e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMiEVPTG-GELYYQgQDL----LKHDPQaqklrRQKIQIVFQNPYGSL 112
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-EVLLDdGRIIYE-QDLivarLQQDPP-----RNVEGTVYDFVAEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 113 nprKKVGQILEEPLLInSNLNKEQRREKALAMMAKVGLKTEHYDRY----------------PHM----FSGGQRQRIAI 172
Cdd:PRK11147 92 ---EEQAEYLKRYHDI-SHLVETDPSEKNLNELAKLQEQLDHHNLWqlenrinevlaqlgldPDAalssLSGGWLRKAAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 527035742 173 ARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQdmglSYVFISHDLSVVEHIA 229
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMA 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
38-249 |
3.72e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.39 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlkhdPQAQKLRRQKIQIVFQnpYGSLNPRKK 117
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLARARIGVVPQ--FDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 118 VgqilEEPLLINSNLNKEQRRE-----KALAMMAKVGLKTehyDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSAL 192
Cdd:PRK13536 131 V----RENLLVFGRYFGMSTREieaviPSLLEFARLESKA---DARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527035742 193 DVSVRAQVLNLMMDLQQdMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG-----TKEQI 249
Cdd:PRK13536 204 DPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGrphalIDEHI 264
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-250 |
9.56e-12 |
|
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: 66.12 E-value: 9.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 24 VKKGLFAPER-LVKALDGVSFTLERGKTLAVVGESGCGKSTL-GRLLTMIEvPTGGELYYQGQdlLKHDPQaqklrrqki 101
Cdd:TIGR00957 639 VHNATFTWARdLPPTLNGITFSIPEGALVAVVGQVGCGKSSLlSALLAEMD-KVEGHVHMKGS--VAYVPQ--------- 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 102 QIVFQNpygslnprkkvgQILEEPLLINSNLNKEQRRE--KALAMMAKV-----GLKTEHYDRYPHMfSGGQRQRIAIAR 174
Cdd:TIGR00957 707 QAWIQN------------DSLRENILFGKALNEKYYQQvlEACALLPDLeilpsGDRTEIGEKGVNL-SGGQKQRVSLAR 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 175 GLMLDPDVVIADEPVSALDVSVRAQVLNLMMDlqqDMGL----SYVFISHDLSVVEHIaDEVMVMYLGRCVEKGTKEQIF 250
Cdd:TIGR00957 774 AVYSNADIYLFDDPLSAVDAHVGKHIFEHVIG---PEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 849
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
32-250 |
1.39e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.37 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 32 ERLVKALDG------VSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQD--LLkhdPQAQKLRRQkiqI 103
Cdd:PRK10895 7 KNLAKAYKGrrvvedVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisLL---PLHARARRG---I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 104 VFQNPYGSLNPRKKVGQILEEPLLINSNLNKEQRREKALAMMAKvgLKTEHY-DRYPHMFSGGQRQRIAIARGLMLDPDV 182
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEE--FHIEHLrDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527035742 183 VIADEPVSALDVSVRAQVLNLMMDLqQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIF 250
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-234 |
1.81e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 32 ERLVKALDGvsFTLE-------RGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYyqgqdllkhdpqaqklrrQKIQIV 104
Cdd:PRK13409 344 PDLTKKLGD--FSLEveggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------------------PELKIS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 105 FQNPYGSLNPRKKVGQILEEpllINSNLNKEQRREKALAmmakvGLKTEH-YDRYPHMFSGGQRQRIAIARGLMLDPDVV 183
Cdd:PRK13409 404 YKPQYIKPDYDGTVEDLLRS---ITDDLGSSYYKSEIIK-----PLQLERlLDKNVKDLSGGELQRVAIAACLSRDADLY 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 527035742 184 IADEPVSALDVSVR---AQVLNLMMDLQqdmGLSYVFISHDLSVVEHIADEVMV 234
Cdd:PRK13409 476 LLDEPSAHLDVEQRlavAKAIRRIAEER---EATALVVDHDIYMIDYISDRLMV 526
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
38-244 |
1.95e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 63.27 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIE--VPTGGELYYQGQDLLKHDPQAQKlrRQKIQIVFQNPY------ 109
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRA--GEGIFMAFQYPVeipgvs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 110 ------GSLNPRKKVGQilEEPL-------LINSNLNKEQRREKALAMMAKVGlktehydryphmFSGGQRQRIAIARGL 176
Cdd:PRK09580 95 nqfflqTALNAVRSYRG--QEPLdrfdfqdLMEEKIALLKMPEDLLTRSVNVG------------FSGGEKKRNDILQMA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 177 MLDPDVVIADEPVSALDVSVRAQVLNLMMDLqQDMGLSYVFISHDLSVVEHIA-DEVMVMYLGRCVEKG 244
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
41-242 |
2.01e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.61 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 41 VSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQklrRQKIQIVFQNPY---GSLNPRKK 117
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY---RKLFSAVFTDFHlfdQLLGPEGK 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 118 VgqilEEPLLINSNLNKEQRREKalammakvgLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVR 197
Cdd:PRK10522 419 P----ANPALVEKWLERLKMAHK---------LELEDGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFR 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 527035742 198 AQVLNLMMDLQQDMGLSYVFISHDLSVVEHiADEVMVMYLGRCVE 242
Cdd:PRK10522 486 REFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
32-204 |
2.53e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.20 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 32 ERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDllKHDPQAQKlrrqkiQIVFQNPYGS 111
Cdd:PRK13539 14 GRVL--FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD--IDDPDVAE------ACHYLGHRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 112 LNPRKKVGQILE--------EPLLInsnlnkeqrrEKALAMMAKVGLKTEHYdrypHMFSGGQRQRIAIARGLMLDPDVV 183
Cdd:PRK13539 84 MKPALTVAENLEfwaaflggEELDI----------AAALEAVGLAPLAHLPF----GYLSAGQKRRVALARLLVSNRPIW 149
|
170 180
....*....|....*....|.
gi 527035742 184 IADEPVSALDVSVRAQVLNLM 204
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELI 170
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-234 |
2.80e-11 |
|
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: 64.42 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 33 RLVKALDGvsFTLE-------RGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELY------YQGQDLL-KHDPQAQKLRR 98
Cdd:COG1245 346 DLTKSYGG--FSLEveggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDedlkisYKPQYISpDYDGTVEEFLR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 99 QKIQIVFQNPYgsLNPrkkvgQILEePLLINSNLNKEqrrekalammakvgLKTehydryphmFSGGQRQRIAIARGLML 178
Cdd:COG1245 424 SANTDDFGSSY--YKT-----EIIK-PLGLEKLLDKN--------------VKD---------LSGGELQRVAIAACLSR 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 527035742 179 DPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMV 234
Cdd:COG1245 473 DADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
38-244 |
3.50e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTL-----GRLLTmiEVPTGGELYYQGQdllkhdPQAQKLRRqkIQIVFQNP--YG 110
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLlnalaGRIQG--NNFTGTILANNRK------PTKQILKR--TGFVTQDDilYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 111 SLNPRKKVgqILEEPLLINSNLNKEQRREKALAMMAKVGL-KTEHY---DRYPHMFSGGQRQRIAIARGLMLDPDVVIAD 186
Cdd:PLN03211 154 HLTVRETL--VFCSLLRLPKSLTKQEKILVAESVISELGLtKCENTiigNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 527035742 187 EPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 244
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-277 |
3.98e-11 |
|
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: 62.43 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 33 RLVKALDGvsFTLE-------RGKTLAVVGESGCGKSTLGRLLTMIEVPTGGE-------LYYQGQDL-LKHDPQAQKLR 97
Cdd:cd03237 5 TMKKTLGE--FTLEveggsisESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDieieldtVSYKPQYIkADYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 98 RQKIQIVFQNPYGSLNprkkvgqiLEEPLLINSnlnkeqrrekalammakvglkteHYDRYPHMFSGGQRQRIAIARGLM 177
Cdd:cd03237 83 SSITKDFYTHPYFKTE--------IAKPLQIEQ-----------------------ILDREVPELSGGELQRVAIAACLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 178 LDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMylgrcveKGtKEQIFTHPRHPY 257
Cdd:cd03237 132 KDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVF-------EG-EPSVNGVANPPQ 203
|
250 260
....*....|....*....|....*...
gi 527035742 258 TQ--------ALLSATPRLNPDDRRERI 277
Cdd:cd03237 204 SLrsgmnrflKNLDITFRRDPETGRPRI 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
38-245 |
6.56e-11 |
|
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: 63.78 E-value: 6.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLgrlLTMIE---VPTGGELYYQGQdlLKHDPQAQKLRRQKIQ--IVFQNPYGSL 112
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSL---LMMIMgelEPSEGKIKHSGR--ISFSPQTSWIMPGTIKdnIIFGLSYDEY 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 113 NPRKKVGQI-LEEpllinsNLNKEQRREKALAMMAKVGLktehydryphmfSGGQRQRIAIARGLMLDPDVVIADEPVSA 191
Cdd:TIGR01271 517 RYTSVIKACqLEE------DIALFPEKDKTVLGEGGITL------------SGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527035742 192 LDVSVRAQVL-----NLMMDLQQdmglsyVFIShdlSVVEHI--ADEVMVMYLGRCVEKGT 245
Cdd:TIGR01271 579 LDVVTEKEIFesclcKLMSNKTR------ILVT---SKLEHLkkADKILLLHEGVCYFYGT 630
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
35-252 |
1.11e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.05 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLgrLLTMIEVP--TGGELYYQGQDLLkhDPQAQKLRRQKIQIVfqnPYGSl 112
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTL--LGTLCGDPraTSGRIVFDGKDIT--DWQTAKIMREAVAIV---PEGR- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 113 npRKKVGQILEEPLLINSNLNKEQRREKALAMMakvglktehYDRYPHMF----------SGGQRQRIAIARGLMLDPDV 182
Cdd:PRK11614 90 --RVFSRMTVEENLAMGGFFAERDQFQERIKWV---------YELFPRLHerriqragtmSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 183 VIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTH 252
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
38-243 |
1.14e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.74 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTmievptggELYYQGQDLLKHDpqaqklrrqkiqiVFQNPYGSlnprkk 117
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA--------GALKGTPVAGCVD-------------VPDNQFGR------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 118 vgqilEEPLLinSNLNKEQRREKALAMMAKVGLKTEH-YDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSV 196
Cdd:COG2401 99 -----EASLI--DAIGRKGDFKDAVELLNAVGLSDAVlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 527035742 197 rAQVLNLMM-DLQQDMGLSYVFISHDLSVVEHIADEVMVM--YLGRCVEK 243
Cdd:COG2401 172 -AKRVARNLqKLARRAGITLVVATHHYDVIDDLQPDLLIFvgYGGVPEEK 220
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
35-249 |
1.18e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDL-LKHDPQA---------QKLRRQKIQIV 104
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFKSSKEAlengismvhQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 105 FQNPYGSLNPRKkvGQILEEpllinsnlNKEQRREKALamMAKVGLKTEHYDRYPHMfSGGQRQRIAIARGLMLDPDVVI 184
Cdd:PRK10982 91 MDNMWLGRYPTK--GMFVDQ--------DKMYRDTKAI--FDELDIDIDPRAKVATL-SVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 185 ADEPVSALDVSVRAQVLNLMMDLqQDMGLSYVFISHDLSVVEHIADEVMVMYLG-----RCVEKGTKEQI 249
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGqwiatQPLAGLTMDKI 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
41-254 |
1.99e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.33 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 41 VSFTLERGKTLAVVGESGCGKSTlgrLLTMIE--VPTGGELYYQGQDLLKHDPQAQKLRR----QKIQIVFQNPygslnp 114
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAglLPGSGSIQFAGQPLEAWSAAELARHRaylsQQQTPPFAMP------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 rkkVGQILEeplLINSNLNKEQRREKALAMMA-KVGLkTEHYDRYPHMFSGG--QRQRIAiARGLMLDPDV------VIA 185
Cdd:PRK03695 86 ---VFQYLT---LHQPDKTRTEAVASALNEVAeALGL-DDKLGRSVNQLSGGewQRVRLA-AVVLQVWPDInpagqlLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527035742 186 DEPVSALDVSVRA---QVLNLMMDLqqdmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTHPR 254
Cdd:PRK03695 158 DEPMNSLDVAQQAaldRLLSELCQQ----GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
38-193 |
2.43e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.19 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQKlrrqkiQIVFQNPYGSLNPRkk 117
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQK------QLCFVGHRSGINPY-- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527035742 118 vgQILEEPLLINSNLNKEQRREKALAMMakvgLKTEHYDRYP-HMFSGGQRQRIAIARGLMLDPDVVIADEPVSALD 193
Cdd:PRK13540 89 --LTLRENCLYDIHFSPGAVGITELCRL----FSLEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
41-234 |
2.43e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 41 VSFTLERGKTLAVVGESGCGKST-LGRLLTMIEVPTGGELYYQGQ--DLLKHDPQAQKLRRQKIQIVFQNPYGSLNPR-- 115
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTvMSLLMRFYDLKNDHHIVFKNEhtNDMTNEQDYQGDEEQNVGMKNVNEFSLTKEGgs 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 116 -------KKVGQIL----------------------EEPLLINSNL------NKEQRREKALAMMAKVGLKTEHYDRYPH 160
Cdd:PTZ00265 1267 gedstvfKNSGKILldgvdicdynlkdlrnlfsivsQEPMLFNMSIyenikfGKEDATREDVKRACKFAAIDEFIESLPN 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 161 MF-----------SGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHiA 229
Cdd:PTZ00265 1347 KYdtnvgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-S 1425
|
....*
gi 527035742 230 DEVMV 234
Cdd:PTZ00265 1426 DKIVV 1430
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
42-227 |
4.08e-10 |
|
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: 60.92 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 42 SFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYyqgqdllkhdpqaqKLRRQKIQIVFQNPYGSLNP------- 114
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLT--------------KPAKGKLFYVPQRPYMTLGTlrdqiiy 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 --------RKKVG-QILEEpLLINSNLNKEQRREKALAMMAKvglktehydrYPHMFSGGQRQRIAIARGLMLDPDVVIA 185
Cdd:TIGR00954 538 pdssedmkRRGLSdKDLEQ-ILDNVQLTHILEREGGWSAVQD----------WMDVLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 527035742 186 DEPVSALDVSVRAQvlnlMMDLQQDMGLSYVFISHDLSVVEH 227
Cdd:TIGR00954 607 DECTSAVSVDVEGY----MYRLCREFGITLFSVSHRKSLWKY 644
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
38-245 |
8.98e-10 |
|
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: 58.71 E-value: 8.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQdlLKHDPQAQKLRRQKIQ--IVFQNPYGSLNPR 115
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--ISFSSQFSWIMPGTIKenIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 116 KKVGQI-LEEPLLinsnlnkeQRREKALAMMAKVGLktehydryphMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDV 194
Cdd:cd03291 131 SVVKACqLEEDIT--------KFPEKDNTVLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 527035742 195 SVRAQVLN-----LMMDLQQdmglsyVFIShdlSVVEHI--ADEVMVMYLGRCVEKGT 245
Cdd:cd03291 193 FTEKEIFEscvckLMANKTR------ILVT---SKMEHLkkADKILILHEGSSYFYGT 241
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
37-252 |
1.15e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.52 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLkhdpqaqklrrqkIQIvfqnPYGSLNPRK 116
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL-------------IAI----SSGLNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 KVGQILEEPLLINsnLNKEQRRE--KALAMMAKVG------LKTehydryphmFSGGQRQRIAIARGLMLDPDVVIADEP 188
Cdd:PRK13545 102 GIENIELKGLMMG--LTKEKIKEiiPEIIEFADIGkfiyqpVKT---------YSSGMKSRLGFAISVHINPDILVIDEA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527035742 189 VSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTH 252
Cdd:PRK13545 171 LSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-245 |
1.58e-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: 59.26 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKH-DPQAQKLRR-QKIQIVFQNpygslnp 114
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNlDAVRQSLGMcPQHNILFHH------- 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 rkkvgQILEEPLLINSNLNKEQRREKALAMMAKVGLKTEHYDRYPHM--FSGGQRQRIAIARGLMLDPDVVIADEPVSAL 192
Cdd:TIGR01257 1018 -----LTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAqdLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 527035742 193 DVSVRAQVLNLMMDLQQdmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGT 245
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
35-251 |
1.79e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.21 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTlGRLLTMIEVPTGGELYYQgqdLLKHDPQAQKLRR-----QKIQIVFQNPY 109
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWR---F*TWCANRRALRRtig*hRPVR*GRRESF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 110 GSLNPRKKVGQILEepllinsnLNKEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPV 189
Cdd:NF000106 102 SGRENLYMIGR*LD--------LSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527035742 190 SALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFT 251
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
28-241 |
3.69e-09 |
|
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: 55.73 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 28 LFAPERLVKA--LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTG---GELYYQGQDLlkhDPQAQKLRRQkiq 102
Cdd:cd03233 11 FTTGKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPY---KEFAEKYPGE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 103 IVFQNPYGSLNPRKKVGQILEEPLLINSNlnkeqrrekalammakvglktehydRYPHMFSGGQRQRIAIARGLMLDPDV 182
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRETLDFALRCKGN-------------------------EFVRGISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 183 VIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSV-VEHIADEVMVMYLGRCV 241
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQI 199
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
42-249 |
3.90e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 42 SFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQD--LLKHDpQAQKLRRQKIQivfQNPYGSLNPR---- 115
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHitRLSFE-QLQKLVSDEWQ---RNNTDMLSPGeddt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 116 -KKVGQIleepllINSNLNKEQRREKaLAmmAKVGLKTEHYDRYPHMfSGGQRQRIAIARGLMLDPDVVIADEPVSALDV 194
Cdd:PRK10938 99 gRTTAEI------IQDEVKDPARCEQ-LA--QQFGITALLDRRFKYL-STGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 527035742 195 SVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVmyLGRC--VEKGTKEQI 249
Cdd:PRK10938 169 ASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGV--LADCtlAETGEREEI 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
163-249 |
1.13e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.67 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 163 SGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLN--LMMDLQQDmglSYVFISHDLSVVEHIaDEVMVMYLGRC 240
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGK---TRVLVTNQLHFLSQV-DRIILVHEGMI 817
|
....*....
gi 527035742 241 VEKGTKEQI 249
Cdd:PLN03130 818 KEEGTYEEL 826
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
42-194 |
1.23e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.41 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 42 SFTLERGKTLAVVGESGCGKSTLGRLLTM--IE-VPTGGELYYQGQDL-----------LKHDPQAQKLRRQKIQIVFQN 107
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTFLRYMAMhaIDgIPKNCQILHVEQEVvgddttalqcvLNTDIERTQLLEEEAQLVAQQ 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 108 PYGSLNPRKKVGQILEeplliNSNLNKE---QRRE----------------KALAMMAKVGLKTEHYDRYPHMFSGGQRQ 168
Cdd:PLN03073 277 RELEFETETGKGKGAN-----KDGVDKDavsQRLEeiykrlelidaytaeaRAASILAGLSFTPEMQVKATKTFSGGWRM 351
|
170 180
....*....|....*....|....*.
gi 527035742 169 RIAIARGLMLDPDVVIADEPVSALDV 194
Cdd:PLN03073 352 RIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
36-239 |
1.25e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 36 KALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDP-QAQKL--------RRQ-----KI 101
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKgmayitesRRDngffpNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 102 QIVfQNPygSLNPRKKVGQILEEPLLINSNlnKEQR-REKALAMMAkvgLKTEHYDRYPHMFSGGQRQRIAIARGLMLDP 180
Cdd:PRK09700 357 SIA-QNM--AISRSLKDGGYKGAMGLFHEV--DEQRtAENQRELLA---LKCHSVNQNITELSGGNQQKVLISKWLCCCP 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 181 DVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGR 486
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
38-255 |
2.27e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.45 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRL----LTMIEVPTG----GELYYQGQDLLKHDPQAQKLRR----QKIQIVF 105
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPRGarvtGDVTLNGEPLAAIDAPRLARLRavlpQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 106 qnPYgSLNPRKKVGQIleePLLINSNLNKEQRREKALAMMAKVGLKTeHYDRYPHMFSGGQRQRIAIARGL--------- 176
Cdd:PRK13547 97 --AF-SAREIVLLGRY---PHARRAGALTHRDGEIAWQALALAGATA-LVGRDVTTLSGGELARVQFARVLaqlwpphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 177 MLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFThPRH 255
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT-PAH 247
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
37-219 |
2.33e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.52 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLlkhDPqaqklrrqkiqivfqnpyGSLNPRK 116
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DA------------------GDIATRR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 KVGQI-----LEEPLLINSNLN---------KEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQRQRIAIARGLMLDPDV 182
Cdd:NF033858 340 RVGYMsqafsLYGELTVRQNLElharlfhlpAAEIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPEL 418
|
170 180 190
....*....|....*....|....*....|....*..
gi 527035742 183 VIADEPVSALDVSVRAQVLNLMMDLQQDMGLSyVFIS 219
Cdd:NF033858 419 LILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFIS 454
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
47-239 |
2.58e-08 |
|
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: 52.38 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 47 RGKTLAVVGESGCGKSTLGRLLtmievptggelyyqgqdllkhdpqAQKLRRQKIQIVFqnpygslnprkkvgqileepl 126
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL------------------------ARELGPPGGGVIY--------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 127 lINSNLNKEQRREKalammakvgLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMD 206
Cdd:smart00382 36 -IDGEDILEEVLDQ---------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEEL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 527035742 207 LQQDMGLSY-----VFISHDLSV-----VEHIADEVMVMYLGR 239
Cdd:smart00382 106 RLLLLLKSEknltvILTTNDEKDlgpalLRRRFDRRIVLLLIL 148
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-250 |
5.41e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 1 MSTQQATTQQPLLQ----AIDLKK-YYPVKKGLFAPerlvkALDGVSFTLERGKTLAVVGESGCGKSTLgrLLTMIevpt 75
Cdd:PLN03232 596 LSEERILAQNPPLQpgapAISIKNgYFSWDSKTSKP-----TLSDINLEIPVGSLVAIVGGTGEGKTSL--ISAML---- 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 76 gGELyyqgqdllKHDPQAQKLRRQKIQIVFQNPYgslnprkKVGQILEEPLLINSNLNKEQ--RREKALAMMAKVGL--- 150
Cdd:PLN03232 665 -GEL--------SHAETSSVVIRGSVAYVPQVSW-------IFNATVRENILFGSDFESERywRAIDVTALQHDLDLlpg 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 151 --KTEHYDRYPHMfSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDlQQDMGLSYVFISHDLSVVEHI 228
Cdd:PLN03232 729 rdLTEIGERGVNI-SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLM 806
|
250 260
....*....|....*....|..
gi 527035742 229 aDEVMVMYLGRCVEKGTKEQIF 250
Cdd:PLN03232 807 -DRIILVSEGMIKEEGTFAELS 827
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
38-239 |
7.52e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.01 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTL-GRLLTMIEVpTGGELYyqgqdllkhdpqAQKlrrqKIQIVFQNPYgSLNPRK 116
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLlQSLLSQFEI-SEGRVW------------AER----SIAYVPQQAW-IMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 KvGQIL---EEPlliNSNLNKEQRREKALAMMAKV--GLKTEHYDRYPHMfSGGQRQRIAIARGLMLDPDVVIADEPVSA 191
Cdd:PTZ00243 738 R-GNILffdEED---AARLADAVRVSQLEADLAQLggGLETEIGEKGVNL-SGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 527035742 192 LDVSVRAQVLNLMMdLQQDMGLSYVFISHDLSVVEHiADEVMVMYLGR 239
Cdd:PTZ00243 813 LDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPR-ADYVVALGDGR 858
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
163-239 |
2.19e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 2.19e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527035742 163 SGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDL-QQDMGLsyVFISHDLSVVEHIADEVMVMYLGR 239
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNGL 468
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
31-251 |
2.92e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.43 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PErLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKhdpqaqklrrqkiqivfqnpYG 110
Cdd:PLN03130 1249 PE-LPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISK--------------------FG 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 111 SLNPRKKVGQILEEPLL----INSNLN-------------------KEQRREKALAMMAKVGLKTEHydryphmFSGGQR 167
Cdd:PLN03130 1308 LMDLRKVLGIIPQAPVLfsgtVRFNLDpfnehndadlweslerahlKDVIRRNSLGLDAEVSEAGEN-------FSVGQR 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 168 QRIAIARGLMLDPDVVIADEPVSALDV--------SVRAQVLNLMMdlqqdmglsyVFISHDLSVVehI-ADEVMVMYLG 238
Cdd:PLN03130 1381 QLLSLARALLRRSKILVLDEATAAVDVrtdaliqkTIREEFKSCTM----------LIIAHRLNTI--IdCDRILVLDAG 1448
|
250
....*....|...
gi 527035742 239 RCVEKGTKEQIFT 251
Cdd:PLN03130 1449 RVVEFDTPENLLS 1461
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-241 |
3.14e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 52.32 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 12 LLQAIDLKKYYPvkkGLFAPerlvkALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHdp 91
Cdd:TIGR01257 1937 ILRLNELTKVYS---GTSSP-----AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN-- 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 92 qaqklrrqkIQIVFQNpYGSLNPRKKVGQIL--EEPLLINSNLN---KEQRREKALAMMAKVGLkTEHYDRYPHMFSGGQ 166
Cdd:TIGR01257 2007 ---------ISDVHQN-MGYCPQFDAIDDLLtgREHLYLYARLRgvpAEEIEKVANWSIQSLGL-SLYADRLAGTYSGGN 2075
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527035742 167 RQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDmGLSYVFISHDLSVVEHIADEVMVMYLG--RCV 241
Cdd:TIGR01257 2076 KRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGafQCL 2151
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
163-236 |
3.32e-07 |
|
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: 49.88 E-value: 3.32e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527035742 163 SGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHIADEVMVMY 236
Cdd:cd03222 73 SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
41-187 |
7.79e-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: 50.57 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 41 VSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQDLLKHDPQAQklrRQKIQIVFQNPYgslnprkkvgq 120
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAY---RQLFSAVFSDFH----------- 416
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527035742 121 iLEEPLLinsNLNKEQRREKALAMMAKVGL--KTEHYDrypHMF-----SGGQRQRIAIARGLMLDPDVVIADE 187
Cdd:COG4615 417 -LFDRLL---GLDGEADPARARELLERLELdhKVSVED---GRFsttdlSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
38-258 |
1.13e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 49.14 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLG----RLLTMIEvptgGELYYQGQDLLKHDPQAQklrRQKIQIVFQNPY---G 110
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSlaffRMVDIFD----GKIVIDGIDISKLPLHTL---RSRLSIILQDPIlfsG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 111 S----LNPRKK-VGQILEEPLLINSNLNKEQRREKALAMMAKVGLKTehydryphmFSGGQRQRIAIARGLMLDPDVVIA 185
Cdd:cd03288 110 SirfnLDPECKcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGEN---------FSVGQRQLFCLARAFVRKSSILIM 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527035742 186 DEPVSALDVSVRAQVLNLMMDLQQDMglSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFTHPRHPYT 258
Cdd:cd03288 181 DEATASIDMATENILQKVVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
35-235 |
1.27e-06 |
|
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: 48.09 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 35 VKALDGVSFTLERGKTLAVVGESGCGKSTLgrlltmieVPTGgeLYYQGQDLLKHDPQaqKLRRQKIqiVFqnpygslnp 114
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTL--------VNEG--LYASGKARLISFLP--KFSRNKL--IF--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 115 rkkVGQileepllinsnlnkeqrrekaLAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIAR--GLMLDPDVVIADEPVSAL 192
Cdd:cd03238 65 ---IDQ---------------------LQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 527035742 193 DVSVRAQVLNLMMDLqQDMGLSYVFISHDLSVVEHiADEVMVM 235
Cdd:cd03238 121 HQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSS-ADWIIDF 161
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
38-221 |
1.42e-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: 49.93 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYqGQDLlkhdpqaqklrrqKIQIVFQNpYGSLNPRKK 117
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-------------KLAYVDQS-RDALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 118 VGQILEEPLLInsnLNKEQRREKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDV-SV 196
Cdd:TIGR03719 403 VWEEISGGLDI---IKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTL 479
|
170 180
....*....|....*....|....*
gi 527035742 197 RAqvlnlMMDLQQDMGLSYVFISHD 221
Cdd:TIGR03719 480 RA-----LEEALLNFAGCAVVISHD 499
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-266 |
1.84e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.59 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 29 FAPErLVKALDGVSFTLERGKTLAVVGESGCGKST-LGRLLTMIEVPTGgELYYQGQDLLKHDpqAQKLRRQkIQIVFQN 107
Cdd:PLN03232 1244 YRPG-LPPVLHGLSFFVSPSEKVGVVGRTGAGKSSmLNALFRIVELEKG-RIMIDDCDVAKFG--LTDLRRV-LSIIPQS 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 108 PY-------GSLNPRKK-----VGQILEEPLLinsnlnKEQRREKALAMMAKVGLKTEHydryphmFSGGQRQRIAIARG 175
Cdd:PLN03232 1319 PVlfsgtvrFNIDPFSEhndadLWEALERAHI------KDVIDRNPFGLDAEVSEGGEN-------FSVGQRQLLSLARA 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 176 LMLDPDVVIADEPVSALDVSVRAQVLNLMMdlQQDMGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFTHPRH 255
Cdd:PLN03232 1386 LLRRSKILVLDEATASVDVRTDSLIQRTIR--EEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTS 1462
|
250
....*....|.
gi 527035742 256 PYTQALLSATP 266
Cdd:PLN03232 1463 AFFRMVHSTGP 1473
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-193 |
2.01e-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: 49.16 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 18 LKKYYPVKKglfaperlvKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQgqdllkhdPQAqklr 97
Cdd:TIGR03719 10 VSKVVPPKK---------EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ--------PGI---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 98 rqKIQIVFQNPYgsLNPRKKVGQILEEPLL-----------INSNLNKEQRR-EKALAMMAKVGLKTEHYD--------- 156
Cdd:TIGR03719 69 --KVGYLPQEPQ--LDPTKTVRENVEEGVAeikdaldrfneISAKYAEPDADfDKLAAEQAELQEIIDAADawdldsqle 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 527035742 157 ------RYP------HMFSGGQRQRIAIARGLMLDPDVVIADEPVSALD 193
Cdd:TIGR03719 145 iamdalRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
31-241 |
4.75e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 31 PERLVkaLDGVSFTLERGKTLAVVGESGCGKSTL---------GRLLTmievptgGELYYQGQDL-LKHDPQAQKlrrQK 100
Cdd:NF040905 271 PERKV--VDDVSLNVRRGEIVGIAGLMGAGRTELamsvfgrsyGRNIS-------GTVFKDGKEVdVSTVSDAID---AG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 101 IQIVFQNpygslnpRKKVGQILEEPLLIN---SNLNK-------EQRREKALAMMAKVGLKTehydRYPHMF------SG 164
Cdd:NF040905 339 LAYVTED-------RKGYGLNLIDDIKRNitlANLGKvsrrgviDENEEIKVAEEYRKKMNI----KTPSVFqkvgnlSG 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527035742 165 GQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLqQDMGLSYVFISHDLSVVEHIADEVMVMYLGRCV 241
Cdd:NF040905 408 GNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINEL-AAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
38-232 |
5.91e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.48 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTL--------GRLLTMIEVPTggelyYQGQDL-LKHDPQAQKLRRQKIQIVFQNP 108
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaeGQRRYVESLSA-----YARQFLgQMDKPDVDSIEGLSPAIAIDQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 109 YGSLNPRKKVGQILEepllINSNLNKEQRRE---KALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIAR--GLMLDPDVV 183
Cdd:cd03270 86 TTSRNPRSTVGTVTE----IYDYLRLLFARVgirERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATqiGSGLTGVLY 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 527035742 184 IADEPVSALDVSVRAQVLNLMMDLqQDMGLSYVFISHDLSVVEHiADEV 232
Cdd:cd03270 162 VLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRA-ADHV 208
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
38-245 |
8.58e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.47 E-value: 8.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLgrLLT---MIEVpTGGELYYQGQDLLKHDpqAQKLRRQkIQIVFQNPY---GS 111
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTL--LLTfmrMVEV-CGGEIRVNGREIGAYG--LRELRRQ-FSMIPQDPVlfdGT 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 112 LnpRKKVgqileEPLLinsnlnkEQRREKALAMMAKVGLK------TEHYDRY----PHMFSGGQRQRIAIARGLM-LDP 180
Cdd:PTZ00243 1400 V--RQNV-----DPFL-------EASSAEVWAALELVGLRervaseSEGIDSRvlegGSNYSVGQRQLMCMARALLkKGS 1465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527035742 181 DVVIADEPVSALDVSVRAQVLNLMMDLQQdmGLSYVFISHDLSVVEHIaDEVMVMYLGRCVEKGT 245
Cdd:PTZ00243 1466 GFILMDEATANIDPALDRQIQATVMSAFS--AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGS 1527
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
38-233 |
1.08e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLT-MIEVPTGGELYYQGQDLLKHDPQAQKLRRQKIQIVFQnpyGSLNPRK 116
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKnEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVID---GDREYRQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 kvgqiLEEPLLINSNLNKEQR----------------REKALAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDP 180
Cdd:PRK10636 94 -----LEAQLHDANERNDGHAiatihgkldaidawtiRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 527035742 181 DVVIADEPVSALDVSVraqVLNLMMDLQQDMGlSYVFISHDLSVVEHIADEVM 233
Cdd:PRK10636 169 DLLLLDEPTNHLDLDA---VIWLEKWLKSYQG-TLILISHDRDFLDPIVDKII 217
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
37-252 |
3.31e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 37 ALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGELYYQGQdllkhdpqaqklrrqkIQIVFQNpyGSLNPRK 116
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE----------------VSVIAIS--AGLSGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 KVGQILEEPLLINSNLNKEQRrekalAMMAKVgLKTEHYDRYPHM----FSGGQRQRIAIARGLMLDPDVVIADEPVSAL 192
Cdd:PRK13546 101 TGIENIEFKMLCMGFKRKEIK-----AMTPKI-IEFSELGEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDEALSVG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 193 DVSVRAQVLNLMMDLQQdMGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFTH 252
Cdd:PRK13546 175 DQTFAQKCLDKIYEFKE-QNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
38-221 |
5.45e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.94 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTLGRLLTmievptgGELyyqgqdllkhDPQAQKLRR-QKIQIVFQNPY-GSLNPR 115
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLML-------GQL----------QADSGRIHCgTKLEVAYFDQHrAELDPE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 116 KKVGQILEE---PLLINSnlnkeqRREKALA---------MMAKVGLKTehydryphmFSGGQRQRIAIARgLMLDP-DV 182
Cdd:PRK11147 398 KTVMDNLAEgkqEVMVNG------RPRHVLGylqdflfhpKRAMTPVKA---------LSGGERNRLLLAR-LFLKPsNL 461
|
170 180 190
....*....|....*....|....*....|....*....
gi 527035742 183 VIADEPVSALDVsvraQVLNLMMDLQQDMGLSYVFISHD 221
Cdd:PRK11147 462 LILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
39-79 |
2.54e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 2.54e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 527035742 39 DGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGEL 79
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
11-238 |
3.43e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 11 PLLQAIDLKKYY----PVKKGLFAPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEvpTGGelYYQGQDL 86
Cdd:PLN03140 865 PLAMSFDDVNYFvdmpAEMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRK--TGG--YIEGDIR 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 87 LKHDPQAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINSNLNKEQR----------------REKALAMMAKVGL 150
Cdd:PLN03140 941 ISGFPKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKmmfvdevmelveldnlKDAIVGLPGVTGL 1020
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 151 KTEhydryphmfsggQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDlQQDMGLSYVFISHDLSV-VEHIA 229
Cdd:PLN03140 1021 STE------------QRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSIdIFEAF 1087
|
....*....
gi 527035742 230 DEVMVMYLG 238
Cdd:PLN03140 1088 DELLLMKRG 1096
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
42-232 |
5.21e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 40.67 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 42 SFTLERGKTLaVVGESGCGKSTLgrlLTMIEVPTGGELYyQGQDLLKHDPQ--AQKLRRQKIQIVFQNPYGslnprKKVg 119
Cdd:cd03240 17 EIEFFSPLTL-IVGQNGAGKTTI---IEALKYALTGELP-PNSKGGAHDPKliREGEVRAQVKLAFENANG-----KKY- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 120 QILEEPLLINSNLNKEQRREKALAMmakvglktEHYDRyphmFSGGQRQ------RIAIARGLMLDPDVVIADEPVSALD 193
Cdd:cd03240 86 TITRSLAILENVIFCHQGESNWPLL--------DMRGR----CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 527035742 194 V-SVRAQVLNLMMDLQQDMGLSYVFISHDLSVVEHiADEV 232
Cdd:cd03240 154 EeNIEESLAEIIEERKSQKNFQLIVITHDEELVDA-ADHI 192
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
32-229 |
1.66e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 32 ERLVKALD------GVSFTLERGKTLAVVGESGCGKSTLGRLLTMIEVPTGGEL---------YYqGQD----------L 86
Cdd:PRK15064 323 ENLTKGFDngplfkNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigYY-AQDhaydfendltL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 87 L---------KHDPQAqklrrqkiqivfqnpygslnprkkVGQILEEPLLINSNLNKEqrrekalammAKVglktehydr 157
Cdd:PRK15064 402 FdwmsqwrqeGDDEQA------------------------VRGTLGRLLFSQDDIKKS----------VKV--------- 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527035742 158 yphmFSGGQRQRIAIARGLMLDPDVVIADEPVSALDV-SVRAqvLNLMMDLQQDmglSYVFISHDLSVVEHIA 229
Cdd:PRK15064 439 ----LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMeSIES--LNMALEKYEG---TLIFVSHDREFVSSLA 502
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
112-274 |
2.69e-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: 39.61 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 112 LNPRKKvgQILEEPLlinsnlnKEQRREkaLAMMAKVGLKTEHYDRYPHMFSGGQRQRIAIAR--GLMLDPDVVIADEPV 189
Cdd:TIGR00630 450 LTPEEK--KIAEEVL-------KEIRER--LGFLIDVGLDYLSLSRAAGTLSGGEAQRIRLATqiGSGLTGVLYVLDEPS 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 190 SALDVSVRAQVLNLMMDLqQDMGLSYVFISHDLSVVEHiADEVMVM------YLGRCVEKGTKEQIFTHPrHPYTQALLS 263
Cdd:TIGR00630 519 IGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDEDTIRA-ADYVIDIgpgageHGGEVVASGTPEEILANP-DSLTGQYLS 595
|
170
....*....|..
gi 527035742 264 ATPRLN-PDDRR 274
Cdd:TIGR00630 596 GRKKIEvPAERR 607
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
38-201 |
2.97e-03 |
|
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: 38.68 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 38 LDGVSFTLERGKTLAVVGESGCGKSTL-GRLLTMIEvpTGGELYYQGQDLlkhdpqaQKLRRQKIQIVFqnpygSLNPRK 116
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLlSAFLRLLN--TEGDIQIDGVSW-------NSVPLQKWRKAF-----GVIPQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527035742 117 KVgqILEEPLLINSNLNKEQRREKALAMMAKVGLKTEhYDRYP-----------HMFSGGQRQRIAIARGLMLDPDVVIA 185
Cdd:cd03289 86 VF--IFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSV-IEQFPgqldfvlvdggCVLSHGHKQLMCLARSVLSKAKILLL 162
|
170
....*....|....*.
gi 527035742 186 DEPVSALDvSVRAQVL 201
Cdd:cd03289 163 DEPSAHLD-PITYQVI 177
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
169-230 |
7.19e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 37.95 E-value: 7.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527035742 169 RIAIARGLMLDPDVVIADEPVSALDV-SVR--AQVLNlmmDLQQDMglsyVFISHDL----SVVEHIAD 230
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDInTIRwlEDVLN---ERNSTM----IIISHDRhflnSVCTHMAD 224
|
|
| |
