|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-325 |
1.28e-167 |
|
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: 468.76 E-value: 1.28e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGsyCVHRGQISLLGEDVLNAREK 84
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPP--GITSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPFELSGGMRQR 164
Cdd:COG0444 79 ELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 165 VMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADV 244
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 245 IHHPRHPYTIGLLQCAPEHGVPRQLLPAIPGTVPNLTHLPEGCAFRDRCYAAGAQC-ENVPALTACGDnNQRCACWYPQQ 323
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCrEEEPPLREVGP-GHRVACHLYEE 317
|
..
gi 446115710 324 EV 325
Cdd:COG0444 318 EA 319
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-274 |
6.26e-133 |
|
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: 388.66 E-value: 6.26e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHrGQISLLGEDVLN 80
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPS-GSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 AREKQLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPFELSGG 160
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 161 MRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGV 240
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
250 260 270
....*....|....*....|....*....|....
gi 446115710 241 TADVIHHPRHPYTIGLLQCAPeHGVPRQLLPAIP 274
Cdd:COG4172 241 TAELFAAPQHPYTRKLLAAEP-RGDPRPVPPDAP 273
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-326 |
5.70e-120 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 348.25 E-value: 5.70e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycVHRGQISLLGEDVLN 80
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANG--RIGGSATFNGREILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 AREKQLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPFELSGG 160
Cdd:PRK09473 86 LPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 161 MRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGV 240
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 241 TADVIHHPRHPYTIGLLQCAPEHGVPRQLLPAIPGTVPNLTHLPEGCAFRDRCYAAGAQCENVPALTACGDNNQRcACWY 320
Cdd:PRK09473 246 ARDVFYQPSHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSSAPPLEEFGPGRLR-ACFK 324
|
....*.
gi 446115710 321 PQQEVI 326
Cdd:PRK09473 325 PVEELL 330
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-239 |
9.96e-108 |
|
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: 313.29 E-value: 9.96e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTGsycvhrGQISLLGEDVLNARE 83
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLkPTS------GSIIFDGKDLLKLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQLRqWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEmQIPDAVEVMSRYPFELSGGMRQ 163
Cdd:cd03257 75 RLRK-IRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLV-GVGLPEEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115710 164 RVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-262 |
5.53e-98 |
|
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: 298.74 E-value: 5.53e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFPGF-NGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVL 79
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR-----PTSGSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 80 NAREKQLRQWRGaRVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDavEVMSRYPFELSG 159
Cdd:COG1123 331 KLSRRSLRELRR-RVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPP--DLADRYPHELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 160 GMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
250 260
....*....|....*....|...
gi 446115710 240 VTADVIHHPRHPYTIGLLQCAPE 262
Cdd:COG1123 488 PTEEVFANPQHPYTRALLAAVPS 510
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-323 |
2.85e-94 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 282.78 E-value: 2.85e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFP---GF----NGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTGsycvhrGQIS 72
Cdd:COG4608 3 MAEPLLEVRDLKKHFPvrgGLfgrtVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEePTS------GEIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 73 LLGEDVLNAREKQLRQWRgARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPdaVEVMSR 152
Cdd:COG4608 77 FDGQDITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLR--PEHADR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 153 YPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYA 232
Cdd:COG4608 154 YPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 233 GSVIESGVTADVIHHPRHPYTIGLLQCAP----EHGVPRQLLpaiPGTVPNLTHLPEGCAFRDRCYAAGAQC-ENVPALT 307
Cdd:COG4608 234 GKIVEIAPRDELYARPLHPYTQALLSAVPvpdpERRRERIVL---EGDVPSPLNPPSGCRFHTRCPYAQDRCaTEEPPLR 310
|
330
....*....|....*.
gi 446115710 308 ACGDnNQRCACWYPQQ 323
Cdd:COG4608 311 EVGP-GHQVACHLAEE 325
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-321 |
4.85e-93 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 279.87 E-value: 4.85e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 4 PVLDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTgSYCVHRGQISLLGEDVLNARE 83
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD-NWHVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQP----ISRREARAK-AIALLEEMQIPDAVEVMSRYPFELS 158
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFkgkwWQRFKWRKKrAIELLHRVGIKDHKDIMNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 159 GGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIES 238
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 239 GVTADVIHHPRHPYTIGLLQCAPEHGVP---RQLLPAIPGTVPNLTHLPEGCAFRDRCYAAGAQCENVPALTAcgDNNQR 315
Cdd:COG4170 241 GPTEQILKSPHHPYTKALLRSMPDFRQPlphKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVETPRLRK--IKGHE 318
|
....*.
gi 446115710 316 CACWYP 321
Cdd:COG4170 319 FACHFP 324
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-280 |
6.60e-93 |
|
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: 285.64 E-value: 6.60e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 3 QPVLDIQQLHLSFPGfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGsyCVHRGQISLLGEDVLNAR 82
Cdd:COG1123 2 TPLLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHG--GRISGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 83 EkqlrQWRGARVAMIFQEPMTALNPTRrIGLQMMDVIRHHQpISRREARAKAIALLEEMQIPDaveVMSRYPFELSGGMR 162
Cdd:COG1123 78 E----ALRGRRIGMVFQDPMTQLNPVT-VGDQIAEALENLG-LSRAEARARVLELLEAVGLER---RLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 163 QRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTA 242
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
250 260 270
....*....|....*....|....*....|....*...
gi 446115710 243 DVIHHPRhpytigLLQCAPEHGVPRQLLPAIPGTVPNL 280
Cdd:COG1123 229 EILAAPQ------ALAAVPRLGAARGRAAPAAAAAEPL 260
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-316 |
1.26e-92 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 278.55 E-value: 1.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYcVHRGQISLLGEDVLNAREK 84
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGR-VMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPFELSGGMRQR 164
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 165 VMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADV 244
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115710 245 IHHPRHPYTIGLLQCAPEHGVPRQLLPAIPGTVPNLTHLPEGCAFRDRCYAAGAQCENV-PALTACGDNNQRC 316
Cdd:PRK11022 242 FRAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEePALNMLAGRQSKC 314
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-262 |
4.67e-84 |
|
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: 263.08 E-value: 4.67e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 4 PVLDIQQLHLSFP---GF----NGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGsycvhrGQISLLGE 76
Cdd:COG4172 274 PLLEARDLKVWFPikrGLfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE------GEIRFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 77 DVLNAREKQLRQWRgARVAMIFQEPMTALNPTRRIGlqmmDVIR-----HHQPISRREARAKAIALLEEMQIPDavEVMS 151
Cdd:COG4172 348 DLDGLSRRALRPLR-RRMQVVFQDPFGSLSPRMTVG----QIIAeglrvHGPGLSAAERRARVAEALEEVGLDP--AARH 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 152 RYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:COG4172 421 RYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMK 500
|
250 260 270
....*....|....*....|....*....|.
gi 446115710 232 AGSVIESGVTADVIHHPRHPYTIGLLQCAPE 262
Cdd:COG4172 501 DGKVVEQGPTEQVFDAPQHPYTRALLAAAPL 531
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-280 |
1.48e-82 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 259.25 E-value: 1.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLN 80
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 AREKQLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPFELSGG 160
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 161 MRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGV 240
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446115710 241 TADVIHHPRHPYTIGLLQCAPEhGVPrqlLPAIPGTVPNL 280
Cdd:PRK15134 241 AATLFSAPTHPYTQKLLNSEPS-GDP---VPLPEPASPLL 276
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-264 |
9.75e-80 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 254.39 E-value: 9.75e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 2 TQPVLDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLL--GEDVL 79
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRrrSRQVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 80 NARE---KQLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPFE 156
Cdd:PRK10261 89 ELSEqsaAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 157 LSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVI 236
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260
....*....|....*....|....*...
gi 446115710 237 ESGVTADVIHHPRHPYTIGLLQCAPEHG 264
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAVPQLG 276
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-266 |
7.04e-78 |
|
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: 238.16 E-value: 7.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQ 85
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLER-----PWSGEVTFDGRPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 LRqwrgARVAMIFQEPMTALNPTRRIGLQMMDVIRHHqpiSRREARAKAIALLEEMQIPDavEVMSRYPFELSGGMRQRV 165
Cdd:COG1124 77 FR----RRVQMVFQDPYASLHPRHTVDRILAEPLRIH---GLPDREERIAELLEQVGLPP--SFLDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 166 MIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVI 245
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250 260
....*....|....*....|.
gi 446115710 246 HHPRHPYTIGLLQCAPEHGVP 266
Cdd:COG1124 228 AGPKHPYTRELLAASLAFERA 248
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
27-257 |
2.17e-74 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 228.79 E-value: 2.17e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 27 NVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVhRGQISLLGEDVLNARekqlrqWRGARVAMIFQEPMTALN 106
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQT-SGEILLDGRPLLPLS------IRGRHIATIMQNPRTAFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 107 PTRRIGLQMMDVIRHHQPISRrEARAKAIALLEEMQIPDAVEVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTA 186
Cdd:TIGR02770 77 PLFTMGNHAIETLRSLGKLSK-QARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115710 187 LDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHPRHPYTIGLL 257
Cdd:TIGR02770 156 LDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLL 226
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-321 |
4.04e-73 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 228.92 E-value: 4.04e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 4 PVLDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLlPTGSYCVHRGQISLLGEDVLNARE 83
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVI-------RHHQPISRREARAkaIALLEEMQIPDAVEVMSRYPFE 156
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgwtykgRWWQRFGWRKRRA--IELLHRVGIKDHKDAMRSFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 157 LSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVI 236
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 237 ESGVTADVIHHPRHPYTIGLLQCAPEHGVP---RQLLPAIPGTVPNLTHLPEGCAFRDRCYAAGAQCENVPALTacGDNN 313
Cdd:PRK15093 239 ETAPSKELVTTPHHPYTQALIRAIPDFGSAmphKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIETPRLT--GAKN 316
|
....*...
gi 446115710 314 QRCACWYP 321
Cdd:PRK15093 317 HLYACHFP 324
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-323 |
1.02e-69 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 220.22 E-value: 1.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFP---GF---NGDVHALNNVSLQINRSEIVGLVGESGSGKSVTA-MLIMRLLPTGsycvhrGQISL 73
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPvkrGLfkpERLVKALDGVSFTLERGKTLAVVGESGCGKSTLArLLTMIETPTG------GELYY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 74 LGEDVLNA---REKQLRQwrgaRVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQI-PdavEV 149
Cdd:PRK11308 75 QGQDLLKAdpeAQKLLRQ----KIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrP---EH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 150 MSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYV 229
Cdd:PRK11308 148 YDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 230 MYAGSVIESGVTADVIHHPRHPYTIGLLQCAPE-HGVPRQLLPAIPGTVPNLTHLPEGCAFRDRCYAAGAQC-ENVPALT 307
Cdd:PRK11308 228 MYLGRCVEKGTKEQIFNNPRHPYTQALLSATPRlNPDDRRERIKLTGELPSPLNPPPGCAFNARCPRAFGRCrQEQPQLR 307
|
330
....*....|....*.
gi 446115710 308 ACGDnnQRCACWYPQQ 323
Cdd:PRK11308 308 DYDG--RLVACFAVEQ 321
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-318 |
1.37e-69 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 219.96 E-value: 1.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 24 ALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQlrqWRGAR--VAMIFQEP 101
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATD-----GEVAWLGKDLLGMKDDE---WRAVRsdIQMIFQDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 102 MTALNPTRRIGLQMMDVIRHHQP-ISRREARAKAIALLeeMQIPDAVEVMSRYPFELSGGMRQRVMIALAFSCEPQLIIA 180
Cdd:PRK15079 108 LASLNPRMTIGEIIAEPLRTYHPkLSRQEVKDRVKAMM--LKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 181 DEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHPRHPYTIGLLQCA 260
Cdd:PRK15079 186 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAV 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115710 261 P------EHGVPRQLLpaiPGTVPNLTHLPEGCAFRDRCYAAGAQC-ENVPALTacGDNNQRCAC 318
Cdd:PRK15079 266 PipdpdlERNKTIQLL---EGELPSPINPPSGCVFRTRCPIAGPECaKTRPVLE--GSFRHAVSC 325
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-260 |
1.87e-55 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 188.38 E-value: 1.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 2 TQPVLDIQQLHLSFPGFNG-------DVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTgsycvhRGQISLL 74
Cdd:PRK15134 272 ASPLLDVEQLQVAFPIRKGilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS------QGEIWFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 75 GEDVLNAREKQLRQWRgARVAMIFQEPMTALNPTrrigLQMMDVI----RHHQP-ISRREARAKAIALLEEMQIpDAvEV 149
Cdd:PRK15134 346 GQPLHNLNRRQLLPVR-HRIQVVFQDPNSSLNPR----LNVLQIIeeglRVHQPtLSAAQREQQVIAVMEEVGL-DP-ET 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 150 MSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYV 229
Cdd:PRK15134 419 RHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIV 498
|
250 260 270
....*....|....*....|....*....|.
gi 446115710 230 MYAGSVIESGVTADVIHHPRHPYTIGLLQCA 260
Cdd:PRK15134 499 LRQGEVVEQGDCERVFAAPQQEYTRQLLALS 529
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
5-258 |
5.87e-55 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 179.90 E-value: 5.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSfpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHrGQISLLGEDVLNArek 84
Cdd:PRK10418 4 QIELRNIALQ-----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTA-GRVLLDGKPVAPC--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 qlrQWRGARVAMIFQEPMTALNPTRriglqmmdVIRHH-----QPISRREARAKAIALLEEMQIPDAVEVMSRYPFELSG 159
Cdd:PRK10418 75 ---ALRGRKIATIMQNPRSAFNPLH--------TMHTHaretcLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 160 GMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:PRK10418 144 GMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQG 223
|
250
....*....|....*....
gi 446115710 240 VTADVIHHPRHPYTIGLLQ 258
Cdd:PRK10418 224 DVETLFNAPKHAVTRSLVS 242
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-273 |
2.64e-54 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 180.66 E-value: 2.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 8 IQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSvTamLImRLL-----PTgsycvhRGQISLLGEDVLNAR 82
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS-T--LI-RCInllerPT------SGSVLVDGVDLTALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 83 EKQLRQWRgARVAMIFQ-----EPMTAL-N---PTRRIGlqmmdvirhhqpISRREARAKAIALLEEMQIPDAVEvmsRY 153
Cdd:COG1135 74 ERELRAAR-RKIGMIFQhfnllSSRTVAeNvalPLEIAG------------VPKAEIRKRVAELLELVGLSDKAD---AY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 154 PFELSGGMRQRVMIALAFSCEPQLIIADEPTTALD-VTVQlQVLRLLKhKARAS-GTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:COG1135 138 PSQLSGGQKQRVGIARALANNPKVLLCDEATSALDpETTR-SILDLLK-DINRElGLTIVLITHEMDVVRRICDRVAVLE 215
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446115710 232 AGSVIESGVTADVIHHPRHPYTIGLLQCAPEHGVPRQLLPAI 273
Cdd:COG1135 216 NGRIVEQGPVLDVFANPQSELTRRFLPTVLNDELPEELLARL 257
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-237 |
2.70e-54 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 177.16 E-value: 2.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 3 QPVLDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSvTAMLIMRLL--PTGsycvhrGQISLLGEDVLN 80
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGLdrPTS------GEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 AREKQLRQWRGARVAMIFQEP-----MTAL-NptrrIGLQMMdvIRHhqpISRREARAKAIALLEEMQIPDaveVMSRYP 154
Cdd:COG1136 75 LSERELARLRRRHIGFVFQFFnllpeLTALeN----VALPLL--LAG---VSRKERRERARELLERVGLGD---RLDHRP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 155 FELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQlCDSVYVMYAGS 234
Cdd:COG1136 143 SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGR 221
|
...
gi 446115710 235 VIE 237
Cdd:COG1136 222 IVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-230 |
7.82e-54 |
|
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: 175.76 E-value: 7.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSvTAMLIMRLL--PTgsycvhRGQISLLGEDVLNARE 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGLdrPT------SGEVRVDGTDISKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQLRQWRGARVAMIFQEP-----MTAL-NptrrIGLQMMdvirhHQPISRREARAKAIALLEEMQIPDAvevMSRYPFEL 157
Cdd:cd03255 74 KELAAFRRRHIGFVFQSFnllpdLTALeN----VELPLL-----LAGVPKKERRERAEELLERVGLGDR---LNHYPSEL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115710 158 SGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSqLCDSVYVM 230
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIEL 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-246 |
1.75e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 175.25 E-value: 1.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTGsycvhrGQISLLGEDVlnarEK 84
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLrPTS------GEVRVLGEDV----AR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRQWRgARVAMIFQEPmtALNPTRRiGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAvevMSRYPFELSGGMRQR 164
Cdd:COG1131 67 DPAEVR-RRIGYVPQEP--ALYPDLT-VRENLRFFARLYGLPRKEARERIDELLELFGLTDA---ADRKVGTLSGGMKQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 165 VMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADV 244
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDPEARRELWELLR-ELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
..
gi 446115710 245 IH 246
Cdd:COG1131 219 KA 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-249 |
3.62e-51 |
|
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: 169.05 E-value: 3.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPGfngDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAREK 84
Cdd:COG1122 1 IELENLSFSYPG---GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLkPT------SGEVLVDGKDITKKNLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRQwrgaRVAMIFQEPMTAL-NPT---------RRIGLqmmdvirhhqpiSRREARAKAIALLEEMQIPDaveVMSRYP 154
Cdd:COG1122 72 ELRR----KVGLVFQNPDDQLfAPTveedvafgpENLGL------------PREEIRERVEEALELVGLEH---LADRPP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 155 FELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGS 234
Cdd:COG1122 133 HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLK-RLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
250
....*....|....*
gi 446115710 235 VIESGVTADVIHHPR 249
Cdd:COG1122 212 IVADGTPREVFSDYE 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-252 |
1.07e-50 |
|
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: 168.23 E-value: 1.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVL 79
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLrPD------SGEILVDGQDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 80 NAREKQLRQWRgARVAMIFQEP-----MTAL-NptrrIGLQMmdviRHHQPISRREARAKAIALLEEMQIPDAVEvmsRY 153
Cdd:COG1127 71 GLSEKELYELR-RRIGMLFQGGalfdsLTVFeN----VAFPL----REHTDLSEAEIRELVLEKLELVGLPGAAD---KM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 154 PFELSGGMRQRVMIALAFSCEPQLIIADEPTTALD-VTVQlQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYA 232
Cdd:COG1127 139 PSELSGGMRKRVALARALALDPEILLYDEPTAGLDpITSA-VIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLAD 217
|
250 260
....*....|....*....|
gi 446115710 233 GSVIESGvTADVIHHPRHPY 252
Cdd:COG1127 218 GKIIAEG-TPEELLASDDPW 236
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-274 |
1.15e-49 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 166.40 E-value: 1.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 12 HLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRL-LPTGsycvhrGQISLLGEDVLNAREKQLRQWR 90
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLeSPSQ------GNVSWRGEPLAKLNRAQRKAFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 91 GArVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDavEVMSRYPFELSGGMRQRVMIALA 170
Cdd:PRK10419 89 RD-IQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDD--SVLDKRPPQLSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 171 FSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHpRH 250
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTF-SS 244
|
250 260
....*....|....*....|....
gi 446115710 251 PYTIgLLQCApehgvprqLLPAIP 274
Cdd:PRK10419 245 PAGR-VLQNA--------VLPAFP 259
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-249 |
1.10e-47 |
|
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: 160.05 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSvTAMLIMRLLPTGSycvhRGQISLLGEDVLNAREK 84
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLERPT----SGSVLVDGTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRQWRgARVAMIFQ-----EPMTALN----PtrrigLQMmdvirHHQPISRREARAKAiaLLEEMQIPDAVEvmsRYPF 155
Cdd:cd03258 76 ELRKAR-RRIGMIFQhfnllSSRTVFEnvalP-----LEI-----AGVPKAEIEERVLE--LLELVGLEDKAD---AYPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 156 ELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:cd03258 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
250
....*....|....
gi 446115710 236 IESGVTADVIHHPR 249
Cdd:cd03258 220 VEEGTVEEVFANPQ 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-261 |
2.67e-47 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 168.50 E-value: 2.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 3 QPVLDIQQLHLSFPGFNG-------DVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLG 75
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG-----GEIIFNG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 76 EDVLNAREKQLRQWRgARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDavEVMSRYPF 155
Cdd:PRK10261 386 QRIDTLSPGKLQALR-RDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLP--EHAWRYPH 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 156 ELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:PRK10261 463 EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
250 260
....*....|....*....|....*.
gi 446115710 236 IESGVTADVIHHPRHPYTIGLLQCAP 261
Cdd:PRK10261 543 VEIGPRRAVFENPQHPYTRKLMAAVP 568
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-251 |
1.05e-46 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 157.85 E-value: 1.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVlNAREK 84
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEE-----PDSGTITVDGEDL-TDSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRQWRgARVAMIFQE----P-MTAL-NPTrrIGLqmmdviRHHQPISRREARAKAIALLEEMQIPDaveVMSRYPFELS 158
Cdd:COG1126 71 DINKLR-RKVGMVFQQfnlfPhLTVLeNVT--LAP------IKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 159 GGMRQRVMIALAFSCEPQLIIADEPTTALD---VTVQLQVLRLLkhkaRASGTAVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:COG1126 139 GGQQQRVAIARALAMEPKVMLFDEPTSALDpelVGEVLDVMRDL----AKEGMTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
250
....*....|....*.
gi 446115710 236 IESGVTADVIHHPRHP 251
Cdd:COG1126 215 VEEGPPEEFFENPQHE 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-253 |
1.63e-46 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 160.35 E-value: 1.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 7 DIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRL-LPTGsycvhrGQISLLGEDVLNAREKQ 85
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLeRPTS------GRVLVDGQDLTALSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 LRQWRgARVAMIFQE---------------PMTALNptrriglqmmdvirhhqpISRREARAKAIALLEEMQIPDAvevM 150
Cdd:PRK11153 77 LRKAR-RQIGMIFQHfnllssrtvfdnvalPLELAG------------------TPKAEIKARVTELLELVGLSDK---A 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 151 SRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVM 230
Cdd:PRK11153 135 DRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVI 214
|
250 260
....*....|....*....|...
gi 446115710 231 YAGSVIESGVTADVIHHPRHPYT 253
Cdd:PRK11153 215 DAGRLVEQGTVSEVFSHPKHPLT 237
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-230 |
2.12e-46 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 157.56 E-value: 2.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQ--PVLDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSvTamlIMRLL-----PTgsycvhRGQISL 73
Cdd:COG1116 1 MSAaaPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS-T---LLRLIaglekPT------SGEVLV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 74 LGEDVLNArekqlrqwrGARVAMIFQEPmtALNPTRRI------GLQMMDVirhhqpiSRREARAKAIALLEEMQIPDAv 147
Cdd:COG1116 71 DGKPVTGP---------GPDRGVVFQEP--ALLPWLTVldnvalGLELRGV-------PKAERRERARELLELVGLAGF- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 148 evMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDV----TVQLQVLRLLkhkaRASGTAVLFISHDM--AVVs 221
Cdd:COG1116 132 --EDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQDELLRLW----QETGKTVLFVTHDVdeAVF- 204
|
....*....
gi 446115710 222 qLCDSVYVM 230
Cdd:COG1116 205 -LADRVVVL 212
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-247 |
3.10e-46 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 156.76 E-value: 3.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 4 PVLDIQQLHLSFPGfngDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAR 82
Cdd:COG3638 1 PMLELRNLSKRYPG---GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVePT------SGEILVDGQDVTALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 83 EKQLRQWRgARVAMIFQEP-----MTALN----------PTRRIGLQMMdvirhhqpisRREARAKAIALLEEMQIPDAV 147
Cdd:COG3638 72 GRALRRLR-RRIGMIFQQFnlvprLSVLTnvlagrlgrtSTWRSLLGLF----------PPEDRERALEALERVGLADKA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 148 EVMSRypfELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSV 227
Cdd:COG3638 141 YQRAD---QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRI 217
|
250 260
....*....|....*....|....
gi 446115710 228 YVMYAGSVI----ESGVTADVIHH 247
Cdd:COG3638 218 IGLRDGRVVfdgpPAELTDAVLRE 241
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-244 |
1.29e-44 |
|
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: 152.70 E-value: 1.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVlnarE 83
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLkPD------SGSILIDGEDV----R 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQLRQWRgARVAMIFQEPMTALNPTRRiglqmmDVIRHH---QPISRREARAKAIALLEEMQIPDaveVMSRYPFELSGG 160
Cdd:COG4555 67 KEPREAR-RQIGVLPDERGLYDRLTVR------ENIRYFaelYGLFDEELKKRIEELIELLGLEE---FLDRRVGELSTG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 161 MRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGV 240
Cdd:COG4555 137 MKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILR-ALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
....
gi 446115710 241 TADV 244
Cdd:COG4555 216 LDEL 219
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
4-258 |
1.87e-44 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 152.68 E-value: 1.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 4 PVLDIQQLHLSFPGFNG-----DVHALNNVSLQINRSEIVGLVGESGSGKSVTA-MLIMRLLPTGsycvhrGQISLLGED 77
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAkMLAGIIEPTS------GEILINGHK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 78 VlnarEKQLRQWRGARVAMIFQEPMTALNPTRRIGlQMMDV-IRHHQPISRREARAKAIALLEemQIPDAVEVMSRYPFE 156
Cdd:COG4167 77 L----EYGDYKYRCKHIRMIFQDPNTSLNPRLNIG-QILEEpLRLNTDLTAEEREERIFATLR--LVGLLPEHANFYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 157 LSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVI 236
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
250 260
....*....|....*....|..
gi 446115710 237 ESGVTADVIHHPRHPYTIGLLQ 258
Cdd:COG4167 230 EYGKTAEVFANPQHEVTKRLIE 251
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-252 |
6.85e-44 |
|
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: 150.34 E-value: 6.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAREK 84
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLrPD------SGEVLIDGEDISGLSEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRQWRgARVAMIFQEPmtALnptrrigLQMMDV-------IRHHQPISRREARAKAIALLEEMQIPDAVEvmsRYPFEL 157
Cdd:cd03261 71 ELYRLR-RRMGMLFQSG--AL-------FDSLTVfenvafpLREHTRLSEEEIREIVLEKLEAVGLRGAED---LYPAEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 158 SGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIE 237
Cdd:cd03261 138 SGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
|
250
....*....|....*
gi 446115710 238 SGvTADVIHHPRHPY 252
Cdd:cd03261 218 EG-TPEELRASDDPL 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-245 |
1.33e-42 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 147.50 E-value: 1.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSvTAM-LIMRLLPtgsycVHRGQISLLGEDVLNARE 83
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKS-TLLrALAGLLK-----PSSGEVLLDGRDLASLSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQLRQwrgaRVAMIFQEPMTALnptrriGLQMMDVIR-----HHQPISR--REARAKAIALLEEMQIPDAVEvmsRYPFE 156
Cdd:COG1120 71 RELAR----RIAYVPQEPPAPF------GLTVRELVAlgrypHLGLFGRpsAEDREAVEEALERTGLEHLAD---RPVDE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 157 LSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVI 236
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
....*....
gi 446115710 237 ESGVTADVI 245
Cdd:COG1120 218 AQGPPEEVL 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-233 |
1.54e-42 |
|
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: 146.07 E-value: 1.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 8 IQQLHLSFPgfNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQLR 87
Cdd:cd03225 2 LKNLSFSYP--DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTS-----GEVLVDGKDLTKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 88 QwrgaRVAMIFQEPMTAL-NPTRR----IGLQmmdvirhHQPISRREARAKAIALLEEMQIPDaveVMSRYPFELSGGMR 162
Cdd:cd03225 75 R----KVGLVFQNPDDQFfGPTVEeevaFGLE-------NLGLPEEEIEERVEEALELVGLEG---LRDRSPFTLSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115710 163 QRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLK-KLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
12-256 |
2.21e-42 |
|
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: 147.60 E-value: 2.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 12 HLSF---PGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAREKQLR 87
Cdd:TIGR04521 5 NVSYiyqPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLkPT------SGTVTIDGRDITAKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 88 QWRgARVAMIFQEP------MT-----ALNPtRRIGLqmmdvirhhqpiSRREARAKAIALLEEMQIPDavEVMSRYPFE 156
Cdd:TIGR04521 79 DLR-KKVGLVFQFPehqlfeETvykdiAFGP-KNLGL------------SEEEAEERVKEALELVGLDE--EYLERSPFE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 157 LSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVI 236
Cdd:TIGR04521 143 LSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIV 222
|
250 260
....*....|....*....|
gi 446115710 237 ESGVTADVIHHPRHPYTIGL 256
Cdd:TIGR04521 223 LDGTPREVFSDVDELEKIGL 242
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-230 |
2.85e-42 |
|
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: 145.69 E-value: 2.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSvTamlIMRLL-----PTgsycvhRGQISLLGEDVln 80
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS-T---LLRIIaglerPT------SGEVLVDGEPV-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 arekqlrQWRGARVAMIFQEPmtALNPTRRI------GLQMmdvirhhQPISRREARAKAIALLEEMQIPDAVevmSRYP 154
Cdd:cd03293 69 -------TGPGPDRGYVFQQD--ALLPWLTVldnvalGLEL-------QGVPKAEARERAEELLELVGLSGFE---NAYP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 155 FELSGGMRQRVMIALAFSCEPQLIIADEPTTALDV----TVQLQVLRLLKHkaraSGTAVLFISHDM--AVVsqLCDSVY 228
Cdd:cd03293 130 HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRE----TGKTVLLVTHDIdeAVF--LADRVV 203
|
..
gi 446115710 229 VM 230
Cdd:cd03293 204 VL 205
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-235 |
4.14e-42 |
|
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: 143.69 E-value: 4.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTGsycvhrGQISLLGEDVLNAREK 84
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPDS------GEIKVLGKDIKKEPEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRqwrgaRVAMIFQEPMtalnptrriglqmmdvirhhqpisrrearakaiaLLEEMQIPDAVEvmsrypfeLSGGMRQR 164
Cdd:cd03230 71 VKR-----RIGYLPEEPS----------------------------------LYENLTVRENLK--------LSGGMKQR 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115710 165 VMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:cd03230 104 LALAQALLHDPELLILDEPTSGLDPESRREFWELLR-ELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-242 |
6.79e-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: 145.27 E-value: 6.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRL-LPTGsycvhrGQISLLGEDVL 79
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLdRPTS------GTVRLAGQDLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 80 NAREKQLRQWRGARVAMIFQE----P-MTAL-NptrriglQMMdvirhhqPI---SRREARAKAIALLEemqipdAVEVM 150
Cdd:COG4181 78 ALDEDARARLRARHVGFVFQSfqllPtLTALeN-------VML-------PLelaGRRDARARARALLE------RVGLG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 151 SR---YPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQlCDSV 227
Cdd:COG4181 138 HRldhYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRV 216
|
250
....*....|....*
gi 446115710 228 YVMYAGSVIESGVTA 242
Cdd:COG4181 217 LRLRAGRLVEDTAAT 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-249 |
2.40e-41 |
|
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: 144.41 E-value: 2.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 2 TQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSvTAM-LImrllpTGSYCVHRGQISLLGEDVLN 80
Cdd:COG0411 1 SDPLLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKT-TLFnLI-----TGFYRPTSGRILFDGRDITG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 arekqLRQWRGAR--VAMIFQEP------------MTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDa 146
Cdd:COG0411 71 -----LPPHRIARlgIARTFQNPrlfpeltvlenvLVAAHARLGRGLLAALLRLPRARREEREARERAEELLERVGLAD- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 147 veVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDS 226
Cdd:COG0411 145 --RADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADR 222
|
250 260
....*....|....*....|...
gi 446115710 227 VYVMYAGSVIESGVTADVIHHPR 249
Cdd:COG0411 223 IVVLDFGRVIAEGTPAEVRADPR 245
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-249 |
8.24e-41 |
|
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: 142.58 E-value: 8.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSvTAM-LIMRLLPTGSycvhrGQISLLGEDVLNAREK 84
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKT-TLFnLISGFLRPTS-----GSVLFDGEDITGLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRQwRGarVAMIFQEP-----MTALNpTRRIGLQMmdviRHHQPI-------SRREARAKAIALLEEMQIPDaveVMSR 152
Cdd:cd03219 71 EIAR-LG--IGRTFQIPrlfpeLTVLE-NVMVAAQA----RTGSGLllararrEEREARERAEELLERVGLAD---LADR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 153 YPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYA 232
Cdd:cd03219 140 PAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIR-ELRERGITVLLVEHDMDVVMSLADRVTVLDQ 218
|
250
....*....|....*..
gi 446115710 233 GSVIESGVTADVIHHPR 249
Cdd:cd03219 219 GRVIAEGTPDEVRNNPR 235
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-253 |
1.08e-40 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 142.76 E-value: 1.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKS-VTAMLIMRLLPTGSYCVHRGQISLLgEDVL 79
Cdd:PRK11701 2 MDQPLLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTtLLNALSARLAPDAGEVHYRMRDGQL-RDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 80 NAREKQLRQWRGARVAMIFQEPMTALNPT----RRIGLQMMDV-IRHHQPIsrreaRAKAIALLEEMQIPdaVEVMSRYP 154
Cdd:PRK11701 77 ALSEAERRRLLRTEWGFVHQHPRDGLRMQvsagGNIGERLMAVgARHYGDI-----RATAGDWLERVEID--AARIDDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 155 FELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGS 234
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
250
....*....|....*....
gi 446115710 235 VIESGVTADVIHHPRHPYT 253
Cdd:PRK11701 230 VVESGLTDQVLDDPQHPYT 248
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-247 |
1.55e-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: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPGfngDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQ 85
Cdd:cd03256 1 IEVENLSKTYPN---GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTS-----GSVLIDGTDINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 LRQWRgARVAMIFQ-----EPMTALN----------PTRRIGLQMMDvirhhqpisrREARAKAIALLEEMQIPDAVEVM 150
Cdd:cd03256 73 LRQLR-RQIGMIFQqfnliERLSVLEnvlsgrlgrrSTWRSLFGLFP----------KEEKQRALAALERVGLLDKAYQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 151 SRypfELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVM 230
Cdd:cd03256 142 AD---QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGL 218
|
250 260
....*....|....*....|.
gi 446115710 231 YAGSVIESG----VTADVIHH 247
Cdd:cd03256 219 KDGRIVFDGppaeLTDEVLDE 239
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-245 |
5.96e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.91 E-value: 5.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSvTAM-LIMRLLPtgsycVHRGQISLLGEDVL 79
Cdd:COG1121 2 MMMPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKS-TLLkAILGLLP-----PTSGTVRLFGKPPR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 80 NAREK-----QLRQwrgarVAMIFqePMTALnptrriglqmmDVIR----HHQPISRR---EARAKAIALLEEMQIPDav 147
Cdd:COG1121 72 RARRRigyvpQRAE-----VDWDF--PITVR-----------DVVLmgryGRRGLFRRpsrADREAVDEALERVGLED-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 148 evMSRYPF-ELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDS 226
Cdd:COG1121 132 --LADRPIgELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELL-RELRREGKTILVVTHDLGAVREYFDR 208
|
250
....*....|....*....
gi 446115710 227 VYVMyAGSVIESGVTADVI 245
Cdd:COG1121 209 VLLL-NRGLVAHGPPEEVL 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-185 |
9.53e-39 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 134.31 E-value: 9.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAREKQLRQwrgaRVAMIFQEPmt 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLsPT------EGTILLDGQDLTDDERKSLRK----EIGYVFQDP-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 104 ALNPTRRIGLQMMDViRHHQPISRREARAKAIALLEEMQIPD-AVEVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADE 182
Cdd:pfam00005 69 QLFPRLTVRENLRLG-LLLKGLSKREKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
...
gi 446115710 183 PTT 185
Cdd:pfam00005 148 PTA 150
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-252 |
2.57e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 139.08 E-value: 2.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLN 80
Cdd:COG3842 1 MAMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFET-----PDSGRILLDGRDVTG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 -AREKqlrqwRGarVAMIFQEP-----MTAL-NptrrI--GLQMMDVirhhqpiSRREARAKAIALLEEMQIPDaveVMS 151
Cdd:COG3842 72 lPPEK-----RN--VGMVFQDYalfphLTVAeN----VafGLRMRGV-------PKAEIRARVAELLELVGLEG---LAD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 152 RYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHD----MAvvsqLCDSV 227
Cdd:COG3842 131 RYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRI 206
|
250 260
....*....|....*....|....*
gi 446115710 228 YVMYAGSVIESGVTADVIHHPRHPY 252
Cdd:COG3842 207 AVMNDGRIEQVGTPEEIYERPATRF 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-260 |
2.94e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 138.74 E-value: 2.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPGFngdvHALNNVSLQINRSEIVGLVGESGSGKSvtamLIMRLL-----PTgsycvhRGQISLLGEDVLN 80
Cdd:COG1118 3 IEVRNISKRFGSF----TLLDDVSLEIASGELVALLGPSGSGKT----TLLRIIagletPD------SGRIVLNGRDLFT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 AREKQLRqwrgaRVAMIFQEPmtALNPTrriglqmMDVIRH------HQPISRREARAKAIALLEEMQIPDAVEvmsRYP 154
Cdd:COG1118 69 NLPPRER-----RVGFVFQHY--ALFPH-------MTVAENiafglrVRPPSKAEIRARVEELLELVQLEGLAD---RYP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 155 FELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGS 234
Cdd:COG1118 132 SQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGR 211
|
250 260
....*....|....*....|....*.
gi 446115710 235 VIESGVTADVIHHPRHPYTIGLLQCA 260
Cdd:COG1118 212 IEQVGTPDEVYDRPATPFVARFLGCV 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-244 |
3.41e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 141.69 E-value: 3.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 2 TQPVLDIQQLHLSFPGfngdVHALNNVSLQINRSEIVGLVGESGSGKSvTAMLIMrllpTGSYCVHRGQISLLGEDV--L 79
Cdd:COG1129 1 AEPLLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKS-TLMKIL----SGVYQPDSGEILLDGEPVrfR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 80 NAREKQlrqwrGARVAMIFQEPMTALNptrriglqmMDV---------IRHHQPISRREARAKAIALLEEMQI---PDA- 146
Cdd:COG1129 72 SPRDAQ-----AAGIAIIHQELNLVPN---------LSVaeniflgrePRRGGLIDWRAMRRRARELLARLGLdidPDTp 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 147 VEvmsrypfELSGGMRQRVMIALAFSCEPQLIIADEPTTAL---DVTVQLQVLRLLKhkarASGTAVLFISHDMAVVSQL 223
Cdd:COG1129 138 VG-------DLSVAQQQLVEIARALSRDARVLILDEPTASLterEVERLFRIIRRLK----AQGVAIIYISHRLDEVFEI 206
|
250 260
....*....|....*....|.
gi 446115710 224 CDSVYVMYAGSVIESGVTADV 244
Cdd:COG1129 207 ADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-239 |
4.70e-37 |
|
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: 131.87 E-value: 4.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNaREKQ 85
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLER-----PDSGEILIDGRDVTG-VPPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 LRqwrgaRVAMIFQEPmtALNPTRRI------GLQMMDVirhhqpiSRREARAKAIALLEEMQIPDaveVMSRYPFELSG 159
Cdd:cd03259 71 RR-----NIGMVFQDY--ALFPHLTVaeniafGLKLRGV-------PKAEIRARVRELLELVGLEG---LLNRYPHELSG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 160 GMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03259 134 GQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
18-247 |
5.37e-37 |
|
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: 132.81 E-value: 5.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 18 FNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTGsycvhrGQISLLGEDVLNAREKQLRQWRgARVAM 96
Cdd:TIGR02315 11 YPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVePSS------GSILLEGTDITKLRGKKLRKLR-RRIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 97 IFQE-----PMTAL----------NPTRRIGLQMMdvirhhqpisRREARAKAIALLEEMQIPDAVEVMSRYpfeLSGGM 161
Cdd:TIGR02315 84 IFQHynlieRLTVLenvlhgrlgyKPTWRSLLGRF----------SEEDKERALSALERVGLADKAYQRADQ---LSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 162 RQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG-- 239
Cdd:TIGR02315 151 QQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGap 230
|
250
....*....|
gi 446115710 240 --VTADVIHH 247
Cdd:TIGR02315 231 seLDDEVLRH 240
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-239 |
6.33e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 131.71 E-value: 6.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFPGfngDVHALNNVSLQINRSEIVGLVGESGSGKSvTAM-LIMRLL-PTgsycvhRGQISLLGEDVLNAR 82
Cdd:COG2884 1 MIRFENVSKRYPG---GREALSDVSLEIEKGEFVFLTGPSGAGKS-TLLkLLYGEErPT------SGQVLVNGQDLSRLK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 83 EKQLRQWRgARVAMIFQEP-----MTAL-N---PTRRIGLqmmdvirhhqpiSRREARAKAIALLEEMQIPDAvevMSRY 153
Cdd:COG2884 71 RREIPYLR-RRIGVVFQDFrllpdRTVYeNvalPLRVTGK------------SRKEIRRRVREVLDLVGLSDK---AKAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 154 PFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:COG2884 135 PHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLE-EINRRGTTVLIATHDLELVDRMPKRVLELEDG 213
|
....*.
gi 446115710 234 SVIESG 239
Cdd:COG2884 214 RLVRDE 219
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-253 |
8.50e-37 |
|
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: 132.65 E-value: 8.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 3 QPVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAR 82
Cdd:TIGR02323 1 KPLLQVSGLSKSY----GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 83 EKQLRQWRGARVAMIFQEPMTALNPT----RRIGLQMMDV-IRHHQPIsrreaRAKAIALLEEMQIPDAVevMSRYPFEL 157
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQNPRDGLRMRvsagANIGERLMAIgARHYGNI-----RATAQDWLEEVEIDPTR--IDDLPRAF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 158 SGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIE 237
Cdd:TIGR02323 150 SGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVE 229
|
250
....*....|....*.
gi 446115710 238 SGVTADVIHHPRHPYT 253
Cdd:TIGR02323 230 SGLTDQVLDDPQHPYT 245
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-241 |
1.50e-36 |
|
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: 131.15 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAREKQ 85
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 LrqWRGARVAMIFQEPmtalNPTR-------RIGLqmmdviRHHQPISRREARAKAIALLEEMQIPDavEVMSR-YPFEL 157
Cdd:cd03260 77 L--ELRRRVGMVFQKP----NPFPgsiydnvAYGL------RLHGIKLKEELDERVEEALRKAALWD--EVKDRlHALGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 158 SGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARAsgTAVLFISHDMAVVSQLCDSVYVMYAGSVIE 237
Cdd:cd03260 143 SGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
....
gi 446115710 238 SGVT 241
Cdd:cd03260 221 FGPT 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
20-233 |
1.63e-36 |
|
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: 129.61 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVlnAREKQLRQWRGARVAMIF 98
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEePD------SGSILIDGEDL--TDLEDELPPLRRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 99 QEPmtALNPTrriglqmMDVirhhqpisrrearakaialLEEMQIPdavevmsrypfeLSGGMRQRVMIALAFSCEPQLI 178
Cdd:cd03229 83 QDF--ALFPH-------LTV-------------------LENIALG------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446115710 179 IADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-233 |
2.06e-36 |
|
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: 128.52 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 8 IQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQLR 87
Cdd:cd00267 2 IENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-----PTSGEILIDGKDIAKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 88 QwrgaRVAMIFQepmtalnptrriglqmmdvirhhqpisrrearakaialleemqipdavevmsrypfeLSGGMRQRVMI 167
Cdd:cd00267 73 R----RIGYVPQ---------------------------------------------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115710 168 ALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLR-ELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-239 |
3.27e-36 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 128.71 E-value: 3.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 7 DIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQL 86
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSS-----GEILLDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 87 RQwrgaRVAMIFQepmtalnptrriglqmmdvirhhqpisrrearakaiaLLEEMQIPDAVEvmsRYPFELSGGMRQRVM 166
Cdd:cd03214 72 AR----KIAYVPQ-------------------------------------ALELLGLAHLAD---RPFNELSGGERQRVL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115710 167 IALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-244 |
1.29e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 130.61 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSvTAM-LIMRLL-PTGsycvhrGQISLLGEDVlnaR 82
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKT-TTIrIILGILaPDS------GEVLWDGEPL---D 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 83 EKQLRQW------RGarvamifqepmtaLNPTRRIGLQMMDVIRHHQpISRREARAKAIALLEEMQIPDA----VEvmsr 152
Cdd:COG4152 67 PEDRRRIgylpeeRG-------------LYPKMKVGEQLVYLARLKG-LSKAEAKRRADEWLERLGLGDRankkVE---- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 153 ypfELSGGMRQRVMIALAFSCEPQLIIADEPTTALD-VTVQL--QVLRLLKhkarASGTAVLFISHDMAVVSQLCDSVYV 229
Cdd:COG4152 129 ---ELSKGNQQKVQLIAALLHDPELLILDEPFSGLDpVNVELlkDVIRELA----AKGTTVIFSSHQMELVEELCDRIVI 201
|
250
....*....|....*
gi 446115710 230 MYAGSVIESGVTADV 244
Cdd:COG4152 202 INKGRKVLSGSVDEI 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-233 |
1.49e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.01 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPGFNGdvhaLNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVlnaREKQ 85
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDP-----PTSGEIYLDGKPL---SAMP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 LRQWRgARVAMIFQEPmtalnptrriglQMM-DVIRHH-----QPISRREARAKAIALLEEMQIPDavEVMSRYPFELSG 159
Cdd:COG4619 69 PPEWR-RQVAYVPQEP------------ALWgGTVRDNlpfpfQLRERKFDRERALELLERLGLPP--DILDKPVERLSG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115710 160 GMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:COG4619 134 GERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-252 |
2.57e-35 |
|
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: 128.92 E-value: 2.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAREKQLRQWRGARVAMIF 98
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIePT------SGKVLIDGQDIAAMSRKELRELRRKKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 99 QEpmTALNPTRRI------GLQMmdvirhhQPISRREARAKAIALLEEMQIPDAVEvmsRYPFELSGGMRQRVMIALAFS 172
Cdd:cd03294 109 QS--FALLPHRTVlenvafGLEV-------QGVPRAEREERAAEALELVGLEGWEH---KYPDELSGGMQQRVGLARALA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 173 CEPQLIIADEPTTALDVTV----QLQVLRLlkhkARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHP 248
Cdd:cd03294 177 VDPDILLMDEAFSALDPLIrremQDELLRL----QAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
....
gi 446115710 249 RHPY 252
Cdd:cd03294 253 ANDY 256
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
18-259 |
3.80e-35 |
|
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: 127.80 E-value: 3.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 18 FNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAREKQLRQwrgaRVAM 96
Cdd:cd03295 10 YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIePT------SGEIFIDGEDIREQDPVELRR----KIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 97 IFQEpmTALNPTRRIgLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAvEVMSRYPFELSGGMRQRVMIALAFSCEPQ 176
Cdd:cd03295 80 VIQQ--IGLFPHMTV-EENIALVPKLLKWPKEKIRERADELLALVGLDPA-EFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 177 LIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHPRHPYTIGL 256
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEF 235
|
...
gi 446115710 257 LQC 259
Cdd:cd03295 236 VGA 238
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-233 |
4.43e-34 |
|
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: 124.18 E-value: 4.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVlNAREKQ 85
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDS-----GTIIIDGLKL-TDDKKN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 LRQWRgARVAMIFQ-----EPMTALNptrRIGLQMMDVirhhQPISRREARAKAIALLEEMQIPDaveVMSRYPFELSGG 160
Cdd:cd03262 71 INELR-QKVGMVFQqfnlfPHLTVLE---NITLAPIKV----KGMSKAEAEERALELLEKVGLAD---KADAYPAQLSGG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115710 161 MRQRVMIALAFSCEPQLIIADEPTTALD---VTVQLQVLRLLKHkaraSGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:cd03262 140 QQQRVAIARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAE----EGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
20-257 |
3.90e-33 |
|
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: 122.45 E-value: 3.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRL-LPTgsycvhRGQISLLGEDV--LNAREKQlrqwrgarVAM 96
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLeRPD------SGTILFGGEDAtdVPVQERN--------VGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 97 IFQ-----EPMTALNPTRrIGLQMmdvirhhQPISRR----EARAKAIALLEEMQIpDAVEvmSRYPFELSGGMRQRVMI 167
Cdd:cd03296 79 VFQhyalfRHMTVFDNVA-FGLRV-------KPRSERppeaEIRAKVHELLKLVQL-DWLA--DRYPAQLSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 168 ALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHH 247
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
250
....*....|
gi 446115710 248 PRHPYTIGLL 257
Cdd:cd03296 228 PASPFVYSFL 237
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-253 |
7.84e-33 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 122.59 E-value: 7.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 22 VHALNNVSLQINRSEIVGLVGESGSGKSVTA-MLIMRLLPTGsycvhrgqisllGEDVLNAREKQL--RQWRGARVAMIF 98
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAkMLAGMIEPTS------------GELLIDDHPLHFgdYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 99 QEPMTALNPTRRIGlQMMDV-IRHHQPISRrEARAKAI--ALLEEMQIPDAVevmSRYPFELSGGMRQRVMIALAFSCEP 175
Cdd:PRK15112 94 QDPSTSLNPRQRIS-QILDFpLRLNTDLEP-EQREKQIieTLRQVGLLPDHA---SYYPHMLAPGQKQRLGLARALILRP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115710 176 QLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHPRHPYT 253
Cdd:PRK15112 169 KVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELT 246
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-236 |
1.76e-32 |
|
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: 118.30 E-value: 1.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPGfngdVHALNNVSLQINRSEIVGLVGESGSGKSvTAMLIMrllpTGSYCVHRGQISLLGEDVlnarekq 85
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKS-TLMKIL----SGLYKPDSGEILVDGKEV------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 lrqwrgarvamifqepmtalnptrriglqmmdvirhhQPISRREARAKAIALLeemqipdavevmsrypFELSGGMRQRV 165
Cdd:cd03216 65 -------------------------------------SFASPRDARRAGIAMV----------------YQLSVGERQMV 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115710 166 MIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVI 236
Cdd:cd03216 92 EIARALARNARLLILDEPTAALTPAEVERLFKVIR-RLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-230 |
1.82e-32 |
|
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: 119.95 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTgsycvHRGQISLLGEDVLNAREkqlrqwrgaRVAMIFQ 99
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP-----TSGSIRVFGKPLEKERK---------RIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 E-------PMTALNptrrigLQMMDVIRH--HQPISRREARAKAIALLEEMQIPDavevMSRYPF-ELSGGMRQRVMIAL 169
Cdd:cd03235 76 RrsidrdfPISVRD------VVLMGLYGHkgLFRRLSKADKAKVDEALERVGLSE----LADRQIgELSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115710 170 AFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVM 230
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLR-ELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
21-237 |
2.92e-31 |
|
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: 117.07 E-value: 2.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 21 DVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRL-LPTGsycvhrGQISLLGEDVLNAREKQLRQWRGARVAMIFQ 99
Cdd:TIGR02211 17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLdNPTS------GEVLFNGQSLSKLSSNERAKLRNKKLGFIYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 -----EPMTALNPTrriglqMMDVIRHHQpiSRREARAKAIALLEEMQIPDAvevMSRYPFELSGGMRQRVMIALAFSCE 174
Cdd:TIGR02211 91 fhhllPDFTALENV------AMPLLIGKK--SVKEAKERAYEMLEKVGLEHR---INHRPSELSGGERQRVAIARALVNQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115710 175 PQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLcDSVYVMYAGSVIE 237
Cdd:TIGR02211 160 PSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-222 |
1.08e-30 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 115.42 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFPGfngDVHALNNVSLQINRSEIVGLVGESGSGKS-VTAMLIMRLLPTgsycvhRGQISLLGEDVLNARE 83
Cdd:TIGR02673 1 MIEFHNVSKAYPG---GVAALHDVSLHIRKGEFLFLTGPSGAGKTtLLKLLYGALTPS------RGQVRIAGEDVNRLRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQLRQWRgARVAMIFQEPMTALNPT--RRIGLQMmdvirHHQPISRREARAKAIALLEEMQIPDAvevMSRYPFELSGGM 161
Cdd:TIGR02673 72 RQLPLLR-RRIGVVFQDFRLLPDRTvyENVALPL-----EVRGKKEREIQRRVGAALRQVGLEHK---ADAFPEQLSGGE 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115710 162 RQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQ 222
Cdd:TIGR02673 143 QQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLL-KRLNKRGTTVIVATHDLSLVDR 202
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-230 |
1.13e-30 |
|
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: 114.02 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPGfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQ 85
Cdd:cd03228 1 IEFKNVSFSYPG--RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD-----PTSGEILIDGVDLRDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 LRQwrgaRVAMIFQEP----MTalnptrriglqMMDVIrhhqpisrrearakaialleemqipdavevmsrypfeLSGGM 161
Cdd:cd03228 74 LRK----NIAYVPQDPflfsGT-----------IRENI-------------------------------------LSGGQ 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446115710 162 RQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLkhKARASGTAVLFISHDMAVVsQLCDSVYVM 230
Cdd:cd03228 102 RQRIAIARALLRDPPILILDEATSALDPETEALILEAL--RALAKGKTVIVIAHRLSTI-RDADRIIVL 167
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-244 |
1.73e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 120.52 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFPGfngdVHALNNVSLQINRSEIVGLVGESGSGKSvTAMLIMrllpTGSYCVHRGQISLLGEDVln 80
Cdd:COG3845 1 MMPPALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKS-TLMKIL----YGLYQPDSGEILIDGKPV-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 arekQLRQWRGAR---VAMIFQ-----EPMTAL------NPTRRIGLqmmdvirhhqpISRREARAKAIALLEE--MQI- 143
Cdd:COG3845 70 ----RIRSPRDAIalgIGMVHQhfmlvPNLTVAenivlgLEPTKGGR-----------LDRKAARARIRELSERygLDVd 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 144 PDA-VEvmsrypfELSGGMRQRVMIALAFSCEPQLIIADEPTTALdvTVQ-----LQVLRLLKhkarASGTAVLFISHDM 217
Cdd:COG3845 135 PDAkVE-------DLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeadelFEILRRLA----AEGKSIIFITHKL 201
|
250 260
....*....|....*....|....*..
gi 446115710 218 AVVSQLCDSVYVMYAGSVIESGVTADV 244
Cdd:COG3845 202 REVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-239 |
2.83e-30 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 114.14 E-value: 2.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPgfNGDVHALNNVSLQINRSEIVGLVGESGSGKSVT-AMLIMRLLPTGsycvhrGQISLLGEDVLNAREK 84
Cdd:cd03263 1 LQIRNLTKTYK--KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTlKMLTGELRPTS------GTAYINGYSIRTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRqwrgaRVAMIFQEPMTALNPTRRIGLQMMDVIRHHqpiSRREARAKAIALLEEMQIPDAVEVMSRypfELSGGMRQR 164
Cdd:cd03263 73 ARQ-----SLGYCPQFDALFDELTVREHLRFYARLKGL---PKSEIKEEVELLLRVLGLTDKANKRAR---TLSGGMKRK 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115710 165 VMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARasGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-251 |
3.03e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.45 E-value: 3.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSvTAMLIMRLLPTGSycvhRGQISLLGEDVLN 80
Cdd:PRK10619 1 MSENKLNVIDLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLEKPS----EGSIVVNGQTINL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 ARE----------KQLRQWRgARVAMIFQE-----PMTALNPTRRIGLQMMDvirhhqpISRREARAKAIALLEEMQIPD 145
Cdd:PRK10619 72 VRDkdgqlkvadkNQLRLLR-TRLTMVFQHfnlwsHMTVLENVMEAPIQVLG-------LSKQEARERAVKYLAKVGIDE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 146 AVEvmSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLfISHDMAVVSQLCD 225
Cdd:PRK10619 144 RAQ--GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSS 220
|
250 260
....*....|....*....|....*.
gi 446115710 226 SVYVMYAGSVIESGVTADVIHHPRHP 251
Cdd:PRK10619 221 HVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
20-248 |
3.42e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 114.80 E-value: 3.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVL--NAREKQLRQWRGarvaMI 97
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEE-----ITSGDLIVDGLKVNdpKVDERLIRQEAG----MV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 98 FQE----P-MTALN-----PTRRIGLqmmdvirhhqpiSRREARAKAIALLEEMQIPdavEVMSRYPFELSGGMRQRVMI 167
Cdd:PRK09493 83 FQQfylfPhLTALEnvmfgPLRVRGA------------SKEEAEKQARELLAKVGLA---ERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 168 ALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLfISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHH 247
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
.
gi 446115710 248 P 248
Cdd:PRK09493 227 P 227
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
20-257 |
4.82e-30 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 114.13 E-value: 4.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDV--LNAREKQlrqwrgarVAMI 97
Cdd:TIGR00968 11 GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDS-----GRIRLNGQDAtrVHARDRK--------IGFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 98 FQEPMTALNPTRRIGLQMMDVIRHHQPIsrrEARAKAIALLEEMQIPdavEVMSRYPFELSGGMRQRVMIALAFSCEPQL 177
Cdd:TIGR00968 78 FQHYALFKHLTVRDNIAFGLEIRKHPKA---KIKARVEELLELVQLE---GLGDRYPNQLSGGQRQRVALARALAVEPQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 178 IIADEPTTALDVTVQLQV---LRLLKHKARAsgTAVlFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHPRHPYTI 254
Cdd:TIGR00968 152 LLLDEPFGALDAKVRKELrswLRKLHDEVHV--TTV-FVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVM 228
|
...
gi 446115710 255 GLL 257
Cdd:TIGR00968 229 SFL 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-244 |
5.45e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.98 E-value: 5.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 4 PVLDIQqlHLSFPGFNGdVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNARE 83
Cdd:COG3845 256 VVLEVE--NLSVRDDRG-VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP-----PASGSIRLDGEDITGLSP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQLRQwrgARVAMIFQEPM-TALNPTrriglqmMDVI------RHHQP-------ISRREARAKAIALLEEMQI-PDAVE 148
Cdd:COG3845 328 RERRR---LGVAYIPEDRLgRGLVPD-------MSVAenlilgRYRRPpfsrggfLDRKAIRAFAEELIEEFDVrTPGPD 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 149 VMSRypfELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVY 228
Cdd:COG3845 398 TPAR---SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLL-ELRDAGAAVLLISEDLDEILALSDRIA 473
|
250
....*....|....*.
gi 446115710 229 VMYAGSVIESGVTADV 244
Cdd:COG3845 474 VMYEGRIVGEVPAAEA 489
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
20-250 |
6.29e-30 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 115.57 E-value: 6.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVT-AMLIMRLLPTGsycvhrGQISLLGEDVLnaRE-KQLRQwrgaRVAMI 97
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTiRMLTTLLRPTS------GTARVAGYDVV--REpRKVRR----SIGIV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 98 FQEPMTALNPTRRIGLQMMDVIrhhQPISRREARAKAIALLEEMQIPDAVEVMSRYpfeLSGGMRQRVMIALAFSCEPQL 177
Cdd:TIGR01188 72 PQYASVDEDLTGRENLEMMGRL---YGLPKDEAEERAEELLELFELGEAADRPVGT---YSGGMRRRLDIAASLIHQPDV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 178 IIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG--------VTADVIHHPR 249
Cdd:TIGR01188 146 LFLDEPTTGLDPRTRRAIWDYIR-ALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGtpeelkrrLGKDTLESRP 224
|
.
gi 446115710 250 H 250
Cdd:TIGR01188 225 R 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-216 |
1.07e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 113.80 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 4 PVLDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVlnare 83
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSS-----GEITLDGVPV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 kqlrQWRGARVAMIFQEpmTALNPTRR------IGLQMmdvirhhQPISRREARAKAIALLEEMQIPDAVEvmsRYPFEL 157
Cdd:COG4525 72 ----TGPGADRGVVFQK--DALLPWLNvldnvaFGLRL-------RGVPKAERRARAEELLALVGLADFAR---RRIWQL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115710 158 SGGMRQRVMIALAFSCEPQLIIADEPTTALDVTV--QLQVLrLLKHKARaSGTAVLFISHD 216
Cdd:COG4525 136 SGGMRQRVGIARALAADPRFLLMDEPFGALDALTreQMQEL-LLDVWQR-TGKGVFLITHS 194
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-253 |
2.26e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 112.70 E-value: 2.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 3 QPVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAR 82
Cdd:PRK14247 1 MNKIEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 83 EKQLRQwrgaRVAMIFQEPmtalNPTRRI--------GLQMMDVIRhhqpiSRREARAKAIALLEEMQIPDAVEVMSRYP 154
Cdd:PRK14247 77 VIELRR----RVQMVFQIP----NPIPNLsifenvalGLKLNRLVK-----SKKELQERVRWALEKAQLWDEVKDRLDAP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 155 F-ELSGGMRQRVMIALAFSCEPQLIIADEPTTALDV--TVQLQVLRL-LKHKarasgTAVLFISHDMAVVSQLCDSVYVM 230
Cdd:PRK14247 144 AgKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPenTAKIESLFLeLKKD-----MTIVLVTHFPQQAARISDYVAFL 218
|
250 260
....*....|....*....|...
gi 446115710 231 YAGSVIESGVTADVIHHPRHPYT 253
Cdd:PRK14247 219 YKGQIVEWGPTREVFTNPRHELT 241
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
18-252 |
5.59e-29 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 112.88 E-value: 5.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 18 FNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAREKQLRqwrgarvam 96
Cdd:COG1125 11 YPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIePT------SGRILIDGEDIRDLDPVELR--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 97 ifqepmtalnptRRIGLqmmdVIRH-----HQPI-------------SRREARAKAIALLEEMQIpDAVEVMSRYPFELS 158
Cdd:COG1125 76 ------------RRIGY----VIQQiglfpHMTVaeniatvprllgwDKERIRARVDELLELVGL-DPEEYRDRYPHELS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 159 GGMRQRVMIALAFSCEPQLIIADEPTTALD-VT-VQLQ--VLRLLkhkaRASGTAVLFISHDM--AVvsQLCDSVYVMYA 232
Cdd:COG1125 139 GGQQQRVGVARALAADPPILLMDEPFGALDpITrEQLQdeLLRLQ----RELGKTIVFVTHDIdeAL--KLGDRIAVMRE 212
|
250 260
....*....|....*....|
gi 446115710 233 GSVIESGVTADVIHHPRHPY 252
Cdd:COG1125 213 GRIVQYDTPEEILANPANDF 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-247 |
6.72e-29 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 116.40 E-value: 6.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 2 TQPVLDIQQLHLSFPGfngDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNA 81
Cdd:COG4988 333 GPPSIELEDVSFSYPG---GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP-----PYSGSILINGVDLSDL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 82 REKQLRQwrgaRVAMIFQEP------------MTALNPTRRiglQMMDVIRhhqpisrreaRAKAIALLEEMqiPDAVEV 149
Cdd:COG4988 405 DPASWRR----QIAWVPQNPylfagtirenlrLGRPDASDE---ELEAALE----------AAGLDEFVAAL--PDGLDT 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 150 M-----SRypfeLSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLkhKARASGTAVLFISHDMAVVSQlC 224
Cdd:COG4988 466 PlgeggRG----LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL--RRLAKGRTVILITHRLALLAQ-A 538
|
250 260
....*....|....*....|...
gi 446115710 225 DSVYVMYAGSVIESGVTADVIHH 247
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-248 |
7.31e-29 |
|
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: 110.89 E-value: 7.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPGFNgdvhaLNNVSLQINRSEIVGLVGESGSGKSVTAMLIMrllptGSYCVHRGQISLLGEDVLNAR-EK 84
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIA-----GFIKPDSGKILLNGKDITNLPpEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QlrqwrgaRVAMIFQEpmTALNPTrriglqmMDVIRH------HQPISRREARAKAIALLEEMQIPdavEVMSRYPFELS 158
Cdd:cd03299 71 R-------DISYVPQN--YALFPH-------MTVYKNiayglkKRKVDKKEIERKVLEIAEMLGID---HLLNRKPETLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 159 GGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIES 238
Cdd:cd03299 132 GGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV 211
|
250
....*....|
gi 446115710 239 GVTADVIHHP 248
Cdd:cd03299 212 GKPEEVFKKP 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
12-256 |
7.61e-29 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 111.75 E-value: 7.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 12 HLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNarEKQLRQWR 90
Cdd:TIGR04520 5 NVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLlPT------SGKVTVDGLDTLD--EENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 91 gARVAMIFQepmtalNPTRRI-----------GLQMMDVIRhhqpisrrearakaiallEEMQ--IPDAVEV--MSRY-- 153
Cdd:TIGR04520 77 -KKVGMVFQ------NPDNQFvgatveddvafGLENLGVPR------------------EEMRkrVDEALKLvgMEDFrd 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 154 --PFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDM--AVvsqLCDSVYV 229
Cdd:TIGR04520 132 rePHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMeeAV---LADRVIV 208
|
250 260
....*....|....*....|....*..
gi 446115710 230 MYAGSVIESGVTADVIHHPRHPYTIGL 256
Cdd:TIGR04520 209 MNKGKIVAEGTPREIFSQVELLKEIGL 235
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-239 |
9.03e-29 |
|
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: 110.54 E-value: 9.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVT-AMLIMRLLPTGsycvhrGQISLLGEDVLnareKQLRQWRgARVAMIF 98
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTiKMLTTLLKPTS------GRATVAGHDVV----REPREVR-RRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 99 QEPMTALNPTRRIGLQMMDVIrhhQPISRREARAKAIALLEEMQIPDAVEVMSRYpfeLSGGMRQRVMIALAFSCEPQLI 178
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARL---YGVPGAERRERIDELLDFVGLLEAADRLVKT---YSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115710 179 IADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-245 |
9.96e-29 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 115.67 E-value: 9.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLP--TGSYCVhrgqisLLGEDVLNAREKQ-LRQWRGAR-VA 95
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEptSGEVNV------RVGDEWVDMTKPGpDGRGRAKRyIG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 96 MIFQEpmTALNPTRRIGLQMMDVIRHHQPisRREARAKAIALLEEMQIPD--AVEVMSRYPFELSGGMRQRVMIALAFSC 173
Cdd:TIGR03269 369 ILHQE--YDLYPHRTVLDNLTEAIGLELP--DELARMKAVITLKMVGFDEekAEEILDKYPDELSEGERHRVALAQVLIK 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115710 174 EPQLIIADEPTTALDVTVQLQVLRLLkHKARAS-GTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVI 245
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVDVTHSI-LKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-234 |
2.15e-28 |
|
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: 109.45 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTqPVLDIQQLHLSFP--GFNG-DVHALNNVSLQINRSEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGE- 76
Cdd:COG4778 1 MT-TLLEVENLSKTFTlhLQGGkRLPVLDGVSFSVAAGECVALTGPSGAGKST----LLKCI-YGNYLPDSGSILVRHDg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 77 ---DVLNAREKQlrqwrgarvamifqepMTALnptRR--IG-----LQMM------DVIRH---HQPISRREARAKAIAL 137
Cdd:COG4778 75 gwvDLAQASPRE----------------ILAL---RRrtIGyvsqfLRVIprvsalDVVAEpllERGVDREEARARAREL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 138 LEEMQIPDavEVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDM 217
Cdd:COG4778 136 LARLNLPE--RLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELI-EEAKARGTAIIGIFHDE 212
|
250
....*....|....*..
gi 446115710 218 AVVSQLCDSVYVMYAGS 234
Cdd:COG4778 213 EVREAVADRVVDVTPFS 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-248 |
2.20e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 112.48 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDV--LNARE 83
Cdd:PRK10851 3 IEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTS-----GHIRFHGTDVsrLHARD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQlrqwrgarVAMIFQ-----EPMTALNPTRrIGLQMMDviRHHQPiSRREARAKAIALLEEMQIPDAVEvmsRYPFELS 158
Cdd:PRK10851 74 RK--------VGFVFQhyalfRHMTVFDNIA-FGLTVLP--RRERP-NAAAIKAKVTQLLEMVQLAHLAD---RYPAQLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 159 GGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIES 238
Cdd:PRK10851 139 GGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQA 218
|
250
....*....|
gi 446115710 239 GVTADVIHHP 248
Cdd:PRK10851 219 GTPDQVWREP 228
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
18-248 |
1.54e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 107.79 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 18 FNGDVHALNNVSLQINRSEIVGLVGESGSGKSvTAMLIMRLLPTGSycvhRGQISLLGEDV-----LNAREKQ-LRQwrg 91
Cdd:COG4161 11 FYGSHQALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLETPD----SGQLNIAGHQFdfsqkPSEKAIRlLRQ--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 92 aRVAMIFQE----P-MTALN-----PTRRIGLqmmdvirhhqpiSRREARAKAIALLEEMQIPDAVEvmsRYPFELSGGM 161
Cdd:COG4161 83 -KVGMVFQQynlwPhLTVMEnlieaPCKVLGL------------SKEQAREKAMKLLARLRLTDKAD---RFPLHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 162 RQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLfISHDMAVVSQLCDSVYVMYAGSVIESGvT 241
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVI-VTHEVEFARKVASQVVYMEKGRIIEQG-D 224
|
....*..
gi 446115710 242 ADVIHHP 248
Cdd:COG4161 225 ASHFTQP 231
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-216 |
1.73e-27 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 110.58 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAREKQLRQWRGARVAMIF 98
Cdd:COG4175 38 GQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIePT------AGEVLIDGEDITKLSKKELRELRRKKMSMVF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 99 QEpmTALNPTRRI------GLQMmdvirhhQPISRREARAKAIALLE-------EmqipdavevmSRYPFELSGGMRQRV 165
Cdd:COG4175 112 QH--FALLPHRTVlenvafGLEI-------QGVPKAERRERAREALElvglagwE----------DSYPDELSGGMQQRV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446115710 166 MIALAFSCEPQLIIADEPTTALD--VTVQLQ--VLRLLK--HKarasgTaVLFISHD 216
Cdd:COG4175 173 GLARALATDPDILLMDEAFSALDplIRREMQdeLLELQAklKK-----T-IVFITHD 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-248 |
2.19e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 107.41 E-value: 2.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 8 IQQLHLSFpgFNGDVHALNNVSLQINRSEIVGLVGESGSGKSvTAMLIMRLLPTGSycvhRGQISLLGEDV---LNAREK 84
Cdd:PRK11124 3 IQLNGINC--FYGAHQALFDITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLEMPR----SGTLNIAGNHFdfsKTPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRQWRgARVAMIFQE----P-MTALN-----PTRRIGLqmmdvirhhqpiSRREARAKAIALLEEMQIPDAVEvmsRYP 154
Cdd:PRK11124 76 AIRELR-RNVGMVFQQynlwPhLTVQQnlieaPCRVLGL------------SKDQALARAEKLLERLRLKPYAD---RFP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 155 FELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLfISHDMAVVSQLCDSVYVMYAGS 234
Cdd:PRK11124 140 LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVI-VTHEVEVARKTASRVVYMENGH 218
|
250
....*....|....
gi 446115710 235 VIESGvTADVIHHP 248
Cdd:PRK11124 219 IVEQG-DASCFTQP 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-248 |
3.07e-27 |
|
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: 106.55 E-value: 3.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLImrllpTGSYCVHRGQISLLGEDVLN--AREKQlrqwrgarVAMI 97
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLI-----AGFETPTSGEILLDGKDITNlpPHKRP--------VNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 98 FQEpmTALNP----TRRI--GLQMmdvirhhQPISRREARAKAIALLEEMQIPdavEVMSRYPFELSGGMRQRVMIALAF 171
Cdd:cd03300 78 FQN--YALFPhltvFENIafGLRL-------KKLPKAEIKERVAEALDLVQLE---GYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446115710 172 SCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHP 248
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-235 |
3.40e-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: 105.21 E-value: 3.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 4 PVLDIQQLHLSfpgfngdvHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVlnaRE 83
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP-----PASGEITLDGKPV---TR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQLRQWRGARVAMIFQEpmtalnptrriglqmmdviRHHQpisrrearakaiALLEEMQIPDAVeVMSRYpfeLSGGMRQ 163
Cdd:cd03215 67 RSPRDAIRAGIAYVPED-------------------RKRE------------GLVLDLSVAENI-ALSSL---LSGGNQQ 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115710 164 RVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLI-RELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
20-227 |
3.93e-27 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 105.78 E-value: 3.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSvTAMLIMRLLPTGSycvhRGQISLLGEDVLNAREKQLRQWRGARVAMIFQ 99
Cdd:TIGR03608 9 GDKVILDDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLLEKFD----SGQVYLNGQETPPLNSKKASKFRREKLGYLFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 EpmTALNPTRRIgLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEvmsRYPFELSGGMRQRVMIALAFSCEPQLII 179
Cdd:TIGR03608 84 N--FALIENETV-EENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLK---QKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446115710 180 ADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQlCDSV 227
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLL-ELNDEGKTIIIVTHDPEVAKQ-ADRV 203
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-237 |
7.19e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.84 E-value: 7.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 16 PGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVtamlIMR-----LLPTgsycvhRGQISLLGEDV-LNAREKQLRQW 89
Cdd:PRK13641 14 PGTPMEKKGLDNISFELEEGSFVALVGHTGSGKST----LMQhfnalLKPS------SGTITIAGYHItPETGNKNLKKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 90 RgARVAMIFQEPMTALnpTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDavEVMSRYPFELSGGMRQRVMIAL 169
Cdd:PRK13641 84 R-KKVSLVFQFPEAQL--FENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSE--DLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115710 170 AFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARAsGTAVLFISHDMAVVSQLCDSVYVMYAGSVIE 237
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-244 |
1.02e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 106.67 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 24 ALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKqLRQWRgARVAMIFQEPM- 102
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTS-----GKIIIDGVDITDKKVK-LSDIR-KKVGLVFQYPEy 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 103 ----------TALNPtRRIGLQmmdvirhHQPISRREARAKAIALLEEMQIPDavevmsRYPFELSGGMRQRVMIALAFS 172
Cdd:PRK13637 95 qlfeetiekdIAFGP-INLGLS-------EEEIENRVKRAMNIVGLDYEDYKD------KSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115710 173 CEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADV 244
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-239 |
1.22e-26 |
|
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: 110.31 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPGfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVlnaREK 84
Cdd:COG2274 474 IELENVSFRYPG--DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYePT------SGRILIDGIDL---RQI 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRQWRgARVAMIFQEPMTaLNPTRRiglqmmDVIRHHQP-ISRREAR--AKAIALLEE-MQIPDAVE-VMSrypfE--- 156
Cdd:COG2274 543 DPASLR-RQIGVVLQDVFL-FSGTIR------ENITLGDPdATDEEIIeaARLAGLHDFiEALPMGYDtVVG----Eggs 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 157 -LSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLkhKARASGTAVLFISHDMAVVsQLCDSVYVMYAGSV 235
Cdd:COG2274 611 nLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL--RRLLKGRTVIIIAHRLSTI-RLADRIIVLDKGRI 687
|
....
gi 446115710 236 IESG 239
Cdd:COG2274 688 VEDG 691
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-272 |
1.46e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 105.24 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 4 PVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTamliMRLLpTGSYCVHRGQISLLGedvlnare 83
Cdd:PRK13548 1 AMLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTL----LRAL-SGELSPDSGEVRLNG-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQLRQWRGA----RVAMIFQE-----PMTALnptrriglqmmDVI---RHHQPISRREARAkaiALLEEMQIPDAVEVMS 151
Cdd:PRK13548 64 RPLADWSPAelarRRAVLPQHsslsfPFTVE-----------EVVamgRAPHGLSRAEDDA---LVAAALAQVDLAHLAG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 152 RYPFELSGGMRQRVMIA--LA----FSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCD 225
Cdd:PRK13548 130 RDYPQLSGGEQQRVQLArvLAqlwePDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYAD 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446115710 226 SVYVMYAGSVIESGVTADVIHHP--RHPYTIGLL-QCAPEHGVPrQLLPA 272
Cdd:PRK13548 210 RIVLLHQGRLVADGTPAEVLTPEtlRRVYGADVLvQPHPETGAP-LVLPR 258
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-239 |
2.34e-26 |
|
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: 103.99 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLnarekq 85
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDA-----GFATVDGFDVV------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 lRQWRGARVAMIFQEPMTALNPtRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPdavEVMSRYPFELSGGMRQRV 165
Cdd:cd03266 71 -KEPAEARRRLGFVSDSTGLYD-RLTARENLEYFAGLYGLKGDELTARLEELADRLGME---ELLDRRVGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115710 166 MIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKaRASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-239 |
3.06e-26 |
|
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: 103.45 E-value: 3.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQ 85
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDS-----GEITFDGKSYQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 lrqwrgARVAMIFQEP-----MTALNPTRRIGLQMMdvirhhqpisRREARAKAIALLEEMQIPDAVEVMSrypfeLSGG 160
Cdd:cd03268 72 ------RRIGALIEAPgfypnLTARENLRLLARLLG----------IRKKRIDEVLDVVGLKDSAKKKVKG-----FSLG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446115710 161 MRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03268 131 MKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELI-LSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-220 |
3.26e-26 |
|
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: 103.26 E-value: 3.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPGfngDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRL-LPTgsycvhRGQISLLGEDVLNAREK 84
Cdd:cd03292 1 IEFINVTKTYPN---GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPT------SGTIRVNGQDVSDLRGR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRQWRgARVAMIFQEpmTALNPTRRIGLQM---MDVIRHhqpiSRREARAKAIALLEEMQIPDAVEVMsryPFELSGGM 161
Cdd:cd03292 72 AIPYLR-RKIGVVFQD--FRLLPDRNVYENVafaLEVTGV----PPREIRKRVPAALELVGLSHKHRAL---PAELSGGE 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446115710 162 RQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVV 220
Cdd:cd03292 142 QQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLK-KINKAGTTVVVATHAKELV 199
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-253 |
4.19e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 104.79 E-value: 4.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 17 GFNGDVhALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAREkqLRQWRgARVAM 96
Cdd:PRK14271 30 GFAGKT-VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRD--VLEFR-RRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 97 IFQEPmtalNPtrrIGLQMMDVI----RHHQPISRREARAKAIALLEEMQIPDAV-EVMSRYPFELSGGMRQRVMIALAF 171
Cdd:PRK14271 106 LFQRP----NP---FPMSIMDNVlagvRAHKLVPRKEFRGVAQARLTEVGLWDAVkDRLSDSPFRLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 172 SCEPQLIIADEPTTALDVTVQLQVLRLLkhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHPRHP 251
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFI--RSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
..
gi 446115710 252 YT 253
Cdd:PRK14271 257 ET 258
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
20-239 |
4.75e-26 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 102.74 E-value: 4.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQ---LRQWRGarvam 96
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS-----GEVLFDGKPLDIAARNRigyLPEERG----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 97 ifqepmtaLNPTRRIGLQMMDVIRHHQpISRREARAKAIALLEEMQIPDAVEVMSRypfELSGGMRQRVMIALAFSCEPQ 176
Cdd:cd03269 81 --------LYPKMKVIDQLVYLAQLKG-LKKEEARRRIDEWLERLELSEYANKRVE---ELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115710 177 LIIADEPTTALD-VTVQL--QVLRLLkhkaRASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03269 149 LLILDEPFSGLDpVNVELlkDVIREL----ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-252 |
5.22e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 106.66 E-value: 5.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 24 ALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAREKQLRQWRGARVAMIFQE-- 100
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePT------RGQVLIDGVDIAKISDAELREVRRKKIAMVFQSfa 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 101 ---PMTALNPTRrIGLQMMDvirhhqpISRREARAKAIALLEEMQIPDAVEvmsRYPFELSGGMRQRVMIALAFSCEPQL 177
Cdd:PRK10070 117 lmpHMTVLDNTA-FGMELAG-------INAEERREKALDALRQVGLENYAH---SYPDELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115710 178 IIADEPTTALDVTVQLQVL-RLLKHKARASGTaVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHPRHPY 252
Cdd:PRK10070 186 LLMDEAFSALDPLIRTEMQdELVKLQAKHQRT-IVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
24-256 |
5.44e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 104.72 E-value: 5.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 24 ALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLlGEDVLNA--REKQLRQWRgARVAMIFQE 100
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqPT------SGTVTI-GERVITAgkKNKKLKPLR-KKVGIVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 101 PMTAL---NPTRRIGLQMMDVirhhqPISRREARAKAIALLEEMQIPDavEVMSRYPFELSGGMRQRVMIALAFSCEPQL 177
Cdd:PRK13634 94 PEHQLfeeTVEKDICFGPMNF-----GVSEEDAKQKAREMIELVGLPE--ELLARSPFELSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446115710 178 IIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHPRHPYTIGL 256
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEAIGL 245
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-250 |
9.19e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 105.16 E-value: 9.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTamliMRLL-----PTGsycvhrGQISLLGEDVLN 80
Cdd:COG3839 4 LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRMIagledPTS------GEILIGGRDVTD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 AREKQlrqwRGarVAMIFQEPmtALNPT---RR---IGLQMMDVirhhqpiSRREARAKAIALLEEMQIPDaveVMSRYP 154
Cdd:COG3839 70 LPPKD----RN--IAMVFQSY--ALYPHmtvYEniaFPLKLRKV-------PKAEIDRRVREAAELLGLED---LLDRKP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 155 FELSGGMRQRVMIALAFSCEPQLIIADEPTTALD----VTVQLQVLRLLkhkaRASGTAVLFISHD----MAvvsqLCDS 226
Cdd:COG3839 132 KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLH----RRLGTTTIYVTHDqveaMT----LADR 203
|
250 260
....*....|....*....|....
gi 446115710 227 VYVMYAGSVIESGVTADVIHHPRH 250
Cdd:COG3839 204 IAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
10-248 |
9.92e-26 |
|
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: 105.18 E-value: 9.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 10 QLHLSFPGFngdvhALNnVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTgsycvHRGQISLLGEDVLNAREkqlRQW 89
Cdd:COG4148 6 DFRLRRGGF-----TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERP-----DSGRIRLGGEVLQDSAR---GIF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 90 RGA---RVAMIFQEPmtALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEemqIPDaveVMSRYPFELSGGMRQRVM 166
Cdd:COG4148 72 LPPhrrRIGYVFQEA--RLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLG---IGH---LLDRRPATLSGGERQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 167 IALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIH 246
Cdd:COG4148 144 IGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
..
gi 446115710 247 HP 248
Cdd:COG4148 224 RP 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
20-239 |
1.97e-25 |
|
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: 101.18 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRL-LPTGsycvhrGQISLLGEDVLNAREKQlrqwRGarVAMIF 98
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLeEPTS------GRIYIGGRDVTDLPPKD----RD--IAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 99 QEpmTALNPTRRI------GLQMmdvirHHQPISRREARAKAIAllEEMQIPdavEVMSRYPFELSGGMRQRVMIALAFS 172
Cdd:cd03301 79 QN--YALYPHMTVydniafGLKL-----RKVPKDEIDERVREVA--ELLQIE---HLLDRKPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446115710 173 CEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-256 |
2.62e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 102.40 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQqlHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLN 80
Cdd:PRK13635 1 MKEEIIRVE--HISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 AREKqlrqwrgarVAMIFQepmtalNPTRR-IGLQMMDVIR---HHQPISRREARAKAIALLEE--MQipdavEVMSRYP 154
Cdd:PRK13635 79 VRRQ---------VGMVFQ------NPDNQfVGATVQDDVAfglENIGVPREEMVERVDQALRQvgME-----DFLNREP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 155 FELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQlCDSVYVMYAGS 234
Cdd:PRK13635 139 HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGE 217
|
250 260
....*....|....*....|..
gi 446115710 235 VIESGVTADVIHHPRHPYTIGL 256
Cdd:PRK13635 218 ILEEGTPEEIFKSGHMLQEIGL 239
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
24-239 |
2.87e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.55 E-value: 2.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 24 ALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLN-AREKQLRQWRgARVAMIFQEP 101
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLkPT------TGTVTVDDITITHkTKDKYIRPVR-KRIGMVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 102 MTAL---NPTRRIGLQ----MMDVirhhqpisrREARAKAIALLEEMQIPDavEVMSRYPFELSGGMRQRVMIALAFSCE 174
Cdd:PRK13646 95 ESQLfedTVEREIIFGpknfKMNL---------DEVKNYAHRLLMDLGFSR--DVMSQSPFQMSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115710 175 PQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-239 |
2.94e-25 |
|
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: 100.73 E-value: 2.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPGfngdVHALNNVSLQINRSeIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKq 85
Cdd:cd03264 1 LQLENLTKRYGK----KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSS-----GTIRIDGQDVLKQPQK- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 LRQwrgaRVAMIFQEPMTALNPTRRIGLQMMDVIRHhqpISRREARAKAIALLEEMQIPDaveVMSRYPFELSGGMRQRV 165
Cdd:cd03264 70 LRR----RIGYLPQEFGVYPNFTVREFLDYIAWLKG---IPSKEVKARVDEVLELVNLGD---RAKKKIGSLSGGMRRRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115710 166 MIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHkaRASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSE--LGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-239 |
3.47e-25 |
|
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: 105.62 E-value: 3.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 2 TQPVLDIQQLHLSFPGfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNA 81
Cdd:COG4987 330 GGPSLELEDVSFRYPG--AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD-----PQSGSITLGGVDLRDL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 82 REKQLRQwrgaRVAMIFQEP----MTalnptrriglqMMDVIRhhqpISRREA-RAKAIALLEEMQIPDAVEvmsRYP-- 154
Cdd:COG4987 403 DEDDLRR----RIAVVPQRPhlfdTT-----------LRENLR----LARPDAtDEELWAALERVGLGDWLA---ALPdg 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 155 ---------FELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLkhKARASGTAVLFISHDMAVVSQlCD 225
Cdd:COG4987 461 ldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL--LEALAGRTVLLITHRLAGLER-MD 537
|
250
....*....|....
gi 446115710 226 SVYVMYAGSVIESG 239
Cdd:COG4987 538 RILVLEDGRIVEQG 551
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-236 |
4.73e-25 |
|
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: 100.02 E-value: 4.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 12 HLSFpGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTgsycvHRGQISLLGEDVLNARekqlrqwRG 91
Cdd:cd03226 4 NISF-SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE-----SSGSILLNGKPIKAKE-------RR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 92 ARVAMIFQEPMTAL---NPTRRIGLQMMDvirhhqpISRREARAKAIalLEEMQIPDAVEvmsRYPFELSGGMRQRVMIA 168
Cdd:cd03226 71 KSIGYVMQDVDYQLftdSVREELLLGLKE-------LDAGNEQAETV--LKDLDLYALKE---RHPLSLSGGQKQRLAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115710 169 LAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARAsGTAVLFISHDMAVVSQLCDSVYVMYAGSVI 236
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
18-253 |
5.80e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 100.98 E-value: 5.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 18 FNGDVhALNNVSLQINRSEIVGLVGESGSGKSvTAMLIMRLL--PTGSYcVHRGQISLLGEDVLNAREKQLRQWRgARVA 95
Cdd:PRK11264 13 FHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLeqPEAGT-IRVGDITIDTARSLSQQKGLIRQLR-QHVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 96 MIFQEpmTALNPTRRIglqmMDVIRHHQPISRREARAKAIALLEEMQIPDAVE-VMSRYPFELSGGMRQRVMIALAFSCE 174
Cdd:PRK11264 89 FVFQN--FNLFPHRTV----LENIIEGPVIVKGEPKEEATARARELLAKVGLAgKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446115710 175 PQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLfISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHPRHPYT 253
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRT 240
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-249 |
8.11e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.38 E-value: 8.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 4 PVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNARE 83
Cdd:PRK09536 2 PMIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA-----GTVLVAGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQLrqwrGARVAMIFQEPMTALNPTRRiglQMMDVIRH-HQPISRREARAKAIALLEEMQIPDAVEVMSRYPFELSGGMR 162
Cdd:PRK09536 73 RAA----SRRVASVPQDTSLSFEFDVR---QVVEMGRTpHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 163 QRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFIsHDMAVVSQLCDSVYVMYAGSVIESGVTA 242
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPA 224
|
....*..
gi 446115710 243 DVIHHPR 249
Cdd:PRK09536 225 DVLTADT 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-255 |
9.43e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 104.24 E-value: 9.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFPGfngdVHALNNVSLQINRSEIVGLVGESGSGKSVtamlIMRLL----PTGSYcvhRGQISLLGE 76
Cdd:PRK13549 1 MMEYLLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKST----LMKVLsgvyPHGTY---EGEIIFEGE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 77 DVlnaREKQLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQ--IPDAVEVMsryp 154
Cdd:PRK13549 70 EL---QASNIRDTERAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKldINPATPVG---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 155 fELSGGMRQRVMIALAFSCEPQLIIADEPTTAL---DVTVQLQVLRLLKHKarasGTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:PRK13549 143 -NLGLGQQQLVEIAKALNKQARLLILDEPTASLtesETAVLLDIIRDLKAH----GIACIYISHKLNEVKAISDTICVIR 217
|
250 260 270
....*....|....*....|....*....|....*....
gi 446115710 232 AGSVI----ESGVTADVI-----------HHPRHPYTIG 255
Cdd:PRK13549 218 DGRHIgtrpAAGMTEDDIitmmvgreltaLYPREPHTIG 256
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-216 |
1.10e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 99.85 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 2 TQPVLDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSvTAMLIMRLLPTGSycvhRGQISLLGEDVLNA 81
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKS-TLLAILAGLDDGS----SGEVSLVGQPLHQM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 82 REKQLRQWRGARVAMIFQEPMtaLNPTRRI--GLQMMDVIRHHqpiSRREARAKAIALLEEMQIPDAVEVMsryPFELSG 159
Cdd:PRK10584 78 DEEARAKLRAKHVGFVFQSFM--LIPTLNAleNVELPALLRGE---SSRQSRNGAKALLEQLGLGKRLDHL---PAQLSG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446115710 160 GMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHD 216
Cdd:PRK10584 150 GEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-239 |
1.15e-24 |
|
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: 99.71 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 21 DVHALNNVSLQINRSEIVGLVGESGSGKSVT-AMLIMRLLPTGsycvhrGQISLLGEDVLNAREKQLRqwrgaRVAMIF- 98
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTlKILSGLLQPTS------GEVRVAGLVPWKRRKKFLR-----RIGVVFg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 99 QEPMTALNPTRRIGLQMMdviRHHQPISRREARAKAIALLEEMQIPDAVEVMSRypfELSGGMRQRVMIALAFSCEPQLI 178
Cdd:cd03267 102 QKTQLWWDLPVIDSFYLL---AAIYDLPPARFKKRLDELSELLDLEELLDTPVR---QLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115710 179 IADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-222 |
1.28e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 104.42 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTqPVLDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSvTAMLIMRLL--PT-GSYCVhrgqislLGED 77
Cdd:PRK10535 1 MT-ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS-TLMNILGCLdkPTsGTYRV-------AGQD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 78 VLNAREKQLRQWRGARVAMIFQE-----PMTALnptrriglQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVmsr 152
Cdd:PRK10535 72 VATLDADALAQLRREHFGFIFQRyhllsHLTAA--------QNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEY--- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 153 YPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQ 222
Cdd:PRK10535 141 QPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAIL-HQLRDRGHTVIIVTHDPQVAAQ 209
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-253 |
2.00e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 99.73 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 2 TQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNA 81
Cdd:COG1117 8 LEPKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIYDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 82 REK--QLRqwrgARVAMIFQEPmtalNP-TRRI------GLqmmdviRHHQPISRREARAKAIALLEEMQIPDavEV--- 149
Cdd:COG1117 84 DVDvvELR----RRVGMVFQKP----NPfPKSIydnvayGL------RLHGIKSKSELDEIVEESLRKAALWD--EVkdr 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 150 MSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQV---LRLLKHKarasgTAVLFISHDMAVVSQLCDS 226
Cdd:COG1117 148 LKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIeelILELKKD-----YTIVIVTHNMQQAARVSDY 222
|
250 260
....*....|....*....|....*..
gi 446115710 227 VYVMYAGSVIESGVTADVIHHPRHPYT 253
Cdd:COG1117 223 TAFFYLGELVEFGPTEQIFTNPKDKRT 249
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-239 |
3.46e-24 |
|
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: 98.14 E-value: 3.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 27 NVSLQINrSEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGEdVLNAREKQLR---QWRgaRVAMIFQEpmT 103
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKST----LLRCI-AGLEKPDGGTIVLNGT-VLFDSRKKINlppQQR--KIGLVFQQ--Y 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 104 ALNPTRRIGLQMMDVIRHHqpiSRREARAKAIALLEEMQIPdavEVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEP 183
Cdd:cd03297 85 ALFPHLNVRENLAFGLKRK---RNREDRISVDELLDLLGLD---HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446115710 184 TTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
236-300 |
4.41e-24 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 93.23 E-value: 4.41e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115710 236 IESGVTADVIHHPRHPYTIGLLQCAPEHGVPRQLLPAIPGTVPNLTHLPEGCAFRDRCYAAGAQC 300
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-253 |
4.67e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 98.76 E-value: 4.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAREKQLRQWRgaRVAMIFQ 99
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEVRR--EVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 EPmtalNP--------TRRIGLQMMDVIRHHQPISRR-EARAKAIALLEEMQipdavEVMSRYPFELSGGMRQRVMIALA 170
Cdd:PRK14267 93 YP----NPfphltiydNVAIGVKLNGLVKSKKELDERvEWALKKAALWDEVK-----DRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 171 FSCEPQLIIADEPTTALDVTVQLQVLRLLkHKARASGTAVLfISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHPRH 250
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELL-FELKKEYTIVL-VTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
...
gi 446115710 251 PYT 253
Cdd:PRK14267 242 ELT 244
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-239 |
4.69e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 98.91 E-value: 4.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 3 QPVLDIQQLHLSFPgfNGDVHALNNVSLQINRSEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGEDVLNAR 82
Cdd:PRK13632 5 SVMIKVENVSFSYP--NSENNALKNVSFEINEGEYVAILGHNGSGKST----ISKIL-TGLLKPQSGEIKIDGITISKEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 83 EKQLRQwrgaRVAMIFQepmtalNPTRR-IGLQMMDVIR---HHQPISRREARAKAIALLEEMQIPDAVEvmsRYPFELS 158
Cdd:PRK13632 78 LKEIRK----KIGIIFQ------NPDNQfIGATVEDDIAfglENKKVPPKKMKDIIDDLAKKVGMEDYLD---KEPQNLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 159 GGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSqLCDSVYVMYAGSVIES 238
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQ 223
|
.
gi 446115710 239 G 239
Cdd:PRK13632 224 G 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-239 |
7.09e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 101.78 E-value: 7.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 12 HLSFpGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGEDVlnaREKQLRQWRg 91
Cdd:COG1132 344 NVSF-SYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF-----YDPTSGRILIDGVDI---RDLTLESLR- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 92 ARVAMIFQEP----MTAlnptrriglqmMDVIRhhqpISRREA------RAKAIALLEE--MQIPDAVE-------VMsr 152
Cdd:COG1132 414 RQIGVVPQDTflfsGTI-----------RENIR----YGRPDAtdeeveEAAKAAQAHEfiEALPDGYDtvvgergVN-- 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 153 ypfeLSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARasGTAVLFISHDMAVVsQLCDSVYVMYA 232
Cdd:COG1132 477 ----LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTI-RNADRILVLDD 549
|
....*..
gi 446115710 233 GSVIESG 239
Cdd:COG1132 550 GRIVEQG 556
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-272 |
8.06e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 97.88 E-value: 8.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSvTamlIMRLLpTGSYCVHRGQISLLGedvlnareKQ 85
Cdd:COG4559 2 LEAENLSVRL----GGRTLLDDVSLTLRPGELTAIIGPNGAGKS-T---LLKLL-TGELTPSSGEVRLNG--------RP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 LRQWRGARVAMI-----------FqePMTALnptrriglqmmDVI---RHHQPISRREARAKAIALLEEMQIPDAVEvmS 151
Cdd:COG4559 65 LAAWSPWELARRravlpqhsslaF--PFTVE-----------EVValgRAPHGSSAAQDRQIVREALALVGLAHLAG--R 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 152 RYPfELSGGMRQRVMIA--LA-----FSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARAsGTAVLFISHDMAVVSQLC 224
Cdd:COG4559 130 SYQ-TLSGGEQQRVQLArvLAqlwepVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYA 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446115710 225 DSVYVMYAGSVIESGVTADVI--HHPRHPYTIGLLQCA-PEHGVPrQLLPA 272
Cdd:COG4559 208 DRILLLHQGRLVAQGTPEEVLtdELLERVYGADLRVLAhPEGGCP-QVLPR 257
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-242 |
1.19e-23 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 100.85 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 2 TQPVLDIQQLHLSFPGfngdVHALNNVSLQINRSEIVGLVGESGSGKSvTAMLIMrllpTGSYCVHRGQISLLGEDVLNA 81
Cdd:PRK10762 1 MQALLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKS-TMMKVL----TGIYTRDAGSILYLGKEVTFN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 82 REKQLRQwrgARVAMIFQEpmtaLN----------------PTRRIGLqmmdvirhhqpISRREARAKAIALLEEMQIPD 145
Cdd:PRK10762 72 GPKSSQE---AGIGIIHQE----LNlipqltiaeniflgreFVNRFGR-----------IDWKKMYAEADKLLARLNLRF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 146 AvevmSRYPF-ELSGGMRQRVMIALAFSCEPQLIIADEPTTAL-DV-TVQL-QVLRLLkhkaRASGTAVLFISHDMAVVS 221
Cdd:PRK10762 134 S----SDKLVgELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTeTESLfRVIREL----KSQGRGIVYISHRLKEIF 205
|
250 260
....*....|....*....|..
gi 446115710 222 QLCDSVYVMYAGSVI-ESGVTA 242
Cdd:PRK10762 206 EICDDVTVFRDGQFIaEREVAD 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
24-247 |
1.22e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 97.89 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 24 ALNNVSLQINRSEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGEDVLN-AREKQLRQWRgARVAMIFQEPM 102
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKST----IMQLL-NGLHVPTQGSVRVDDTLITStSKNKDIKQIR-KKVGLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 103 TAL-NPTrriglQMMDVIRHHQP--ISRREARAKAIALLEEMQIPDavEVMSRYPFELSGGMRQRVMIALAFSCEPQLII 179
Cdd:PRK13649 96 SQLfEET-----VLKDVAFGPQNfgVSQEEAEALAREKLALVGISE--SLFEKNPFELSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115710 180 ADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHH 247
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFK-KLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-256 |
1.46e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.86 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFPGfNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAREK 84
Cdd:PRK13642 4 ILEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 qlrqwrgarVAMIFQEPmtalnPTRRIGLQMMDVI---RHHQPISRREARAKaiaLLEEMQIPDAVEVMSRYPFELSGGM 161
Cdd:PRK13642 83 ---------IGMVFQNP-----DNQFVGATVEDDVafgMENQGIPREEMIKR---VDEALLAVNMLDFKTREPARLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 162 RQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESGVT 241
Cdd:PRK13642 146 KQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAP 224
|
250
....*....|....*
gi 446115710 242 ADVIHHPRHPYTIGL 256
Cdd:PRK13642 225 SELFATSEDMVEIGL 239
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-239 |
1.68e-23 |
|
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: 96.53 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 17 GFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGEDVLNAREKQLRQwrgaRVAM 96
Cdd:cd03254 11 SYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRF-----YDPQKGQILIDGIDIRDISRKSLRS----MIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 97 IFQEPmTALNPTrriglqMMDVIRHHQPISRRE---ARAKAIALLEE-MQIPDAVE-VMSRYPFELSGGMRQRVMIALAF 171
Cdd:cd03254 82 VLQDT-FLFSGT------IMENIRLGRPNATDEeviEAAKEAGAHDFiMKLPNGYDtVLGENGGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115710 172 SCEPQLIIADEPTTALDV----TVQLQVLRLLKhkarasGTAVLFISHDMAVVsQLCDSVYVMYAGSVIESG 239
Cdd:cd03254 155 LRDPKILILDEATSNIDTetekLIQEALEKLMK------GRTSIIIAHRLSTI-KNADKILVLDDGKIIEEG 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-253 |
2.86e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.38 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLN 80
Cdd:PRK14239 1 MTEPILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 AREK--QLRQwrgaRVAMIFQEPmtalNP-------TRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQipdavEVMS 151
Cdd:PRK14239 77 PRTDtvDLRK----EIGMVFQQP----NPfpmsiyeNVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVK-----DRLH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 152 RYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQV---LRLLKHKarasgTAVLFISHDMAVVSQLCDSVY 228
Cdd:PRK14239 144 DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIeetLLGLKDD-----YTMLLVTRSMQQASRISDRTG 218
|
250 260
....*....|....*....|....*
gi 446115710 229 VMYAGSVIESGVTADVIHHPRHPYT 253
Cdd:PRK14239 219 FFLDGDLIEYNDTKQMFMNPKHKET 243
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-267 |
4.44e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.73 E-value: 4.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 24 ALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGedvlNAREKQLRQWRgARVAMIFQEPMT 103
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSS----TSKQKEIKPVR-KKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 104 ALnpTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIpdAVEVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEP 183
Cdd:PRK13643 96 QL--FEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGL--ADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 184 TTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHprhpytIGLLQcAPEH 263
Cdd:PRK13643 172 TAGLDPKARIEMMQLFE-SIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE------VDFLK-AHEL 243
|
....
gi 446115710 264 GVPR 267
Cdd:PRK13643 244 GVPK 247
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
25-249 |
5.08e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 95.48 E-value: 5.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNarekqLRQWRGARVAMIF--QEP- 101
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK-----PDSGRIFLDGEDITH-----LPMHKRARLGIGYlpQEAs 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 102 ----MTALNPTRRIgLQMmdvirhhQPISRREARAKAIALLEEMQIpdaVEVMSRYPFELSGGMRQRVMIALAFSCEPQL 177
Cdd:COG1137 89 ifrkLTVEDNILAV-LEL-------RKLSKKEREERLEELLEEFGI---THLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115710 178 IIADEPTTALD-VTVQ-LQ-VLRLLKHKarasGTAVLFISHDmavVS---QLCDSVYVMYAGSVIESGVTADVIHHPR 249
Cdd:COG1137 158 ILLDEPFAGVDpIAVAdIQkIIRHLKER----GIGVLITDHN---VRetlGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-247 |
7.36e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.15 E-value: 7.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSvTamlIMRLL-----PTgsycvhRGQISLLGedvlnarekqlrqwrgaRV 94
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKS-T---LLKLIagilePT------SGRVEVNG-----------------RV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 95 AMIFqEPMTALNPT---R---RIGLQMMDvirhhqpISRREARAKaialleemqIPDAVEV----------MSRYpfelS 158
Cdd:COG1134 90 SALL-ELGAGFHPEltgReniYLNGRLLG-------LSRKEIDEK---------FDEIVEFaelgdfidqpVKTY----S 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 159 GGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKaRASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIES 238
Cdd:COG1134 149 SGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
....*....
gi 446115710 239 GVTADVIHH 247
Cdd:COG1134 228 GDPEEVIAA 236
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-239 |
7.50e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 96.69 E-value: 7.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 22 VHALNNVSLQINRSEIVGLVGESGSGKSVT-AMLIMRLLPTGsycvhrGQISLLGEDVlNAREKQLRqwrgarvamifqe 100
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTiKMLTGILVPTS------GEVRVLGYVP-FKRRKEFA------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 101 pmtalnptRRIGLQM---------------MDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRypfELSGGMRQRV 165
Cdd:COG4586 95 --------RRIGVVFgqrsqlwwdlpaidsFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVR---QLSLGQRMRC 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115710 166 MIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:COG4586 164 ELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDG 237
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-239 |
7.63e-23 |
|
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: 94.52 E-value: 7.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 13 LSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGedvlnarekqlrqwrga 92
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKST----LLRLL-AGIYPPDSGTVTVRG----------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 93 RVAMIFqEPMTALNP-------TRRIGLqMMDvirhhqpISRREARAKAIALLEEMQIPDAVEV-MSRYpfelSGGMRQR 164
Cdd:cd03220 84 RVSSLL-GLGGGFNPeltgrenIYLNGR-LLG-------LSRKEIDEKIDEIIEFSELGDFIDLpVKTY----SSGMKAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115710 165 VMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKaRASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-236 |
8.37e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.55 E-value: 8.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 4 PVLDIQqlHLSFPGfngdvhALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVlnaRE 83
Cdd:COG1129 255 VVLEVE--GLSVGG------VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADP-----ADSGEIRLDGKPV---RI 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQLRQWRGARVAMIfqeP----MTALNPTRRIG----LQMMDVIRHHQPISRREARAKAIALLEEMQI----PDAvEVMS 151
Cdd:COG1129 319 RSPRDAIRAGIAYV---PedrkGEGLVLDLSIRenitLASLDRLSRGGLLDRRRERALAEEYIKRLRIktpsPEQ-PVGN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 152 rypfeLSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:COG1129 395 -----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLI-RELAAEGKAVIVISSELPELLGLSDRILVMR 468
|
....*
gi 446115710 232 AGSVI 236
Cdd:COG1129 469 EGRIV 473
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-244 |
8.58e-23 |
|
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: 94.42 E-value: 8.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAR-EK 84
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP-----PRSGSIRFDGRDITGLPpHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRqwRGarVAMIFQEpmtalnptRRI--GLQMMDVIRHHQPISRREARAKAIALLEEMqIPDAVEVMSRYPFELSGGMR 162
Cdd:cd03224 72 RAR--AG--IGYVPEG--------RRIfpELTVEENLLLGAYARRRAKRKARLERVYEL-FPRLKERRKQLAGTLSGGEQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 163 QRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTA 242
Cdd:cd03224 139 QMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIR-ELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAA 217
|
..
gi 446115710 243 DV 244
Cdd:cd03224 218 EL 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
24-239 |
9.12e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.85 E-value: 9.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 24 ALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQiSLLGEDVLNAREKQLRQWRGAR--VAMIFQEP 101
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISET-----GQ-TIVGDYAIPANLKKIKEVKRLRkeIGLVFQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 102 MTALnptrriglqMMDVIRH-------HQPISRREARAKAIALLEEMQIPDavEVMSRYPFELSGGMRQRVMIALAFSCE 174
Cdd:PRK13645 100 EYQL---------FQETIEKdiafgpvNLGENKQEAYKKVPELLKLVQLPE--DYVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115710 175 PQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-239 |
1.33e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 94.36 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMrllptG--SYCVHRGQISLLGEDVLN--- 80
Cdd:COG0396 1 LEIKNLHVSV----EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLM-----GhpKYEVTSGSILLDGEDILElsp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 ---ARekqlrqwrgARVAMIFQEPMtalnptrRI-GLQMMDVIR------HHQPISRREARAKAIALLEEMQIPDavEVM 150
Cdd:COG0396 72 derAR---------AGIFLAFQYPV-------EIpGVSVSNFLRtalnarRGEELSAREFLKLLKEKMKELGLDE--DFL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 151 SRYPFE-LSGGMRQRV----MIALafscEPQLIIADEPTTALDVTVqLQVLRLLKHKARASGTAVLFISH-----DMAVV 220
Cdd:COG0396 134 DRYVNEgFSGGEKKRNeilqMLLL----EPKLAILDETDSGLDIDA-LRIVAEGVNKLRSPDRGILIITHyqrilDYIKP 208
|
250
....*....|....*....
gi 446115710 221 sqlcDSVYVMYAGSVIESG 239
Cdd:COG0396 209 ----DFVHVLVDGRIVKSG 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-245 |
1.69e-22 |
|
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: 93.83 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 12 HLSFpGFNGD-VHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGEDVlnaREKQLRQWR 90
Cdd:cd03251 5 NVTF-RYPGDgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRF-----YDVDSGRILIDGHDV---RDYTLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 91 gARVAMIFQEPMTaLNPTrriglqMMDVIRHHQP-ISRREARAKA-IALLEE--MQIPDAVE-VMSRYPFELSGGMRQRV 165
Cdd:cd03251 76 -RQIGLVSQDVFL-FNDT------VAENIAYGRPgATREEVEEAArAANAHEfiMELPEGYDtVIGERGVKLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 166 MIALAFSCEPQLIIADEPTTALDVT----VQLQVLRLLKHKarasgtAVLFISHDMAVVSQlCDSVYVMYAGSVIESGVT 241
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTEserlVQAALERLMKNR------TTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTH 220
|
....
gi 446115710 242 ADVI 245
Cdd:cd03251 221 EELL 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-239 |
2.08e-22 |
|
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: 93.83 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 12 HLSFpGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGEDVLNAREKQLRQwrg 91
Cdd:cd03253 5 NVTF-AYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRF-----YDVSSGSILIDGQDIREVTLDSLRR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 92 aRVAMIFQEpmTAL-NPTrriglqMMDVIRHHQPISRRE---ARAKAIALLEE-MQIPDAVE-VMSRYPFELSGGMRQRV 165
Cdd:cd03253 76 -AIGVVPQD--TVLfNDT------IGYNIRYGRPDATDEeviEAAKAAQIHDKiMRFPDGYDtIVGERGLKLSGGEKQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115710 166 MIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLkhKARASGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESG 239
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAAL--RDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
27-245 |
2.13e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 93.80 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 27 NVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLP--TGSYCVHRGQISLLGedvLNAREKqlrqwRGarVAMIFQEPmta 104
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPrdAGNIIIDDEDISLLP---LHARAR-----RG--IGYLPQEA--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 105 lNPTRRIGL--QMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRypfELSGGMRQRVMIALAFSCEPQLIIADE 182
Cdd:PRK10895 88 -SIFRRLSVydNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQ---SLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115710 183 PTTALDVTVQLQVLRLLKHkARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVI 245
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-239 |
2.79e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 95.30 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 19 NGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPT--GSYCV---HRGQISLLGEDVLNAREKQLRQWRGAR 93
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSkyGTIQVgdiYIGDKKNNHELITNPYSKKIKNFKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 94 --VAMIFQEPMTALNPTrRIGLQMMdvirhHQPI----SRREARAKAIALLEEMQIPDAveVMSRYPFELSGGMRQRVMI 167
Cdd:PRK13631 116 rrVSMVFQFPEYQLFKD-TIEKDIM-----FGPValgvKKSEAKKLAKFYLNKMGLDDS--YLERSPFGLSGGQKRRVAI 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115710 168 ALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKGEHEMMQLIL-DAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-216 |
3.20e-22 |
|
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: 92.54 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 4 PVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSvTAM-LIMRLLPtgsycVHRGQISLLGEDVLNAR 82
Cdd:COG4133 1 MMLEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKT-TLLrILAGLLP-----PSAGEVLWNGEPIRDAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 83 EkqlrQWRgARVAMIFQEP-----MTALnptrriglqmmDVIRHHQPISRREARAKAI-ALLEEMQIPDAVEVMSRYpfe 156
Cdd:COG4133 71 E----DYR-RRLAYLGHADglkpeLTVR-----------ENLRFWAALYGLRADREAIdEALEAVGLAGLADLPVRQ--- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 157 LSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHkARASGTAVLFISHD 216
Cdd:COG4133 132 LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-239 |
5.93e-22 |
|
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: 92.60 E-value: 5.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 21 DVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGEDVlnaREKQLRQWRgARVAMIFQE 100
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERF-----YDPTSGEILLDGVDI---RDLNLRWLR-SQIGLVSQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 101 PMTaLNPTrriglqMMDVIRH--HQPISRREARAKAIALLEE--MQIPDAVE-VMSRYPFELSGGMRQRVMIALAFSCEP 175
Cdd:cd03249 86 PVL-FDGT------IAENIRYgkPDATDEEVEEAAKKANIHDfiMSLPDGYDtLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115710 176 QLIIADEPTTALDVTVQLQVLRLLKhKARAsGTAVLFISHDMAVVsQLCDSVYVMYAGSVIESG 239
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALD-RAMK-GRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQG 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
23-248 |
6.04e-22 |
|
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: 92.22 E-value: 6.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 23 HALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVlnareKQLRQWRGARVAMIF--QE 100
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS-----GKILLDGQDI-----TKLPMHKRARLGIGYlpQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 101 P-----MTAlnptrrigLQMMDVIRHHQPISRREARAKAIALLEEMQIpdaVEVMSRYPFELSGGMRQRVMIALAFSCEP 175
Cdd:cd03218 84 AsifrkLTV--------EENILAVLEIRGLSKKEREEKLEELLEEFHI---THLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115710 176 QLIIADEPTTALD-VTVQLqvLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHP 248
Cdd:cd03218 153 KFLLLDEPFAGVDpIAVQD--IQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-255 |
9.60e-22 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 95.28 E-value: 9.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYcvhRGQISLLGEDVlnaREKQLRQWRGARVAMIFQ 99
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTW---DGEIYWSGSPL---KASNIRDTERAGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 EPMTALNPTRRIGLQMMDVIRHHQPISRREARA-KAIALLEEMQIPDavEVMSRYPFELSGGMRQRVMIALAFSCEPQLI 178
Cdd:TIGR02633 86 ELTLVPELSVAENIFLGNEITLPGGRMAYNAMYlRAKNLLRELQLDA--DNVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 179 IADEPTTAL---DVTVQLQVLRLLKhkarASGTAVLFISHDMAVVSQLCDSVYVMYAGSVI----ESGVTADVI------ 245
Cdd:TIGR02633 164 ILDEPSSSLtekETEILLDIIRDLK----AHGVACVYISHKLNEVKAVCDTICVIRDGQHVatkdMSTMSEDDIitmmvg 239
|
250
....*....|....*
gi 446115710 246 -----HHPRHPYTIG 255
Cdd:TIGR02633 240 reitsLYPHEPHEIG 254
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-251 |
1.18e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 91.35 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 29 SLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREkqlrqwrGAR-VAMIFQEP-----M 102
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDS-----GRILWNGQDLTALPP-------AERpVSMLFQENnlfphL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 103 T-------ALNPTRRIglqmmdvirhhqpisRREARAKAIALLEEMQIPDaveVMSRYPFELSGGMRQRVMIALAFSCEP 175
Cdd:COG3840 87 TvaqniglGLRPGLKL---------------TAEQRAQVEQALERVGLAG---LLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115710 176 QLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHPRHP 251
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-242 |
1.41e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.49 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 19 NGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLG-----EDVLNAREKqlrqwrgar 93
Cdd:PRK13650 17 DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES-----GQIIIDGdllteENVWDIRHK--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 94 VAMIFQEPmtalnPTRRIGLQMMDVIR---HHQPISRREARAKaiaLLEEMQIPDAVEVMSRYPFELSGGMRQRVMIALA 170
Cdd:PRK13650 83 IGMVFQNP-----DNQFVGATVEDDVAfglENKGIPHEEMKER---VNEALELVGMQDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115710 171 FSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSqLCDSVYVMYAGSViESGVTA 242
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV-ESTSTP 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-239 |
4.21e-21 |
|
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: 90.24 E-value: 4.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 24 ALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGEDVLNAREKQLRqwrgARVAMIFQEPmT 103
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF-----YVPENGRVLVDGHDLALADPAWLR----RQVGVVLQEN-V 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 104 ALNPTRRIGLQMMDvirHHQPISRREARAK-AIALLEEMQIPDAVE-VMSRYPFELSGGMRQRVMIALAFSCEPQLIIAD 181
Cdd:cd03252 87 LFNRSIRDNIALAD---PGMSMERVIEAAKlAGAHDFISELPEGYDtIVGEQGAGLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446115710 182 EPTTALDVTVQLQVLRLLkhKARASGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESG 239
Cdd:cd03252 164 EATSALDYESEHAIMRNM--HDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-245 |
5.67e-21 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 90.14 E-value: 5.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 3 QPVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhRGQISLLGEDV--LN 80
Cdd:COG1119 1 DPLLELRNVTVRR----GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTY----GNDVRLFGERRggED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 AREkqLRQ---WRGARVAMIFQEPMTALNptrriglqmM------DVIRHHQPISRREaRAKAIALLEEMQIpdaVEVMS 151
Cdd:COG1119 73 VWE--LRKrigLVSPALQLRFPRDETVLD---------VvlsgffDSIGLYREPTDEQ-RERARELLELLGL---AHLAD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 152 RYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:COG1119 138 RPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLK 217
|
250
....*....|....
gi 446115710 232 AGSVIESGVTADVI 245
Cdd:COG1119 218 DGRVVAAGPKEEVL 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-253 |
5.80e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.11 E-value: 5.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 3 QPVLDIQQLHLsfpgFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPT-GSYCVHRGQISLLGEDVLNA 81
Cdd:PRK14246 8 EDVFNISRLYL----YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSKIKVDGKVLYFGKDIFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 82 REKQLRQwrgaRVAMIFQEPmtalNPTRRIGL--QMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPF-ELS 158
Cdd:PRK14246 84 DAIKLRK----EVGMVFQQP----NPFPHLSIydNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPAsQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 159 GGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARAsgTAVLFISHDMAVVSQLCDSVYVMYAGSVIES 238
Cdd:PRK14246 156 GGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEW 233
|
250
....*....|....*
gi 446115710 239 GVTADVIHHPRHPYT 253
Cdd:PRK14246 234 GSSNEIFTSPKNELT 248
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-249 |
6.06e-21 |
|
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: 89.66 E-value: 6.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 4 PVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNARE 83
Cdd:COG0410 2 PMLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP-----PRSGSIRFDGEDITGLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQLRQwRGarVAM------IFQEpMTAL-NptrrigLQMMDVIRHHQPiSRREARAKAIAL---LEEMQipdavevmSRY 153
Cdd:COG0410 73 HRIAR-LG--IGYvpegrrIFPS-LTVEeN------LLLGAYARRDRA-EVRADLERVYELfprLKERR--------RQR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 154 PFELSGGMRQRVMIALAFSCEPQLIIADEPTTALD-VTVQlQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYA 232
Cdd:COG0410 134 AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLApLIVE-EIFEIIR-RLNREGVTILLVEQNARFALEIADRAYVLER 211
|
250
....*....|....*..
gi 446115710 233 GSVIESGVTADVIHHPR 249
Cdd:COG0410 212 GRIVLEGTAAELLADPE 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
12-256 |
7.55e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 90.63 E-value: 7.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 12 HLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycVHRGQISLLG-----EDVLNAREKql 86
Cdd:PRK13640 10 HVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD--NPNSKITVDGitltaKTVWDIREK-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 87 rqwrgarVAMIFQEPmtalnPTRRIGLQMMDVIR---HHQPISRREARAKAIALLEEMqipDAVEVMSRYPFELSGGMRQ 163
Cdd:PRK13640 86 -------VGIVFQNP-----DNQFVGATVGDDVAfglENRAVPRPEMIKIVRDVLADV---GMLDYIDSEPANLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 164 RVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESGVTAD 243
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVE 229
|
250
....*....|...
gi 446115710 244 VIHHPRHPYTIGL 256
Cdd:PRK13640 230 IFSKVEMLKEIGL 242
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-245 |
8.46e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 89.76 E-value: 8.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 7 DIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQL 86
Cdd:COG4604 3 EIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLP-----PDSGEVLVDGLDVATTPSREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 87 RQwrgaRVAMIFQEPMTALNPTRRiglqmmDVIR-----HHQpiSR-----REARAKAIALLEEMQIPDavevmsRYPFE 156
Cdd:COG4604 74 AK----RLAILRQENHINSRLTVR------ELVAfgrfpYSK--GRltaedREIIDEAIAYLDLEDLAD------RYLDE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 157 LSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVI 236
Cdd:COG4604 136 LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVV 215
|
....*....
gi 446115710 237 ESGVTADVI 245
Cdd:COG4604 216 AQGTPEEII 224
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
234-320 |
1.19e-20 |
|
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: 84.72 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 234 SVIESGVTADVIHHPRHPYTIGLLQCAPEHGVPRQLLPAIPGTVPNLTHLPEGCAFRDRCYAAGAQCENVPALTACGDNN 313
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVEIAEG 80
|
....*..
gi 446115710 314 QRCACWY 320
Cdd:TIGR01727 81 HRVACHL 87
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
11-252 |
1.20e-20 |
|
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: 90.94 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 11 LHLSFPGFNGDvHALNnVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTGsycvhrGQISLLGEDVLNAREKQLRQW 89
Cdd:TIGR02142 1 LSARFSKRLGD-FSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTrPDE------GEIVLNGRTLFDSRKGIFLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 90 RGARVAMIFQE----PMTALNPTRRIGLQMMDvirhhqPISRREARAKAIALLeemqipdAVE-VMSRYPFELSGGMRQR 164
Cdd:TIGR02142 73 EKRRIGYVFQEarlfPHLSVRGNLRYGMKRAR------PSERRISFERVIELL-------GIGhLLGRLPGRLSGGEKQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 165 VMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADV 244
Cdd:TIGR02142 140 VAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
....*...
gi 446115710 245 IHHPRHPY 252
Cdd:TIGR02142 220 WASPDLPW 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-239 |
1.27e-20 |
|
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: 87.37 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPgfNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLImrllpTGSYCVHRGQISLLGEDVLNArEKQ 85
Cdd:cd03247 1 LSINNVSFSYP--EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLL-----TGDLKPQQGEITLDGVPVSDL-EKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 LRQwrgaRVAMIFQEPMTaLNPTRRiglqmmdvirhhQPISRRearakaialleemqipdavevmsrypfeLSGGMRQRV 165
Cdd:cd03247 73 LSS----LISVLNQRPYL-FDTTLR------------NNLGRR----------------------------FSGGERQRL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115710 166 MIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARasGTAVLFISHDMAVVSQLcDSVYVMYAGSVIESG 239
Cdd:cd03247 108 ALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-221 |
1.73e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.29 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGqisllgedvlnarekqlrqwRGARVAMIFQ 99
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA--------------------GGARVAYVPQ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 EpmTALN---PTRRIGLQMMDVIRHHQPISR--REARAKAIALLEEMQIPDavevMSRYPF-ELSGGMRQRVMIALAFSC 173
Cdd:NF040873 63 R--SEVPdslPLTVRDLVAMGRWARRGLWRRltRDDRAAVDDALERVGLAD----LAGRQLgELSGGQRQRALLAQGLAQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446115710 174 EPQLIIADEPTTALDVTVQLQVLRLLKHkARASGTAVLFISHDMAVVS 221
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAE-EHARGATVVVVTHDLELVR 183
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-217 |
2.22e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.60 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPGfngdVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVlnarekq 85
Cdd:PRK11248 2 LQISHLYADYGG----KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQH-----GSITLDGKPV------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 lrQWRGARVAMIFQEpmTALNPTRRI------GLQMMDVirhhqpiSRREARAKAIALLEEMqipDAVEVMSRYPFELSG 159
Cdd:PRK11248 66 --EGPGAERGVVFQN--EGLLPWRNVqdnvafGLQLAGV-------EKMQRLEIAHQMLKKV---GLEGAEKRYIWQLSG 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446115710 160 GMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDM 217
Cdd:PRK11248 132 GQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-241 |
3.59e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.40 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFPgfNGDVhALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLN 80
Cdd:PRK15056 2 MQQAGIVVNDVTVTWR--NGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLAS-----GKISILGQPTRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 AREKQLrqwrgarVAMIFQ-EPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIaLLEEMQIPDAVEVMSRYPFELSG 159
Cdd:PRK15056 74 ALQKNL-------VAYVPQsEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQI-VTAALARVDMVEFRHRQIGELSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 160 GMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVyVMYAGSVIESG 239
Cdd:PRK15056 146 GQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLR-ELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASG 223
|
..
gi 446115710 240 VT 241
Cdd:PRK15056 224 PT 225
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-237 |
5.66e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 89.24 E-value: 5.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGEDVLN 80
Cdd:PRK09452 10 SLSPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTT----VLRLI-AGFETPDSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 AREKQlRQwrgarVAMIFQEpmTALNPTRRI------GLQMMDVirHHQPISRREARAKAIALLEEMQipdavevmSRYP 154
Cdd:PRK09452 81 VPAEN-RH-----VNTVFQS--YALFPHMTVfenvafGLRMQKT--PAAEITPRVMEALRMVQLEEFA--------QRKP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 155 FELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGs 234
Cdd:PRK09452 143 HQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG- 221
|
...
gi 446115710 235 VIE 237
Cdd:PRK09452 222 RIE 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-248 |
5.83e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.94 E-value: 5.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 18 FNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQLRQWrgarVAMI 97
Cdd:PRK13652 13 YSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTS-----GSVLIRGEPITKENIREVRKF----VGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 98 FQEPMTAL-NPT--RRIGLQMMDVIRHHQPISRREARAKAIALLEEMQipdavevmSRYPFELSGGMRQRVMIALAFSCE 174
Cdd:PRK13652 84 FQNPDDQIfSPTveQDIAFGPINLGLDEETVAHRVSSALHMLGLEELR--------DRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115710 175 PQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHP 248
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-244 |
6.35e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 87.83 E-value: 6.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFPGfngDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PT-GSYCVHRGQISLLGEDVLNAR 82
Cdd:PRK13639 1 ILETRDLKYSYPD---GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkPTsGEVLIKGEPIKYDKKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 83 EKqlrqwrgarVAMIFQEPMTAL-NPTRR---------IGLQMMDVirhhqpisrrEARAKaialleemqipDAVEV--M 150
Cdd:PRK13639 78 KT---------VGIVFQNPDDQLfAPTVEedvafgplnLGLSKEEV----------EKRVK-----------EALKAvgM 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 151 SRY----PFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDS 226
Cdd:PRK13639 128 EGFenkpPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLL-YDLNKEGITIIISTHDVDLVPVYADK 206
|
250
....*....|....*...
gi 446115710 227 VYVMYAGSVIESGVTADV 244
Cdd:PRK13639 207 VYVMSDGKIIKEGTPKEV 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-245 |
6.57e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 90.25 E-value: 6.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVtamLIMRLLPTGSYCVHRGQI----------------SLLGE------- 76
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSV---LMHVLRGMDQYEPTSGRIiyhvalcekcgyverpSKVGEpcpvcgg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 77 -------DVLNAREKQLRQWRgARVAMIFQEPMtALNPTRRIglqMMDVIRHHQPI--SRREARAKAIALLEEMQIPDAV 147
Cdd:TIGR03269 88 tlepeevDFWNLSDKLRRRIR-KRIAIMLQRTF-ALYGDDTV---LDNVLEALEEIgyEGKEAVGRAVDLIEMVQLSHRI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 148 EVMSRypfELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSV 227
Cdd:TIGR03269 163 THIAR---DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*...
gi 446115710 228 YVMYAGSVIESGVTADVI 245
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVV 257
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-244 |
8.83e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.84 E-value: 8.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFPGfngdVHALNNVSLQINRSEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGEDvLN 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKST----LMKVL-SGIHEPTKGTITINNIN-YN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 AREKQLRQWRGarVAMIFQE-----PMTALN-------PTRRI-GLQMMDVirhhqpisrREARAKAIALLEEMQIPDAV 147
Cdd:PRK09700 71 KLDHKLAAQLG--IGIIYQElsvidELTVLEnlyigrhLTKKVcGVNIIDW---------REMRVRAAMMLLRVGLKVDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 148 EVMSRypfELSGGMRQRVMIALAFSCEPQLIIADEPTTALdVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSV 227
Cdd:PRK09700 140 DEKVA---NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRY 215
|
250
....*....|....*..
gi 446115710 228 YVMYAGSVIESGVTADV 244
Cdd:PRK09700 216 TVMKDGSSVCSGMVSDV 232
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-239 |
9.41e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 85.66 E-value: 9.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMrllptG--SYCVHRGQISLLGEDVLNArE 83
Cdd:cd03217 1 LEIKDLHVSV----GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIM-----GhpKYEVTEGEILFKGEDITDL-P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQLRQWRGarVAMIFQEPMtalnptrRI-GLQMMDVIrhhqpisrrearakaialleemqipdavevmsRYPFE-LSGGM 161
Cdd:cd03217 71 PEERARLG--IFLAFQYPP-------EIpGVKNADFL--------------------------------RYVNEgFSGGE 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446115710 162 RQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQL-CDSVYVMYAGSVIESG 239
Cdd:cd03217 110 KKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVIN-KLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-223 |
1.00e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.41 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRL-LPTGSYCVHRGQiSLlgeDVL 79
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQ-PM---SKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 80 NAREKQlrQWRGARVAMIFQ-----EPMTALNptrriGLQMMDVIRHHQPisrREARAKAIALLEemqipdAVEVMSR-- 152
Cdd:PRK11629 77 SSAAKA--ELRNQKLGFIYQfhhllPDFTALE-----NVAMPLLIGKKKP---AEINSRALEMLA------AVGLEHRan 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115710 153 -YPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQL 223
Cdd:PRK11629 141 hRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-253 |
1.13e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 88.74 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFPGfngdVHALNNVSLQINRSEIVGLVGESGSGKSVtamlIMRLL-----PTgsycvhRGQISLLG 75
Cdd:PRK11607 15 ALTPLLEIRNLTKSFDG----QHAVDDVSLTIYKGEIFALLGASGCGKST----LLRMLagfeqPT------AGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 76 EDVLNAREKQlrqwrgARVAMIFQE----PMTALNPTRRIGLQmmdvirhHQPISRREARAKAIALLE--EMQipdavEV 149
Cdd:PRK11607 81 VDLSHVPPYQ------RPINMMFQSyalfPHMTVEQNIAFGLK-------QDKLPKAEIASRVNEMLGlvHMQ-----EF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 150 MSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTV----QLQVLRLLKhkaRASGTAVLfISHDMAVVSQLCD 225
Cdd:PRK11607 143 AKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILE---RVGVTCVM-VTHDQEEAMTMAG 218
|
250 260
....*....|....*....|....*...
gi 446115710 226 SVYVMYAGSVIESGVTADVIHHPRHPYT 253
Cdd:PRK11607 219 RIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
24-256 |
1.36e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 87.07 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 24 ALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTGsycvhrGQISLLGEDVLNarEKQLRQWRgARVAMIFQEPM 102
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLiPSE------GKVYVDGLDTSD--EENLWDIR-NKAGMVFQNPD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 103 TALNPT----------RRIGLQMmDVIRhhqpiSRREARAKAIALLEEMQIPdavevmsryPFELSGGMRQRVMIALAFS 172
Cdd:PRK13633 96 NQIVATiveedvafgpENLGIPP-EEIR-----ERVDESLKKVGMYEYRRHA---------PHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 173 CEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESGVTADVIHHPRHPY 252
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMMK 239
|
....
gi 446115710 253 TIGL 256
Cdd:PRK13633 240 KIGL 243
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-238 |
1.93e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.81 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 2 TQPVLDIQQLHLSFPGfngdVHALNNVSLQINRSEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGEDVL-- 79
Cdd:PRK11288 1 SSPYLSFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKST----LLKIL-SGNYQPDAGSILIDGQEMRfa 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 80 NAREKQlrqwrGARVAMIFQE----P-MT-ALN------PTRRiGLqmmdvirhhqpISRREARAKAIALLEEMQI---P 144
Cdd:PRK11288 72 STTAAL-----AAGVAIIYQElhlvPeMTvAENlylgqlPHKG-GI-----------VNRRLLNYEAREQLEHLGVdidP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 145 DAvevmsryPF-ELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQL 223
Cdd:PRK11288 135 DT-------PLkYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIR-ELRAEGRVILYVSHRMEEIFAL 206
|
250
....*....|....*
gi 446115710 224 CDSVYVMYAGSVIES 238
Cdd:PRK11288 207 CDAITVFKDGRYVAT 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
13-239 |
2.74e-19 |
|
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: 85.02 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 13 LSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrgqiSLLGEDVLNAREKQLRQWRgA 92
Cdd:cd03234 11 LKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGG--------TTSGQILFNGQPRKPDQFQ-K 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 93 RVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPiSRREARAKAIALLEEMQIPDAVeVMSRYPFELSGGMRQRVMIALAFS 172
Cdd:cd03234 82 CVAYVRQDDILLPGLTVRETLTYTAILRLPRK-SSDAIRKKRVEDVLLRDLALTR-IGGNLVKGISGGERRRVSIAVQLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446115710 173 CEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-239 |
3.36e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.56 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFPGfngDVHALNNVSLQINRSEIVGLVGESGSGKSVtamLIMRLlpTGSYCVHRGQISLLGEDVLNAREK 84
Cdd:PRK13647 4 IIEVEDLHFRYKD---GTKALKGLSLSIPEGSKTALLGPNGAGKST---LLLHL--NGIYLPQRGRVKVMGREVNAENEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRqwrgARVAMIFQEP------MT-----ALNPtRRIGLQMMDVIRhhqpisRREARAKAIalleEMQipdavEVMSRY 153
Cdd:PRK13647 76 WVR----SKVGLVFQDPddqvfsSTvwddvAFGP-VNMGLDKDEVER------RVEEALKAV----RMW-----DFRDKP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 154 PFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:PRK13647 136 PYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILD-RLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
....*.
gi 446115710 234 SVIESG 239
Cdd:PRK13647 215 RVLAEG 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-245 |
4.42e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.07 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQ 85
Cdd:PRK11231 3 LRTENLTVGY----GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQS-----GTVFLGDKPISMLSSRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 LRQwrgaRVAMIFQEPMTALNPTRRiglQMMDVIR-----HHQPISRREaRAKAIALLEEMQIpdaVEVMSRYPFELSGG 160
Cdd:PRK11231 74 LAR----RLALLPQHHLTPEGITVR---ELVAYGRspwlsLWGRLSAED-NARVNQAMEQTRI---NHLADRRLTDLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 161 MRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGV 240
Cdd:PRK11231 143 QRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMR-ELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
....*
gi 446115710 241 TADVI 245
Cdd:PRK11231 222 PEEVM 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-230 |
4.93e-19 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 87.73 E-value: 4.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 4 PVLDIQQLHLSFPGFNgdvHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNARE 83
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD-----PTEGSIAVNGVPLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQLRQwrgaRVAMIFQEPmTALNPTrriglqMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPF-----ELS 158
Cdd:TIGR02857 392 DSWRD----QIAWVPQHP-FLFAGT------IAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIgeggaGLS 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115710 159 GGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLkhKARASGTAVLFISHDMAVVsQLCDSVYVM 230
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEAL--RALAQGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
6-244 |
7.37e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.12 E-value: 7.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSfpgfngdvHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycvHRGQISLLGEDVLNAREKQ 85
Cdd:COG4138 1 LQLNDVAVA--------GRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP------GQGEILLNGRPLSDWSAAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 LRQWRgarvAMIFQEPMTALnptrriglqMMDV---IRHHQP-ISRREARAKAIA-LLEEMQIPDAvevMSRYPFELSGG 160
Cdd:COG4138 67 LARHR----AYLSQQQSPPF---------AMPVfqyLALHQPaGASSEAVEQLLAqLAEALGLEDK---LSRPLTQLSGG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 161 MRQRVMIALAF-----SCEP--QLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLfISHDMAVVSQLCDSVYVMYAG 233
Cdd:COG4138 131 EWQRVRLAAVLlqvwpTINPegQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVM-SSHDLNHTLRHADRVWLLKQG 209
|
250
....*....|.
gi 446115710 234 SVIESGVTADV 244
Cdd:COG4138 210 KLVASGETAEV 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-247 |
9.73e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.86 E-value: 9.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVT-AMLIMRLLPTGsycvhrGQISLLGEDVl 79
Cdd:PRK13537 3 MSVAPIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTlRMLLGLTHPDA------GSISLCGEPV- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 80 NAREKQLRQwrgaRVAMIFQepMTALNP--TRRIGLQmmdVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRypfEL 157
Cdd:PRK13537 72 PSRARHARQ----RVGVVPQ--FDNLDPdfTVRENLL---VFGRYFGLSAAAARALVPPLLEFAKLENKADAKVG---EL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 158 SGGMRQRVMIALAFSCEPQLIIADEPTTALDVtvqlQVLRLLKHKAR---ASGTAVLFISHDMAVVSQLCDSVYVMYAGS 234
Cdd:PRK13537 140 SGGMKRRLTLARALVNDPDVLVLDEPTTGLDP----QARHLMWERLRsllARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
250
....*....|...
gi 446115710 235 VIESGVTADVIHH 247
Cdd:PRK13537 216 KIAEGAPHALIES 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-244 |
1.42e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 84.13 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFPGfngDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQIsLLGEDVLN 80
Cdd:PRK13636 1 MEDYILKVEELNYNYSD---GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSS-----GRI-LFDGKPID 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 81 AREKQLRQWRGArVAMIFQEPMTAL---NPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQipdavevmSRYPFEL 157
Cdd:PRK13636 72 YSRKGLMKLRES-VGMVFQDPDNQLfsaSVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLK--------DKPTHCL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 158 SGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIE 237
Cdd:PRK13636 143 SFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVIL 222
|
....*..
gi 446115710 238 SGVTADV 244
Cdd:PRK13636 223 QGNPKEV 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-216 |
1.48e-18 |
|
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: 86.26 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 4 PVLDIQQLHLSFPGfngDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTgsycvHRGQISLLGEDVLNARE 83
Cdd:TIGR02868 333 PTLELRDLSAGYPG---APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP-----LQGEVTLDGVPVSSLDQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQLRqwrgARVAMIFQEPM---TALNPTRRIGL------QMMDVIRhhqpisrreaRAKAIALLEEMqiPDAVE-VMSRY 153
Cdd:TIGR02868 405 DEVR----RRVSVCAQDAHlfdTTVRENLRLARpdatdeELWAALE----------RVGLADWLRAL--PDGLDtVLGEG 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115710 154 PFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLkhKARASGTAVLFISHD 216
Cdd:TIGR02868 469 GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-245 |
3.28e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.84 E-value: 3.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 14 SFPGfngdVHALNNVSLQINRSEIVGLVGESGSGKSVtamlIMRLL----PTGSYcvhRGQISLLGEdvlnarekqLRQW 89
Cdd:NF040905 10 TFPG----VKALDDVNLSVREGEIHALCGENGAGKST----LMKVLsgvyPHGSY---EGEILFDGE---------VCRF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 90 RGAR------VAMIFQEpmTAL-------------NPTRRIGLqmmdvirhhqpISRREARAKAIALLEE--MQIPDAVE 148
Cdd:NF040905 70 KDIRdsealgIVIIHQE--LALipylsiaeniflgNERAKRGV-----------IDWNETNRRARELLAKvgLDESPDTL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 149 VMsrypfELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHkARASGTAVLFISHDMAVVSQLCDSVY 228
Cdd:NF040905 137 VT-----DIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLE-LKAQGITSIIISHKLNEIRRVADSIT 210
|
250 260
....*....|....*....|...
gi 446115710 229 VMYAGSVIES------GVTADVI 245
Cdd:NF040905 211 VLRDGRTIETldcradEVTEDRI 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-245 |
7.44e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.96 E-value: 7.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMrllptGSYCVHRGQISLLGEDVlnarEKQLRQWRgARVAMIFQ 99
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIL-----GMTSPDAGKITVLGVPV----PARARLAR-ARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 EPMTALNPTRRIGLQmmdVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRypfELSGGMRQRVMIALAFSCEPQLII 179
Cdd:PRK13536 122 FDNLDLEFTVRENLL---VFGRYFGMSTREIEAVIPSLLEFARLESKADARVS---DLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115710 180 ADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVI 245
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLR-SLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-249 |
8.37e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.57 E-value: 8.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLImrllpTGSYCVHRGQISLLGEDV-- 78
Cdd:PRK11300 1 MSQPLLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCL-----TGFYKPTGGTILLRGQHIeg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 79 ----LNAREKQLRQWRGARvamIFQEpMTALnptrriglQMMDVIRHHQ------------PISRR---EARAKAIALLE 139
Cdd:PRK11300 72 lpghQIARMGVVRTFQHVR---LFRE-MTVI--------ENLLVAQHQQlktglfsgllktPAFRRaesEALDRAATWLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 140 EMQIpdaVEVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDV--TVQLQVL-RLLKhkaRASGTAVLFISHD 216
Cdd:PRK11300 140 RVGL---LEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPkeTKELDELiAELR---NEHNVTVLLIEHD 213
|
250 260 270
....*....|....*....|....*....|...
gi 446115710 217 MAVVSQLCDSVYVMYAGSVIESGVTADVIHHPR 249
Cdd:PRK11300 214 MKLVMGISDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
24-245 |
1.20e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 81.67 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 24 ALNNVSLQINRSEIVGLVGESGSGKSV-TAMLIMRLLPTgsycvhRGQISLLGEDVLNAREKQLRQWRGARVAM---IFQ 99
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTfIEHLNALLLPD------TGTIEWIFKDEKNKKKTKEKEKVLEKLVIqktRFK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 EPMTALNPTRRIGL-------QMM------DVIrhHQPIS----RREARAKAIALLEEMQIPdaVEVMSRYPFELSGGMR 162
Cdd:PRK13651 96 KIKKIKEIRRRVGVvfqfaeyQLFeqtiekDII--FGPVSmgvsKEEAKKRAAKYIELVGLD--ESYLQRSPFELSGGQK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 163 QRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTA 242
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIF-DNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTY 250
|
...
gi 446115710 243 DVI 245
Cdd:PRK13651 251 DIL 253
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-217 |
1.24e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.90 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSF-PGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSvTAM-LImrllpTGSYCVHRGQISLLGEDVLNARE 83
Cdd:COG1101 2 LELKNLSKTFnPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKS-TLLnAI-----AGSLPPDSGSILIDGKDVTKLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQlrqwRGARVAMIFQEP-------MT-------ALNPTRRIGLqmmdviRHHQPISRREARAKAIALLE---EMQIPDA 146
Cdd:COG1101 76 YK----RAKYIGRVFQDPmmgtapsMTieenlalAYRRGKRRGL------RRGLTKKRRELFRELLATLGlglENRLDTK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115710 147 VEVmsrypfeLSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDM 217
Cdd:COG1101 146 VGL-------LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-239 |
1.56e-17 |
|
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: 79.94 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 14 SFPgfNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDvlnarekqLRQWRGA 92
Cdd:cd03245 11 SYP--NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYkPT------SGSVLLDGTD--------IRQLDPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 93 RVamifqepmtalnpTRRIGLQMMDV------IRHHQPISRREARAKAIalLEEMQIPDAVEVMSRYP-----------F 155
Cdd:cd03245 75 DL-------------RRNIGYVPQDVtlfygtLRDNITLGAPLADDERI--LRAAELAGVTDFVNKHPngldlqigergR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 156 ELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLkhKARASGTAVLFISHDMAVVsQLCDSVYVMYAGSV 235
Cdd:cd03245 140 GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERL--RQLLGDKTLIIITHRPSLL-DLVDRIIVMDSGRI 216
|
....
gi 446115710 236 IESG 239
Cdd:cd03245 217 VADG 220
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
5-247 |
1.79e-17 |
|
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: 82.78 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFPGFNGDVhaLNNVSLQINRSEIVGLVGESGSGKSVTAMLImrllpTGSYCVHRGQISLLGEDvlnarek 84
Cdd:TIGR01842 316 HLSVENVTIVPPGGKKPT--LRGISFSLQAGEALAIIGPSGSGKSTLARLI-----VGIWPPTSGSVRLDGAD------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 qLRQWR----GARVAMIFQepmtalnptrriGLQMMD-VIRhhQPISRREARAKAIALLEEMQIPDAVEVMSRYP----- 154
Cdd:TIGR01842 382 -LKQWDretfGKHIGYLPQ------------DVELFPgTVA--ENIARFGENADPEKIIEAAKLAGVHELILRLPdgydt 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 155 ------FELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHkARASGTAVLFISHDMAVVsQLCDSVY 228
Cdd:TIGR01842 447 vigpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKA-LKARGITVVVITHRPSLL-GCVDKIL 524
|
250
....*....|....*....
gi 446115710 229 VMYAGSVIESGVTADVIHH 247
Cdd:TIGR01842 525 VLQDGRIARFGERDEVLAK 543
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-239 |
3.85e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.02 E-value: 3.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 23 HALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrgQISllGEDVLNAREKQLRQWRgARVAMIFQEPM 102
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGV------KGS--GSVLLNGMPIDAKEMR-AISAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 103 TALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEM----------QIPDAVEVmsrypfeLSGGMRQRvmiaLAFS 172
Cdd:TIGR00955 110 FIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALglrkcantriGVPGRVKG-------LSGGERKR----LAFA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115710 173 CE----PQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:TIGR00955 179 SElltdPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLG 249
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-244 |
3.94e-17 |
|
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: 78.74 E-value: 3.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 30 LQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQlrQWRGARVAMIFQEPM----TAL 105
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIP-----PAKGTVKVAGASPGKGWRHI--GYVPQRHEFAWDFPIsvahTVM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 106 N-PTRRIGLqmmdvirhhqpiSRREARAKAIALLEEMQIPDAVEVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPT 184
Cdd:TIGR03771 74 SgRTGHIGW------------LRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPF 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 185 TALDVTVQLQVLRLLKHKArASGTAVLFISHDMAVVSQLCDSVyVMYAGSVIESGVTADV 244
Cdd:TIGR03771 142 TGLDMPTQELLTELFIELA-GAGTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQL 199
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-247 |
5.28e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 81.64 E-value: 5.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 3 QPVLDIQQLhlSFPGFNgdvhalnNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVlNAR 82
Cdd:PRK15439 266 APVLTVEDL--TGEGFR-------NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARG-----GRIMLNGKEI-NAL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 83 EKQLRQWRGArVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIalLEE------MQIPDAVEVMSRypfe 156
Cdd:PRK15439 331 STAQRLARGL-VYLPEDRQSSGLYLDAPLAWNVCALTHNRRGFWIKPARENAV--LERyrralnIKFNHAEQAART---- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 157 LSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKArASGTAVLFISHDMAVVSQLCDSVYVM----YA 232
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMhqgeIS 482
|
250
....*....|....*
gi 446115710 233 GSVIESGVTADVIHH 247
Cdd:PRK15439 483 GALTGAAINVDTIMR 497
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-248 |
5.51e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 80.53 E-value: 5.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVtamlIMRLL-----PTGsycvhrGQISLLGEDVLNaREKQLRQwrgarV 94
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTT----VLRLVaglekPTE------GQIFIDGEDVTH-RSIQQRD-----I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 95 AMIFQEpmTALNPTRRI------GLQMMDVirhhqPISRREARAKaiallEEMQIPDAVEVMSRYPFELSGGMRQRVMIA 168
Cdd:PRK11432 81 CMVFQS--YALFPHMSLgenvgyGLKMLGV-----PKEERKQRVK-----EALELVDLAGFEDRYVDQISGGQQQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 169 LAFSCEPQLIIADEPTTALDVTVQlqvlRLLKHKAR----ASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADV 244
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLR----RSMREKIRelqqQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
....
gi 446115710 245 IHHP 248
Cdd:PRK11432 225 YRQP 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-250 |
8.20e-17 |
|
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: 78.28 E-value: 8.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRL-LPT-GSYCVHRGQISLLGEDVLNA-REKQLRQWRGARvamifqep 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTsGGVILEGKQITEPGPDRMVVfQNYSLLPWLTVR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 102 mtalnptRRIGLQMmDVIRHHQPISRREARAKaiallEEMQIPDAVEVMSRYPFELSGGMRQRVMIALAFSCEPQLIIAD 181
Cdd:TIGR01184 73 -------ENIALAV-DRVLPDLSKSERRAIVE-----EHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLD 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 182 EPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADV-IHHPRH 250
Cdd:TIGR01184 140 EPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-248 |
1.04e-16 |
|
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: 79.46 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 40 LVGESGSGKSVTAMLImrllpTGSYCVHRGQISLLGEDVLNaREKQLRQwrgarVAMIFQEpmTALNPTRRI------GL 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLL-----AGFEQPDSGSIMLDGEDVTN-VPPHLRH-----INMVFQS--YALFPHMTVeenvafGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 114 QMMDVirhhqPISRREARAKAIALLEEMQipdavEVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQL 193
Cdd:TIGR01187 68 KMRKV-----PRAEIKPRVLEALRLVQLE-----EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRD 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446115710 194 QVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHP 248
Cdd:TIGR01187 138 QMQLELKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
27-218 |
1.21e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 77.14 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 27 NVSLQINRSEIVGLVGESGSGKS-VTAMLIMRLLPTGSYcvhRGQISLLGEDvLNAREKQLRqwrgaRVAMIFQEPMtaL 105
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKStLLAAIAGTLSPAFSA---SGEVLLNGRR-LTALPAEQR-----RIGILFQDDL--L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 106 NPTRRIGLQMMDVIRHHqpISRREARAKAIALLEEMQIPDaveVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTT 185
Cdd:COG4136 88 FPHLSVGENLAFALPPT--IGRAQRRARVEQALEEAGLAG---FADRDPATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190
....*....|....*....|....*....|...
gi 446115710 186 ALDVTVQLQVLRLLKHKARASGTAVLFISHDMA 218
Cdd:COG4136 163 KLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-227 |
1.26e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.45 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 11 LHLSFPGFN-GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAREKQLRQ 88
Cdd:PRK10247 8 LQLQNVGYLaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPT------SGTLLFEGEDISTLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 89 wrgaRVAMIFQEPMTaLNPTRRIGLQMMDVIRHHQPisrreARAKAIALLEEMQIPDavEVMSRYPFELSGGMRQRVMIA 168
Cdd:PRK10247 82 ----QVSYCAQTPTL-FGDTVYDNLIFPWQIRNQQP-----DPAIFLDDLERFALPD--TILTKNIAELSGGEKQRISLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446115710 169 LAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQlCDSV 227
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-222 |
2.14e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.84 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRL-LPTGsycvhrGQISLLGEDVLNAREKQLRQWRgARVAMIF 98
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIeRPSA------GKIWFSGHDITRLKNREVPFLR-RQIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 99 QEPMTALNPTRRIGLQMMDVIrhhQPISRREARAKAIALLEEMQIPDAVEvmsRYPFELSGGMRQRVMIALAFSCEPQLI 178
Cdd:PRK10908 86 QDHHLLMDRTVYDNVAIPLII---AGASGDDIRRRVSAALDKVGLLDKAK---NFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446115710 179 IADEPTTALDVTVQLQVLRLLKHKARAsGTAVLFISHDMAVVSQ 222
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISR 202
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-239 |
2.26e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.48 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 2 TQPVLDIQQLHLSFPgfNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRllptgSYCVHRGQISLLGEDVLNA 81
Cdd:PRK11160 335 DQVSLTLNNVSFTYP--DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTR-----AWDPQQGEILLNGQPIADY 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 82 REKQLRQwrgarvAMIF--QEPMTaLNPTRRIGLQMmdvirhhqpisrrearAKAIALLEEMqipdaVEVMSRYPFE--- 156
Cdd:PRK11160 408 SEAALRQ------AISVvsQRVHL-FSATLRDNLLL----------------AAPNASDEAL-----IEVLQQVGLEkll 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 157 ----------------LSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARasGTAVLFISHDMAVV 220
Cdd:PRK11160 460 eddkglnawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGL 537
|
250
....*....|....*....
gi 446115710 221 SQLcDSVYVMYAGSVIESG 239
Cdd:PRK11160 538 EQF-DRICVMDNGQIIEQG 555
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-247 |
2.43e-16 |
|
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: 79.76 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 7 DIQQLHLSFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRL-LPTGsycvhrGQISLLGEDVLNAREKQ 85
Cdd:TIGR02203 330 DVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFyEPDS------GQILLDGHDLADYTLAS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 LRqwrgARVAMIFQEpMTALNPTrriglqMMDVIRHHQP--ISRREA-RAKAIALLEEM--QIPDAVE-VMSRYPFELSG 159
Cdd:TIGR02203 404 LR----RQVALVSQD-VVLFNDT------IANNIAYGRTeqADRAEIeRALAAAYAQDFvdKLPLGLDtPIGENGVLLSG 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 160 GMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARasGTAVLFISHDMAVVsQLCDSVYVMYAGSVIESG 239
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTI-EKADRIVVMDDGRIVERG 549
|
....*...
gi 446115710 240 VTADVIHH 247
Cdd:TIGR02203 550 THNELLAR 557
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
25-235 |
2.82e-16 |
|
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: 75.33 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQLRQwrgarvamifqepmta 104
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTS-----GRVRLDGADISQWDPNELGD---------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 105 lnptrRIGLQMMDVIrhhqpisrrearakaialLEEMQIPDAVevmsrypfeLSGGMRQRVMIALAFSCEPQLIIADEPT 184
Cdd:cd03246 77 -----HVGYLPQDDE------------------LFSGSIAENI---------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446115710 185 TALDVTVQLQVLRLLKHkARASGTAVLFISHDMAVVSQlCDSVYVMYAGSV 235
Cdd:cd03246 125 SHLDVEGERALNQAIAA-LKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-237 |
3.20e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.95 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 4 PVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSvTamlIMRLLpTGSYCVHRGQISLlGEDVlnare 83
Cdd:COG0488 314 KVLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKS-T---LLKLL-AGELEPDSGTVKL-GETV----- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 kqlrqwrgaRVAMIFQEpMTALNPTRRIglqmMDVIRHHQP-ISRREARAkaiaLLEEMQIP--DA---VEVmsrypfeL 157
Cdd:COG0488 379 ---------KIGYFDQH-QEELDPDKTV----LDELRDGAPgGTEQEVRG----YLGRFLFSgdDAfkpVGV-------L 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 158 SGGMRQRVMIALAFSCEPQLIIADEPTTALDV-TvqLQVL-RLLKHkarASGTaVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeT--LEALeEALDD---FPGT-VLLVSHDRYFLDRVATRILEFEDGGV 507
|
..
gi 446115710 236 IE 237
Cdd:COG0488 508 RE 509
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
12-256 |
3.30e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.10 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 12 HLSFPgFNGDV-HALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMrllptGSYCVHRGQISLLGEDVLNAREKQLRQwr 90
Cdd:PRK13648 12 NVSFQ-YQSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMI-----GIEKVKSGEIFYNNQAITDDNFEKLRK-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 91 gaRVAMIFQEPMTALnptrrIG-LQMMDVI--RHHQPISRREARAKAIALLEEMqipDAVEVMSRYPFELSGGMRQRVMI 167
Cdd:PRK13648 84 --HIGIVFQNPDNQF-----VGsIVKYDVAfgLENHAVPYDEMHRRVSEALKQV---DMLERADYEPNALSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 168 ALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESGVTADVIHH 247
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
....*....
gi 446115710 248 PRHPYTIGL 256
Cdd:PRK13648 233 AEELTRIGL 241
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-245 |
3.76e-16 |
|
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: 79.02 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPGfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAmlimRLLpTGSYCVHRGQISLLGEDvlnarekq 85
Cdd:COG4618 331 LSVENLTVVPPG--SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLA----RLL-VGVWPPTAGSVRLDGAD-------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 LRQWRGARVAmifqepmtalnptRRIGLQMMDV------IRhhQPISR-REARAKAIalLEEMQIPDAVEVMSRYP---- 154
Cdd:COG4618 396 LSQWDREELG-------------RHIGYLPQDVelfdgtIA--ENIARfGDADPEKV--VAAAKLAGVHEMILRLPdgyd 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 155 -------FELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHkARASGTAVLFISHDMAVVSQlCDSV 227
Cdd:COG4618 459 trigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRA-LKARGATVVVITHRPSLLAA-VDKL 536
|
250
....*....|....*...
gi 446115710 228 YVMYAGSVIESGVTADVI 245
Cdd:COG4618 537 LVLRDGRVQAFGPRDEVL 554
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-235 |
4.06e-16 |
|
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: 75.97 E-value: 4.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFPGfNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGEDVLNAREK 84
Cdd:cd03248 11 IVKFQNVTFAYPT-RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENF-----YQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRQwrgaRVAMIFQEP-MTALNPTRRIGLQMMDVirHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPfELSGGMRQ 163
Cdd:cd03248 85 YLHS----KVSLVGQEPvLFARSLQDNIAYGLQSC--SFECVKEAAQKAHAHSFISELASGYDTEVGEKGS-QLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115710 164 RVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARAsgTAVLFISHDMAVVSQlCDSVYVMYAGSV 235
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-244 |
4.12e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.97 E-value: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 21 DVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTgsycvHRGQISLLGEdVLNAREKQLRQWRgARVAMIFQE 100
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRP-----QKGAVLWQGK-PLDYSKRGLLALR-QQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 101 PMTALNPT---RRIGLQMMDVIRHHQPISRRearakaiaLLEEMQIPDAvEVMSRYPFE-LSGGMRQRVMIALAFSCEPQ 176
Cdd:PRK13638 86 PEQQIFYTdidSDIAFSLRNLGVPEAEITRR--------VDEALTLVDA-QHFRHQPIQcLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115710 177 LIIADEPTTALDVTVQLQVLRLLKHKArASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADV 244
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIV-AQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-248 |
4.76e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.61 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAREKQLRQWRgaRVAMIFQEP--- 101
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLNRLRR--QVSMVHPKPnlf 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 102 -MTALNPT----RRIG----LQMMDVIrhhqpisrrEARAKAIALLEEMQipdavEVMSRYPFELSGGMRQRVMIALAFS 172
Cdd:PRK14258 101 pMSVYDNVaygvKIVGwrpkLEIDDIV---------ESALKDADLWDEIK-----HKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 173 CEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYA-----GSVIESGVTADVIHH 247
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNS 246
|
.
gi 446115710 248 P 248
Cdd:PRK14258 247 P 247
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-239 |
5.96e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 78.61 E-value: 5.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFPGfNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTGsycvhrGQISLLGEDVLNARE 83
Cdd:TIGR00958 478 LIEFQDVSFSYPN-RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYqPTG------GQVLLDGVPLVQYDH 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQLRQwrgaRVAMIFQEPM---------TALNPTRRIGLQMMDVIRhhqpisrreaRAKAIALLEEMQIPDAVEVMSRYP 154
Cdd:TIGR00958 551 HYLHR----QVALVGQEPVlfsgsvrenIAYGLTDTPDEEIMAAAK----------AANAHDFIMEFPNGYDTEVGEKGS 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 155 FeLSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQlqvlRLLKHKARASGTAVLFISHDMAVVSQlCDSVYVMYAGS 234
Cdd:TIGR00958 617 Q-LSGGQKQRIAIARALVRKPRVLILDEATSALDAECE----QLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGS 690
|
....*
gi 446115710 235 VIESG 239
Cdd:TIGR00958 691 VVEMG 695
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-216 |
7.27e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.18 E-value: 7.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 8 IQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSvTamlIMRLLpTGSYCVHRGQISLLgedvlnarekqlr 87
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKS-T---LLKIL-AGELEPDSGEVSIP------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 88 qwRGARVAMIFQEP------------MTALNPTRRIGLQM-----------MDVIRHHQPISR--------REARAKAIa 136
Cdd:COG0488 59 --KGLRIGYLPQEPpldddltvldtvLDGDAELRALEAELeeleaklaepdEDLERLAELQEEfealggweAEARAEEI- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 137 lLEEMQIPDAV--EVMSrypfELSGGMRQRVMIALAFSCEPQLIIADEPTTALDV-TVQ-LQvlRLLKhkaRASGTaVLF 212
Cdd:COG0488 136 -LSGLGFPEEDldRPVS----ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIEwLE--EFLK---NYPGT-VLV 204
|
....
gi 446115710 213 ISHD 216
Cdd:COG0488 205 VSHD 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-239 |
8.25e-16 |
|
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: 74.84 E-value: 8.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 29 SLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVlNAREKQLRQwrgarVAMIFQEP--MTALN 106
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQS-----GRVLINGVDV-TAAPPADRP-----VSMLFQENnlFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 107 PTRRIGLQMMDVIRhhqpiSRREARAKAIALLEEMQIPdavEVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTA 186
Cdd:cd03298 87 VEQNVGLGLSPGLK-----LTAEDRQAIEVALARVGLA---GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446115710 187 LDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
20-278 |
1.47e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.19 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTgsycvHRGQISLLGEDVLNAREKQLRQWRgARVAMIFQ 99
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAP-----DHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 EP--MTALNPTRRIGLQMmdviRHHQPISRREARAKAIALLEEMQIPDAVEVMsryPFELSGGMRQRVMIALAFSCEPQL 177
Cdd:PRK11831 92 SGalFTDMNVFDNVAYPL----REHTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 178 IIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADvihhprhpytiglL 257
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA-------------L 231
|
250 260
....*....|....*....|..
gi 446115710 258 QCAPEHGVpRQLLPAIP-GTVP 278
Cdd:PRK11831 232 QANPDPRV-RQFLDGIAdGPVP 252
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
14-247 |
4.30e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.83 E-value: 4.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 14 SFPGfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGEDVLNAREKQLRQwrgaR 93
Cdd:PRK11176 350 TYPG--KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRF-----YDIDEGEILLDGHDLRDYTLASLRN----Q 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 94 VAMIFQEpMTALNPT--RRIGLQMMDVIRHHQpISRREARAKAIALLEEMqiPDAVE-VMSRYPFELSGGMRQRVMIALA 170
Cdd:PRK11176 419 VALVSQN-VHLFNDTiaNNIAYARTEQYSREQ-IEEAARMAYAMDFINKM--DNGLDtVIGENGVLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 171 FSCEPQLIIADEPTTALDV----TVQLQVLRLLKHKarasgtAVLFISHDMAVVSQlCDSVYVMYAGSVIESGVTADVIH 246
Cdd:PRK11176 495 LLRDSPILILDEATSALDTeserAIQAALDELQKNR------TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567
|
.
gi 446115710 247 H 247
Cdd:PRK11176 568 Q 568
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-245 |
7.76e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.10 E-value: 7.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPV--LDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDV 78
Cdd:PRK10253 1 MTESVarLRGEQLTLGY----GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAH-----GHVWLDGEHI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 79 LNAREKQLRQwrgaRVAMIFQEPMTALNPTRRiglQMMDVIRH-HQPISRREARAKAIALLEEMQIPDAVEVMSRYPFEL 157
Cdd:PRK10253 72 QHYASKEVAR----RIGLLAQNATTPGDITVQ---ELVARGRYpHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 158 SGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIE 237
Cdd:PRK10253 145 SGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVA 224
|
250
....*....|...
gi 446115710 238 SG-----VTADVI 245
Cdd:PRK10253 225 QGapkeiVTAELI 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-239 |
8.40e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 75.00 E-value: 8.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 7 DIQQLHLSFpGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTGsycvhrGQISLLGEDVLNAREKQ 85
Cdd:PRK13657 334 AVEFDDVSF-SYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFdPQS------GRILIDGTDIRTVTRAS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 LRQwrgaRVAMIFQEPMTaLNptRRIGlqmmDVIRhhqpisrreaRAKAIALLEEM----QIPDAVEVMSRYP--FE--- 156
Cdd:PRK13657 407 LRR----NIAVVFQDAGL-FN--RSIE----DNIR----------VGRPDATDEEMraaaERAQAHDFIERKPdgYDtvv 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 157 ------LSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVlfISHDMAVVSQlCDSVYVM 230
Cdd:PRK13657 466 gergrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI--IAHRLSTVRN-ADRILVF 542
|
....*....
gi 446115710 231 YAGSVIESG 239
Cdd:PRK13657 543 DNGRVVESG 551
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
25-239 |
1.48e-14 |
|
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: 71.04 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSvTAM--LIMRLLPTGsycvhrgqisLLGEDVLNAREKQLRQWRgARVAMIFQEPM 102
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKS-TLLnaLAGRRTGLG----------VSGEVLINGRPLDKRSFR-KIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 103 talnptrriglqmmdvirHHQPISRREArakaialleeMQIpdAVEVMSrypfeLSGGMRQRVMIALAFSCEPQLIIADE 182
Cdd:cd03213 93 ------------------LHPTLTVRET----------LMF--AAKLRG-----LSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446115710 183 PTTALDVTVQLQVLRLLKHKARaSGTAVLFISHDM-AVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03213 138 PTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-235 |
2.22e-14 |
|
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: 71.05 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 29 SLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQlrqwrgARVAMIFQEP--MTALN 106
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPAS-----GSIKVNDQSHTGLAPYQ------RPVSMLFQENnlFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 107 PTRRIGLQMMDVIRHHQpisrrEARAKAIALLEEMQIPDaveVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTA 186
Cdd:TIGR01277 87 VRQNIGLGLHPGLKLNA-----EQQEKVVDAAQQVGIAD---YLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446115710 187 LDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:TIGR01277 159 LDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
24-239 |
2.68e-14 |
|
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: 70.99 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 24 ALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQLRQwrgaRVAMIFQEPmT 103
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSS-----GSILIDGVDISKIGLHDLRS----RISIIPQDP-V 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 104 ALNPTRRIGLqmmDVIRHHQPisrrEARAKAialLEEMQIPDAVEVMS---RYPFE-----LSGGMRQRVMIALAFSCEP 175
Cdd:cd03244 89 LFSGTIRSNL---DPFGEYSD----EELWQA---LERVGLKEFVESLPgglDTVVEeggenLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115710 176 QLIIADEPTTALDVTVQLQVLRLLKHKarASGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESG 239
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREA--FKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-248 |
4.00e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.18 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPGfngDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVlNAREKQ 85
Cdd:PRK11650 4 LKLQAVRKSYDG---KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITS-----GEIWIGGRVV-NELEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 LRQwrgarVAMIFQEpmTALNP--TRR----IGLQMMDVIRHHqpISRREARAKAIALLEEMqipdavevMSRYPFELSG 159
Cdd:PRK11650 75 DRD-----IAMVFQN--YALYPhmSVRenmaYGLKIRGMPKAE--IEERVAEAARILELEPL--------LDRKPRELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 160 GMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQvLRL-LKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIES 238
Cdd:PRK11650 138 GQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ-MRLeIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQI 216
|
250
....*....|
gi 446115710 239 GVTADVIHHP 248
Cdd:PRK11650 217 GTPVEVYEKP 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-265 |
4.16e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.17 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 24 ALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTgsycvHRGQISLLGEDVLNAREKQlrqwrGAR--VAMIFQEP 101
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRP-----QKGKVLVSGIDTGDFSKLQ-----GIRklVGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 102 MTAL---NPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQipdavevmSRYPFELSGGMRQRVMIALAFSCEPQLI 178
Cdd:PRK13644 87 ETQFvgrTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYR--------HRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 179 IADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVsQLCDSVYVMYAGSVIESGVTADVIHHPR-------HP 251
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIK-KLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSlqtlgltPP 236
|
250
....*....|....
gi 446115710 252 YTIGLLQCAPEHGV 265
Cdd:PRK13644 237 SLIELAENLKMHGV 250
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-244 |
4.62e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.73 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 28 VSLQINRSEIVGLVGESGSGKSvTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQLRQWRgarvAMIFQEPMTALNp 107
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKS-TLLARMAGLLPGS-----GSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFA- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 108 trriglqmMDVIRH---HQPISRREAR-AKAIALLEEM-QIPDAVEVMSRypfELSGGMRQRVMIALAF-----SCEP-- 175
Cdd:PRK03695 84 --------MPVFQYltlHQPDKTRTEAvASALNEVAEAlGLDDKLGRSVN---QLSGGEWQRVRLAAVVlqvwpDINPag 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446115710 176 QLIIADEPTTALDVTVQLQVLRLLKHKARAsGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADV 244
Cdd:PRK03695 153 QLLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
25-278 |
9.55e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.20 E-value: 9.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrgqisllGEDVLNarEKQLRQWRG---AR-VAMIFQE 100
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSE-----------GEILLD--AQPLESWSSkafARkVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 101 PMTALNPTRRiglQMMDVIRH--HQPISR-----REARAKAIALLeemqipDAVEVMSRYPFELSGGMRQRVMIALAFSC 173
Cdd:PRK10575 94 LPAAEGMTVR---ELVAIGRYpwHGALGRfgaadREKVEEAISLV------GLKPLAHRLVDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 174 EPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHPrhpyT 253
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE----T 240
|
250 260
....*....|....*....|....*
gi 446115710 254 IGLLqcapeHGVPRQLLPAIPGTVP 278
Cdd:PRK10575 241 LEQI-----YGIPMGILPHPAGAAP 260
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
24-239 |
1.14e-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: 68.98 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 24 ALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQLRQwrgaRVAMIFQEPmT 103
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLE-----AEEGKIEIDGIDISTIPLEDLRS----SLTIIPQDP-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 104 ALNPTRRIGLqmmDVIRHHqpisrrearakaiallEEMQIPDAVEVmSRYPFELSGGMRQRVMIALAFSCEPQLIIADEP 183
Cdd:cd03369 93 LFSGTIRSNL---DPFDEY----------------SDEEIYGALRV-SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446115710 184 TTALDVTVQLQVLRLLKHKarASGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESG 239
Cdd:cd03369 153 TASIDYATDALIQKTIREE--FTNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-245 |
1.33e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.30 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 14 SFPGfngdVHALNNVSLQINRSEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGEDVLNAREKQLRQwrgAR 93
Cdd:PRK10982 7 SFPG----VKALDNVNLKVRPHSIHALMGENGAGKST----LLKCL-FGIYQKDSGSILFQGKEIDFKSSKEALE---NG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 94 VAMIFQEpmtaLNPTRRigLQMMDVI---RHHQP---ISRREARAKAIALLEEMQIP-DAVEVMSrypfELSGGMRQRVM 166
Cdd:PRK10982 75 ISMVHQE----LNLVLQ--RSVMDNMwlgRYPTKgmfVDQDKMYRDTKAIFDELDIDiDPRAKVA----TLSVSQMQMIE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 167 IALAFSCEPQLIIADEPTTAL---DVTVQLQVLRLLKHKarasGTAVLFISHDMAVVSQLCDSVYVMYAGSVIE----SG 239
Cdd:PRK10982 145 IAKAFSYNAKIVIMDEPTSSLtekEVNHLFTIIRKLKER----GCGIVYISHKMEEIFQLCDEITILRDGQWIAtqplAG 220
|
....*.
gi 446115710 240 VTADVI 245
Cdd:PRK10982 221 LTMDKI 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
20-257 |
1.62e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.44 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQIsLLGEDVLNAREKQLRQwrgarVAMIFQ 99
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITS-----GDL-FIGEKRMNDVPPAERG-----VGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 EpmTALNPTRRI------GLQMMDVIRhhqpiSRREARAKAIAllEEMQIPDAVEvmsRYPFELSGGMRQRVMIALAFSC 173
Cdd:PRK11000 83 S--YALYPHLSVaenmsfGLKLAGAKK-----EEINQRVNQVA--EVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 174 EPQLIIADEPTTALD----VTVQLQVLRLlkHKARasGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHPR 249
Cdd:PRK11000 151 EPSVFLLDEPLSNLDaalrVQMRIEISRL--HKRL--GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
....*...
gi 446115710 250 HPYTIGLL 257
Cdd:PRK11000 227 NRFVAGFI 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-230 |
1.97e-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: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSvtamlimRLLptgsycvhrgQIsLLGEdvlnarekq 85
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKS-------TLL----------KL-IAGE--------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 86 lrqwrgarvamifqepmtaLNPTRRIglqmmdvIRHHQPISrrearakaIALLEEmqipdavevmsrypfeLSGGMRQRV 165
Cdd:cd03221 50 -------------------LEPDEGI-------VTWGSTVK--------IGYFEQ----------------LSGGEKMRL 79
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115710 166 MIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARasgtAVLFISHDMAVVSQLCDSVYVM 230
Cdd:cd03221 80 ALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIEL 140
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-247 |
5.45e-13 |
|
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: 69.47 E-value: 5.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIMrllptGSY-CVHRGQISLLGEDVlNAREKQlrQWRGARVAMIFQE-PM 102
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALF-----GAYpGKFEGNVFINGKPV-DIRNPA--QAIRAGIAMVPEDrKR 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 103 TALNPTRRIGLQM-MDVIRHHQPISRREARAKAIALLEEMQipdAVEVMSRYPF----ELSGGMRQRVMIALAFSCEPQL 177
Cdd:TIGR02633 348 HGIVPILGVGKNItLSVLKSFCFKMRIDAAAELQIIGSAIQ---RLKVKTASPFlpigRLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 178 IIADEPTTALDVTVQLQVLRLLKHKARaSGTAVLFISHDMAVVSQLCDSVYVMYAGSviesgVTADVIHH 247
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGK-----LKGDFVNH 488
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-236 |
7.37e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.21 E-value: 7.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVtamlimrLLPT--GSYCVHRGQISLLGEDV 78
Cdd:PRK11614 1 MEKVMLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTT-------LLGTlcGDPRATSGRIVFDGKDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 79 lnarekqlRQWRGARvamIFQEPMTALNPTRRI--------GLQMMDVIRHHQPISRREARAKAIalleemqIPDAVEVM 150
Cdd:PRK11614 70 --------TDWQTAK---IMREAVAIVPEGRRVfsrmtveeNLAMGGFFAERDQFQERIKWVYEL-------FPRLHERR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 151 SRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVM 230
Cdd:PRK11614 132 IQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIE-QLREQGMTIFLVEQNANQALKLADRGYVL 210
|
....*.
gi 446115710 231 YAGSVI 236
Cdd:PRK11614 211 ENGHVV 216
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
9-215 |
7.91e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.91 E-value: 7.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 9 QQLHLSFpgfngdvhalnnvSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQlrq 88
Cdd:PRK10771 12 HHLPMRF-------------DLTVERGERVAILGPSGAGKSTLLNLIAGFLT-----PASGSLTLNGQDHTTTPPSR--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 89 wrgaR-VAMIFQEP--MTALNPTRRIGLQMMDVIR--HHQpisrreaRAKAIALLEEMQIPDaveVMSRYPFELSGGMRQ 163
Cdd:PRK10771 71 ----RpVSMLFQENnlFSHLTVAQNIGLGLNPGLKlnAAQ-------REKLHAIARQMGIED---LLARLPGQLSGGQRQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446115710 164 RVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISH 215
Cdd:PRK10771 137 RVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
27-248 |
9.57e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.98 E-value: 9.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 27 NVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PtgsycvHRGQISLlGEDVLNAREKQL------RqwrgaRVAMIFQ 99
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTrP------QKGRIVL-NGRVLFDAEKGIclppekR-----RIGYVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 EpmTALNPTRRIGLQMMDVIRHhqpiSRREARAKAIALLeemqipdAVE-VMSRYPFELSGGMRQRVMIALAFSCEPQLI 178
Cdd:PRK11144 84 D--ARLFPHYKVRGNLRYGMAK----SMVAQFDKIVALL-------GIEpLLDRYPGSLSGGEKQRVAIGRALLTAPELL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 179 IADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHP 248
Cdd:PRK11144 151 LMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-239 |
1.31e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.21 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 7 DIQQLHLSFpGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMrllptGSYCVHRGQISLLGEDVLNAREKQL 86
Cdd:PRK10790 340 RIDIDNVSF-AYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLM-----GYYPLTEGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 87 RQwrgaRVAMIFQEPMTalnptrriglqMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPF--------ELS 158
Cdd:PRK10790 414 RQ----GVAMVQQDPVV-----------LADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYtplgeqgnNLS 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 159 GGMRQRVMIALAFSCEPQLIIADEPTTALDV----TVQlQVLRLLKHKarasgTAVLFISHDMAVVSQlCDSVYVMYAGS 234
Cdd:PRK10790 479 VGQKQLLALARVLVQTPQILILDEATANIDSgteqAIQ-QALAAVREH-----TTLVVIAHRLSTIVE-ADTILVLHRGQ 551
|
....*
gi 446115710 235 VIESG 239
Cdd:PRK10790 552 AVEQG 556
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-237 |
2.80e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 21 DVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDV-----LNAREKQL------RQW 89
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG-----GEIRLNGKDIsprspLDAVKKGMayitesRRD 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 90 RGARVAMIFQEPMTALNPTRRIGLQ-MMDVIRHHQPISRREARAKAIALleemqipdAVEVMSRYPFELSGGMRQRVMIA 168
Cdd:PRK09700 350 NGFFPNFSIAQNMAISRSLKDGGYKgAMGLFHEVDEQRTAENQRELLAL--------KCHSVNQNITELSGGNQQKVLIS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446115710 169 LAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARaSGTAVLFISHDMAVVSQLCDSVYVMYAGSVIE 237
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-229 |
6.99e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 64.35 E-value: 6.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 32 INRSEIVGLVGESGSGKSVTA-MLIMRLLPTGsycvhrGQISLLGEDVlnarekqlrQWRGARVAMIFQEPMTALnptrr 110
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIkMLAGVLKPDE------GDIEIELDTV---------SYKPQYIKADYEGTVRDL----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 111 iglqMMDVIRHH--QPISRREarakaiaLLEEMQIPDaveVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALD 188
Cdd:cd03237 82 ----LSSITKDFytHPYFKTE-------IAKPLQIEQ---ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446115710 189 VTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYV 229
Cdd:cd03237 148 VEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
20-235 |
9.03e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 64.31 E-value: 9.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVtamlIMRLL-----PTGsycvhrGQIsLLGEDVLNAREKQLRqwrgarv 94
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKST----LLRLLagletPSA------GEL-LAGTAPLAEAREDTR------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 95 aMIFQEpmTALNPTRRI----GLQMmdvirhhqpisRREARAKAIALLEEMQIPD-AVEvmsrYPFELSGGMRQRVMIAL 169
Cdd:PRK11247 85 -LMFQD--ARLLPWKKVidnvGLGL-----------KGQWRDAALQALAAVGLADrANE----WPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115710 170 AFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
20-239 |
9.59e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.14 E-value: 9.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAmlimrlLPTgsycvhrgqiSLLGEDVlNAREKQLRQW----RGARVA 95
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA------LPA----------HV*GPDA-GRRPWRF*TWcanrRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 96 MIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVevmSRYPFELSGGMRQRVMIALAFSCEP 175
Cdd:NF000106 87 IG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAA---GRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115710 176 QLIIADEPTTALDVTVQLQVLRLLKHKARaSGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-233 |
1.05e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 12 HLSFPGfngdvhaLNNVSLQINRSEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGEDVlNAREKQL----- 86
Cdd:PRK10762 262 NLSGPG-------VNDVSFTLRKGEILGVSGLMGAGRTE----LMKVL-YGALPRTSGYVTLDGHEV-VTRSPQDglang 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 87 -------RQWRGARVAMIFQEPM--TALNPTRRIGLQmmdvIRHHQpisRREARAKAIALLEeMQIPDavevMSRYPFEL 157
Cdd:PRK10762 329 ivyisedRKRDGLVLGMSVKENMslTALRYFSRAGGS----LKHAD---EQQAVSDFIRLFN-IKTPS----MEQAIGLL 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115710 158 SGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLI-NQFKAEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-230 |
1.14e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 23 HALNNVSLQINRSEIVGLVGESGSGKSVtamlIMRLLptgsycvhrgqisllgedvlnarekqLRQWRGARVAMIFQEPM 102
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKST----LLRLL--------------------------AGALKGTPVAGCVDVPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 103 TALNPTRRIglqmmdvIRHhqpISRREARAKAIALLEEMQIPDAVEVMSRYPfELSGGMRQRVMIALAFSCEPQLIIADE 182
Cdd:COG2401 94 NQFGREASL-------IDA---IGRKGDFKDAVELLNAVGLSDAVLWLRRFK-ELSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446115710 183 PTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVM 230
Cdd:COG2401 163 FCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-225 |
1.70e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 63.65 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 2 TQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNA 81
Cdd:PRK14243 7 TETVLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 82 REKQLRQWRgaRVAMIFQEPmtalNP------------TRRIGLQM-MD--VIRhhqpiSRREArakaiALLEEMQipda 146
Cdd:PRK14243 83 DVDPVEVRR--RIGMVFQKP----NPfpksiydniaygARINGYKGdMDelVER-----SLRQA-----ALWDEVK---- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446115710 147 vEVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARAsgTAVLFISHDMAVVSQLCD 225
Cdd:PRK14243 143 -DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSD 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
156-229 |
2.46e-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: 2.46e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115710 156 ELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYV 229
Cdd:COG1245 455 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-239 |
3.36e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 62.72 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 3 QPVLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSvTAMLIMRLLPTGSYCVHrGQISLLGEDVLNAR 82
Cdd:PRK09984 2 QTIIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKS-TLLRHLSGLITGDKSAG-SHIELLGRTVQREG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 83 E--KQLRQWRgARVAMIFQEpmtaLNPTRRIGLqMMDVI---RHHQPISRrearaKAIALLEEMQIPDAVEVMSRYPF-- 155
Cdd:PRK09984 76 RlaRDIRKSR-ANTGYIFQQ----FNLVNRLSV-LENVLigaLGSTPFWR-----TCFSWFTREQKQRALQALTRVGMvh 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 156 -------ELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVY 228
Cdd:PRK09984 145 fahqrvsTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIV 224
|
250
....*....|.
gi 446115710 229 VMYAGSVIESG 239
Cdd:PRK09984 225 ALRQGHVFYDG 235
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
137-229 |
5.03e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 137 LLEEMQIPDaveVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHD 216
Cdd:PRK13409 437 IIKPLQLER---LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD 513
|
90
....*....|...
gi 446115710 217 MAVVSQLCDSVYV 229
Cdd:PRK13409 514 IYMIDYISDRLMV 526
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-239 |
5.33e-11 |
|
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: 63.30 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 12 HLSFpGFNGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGEDVLNAREKQLRqwrg 91
Cdd:COG5265 362 NVSF-GYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF-----YDVTSGRILIDGQDIRDVTQASLR---- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 92 ARVAMIFQEpmTAL-NPTrrIGLQmmdvIRHHQP-ISRREARAKA-IALLEE--MQIPDAVE--VMSRyPFELSGGMRQR 164
Cdd:COG5265 432 AAIGIVPQD--TVLfNDT--IAYN----IAYGRPdASEEEVEAAArAAQIHDfiESLPDGYDtrVGER-GLKLSGGEKQR 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115710 165 VMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARasGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESG 239
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-231 |
6.78e-11 |
|
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: 61.61 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 36 EIVGLVGESGSGKSvTAMLIM--RLLPtgSYCVHRGQISLlgEDVLNArekqlrqWRGARVamifQEPMTALNPTRrigl 113
Cdd:cd03236 27 QVLGLVGPNGIGKS-TALKILagKLKP--NLGKFDDPPDW--DEILDE-------FRGSEL----QNYFTKLLEGD---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 114 qmMDVIRHHQPISR--REARAKAIALLEEM-------QIPDAVE---VMSRYPFELSGGMRQRVMIALAFSCEPQLIIAD 181
Cdd:cd03236 87 --VKVIVKPQYVDLipKAVKGKVGELLKKKdergkldELVDQLElrhVLDRNIDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446115710 182 EPTTALDVTVQLQVLRLLKHKARaSGTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:cd03236 165 EPSSYLDIKQRLNAARLIRELAE-DDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-247 |
7.61e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.99 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 19 NGDVH-ALNNVSLQINRSEIVGLVGESGSGKSVTAMLImrllpTGSYCVHRGQISLLGEDVLNAREKQLrqwrgarvami 97
Cdd:PRK13545 33 DGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLI-----AGVTMPNKGTVDIKGSAALIAISSGL----------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 98 fQEPMTALNPTRRIGLqMMDVIRhhqpisrrearakaiallEEMQ--IPDAVEVMSRYPF------ELSGGMRQRVMIAL 169
Cdd:PRK13545 97 -NGQLTGIENIELKGL-MMGLTK------------------EKIKeiIPEIIEFADIGKFiyqpvkTYSSGMKSRLGFAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115710 170 AFSCEPQLIIADEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHH 247
Cdd:PRK13545 157 SVHINPDILVIDEALSVGDQTFTKKCLDKM-NEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-239 |
8.62e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.83 E-value: 8.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTamliMRLLpTGSYCVHRGQISLLGEDVlNAREKQLRqwrgarvamifq 99
Cdd:NF033858 277 GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTT----MKML-TGLLPASEGEAWLFGQPV-DAGDIATR------------ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 epmtalnptRRIG--------------LQMMDVirH----HQPISRREARAKAiaLLEEMqipDAVEVMSRYPFELSGGM 161
Cdd:NF033858 339 ---------RRVGymsqafslygeltvRQNLEL--HarlfHLPAAEIAARVAE--MLERF---DLADVADALPDSLPLGI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 162 RQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVlFIS-HDM--AvvsQLCDSVYVMYAGSVIES 238
Cdd:NF033858 403 RQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTI-FIStHFMneA---ERCDRISLMHAGRVLAS 478
|
.
gi 446115710 239 G 239
Cdd:NF033858 479 D 479
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-227 |
8.97e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.28 E-value: 8.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISllgedvlnaREKQLRQwrGARVAMIFQ 99
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDE-----GVIK---------RNGKLRI--GYVPQKLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 EPMTALNPTR----RIGLQMMDVIrhhqPISRRearAKAIALLEE-MQipdavevmsrypfELSGGMRQRVMIALAFSCE 174
Cdd:PRK09544 79 DTTLPLTVNRflrlRPGTKKEDIL----PALKR---VQAGHLIDApMQ-------------KLSGGETQRVLLARALLNR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446115710 175 PQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSV 227
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
156-249 |
1.29e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 156 ELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHkaRASGTAVLFISHDMAVVSQLCDSVYVMYAgsv 235
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRE--LAEGKYVLVVEHDLAVLDYLADNVHIAYG--- 286
|
90
....*....|....
gi 446115710 236 iESGVTAdVIHHPR 249
Cdd:PRK13409 287 -EPGAYG-VVSKPK 298
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-233 |
1.91e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.73 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIMrllptG-SYcvhrGQ-ISllGEDVLNAREKQLRQWRGARVAMIfqepM 102
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVF-----GrSY----GRnIS--GTVFKDGKEVDVSTVSDAIDAGL----A 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 103 TALNPTRRIGLQMMDVIRHH------QPISRR----EARAKAIAllEE----MQI--PDAVEVMSRypfeLSGGMRQRVM 166
Cdd:NF040905 341 YVTEDRKGYGLNLIDDIKRNitlanlGKVSRRgvidENEEIKVA--EEyrkkMNIktPSVFQKVGN----LSGGNQQKVV 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446115710 167 IALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKArASGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:NF040905 415 LSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELA-AEGKGVIVISSELPELLGMCDRIYVMNEG 480
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
24-234 |
1.94e-10 |
|
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: 59.41 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 24 ALNNVSLQINRSEIVGLVGESGSGKSvtaMLIMRLLptGSYCVHRGQISLLGedvlnarekqlrqwrgaRVAMIFQEPMt 103
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKS---SLLSALL--GELEKLSGSVSVPG-----------------SIAYVSQEPW- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 104 ALNPTRRiglqmmDVIRHHQPI-SRREARA-KAIALLEEMQI-P--DAVEVMSRyPFELSGGMRQRVMIALAFSCEPQLI 178
Cdd:cd03250 77 IQNGTIR------ENILFGKPFdEERYEKViKACALEPDLEIlPdgDLTEIGEK-GINLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446115710 179 IADEPTTALDVTVQLQVL-RLLKHKARASGTAVLfISHDMAVVSQlCDSVYVMYAGS 234
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRIL-VTHQLQLLPH-ADQIVVLDNGR 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
156-231 |
2.95e-10 |
|
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: 60.95 E-value: 2.95e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115710 156 ELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARaSGTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAE-EGKYVLVVEHDLAILDYLADYVHILY 286
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-237 |
6.72e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 6.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSF-PGFNGDVHALnnvSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREK 84
Cdd:PLN03232 1235 IKFEDVHLRYrPGLPPVLHGL---SFFVSPSEKVGVVGRTGAGKSSMLNALFRIVE-----LEKGRIMIDDCDVAKFGLT 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRqwrgaRVAMIFQEPMTALNPTRRIGLqmmDVIRHHQPISRREArakaialLEEMQIPDAVevmSRYPFEL------- 157
Cdd:PLN03232 1307 DLR-----RVLSIIPQSPVLFSGTVRFNI---DPFSEHNDADLWEA-------LERAHIKDVI---DRNPFGLdaevseg 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 158 ----SGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARAsgTAVLFISHDMAVVSQlCDSVYVMYAG 233
Cdd:PLN03232 1369 genfSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS--CTMLVIAHRLNTIID-CDKILVLSSG 1445
|
....
gi 446115710 234 SVIE 237
Cdd:PLN03232 1446 QVLE 1449
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-239 |
8.54e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.86 E-value: 8.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycvHRGQISLLGEDVlnaREKQLRQWRgARVAMIFQEPMTa 104
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP------YQGSLKINGIEL---RELDPESWR-KHLSWVGQNPQL- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 105 LNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEM------QIPDAvevMSRypfeLSGGMRQRVMIALAFSCEPQLI 178
Cdd:PRK11174 435 PHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLpqgldtPIGDQ---AAG----LSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115710 179 IADEPTTALDVTVQLQVLRLLKHKARasGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESG 239
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQG 565
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-233 |
1.52e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.12 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIMrllptgsycvhrGQI---SLLGEDVLNARE--KQLRQwrgaRVAMIFQ 99
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALA------------GRIqgnNFTGTILANNRKptKQILK----RTGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 EPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPF--ELSGGMRQRVMIALAFSCEPQL 177
Cdd:PLN03211 148 DDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFirGISGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446115710 178 IIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEG 283
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-239 |
2.24e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.87 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 24 ALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKqLRQWRGarvamifqepmt 103
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTS-----GTVLVGGKDIETNLDA-VRQSLG------------ 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 104 aLNPTRRIGLQMMDVIRHH------QPISRREARAKAIALLEEMQIPDAVEVMSRypfELSGGMRQRVMIALAFSCEPQL 177
Cdd:TIGR01257 1007 -MCPQHNILFHHLTVAEHIlfyaqlKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQ---DLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115710 178 IIADEPTTALDVTVQLQVLR-LLKHKaraSGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDlLLKYR---SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-243 |
2.31e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.14 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 4 PVLDIQQLHLSFPGfngdVHALNNVSLQINRSEIVGLVGESGSGKSvTAMLIMR-LLPTGSycvhrGQISLLGEDVLNAR 82
Cdd:PRK15439 10 PLLCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKS-TLMKIIAgIVPPDS-----GTLEIGGNPCARLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 83 EKQLRQWRgarVAMIFQEPMTALNPTRR----IGLQmmdvirhhqpiSRREARAKAIALLEEMQI---PDA----VEVMS 151
Cdd:PRK15439 80 PAKAHQLG---IYLVPQEPLLFPNLSVKenilFGLP-----------KRQASMQKMKQLLAALGCqldLDSsagsLEVAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 152 RYPFE-LSGGMRqrvmialafscEPQLIIADEPTTALdvtVQLQVLRLLKH--KARASGTAVLFISHDMAVVSQLCDSVY 228
Cdd:PRK15439 146 RQIVEiLRGLMR-----------DSRILILDEPTASL---TPAETERLFSRirELLAQGVGIVFISHKLPEIRQLADRIS 211
|
250
....*....|....*
gi 446115710 229 VMYAGSVIESGVTAD 243
Cdd:PRK15439 212 VMRDGTIALSGKTAD 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
153-215 |
2.98e-09 |
|
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: 55.24 E-value: 2.98e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115710 153 YPF--ELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhkarASGTAVLFISH 215
Cdd:cd03223 86 YPWddVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-215 |
3.30e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.89 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQLHLSFPgfNGDVhALNNVSLQINRSEIVGLVGESGSGKSvtamLIMR----LLPTGSycvhrGQISLLgedvlna 81
Cdd:COG4178 363 LALEDLTLRTP--DGRP-LLEDLSLSLKPGERLLITGPSGSGKS----TLLRaiagLWPYGS-----GRIARP------- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 82 rekqlrqwRGARVAMIFQEPMTALNPTRriglqmmDVI---RHHQPISRREARAkaiaLLEEMQIPDAVEVM------SR 152
Cdd:COG4178 424 --------AGARVLFLPQRPYLPLGTLR-------EALlypATAEAFSDAELRE----ALEAVGLGHLAERLdeeadwDQ 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115710 153 ypfELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHkaRASGTAVLFISH 215
Cdd:COG4178 485 ---VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-235 |
3.84e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.61 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 28 VSLQINRSEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGEDVlnarekQLRQWRGARVAMIfqepmtALNP 107
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSE----LMKLL-YGATRRTAGQVYLDGKPI------DIRSPRDAIRAGI------MLCP 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 108 TRR-----IGLQ-MMDVI-----RHHQP----ISRREARAKAIALLEEMQI--PDAVEVMSrypfELSGGMRQRVMIALA 170
Cdd:PRK11288 335 EDRkaegiIPVHsVADNInisarRHHLRagclINNRWEAENADRFIRSLNIktPSREQLIM----NLSGGNQQKAILGRW 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115710 171 FSCEPQLIIADEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:PRK11288 411 LSEDMKVILLDEPTRGIDVGAKHEIYNVI-YELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-239 |
1.05e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.18 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFPgfngDVHALNNVSLQINRSEIVGLVGESGSGKS-VTAMLIMRllptGSYCVHRGQISLLGEDVLnarE 83
Cdd:PRK09580 1 MLSIKDLHVSVE----DKAILRGLNLEVRPGEVHAIMGPNGSGKStLSATLAGR----EDYEVTGGTVEFKGKDLL---E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 84 KQLRQWRGARVAMIFQEPM------------TALNPTRRIglqmmdviRHHQPISRREARAKAIALLEEMQIPDavEVMS 151
Cdd:PRK09580 70 LSPEDRAGEGIFMAFQYPVeipgvsnqfflqTALNAVRSY--------RGQEPLDRFDFQDLMEEKIALLKMPE--DLLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 152 R-YPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVqLQVLRLLKHKARASGTAVLFISHDMAVVSQL-CDSVYV 229
Cdd:PRK09580 140 RsVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDA-LKIVADGVNSLRDGKRSFIIVTHYQRILDYIkPDYVHV 218
|
250
....*....|
gi 446115710 230 MYAGSVIESG 239
Cdd:PRK09580 219 LYQGRIVKSG 228
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
156-231 |
1.19e-08 |
|
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: 53.73 E-value: 1.19e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115710 156 ELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
5-248 |
1.46e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.87 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFPGfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGedvLNAREK 84
Cdd:PRK10789 313 ELDVNIRQFTYPQ--TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRH-----FDVSEGDIRFHD---IPLTKL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRQWRGaRVAMIFQEPMTalnptrriglqMMDVIRHHQPISRREA------RAKAIALLEE--MQIPDAVE-------V 149
Cdd:PRK10789 383 QLDSWRS-RLAVVSQTPFL-----------FSDTVANNIALGRPDAtqqeieHVARLASVHDdiLRLPQGYDtevgergV 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 150 MsrypfeLSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARasGTAVLFISHDMAVVSQlCDSVYV 229
Cdd:PRK10789 451 M------LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILV 521
|
250
....*....|....*....
gi 446115710 230 MYAGSVIESGVTADVIHHP 248
Cdd:PRK10789 522 MQHGHIAQRGNHDQLAQQS 540
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-247 |
3.11e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 26 NNVSLQINRSEIVGLVGESGSGKSVTAMLIMrllptGSYcvhRGQISllGEDVLNAREKQLRQWRGARVAMIfqepmtAL 105
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLF-----GAY---PGRWE--GEIFIDGKPVKIRNPQQAIAQGI------AM 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 106 NPT--RRIGL-QMMDVIrhhQPIS----RREARAKAI-ALLEEMQIPDAVE---VMSRYPF----ELSGGMRQRVMIALA 170
Cdd:PRK13549 343 VPEdrKRDGIvPVMGVG---KNITlaalDRFTGGSRIdDAAELKTILESIQrlkVKTASPElaiaRLSGGNQQKAVLAKC 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446115710 171 FSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARaSGTAVLFISHDMAVVSQLCDSVYVMYAGSviesgVTADVIHH 247
Cdd:PRK13549 420 LLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGK-----LKGDLINH 490
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-247 |
3.79e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.67 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 19 NGDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHR-GQISLLGEDV-LNAREKQLRQWRGARVAM 96
Cdd:PRK13546 34 NKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRnGEVSVIAISAgLSGQLTGIENIEFKMLCM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 97 IF-QEPMTALNPTRRIGLQMMDVIrhHQPISRrearakaialleemqipdavevmsrypfeLSGGMRQRVMIALAFSCEP 175
Cdd:PRK13546 114 GFkRKEIKAMTPKIIEFSELGEFI--YQPVKK-----------------------------YSSGMRAKLGFSINITVNP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115710 176 QLIIADEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHH 247
Cdd:PRK13546 163 DILVIDEALSVGDQTFAQKCLDKI-YEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-278 |
6.18e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.91 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSY---CVHRGQISLLGEDVLNAREKQLRQWRgarvAMIFQ-- 99
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAprgARVTGDVTLNGEPLAAIDAPRLARLR----AVLPQaa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 EPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALleemQIPDAVEVMSRYPFELSGGMRQRVMIALAFS------- 172
Cdd:PRK13547 93 QPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQAL----ALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 173 --CEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIhHPRH 250
Cdd:PRK13547 169 aaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL-TPAH 247
|
250 260
....*....|....*....|....*...
gi 446115710 251 pytigLLQCapeHGVPRQLLPAIPGTVP 278
Cdd:PRK13547 248 -----IARC---YGFAVRLVDAGDGVPP 267
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
13-222 |
6.91e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.55 E-value: 6.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 13 LSFPGFNgdVHALNNVSLQINRSEIVGLVGESGSGKSvtamlimrllptgsycvhrgqiSLLGEDVLNAREKQLRQWRga 92
Cdd:cd03238 1 LTVSGAN--VHNLQNLDVSIPLNVLVVVTGVSGSGKS----------------------TLVNEGLYASGKARLISFL-- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 93 rvamifqePMTALNPTRRIG-LQ-MMDVIRHHQPISRrearakaialleEMQipdavevmsrypfELSGGMRQRVMIA-- 168
Cdd:cd03238 55 --------PKFSRNKLIFIDqLQfLIDVGLGYLTLGQ------------KLS-------------TLSGGELQRVKLAse 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446115710 169 LAFSCEPQLIIADEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQ 222
Cdd:cd03238 102 LFSEPPGTLFILDEPSTGLHQQDINQLLEVIK-GLIDLGNTVILIEHNLDVLSS 154
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
157-239 |
7.57e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.88 E-value: 7.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 157 LSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFIshdmavVSQ-------LCDSVYV 229
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS------LYQasdeiydLFDKVLV 192
|
90
....*....|
gi 446115710 230 MYAGSVIESG 239
Cdd:cd03233 193 LYEGRQIYYG 202
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-216 |
8.18e-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: 50.83 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 34 RSEIVGLVGESGSGKSVTAMLIMRLLPtgsyCVHRGQISLLGEDVLNAREKQLRQwrgarvamifqepmtalnptrrigl 113
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELG----PPGGGVIYIDGEDILEEVLDQLLL------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 114 qmmdvirhhqpisrrearakaialleemqipdavEVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQ- 192
Cdd:smart00382 52 ----------------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEa 97
|
170 180
....*....|....*....|....*...
gi 446115710 193 ----LQVLRLLKHKARASGTAVLFISHD 216
Cdd:smart00382 98 llllLEELRLLLLLKSEKNLTVILTTND 125
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-234 |
1.20e-07 |
|
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: 51.56 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 21 DVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAREKQlrqwRGArVAMIFQE 100
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRN----RYS-VAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 101 PMTaLNPTrriglqMMDVIRHHQPISRREARA--KAIALLEEMQI---PDAVEVMSRyPFELSGGMRQRVMIALAFSCEP 175
Cdd:cd03290 88 PWL-LNAT------VEENITFGSPFNKQRYKAvtDACSLQPDIDLlpfGDQTEIGER-GINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115710 176 QLIIADEPTTALDV-----TVQLQVLRLLKHKARasgtAVLFISHDMAVVSQlCDSVYVMYAGS 234
Cdd:cd03290 160 NIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAMKDGS 218
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-222 |
1.21e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 51.34 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 27 NVSLQINRSEIVGLVGESGSGKsvTAMLimRLL-----PTGsycvhrGQISLLGEDVLNAREKQLRQ--WRGaRVAMIFQ 99
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGK--TSLL--RILaglarPDA------GEVLWQGEPIRRQRDEYHQDllYLG-HQPGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 EpMTAL-NptrrigLQMMdvIRHHQPISRrEARAKAIA---LLEEMQIPDAVevmsrypfeLSGGMRQRVmiALA--FSC 173
Cdd:PRK13538 88 E-LTALeN------LRFY--QRLHGPGDD-EALWEALAqvgLAGFEDVPVRQ---------LSAGQQRRV--ALArlWLT 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446115710 174 EPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQ 222
Cdd:PRK13538 147 RAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVASD 195
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-188 |
1.47e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.82 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLImrllpTGSYCVHRGQISLLGEDVLNAREkqlRQWRGARVAMIFQ 99
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-----AGARKIQQGRVEVLGGDMADARH---RRAVCPRIAYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 EPMTALNPT-----------RRIGLqmmdvirhhqpiSRREARAKAIALLEEMQIpdavevmsrYPF------ELSGGMR 162
Cdd:NF033858 84 GLGKNLYPTlsvfenldffgRLFGQ------------DAAERRRRIDELLRATGL---------APFadrpagKLSGGMK 142
|
170 180 190
....*....|....*....|....*....|
gi 446115710 163 QRvmiaLAFSC----EPQLIIADEPTTALD 188
Cdd:NF033858 143 QK----LGLCCalihDPDLLILDEPTTGVD 168
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
18-220 |
1.72e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 51.46 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 18 FNGDVHALNNVSLQINRSEIVGLVGESGSGKSVtamLIMRLL-PTGSYCVHRGQISLLGEDVLNAREKQlrqwrgARVAM 96
Cdd:cd03271 4 KGARENNLKNIDVDIPLGVLTCVTGVSGSGKSS---LINDTLyPALARRLHLKKEQPGNHDRIEGLEHI------DKVIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 97 IFQEPM---TALNPTRRIGLqmMDVIR------------HHQPISRReARAKAIALLEEMQIPDAVEVMSRYP------- 154
Cdd:cd03271 75 IDQSPIgrtPRSNPATYTGV--FDEIRelfcevckgkryNRETLEVR-YKGKSIADVLDMTVEEALEFFENIPkiarklq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 155 ----------------FELSGGMRQRVMIA--LAF-SCEPQLIIADEPTTAL---DVTVQLQVLrllkHKARASGTAVLF 212
Cdd:cd03271 152 tlcdvglgyiklgqpaTTLSGGEAQRIKLAkeLSKrSTGKTLYILDEPTTGLhfhDVKKLLEVL----QRLVDKGNTVVV 227
|
....*...
gi 446115710 213 ISHDMAVV 220
Cdd:cd03271 228 IEHNLDVI 235
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-244 |
6.70e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 21 DVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLlgEDVLNAREKQLRQWRgARVAMIFQ 99
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPT------EGDIII--NDSHNLKDINLKWWR-SKIGVVSQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 EPMTALNPTRR------IGLQMMDVIRHH----------QPISRREARAKAIALLEEM---------------------- 141
Cdd:PTZ00265 468 DPLLFSNSIKNnikyslYSLKDLEALSNYynedgndsqeNKNKRNSCRAKCAGDLNDMsnttdsneliemrknyqtikds 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 142 ----------------QIPDAVEVM-SRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKAR 204
Cdd:PTZ00265 548 evvdvskkvlihdfvsALPDKYETLvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKG 627
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446115710 205 ASGTAVLFISHDMAVVsQLCDSVYVMyagSVIESGVTADV 244
Cdd:PTZ00265 628 NENRITIIIAHRLSTI-RYANTIFVL---SNRERGSTVDV 663
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-211 |
6.73e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.06 E-value: 6.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTgsycvhRGQISLlgeDVLNAREKQLRQWRGArVAMIFQEpMTA 104
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST------EGEIQI---DGVSWNSVTLQTWRKA-FGVIPQK-VFI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 105 LNPTRRIGL----QMMDvirhhQPISRREARAKAIALLEemQIPDAVE-VMSRYPFELSGGMRQRVMIALAFSCEPQLII 179
Cdd:TIGR01271 1304 FSGTFRKNLdpyeQWSD-----EEIWKVAEEVGLKSVIE--QFPDKLDfVLVDGGYVLSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190
....*....|....*....|....*....|..
gi 446115710 180 ADEPTTALDvTVQLQVLRLLKHKARASGTAVL 211
Cdd:TIGR01271 1377 LDEPSAHLD-PVTLQIIRKTLKQSFSNCTVIL 1407
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
25-230 |
1.10e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 48.39 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVtamlimrLLPTGSYCVHRGQISllGEDVLNAREKQlrqwrgarvaMIFQepmta 104
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTT-------LLDVLAGRKTAGVIT--GEILINGRPLD----------KNFQ----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 105 lnptRRIG-LQMMDVirhHQPISR-REArakaialLEemqipdavevMSRYPFELSGGMRQRVMIALAFSCEPQLIIADE 182
Cdd:cd03232 79 ----RSTGyVEQQDV---HSPNLTvREA-------LR----------FSALLRGLSVEQRKRLTIGVELAAKPSILFLDE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446115710 183 PTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVM 230
Cdd:cd03232 135 PTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLL 182
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-239 |
1.57e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.78 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQLRQwrgaRVAMIFQEPM-- 102
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVE-----VCGGEIRVNGREIGAYGLRELRR----QFSMIPQDPVlf 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 103 ---TALNPTRRIGLQMMDVIRHHQPISRREARAKaiallEEMQIPDAV-EVMSRYpfelSGGMRQRVMIALA-FSCEPQL 177
Cdd:PTZ00243 1397 dgtVRQNVDPFLEASSAEVWAALELVGLRERVAS-----ESEGIDSRVlEGGSNY----SVGQRQLMCMARAlLKKGSGF 1467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115710 178 IIADEPTT----ALDVTVQLQVLRLLkhkaraSGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESG 239
Cdd:PTZ00243 1468 ILMDEATAnidpALDRQIQATVMSAF------SAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMG 1526
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-239 |
1.91e-06 |
|
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: 49.56 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 14 SFPGFNGDVHALNNVSLQINRSEIVGLVGESGSGKS--VTAMLimrllptGSYCVHRGQISLLGEdVLNAREKQLRQWRG 91
Cdd:TIGR00957 643 TFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSslLSALL-------AEMDKVEGHVHMKGS-VAYVPQQAWIQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 92 ARVAMIFQEPmtaLNPtrriglqmmdvirhhqpiSRREARAKAIALLEEMQI-P--DAVEVMSRyPFELSGGMRQRVMIA 168
Cdd:TIGR00957 715 LRENILFGKA---LNE------------------KYYQQVLEACALLPDLEIlPsgDRTEIGEK-GVNLSGGQKQRVSLA 772
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115710 169 LAFSCEPQLIIADEPTTALDVTVQLQVLR-------LLKHKARasgtavLFISHDMAVVSQLcDSVYVMYAGSVIESG 239
Cdd:TIGR00957 773 RAVYSNADIYLFDDPLSAVDAHVGKHIFEhvigpegVLKNKTR------ILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-222 |
2.07e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFPgfngDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLL-------------PTG--------- 62
Cdd:PTZ00265 1168 IMDVNFRYISRP----NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfkneHTNdmtneqdyq 1243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 63 -------------------------SYCVHR--GQISLLGEDVLNAREKQLRQWrgarVAMIFQEPMTalnptrrIGLQM 115
Cdd:PTZ00265 1244 gdeeqnvgmknvnefsltkeggsgeDSTVFKnsGKILLDGVDICDYNLKDLRNL----FSIVSQEPML-------FNMSI 1312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 116 MDVIRHHQPISRRE--ARAKAIALLEEM--QIPDAVEV-MSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVT 190
Cdd:PTZ00265 1313 YENIKFGKEDATREdvKRACKFAAIDEFieSLPNKYDTnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1392
|
250 260 270
....*....|....*....|....*....|...
gi 446115710 191 VQLQVLR-LLKHKARASGTaVLFISHDMAVVSQ 222
Cdd:PTZ00265 1393 SEKLIEKtIVDIKDKADKT-IITIAHRIASIKR 1424
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
157-227 |
2.48e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.44 E-value: 2.48e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446115710 157 LSGGMRQRVMIA---LAFSCEPQLIIADEPTTAL---DVTVQLQVLRLLKHKarasGTAVLFISHDMAVVsQLCDSV 227
Cdd:PRK00635 810 LSGGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLhthDIKALIYVLQSLTHQ----GHTVVIIEHNMHVV-KVADYV 881
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-237 |
2.98e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQLRQwrgaRVAMIFQEPMTa 104
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVE-----LERGRILIDGCDISKFGLMDLRK----VLGIIPQAPVL- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 105 LNPTRRIGLqmmDVIRHHQPISRREArakaialLEEMQIPDAVEvmsRYPFEL-----------SGGMRQRVMIALAFSC 173
Cdd:PLN03130 1325 FSGTVRFNL---DPFNEHNDADLWES-------LERAHLKDVIR---RNSLGLdaevseagenfSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115710 174 EPQLIIADEPTTALDVTVQLQVLRLLKHKARAsgTAVLFISHDMAVVSQlCDSVYVMYAGSVIE 237
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIREEFKS--CTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-216 |
5.19e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 13 LSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQIsLLGEDVLNAREKQ--LRQWR 90
Cdd:PRK11147 11 LSF----SDAPLLDNAELHIEDNERVCLVGRNGAGKST----LMKIL-NGEVLLDDGRI-IYEQDLIVARLQQdpPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 91 G---ARVAMIFQEPMTALNPTRRIGLQMMdvirhHQPISRREAR-AKAIALLE-------EMQIPDAVEVMSRYP----F 155
Cdd:PRK11147 81 GtvyDFVAEGIEEQAEYLKRYHDISHLVE-----TDPSEKNLNElAKLQEQLDhhnlwqlENRINEVLAQLGLDPdaalS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115710 156 ELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHkarASGtAVLFISHD 216
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT---FQG-SIIFISHD 212
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-246 |
5.92e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.20 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKS--VTAMLimRLLPT--GSYCVHRGQISLLgedvlnarekqlrqwrgARVA 95
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTslISAML--GELPPrsDASVVIRGTVAYV-----------------PQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 96 MIFqepmtalNPTRRiglqmmDVIRHHQPI--SRREARAKAIALLEEMQI-P--DAVEVMSRyPFELSGGMRQRVMIALA 170
Cdd:PLN03130 689 WIF-------NATVR------DNILFGSPFdpERYERAIDVTALQHDLDLlPggDLTEIGER-GVNISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 171 FSCEPQLIIADEPTTALDVTVQLQVL-----RLLKHKARASGTAVL-FISHdmavvsqlCDSVYVMYAGSVIESGVTADV 244
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHVGRQVFdkcikDELRGKTRVLVTNQLhFLSQ--------VDRIILVHEGMIKEEGTYEEL 826
|
..
gi 446115710 245 IH 246
Cdd:PLN03130 827 SN 828
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
25-254 |
8.18e-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: 46.44 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQLRqwrgARVAMIFQEPMT- 103
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVD-----IFDGKIVIDGIDISKLPLHTLR----SRLSIILQDPILf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 104 ------ALNPTRRIglqmmdvirhhqpISRREARAKAIALLEEM--QIPDAVEVMSRYPFE-LSGGMRQRVMIALAFSCE 174
Cdd:cd03288 108 sgsirfNLDPECKC-------------TDDRLWEALEIAQLKNMvkSLPGGLDAVVTEGGEnFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 175 PQLIIADEPTTALDVTVQlQVLRLLKHKARASGTaVLFISHDMAVVSQlCDSVYVMYAGSVIESGVTADVIHHPRHPYTI 254
Cdd:cd03288 175 SSILIMDEATASIDMATE-NILQKVVMTAFADRT-VVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFAS 251
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
25-211 |
9.94e-06 |
|
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: 46.39 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTgsycvhRGQISLlgeDVLNAREKQLRQWRGArVAMIFQEPMTA 104
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT------EGDIQI---DGVSWNSVPLQKWRKA-FGVIPQKVFIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 105 LNPTRriglQMMDVIRHH--QPISRREARAKAIALLEemQIPDAVE-VMSRYPFELSGGMRQRVMIALAFSCEPQLIIAD 181
Cdd:cd03289 90 SGTFR----KNLDPYGKWsdEEIWKVAEEVGLKSVIE--QFPGQLDfVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190
....*....|....*....|....*....|
gi 446115710 182 EPTTALDvTVQLQVLRLLKHKARASGTAVL 211
Cdd:cd03289 164 EPSAHLD-PITYQVIRKTLKQAFADCTVIL 192
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
157-235 |
1.12e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 1.12e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446115710 157 LSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARaSGTAVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
157-222 |
1.28e-05 |
|
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: 46.93 E-value: 1.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115710 157 LSGGMRQRVMIALAFSCE---PQLIIADEPTTAL---DVTVQLQVLRLLKHKarasGTAVLFISHDMAVVSQ 222
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIKKLLEVLQRLVDK----GNTVVVIEHNLDVIKT 897
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
157-216 |
1.56e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.66 E-value: 1.56e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115710 157 LSGGMRQRVMIALAF---SCEP-QLIIADEPTTALDVTVQLQVLRLLKHKaRASGTAVLFISHD 216
Cdd:cd03227 78 LSGGEKELSALALILalaSLKPrPLYILDEIDRGLDPRDGQALAEAILEH-LVKGAQVIVITHL 140
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-234 |
1.83e-05 |
|
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: 45.62 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIM-RLLPTGSYCVHRGQISLlgedvlnarekqlrqwrGARVAMIFqePMT 103
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIKHSGRISF-----------------SSQFSWIM--PGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 104 aLNPTRRIGLQmMDVIRHHQPIsrrearaKAIALLEEM-QIPDAVE-VMSRYPFELSGGMRQRVMIALAFSCEPQLIIAD 181
Cdd:cd03291 114 -IKENIIFGVS-YDEYRYKSVV-------KACQLEEDItKFPEKDNtVLGEGGITLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446115710 182 EPTTALDVTVQLQVLRLLKHKARASGTAVLFISHdmavVSQL--CDSVYVMYAGS 234
Cdd:cd03291 185 SPFGYLDVFTEKEIFESCVCKLMANKTRILVTSK----MEHLkkADKILILHEGS 235
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-216 |
2.13e-05 |
|
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: 46.08 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 5 VLDIQQLHLSFpgfnGDVHALNNVSLQINRSEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLlGEDVLNAREK 84
Cdd:TIGR03719 322 VIEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKST----LFRMI-TGQEQPDSGTIEI-GETVKLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 85 QLRQwrgarvamifqepmtALNPTRRI------GLQMMDVIRHHQPisrreARAkaialleemqipdaveVMSRYPF--- 155
Cdd:TIGR03719 392 QSRD---------------ALDPNKTVweeisgGLDIIKLGKREIP-----SRA----------------YVGRFNFkgs 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115710 156 -------ELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVtvqlQVLRLLKHKARASGTAVLFISHD 216
Cdd:TIGR03719 436 dqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISHD 499
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-216 |
2.30e-05 |
|
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: 45.70 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 18 FNGDVHALNNVSLQINRSEIVGLVGESGSGKSvTAMLIMRLLPTgsycvhrgqiSLLGEDVLNArekqlrqwrGARVAMI 97
Cdd:TIGR03719 14 VPPKKEILKDISLSFFPGAKIGVLGLNGAGKS-TLLRIMAGVDK----------DFNGEARPQP---------GIKVGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 98 FQEPmtALNPTRRIGLQMMDVIRHHQPISRR---------EARAKAIALLEEM----QIPDA---------VEVMS---R 152
Cdd:TIGR03719 74 PQEP--QLDPTKTVRENVEEGVAEIKDALDRfneisakyaEPDADFDKLAAEQaelqEIIDAadawdldsqLEIAMdalR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 153 YP------FELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTvqlQVLRLLKHKARASGTaVLFISHD 216
Cdd:TIGR03719 152 CPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEYPGT-VVAVTHD 217
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-78 |
3.15e-05 |
|
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: 45.56 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 2 TQPVLDIQQLHL-----SFPGFNGDVH-ALNNVSLQINRSEIVGLVGESGSGKSVTAMLImrllpTGSYCVHRGQISLLG 75
Cdd:COG4615 319 PPAPADFQTLELrgvtyRYPGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLL-----TGLYRPESGEILLDG 393
|
...
gi 446115710 76 EDV 78
Cdd:COG4615 394 QPV 396
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
158-239 |
3.34e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 158 SGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLfishdMAVV--SQ----LCDSVYVMY 231
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPL-----VAIYqcSQdayeLFDKVIVLY 285
|
....*...
gi 446115710 232 AGSVIESG 239
Cdd:TIGR00956 286 EGYQIYFG 293
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
24-215 |
3.79e-05 |
|
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: 43.89 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 24 ALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQLRQ--WRGARVAMifqep 101
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDS-----GEVRWNGTPLAEQRDEPHENilYLGHLPGL----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 102 MTALNPTRRIglqmmdviRHHQPISRREARAkAIALLEEMQIPDAVEVMSRYpfeLSGGMRQRVMIALAFSCEPQLIIAD 181
Cdd:TIGR01189 85 KPELSALENL--------HFWAAIHGGAQRT-IEDALAAVGLTGFEDLPAAQ---LSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|....*
gi 446115710 182 EPTTALDVT-VQLQVLRLLKHKARasGTAVLFISH 215
Cdd:TIGR01189 153 EPTTALDKAgVALLAGLLRAHLAR--GGIVLLTTH 185
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-214 |
4.79e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 45.29 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIM-RLLPTGSYCVHRGQISLlgedvlnarekqlrqwrGARVAMIFqePMT 103
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMgELEPSEGKIKHSGRISF-----------------SPQTSWIM--PGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 104 aLNPTRRIGLQmMDVIRHHQPIsrrearaKAIALLEEMQI-PDAVE-VMSRYPFELSGGMRQRVMIALAFSCEPQLIIAD 181
Cdd:TIGR01271 503 -IKDNIIFGLS-YDEYRYTSVI-------KACQLEEDIALfPEKDKtVLGEGGITLSGGQRARISLARAVYKDADLYLLD 573
|
170 180 190
....*....|....*....|....*....|...
gi 446115710 182 EPTTALDVTVQLQVLRLLKHKARASGTAVLFIS 214
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFESCLCKLMSNKTRILVTS 606
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-244 |
6.50e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.97 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKS--VTAMLiMRLLPTGSYCVH-RGQISLLgedvlnarekqlrqwrgARVAMIFqep 101
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTslISAML-GELSHAETSSVViRGSVAYV-----------------PQVSWIF--- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 102 mtalNPTRRiglqmMDVIRHHQPISRREARA-KAIALLEEMQI---PDAVEVMSRyPFELSGGMRQRVMIALAFSCEPQL 177
Cdd:PLN03232 692 ----NATVR-----ENILFGSDFESERYWRAiDVTALQHDLDLlpgRDLTEIGER-GVNISGGQKQRVSMARAVYSNSDI 761
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115710 178 IIADEPTTALDVTVQLQVL-RLLKHKARasGTAVLFISHDMAVVSQLcDSVYVMYAGSVIESGVTADV 244
Cdd:PLN03232 762 YIFDDPLSALDAHVAHQVFdSCMKDELK--GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAEL 826
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
158-234 |
6.99e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 44.62 E-value: 6.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446115710 158 SGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARaSGTAVLFISHDMAVVSQLCDSVYVMYAGS 234
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
16-216 |
1.53e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.42 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 16 PGFngdvhALNNVSLQINRSEIVGLVGESGSGKSVTAMLImrllpTGSYCVHRGQISLLGEDVlnaREKQLRQWRgARVA 95
Cdd:PRK10522 335 NGF-----SVGPINLTIKRGELLFLIGGNGSGKSTLAMLL-----TGLYQPQSGEILLDGKPV---TAEQPEDYR-KLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 96 MIF--------------QEPMTALNPTRRIGLQMMDVIRhhqpisrrearakaialLEEMQIPDavevmsrypFELSGGM 161
Cdd:PRK10522 401 AVFtdfhlfdqllgpegKPANPALVEKWLERLKMAHKLE-----------------LEDGRISN---------LKLSKGQ 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446115710 162 RQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHD 216
Cdd:PRK10522 455 KKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD 509
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
25-220 |
2.04e-04 |
|
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: 41.71 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQLRQ--WRGARVAMifqepM 102
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLA-----GRVLLNGGPLDFQRDSIARGllYLGHAPGI-----K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 103 TALNPtrriglqmMDVIRHHQPISRREARAKAIALLEEMQIPDAvevmsryPF-ELSGGMRQRVMIALAFSCEPQLIIAD 181
Cdd:cd03231 86 TTLSV--------LENLRFWHADHSDEQVEEALARVGLNGFEDR-------PVaQLSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 446115710 182 EPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVV 220
Cdd:cd03231 151 EPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-211 |
2.69e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 6 LDIQQ--LHLSfpgfngDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLP--TGSYCVHRGQISLLGEDvlna 81
Cdd:PRK10938 4 LQISQgtFRLS------DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPllSGERQSQFSHITRLSFE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 82 rekQLRQwrgaRVAMIFQEPMT-ALNPTRR-IGLQMMDVIRHHqpiSRREARAKAIAllEEMQIPDaveVMSRyPFE-LS 158
Cdd:PRK10938 74 ---QLQK----LVSDEWQRNNTdMLSPGEDdTGRTTAEIIQDE---VKDPARCEQLA--QQFGITA---LLDR-RFKyLS 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446115710 159 GGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVL 211
Cdd:PRK10938 138 TGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVL 190
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
39-189 |
2.91e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 39 GLVGESGSGKSV----TAMLIMRLLPTGSYCVHRGQiSLLGED------VLNA---------REKQL-RQWRGARVAMIF 98
Cdd:PLN03073 207 GLVGRNGTGKTTflryMAMHAIDGIPKNCQILHVEQ-EVVGDDttalqcVLNTdiertqlleEEAQLvAQQRELEFETET 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 99 QEPMTALNPTRR---IGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPFelSGGMRQRVMIALAFSCEP 175
Cdd:PLN03073 286 GKGKGANKDGVDkdaVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQVKATKTF--SGGWRMRIALARALFIEP 363
|
170
....*....|....
gi 446115710 176 QLIIADEPTTALDV 189
Cdd:PLN03073 364 DLLLLDEPTNHLDL 377
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
157-220 |
2.95e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.63 E-value: 2.95e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115710 157 LSGGMRQRVMIALAFSCEPQLIIADEPTTALDVtvqlQVLRLLKHK-ARASGTaVLFISHDMAVV 220
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELlDSYQGT-VLLVSHDRQFV 500
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-248 |
2.96e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.84 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVtamLIMRLLptGSYCVHRGqisllgedvlnarekqlRQWRGARVAMIFQEPMTa 104
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKST---LLQSLL--SQFEISEG-----------------RVWAERSIAYVPQQAWI- 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 105 LNPTRRIGLQMMDvirhhqpiSRREAR-AKAIAL--LEE--MQIPDAVEV-MSRYPFELSGGMRQRVMIALAFSCEPQLI 178
Cdd:PTZ00243 733 MNATVRGNILFFD--------EEDAARlADAVRVsqLEAdlAQLGGGLETeIGEKGVNLSGGQKARVSLARAVYANRDVY 804
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 179 IADEPTTALDVTVQLQVLRLLKHKARASGTAVLfISHDMAVVSqLCDSVYVMYAGSVIESGVTADVIHHP 248
Cdd:PTZ00243 805 LLDDPLSALDAHVGERVVEECFLGALAGKTRVL-ATHQVHVVP-RADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
158-216 |
3.94e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 3.94e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446115710 158 SGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHkarASGTAVLfISHD 216
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKS---YQGTLIL-ISHD 205
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
135-215 |
4.04e-04 |
|
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: 42.04 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 135 IALLEEMQIPDAVE------VMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKarasGT 208
Cdd:TIGR00954 555 EQILDNVQLTHILEreggwsAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF----GI 630
|
....*..
gi 446115710 209 AVLFISH 215
Cdd:TIGR00954 631 TLFSVSH 637
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
117-215 |
9.34e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 9.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 117 DVIRHHQPISRREaRAKAIALLEEMQIPDAvevMSRYPFE-LSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQV 195
Cdd:PRK10938 365 DSIGIYQAVSDRQ-QKLAQQWLDILGIDKR---TADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLV 440
|
90 100
....*....|....*....|
gi 446115710 196 LRLLKHKARASGTAVLFISH 215
Cdd:PRK10938 441 RRFVDVLISEGETQLLFVSH 460
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-215 |
1.03e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.86 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 25 LNNVSLQINRSEIVGLVGESGSGKSVtamlimrLLPTGSYCVHRGQISlLGEDVLNAREKQLRQWRgaRVAMIFQEPMTA 104
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTT-------LLNVLAERVTTGVIT-GGDRLVNGRPLDSSFQR--SIGYVQQQDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 105 LNPTRRIGLQMMDVIRHHQPISRREARA---KAIALLEEMQIPDAVEVMsryPFE-LSGGMRQRVMIALAFSCEPQLII- 179
Cdd:TIGR00956 849 PTSTVRESLRFSAYLRQPKSVSKSEKMEyveEVIKLLEMESYADAVVGV---PGEgLNVEQRKRLTIGVELVAKPKLLLf 925
|
170 180 190
....*....|....*....|....*....|....*.
gi 446115710 180 ADEPTTALDVTVQLQVLRLLKHKARAsGTAVLFISH 215
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIH 960
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
155-235 |
1.53e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 155 FELSGGMRQRVMIALAFSCEPQLIIADEPTTALD---VTVQLQVLRLLKhkarasgTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:PLN03073 626 YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDldaVEALIQGLVLFQ-------GGVLMVSHDEHLISGSVDELWVVS 698
|
....
gi 446115710 232 AGSV 235
Cdd:PLN03073 699 EGKV 702
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
157-220 |
2.07e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 2.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 157 LSGGMRQRVMIALAFSCEPQ---LIIADEPTTAL---DVTVQLQVLrllkHKARASGTAVLFISHDMAVV 220
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfhDIRKLLEVL----HRLVDKGNTVVVIEHNLDVI 892
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
22-216 |
2.27e-03 |
|
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: 38.78 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 22 VHALNNVSLQINRSEIVGLVGESGSGKSVTAM-LIM-----RLLPT-GSYCvhRGQISLLGEDVLNAREkqlrqwrGARV 94
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFdTIYaegqrRYVESlSAYA--RQFLGQMDKPDVDSIE-------GLSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 95 AMIFQEPMTALNPTRRIG--LQMMDVIRhhqpisRREARAKAIALLEEMqipdaVEV------MSRYPFELSGGMRQRvm 166
Cdd:cd03270 79 AIAIDQKTTSRNPRSTVGtvTEIYDYLR------LLFARVGIRERLGFL-----VDVglgyltLSRSAPTLSGGEAQR-- 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446115710 167 IALAFSCEPQLI----IADEPTTALDvtvQLQVLRLLK--HKARASGTAVLFISHD 216
Cdd:cd03270 146 IRLATQIGSGLTgvlyVLDEPSIGLH---PRDNDRLIEtlKRLRDLGNTVLVVEHD 198
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-211 |
2.58e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 38.32 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 20 GDVHALNNVSLQINRSEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQLRQWRGARVAMifq 99
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAA-----GTIKLDGGDIDDPDVAEACHYLGHRNAM--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 100 epmtalNPTrrigLQMMDVIRHHQPIsRREARAKAIALLEEMQIPDAVEVMSRYpfeLSGGMRQRVMIA-LAFSCEPqLI 178
Cdd:PRK13539 85 ------KPA----LTVAENLEFWAAF-LGGEELDIAAALEAVGLAPLAHLPFGY---LSAGQKRRVALArLLVSNRP-IW 149
|
170 180 190
....*....|....*....|....*....|...
gi 446115710 179 IADEPTTALDVTVQLQVLRLLKHKARASGTAVL 211
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIRAHLAQGGIVIA 182
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
18-216 |
6.42e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.18 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 18 FNGDVHALNNVSLQINRSEIVGLVGESGSGKSvTAMLIMRLLPTGSycvhrgqislLGEDVLNArekqlrqwrGARVAMI 97
Cdd:PRK11819 16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKS-TLLRIMAGVDKEF----------EGEARPAP---------GIKVGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 98 FQEPmtALNPTRRI------GLQ-MMDVIRHHQPISRR--EARAKAIALLEEM-----QI-------------------- 143
Cdd:PRK11819 76 PQEP--QLDPEKTVrenveeGVAeVKAALDRFNEIYAAyaEPDADFDALAAEQgelqeIIdaadawdldsqleiamdalr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 144 ---PDA-VEVmsrypfeLSGGMRQRVmiALafsC-----EPQLIIADEPTTALDVTvqlQVLRLLKHKARASGTaVLFIS 214
Cdd:PRK11819 154 cppWDAkVTK-------LSGGERRRV--AL---CrllleKPDMLLLDEPTNHLDAE---SVAWLEQFLHDYPGT-VVAVT 217
|
..
gi 446115710 215 HD 216
Cdd:PRK11819 218 HD 219
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
157-239 |
8.77e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.90 E-value: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115710 157 LSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVM-YAGSV 235
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMkRGGQV 1099
|
....
gi 446115710 236 IESG 239
Cdd:PLN03140 1100 IYSG 1103
|
|
| |
