|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-321 |
9.43e-163 |
|
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: 456.05 E-value: 9.43e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGsyCVHRGQISLLGEDVLNAREK 84
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPP--GITSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 QLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPFELSGGMRQR 164
Cdd:COG0444 79 ELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 165 VMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADV 244
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 245 IHHPRHPYTIGLLQCAPEHGVPRQPLPAIPGTVPNLTHLPDGCAFRDRCYAAGAQC-----ALTACGDnNQHCTCWYPQQ 319
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCreeepPLREVGP-GHRVACHLYEE 317
|
..
gi 446115686 320 EV 321
Cdd:COG0444 318 EA 319
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-274 |
1.65e-132 |
|
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: 387.50 E-value: 1.65e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHrGQISLLGEDVLN 80
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPS-GSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 81 AREKQLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPFELSGG 160
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 161 MRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGG 240
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
250 260 270
....*....|....*....|....*....|....
gi 446115686 241 TADVIHHPRHPYTIGLLQCAPeHGVPRQPLPAIP 274
Cdd:COG4172 241 TAELFAAPQHPYTRKLLAAEP-RGDPRPVPPDAP 273
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-322 |
4.20e-113 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 330.92 E-value: 4.20e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycVHRGQISLLGEDVLN 80
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANG--RIGGSATFNGREILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 81 AREKQLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPFELSGG 160
Cdd:PRK09473 86 LPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 161 MRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGG 240
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 241 TADVIHHPRHPYTIGLLQCAPEHGVPRQPLPAIPGTVPNLTHLPDGCAFRDRCYAAGAQCA----LTACGDNNQHcTCWY 316
Cdd:PRK09473 246 ARDVFYQPSHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSsappLEEFGPGRLR-ACFK 324
|
....*.
gi 446115686 317 PQQEVI 322
Cdd:PRK09473 325 PVEELL 330
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-239 |
1.84e-106 |
|
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: 310.21 E-value: 1.84e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTGsycvhrGQISLLGEDVLNARE 83
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLkPTS------GSIIFDGKDLLKLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 KQLRqWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEmQIPDAVEVMSRYPFELSGGMRQ 163
Cdd:cd03257 75 RLRK-IRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLV-GVGLPEEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115686 164 RVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-262 |
7.39e-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: 297.97 E-value: 7.39e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFPGF-NGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVL 79
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR-----PTSGSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 80 NAREKQLRQWRGaRVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDavEVMSRYPFELSG 159
Cdd:COG1123 331 KLSRRSLRELRR-RVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPP--DLADRYPHELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 160 GMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
250 260
....*....|....*....|...
gi 446115686 240 GTADVIHHPRHPYTIGLLQCAPE 262
Cdd:COG1123 488 PTEEVFANPQHPYTRALLAAVPS 510
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-280 |
3.89e-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: 286.03 E-value: 3.89e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 3 QPVLDIQQLHLSFPGfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGsyCVHRGQISLLGEDVLNAR 82
Cdd:COG1123 2 TPLLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHG--GRISGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 83 EkqlrQWRGARVAMIFQEPMTALNPTRrIGLQMMDVIRHHQpISRREARAKAIALLEEMQIPDaveVMSRYPFELSGGMR 162
Cdd:COG1123 78 E----ALRGRRIGMVFQDPMTQLNPVT-VGDQIAEALENLG-LSRAEARARVLELLEAVGLER---RLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 163 QRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTA 242
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
250 260 270
....*....|....*....|....*....|....*...
gi 446115686 243 DVIHHPRhpytigLLQCAPEHGVPRQPLPAIPGTVPNL 280
Cdd:COG1123 229 EILAAPQ------ALAAVPRLGAARGRAAPAAAAAEPL 260
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-319 |
7.53e-91 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 273.92 E-value: 7.53e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFP---GF----NGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTGsycvhrGQIS 72
Cdd:COG4608 3 MAEPLLEVRDLKKHFPvrgGLfgrtVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEePTS------GEIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 73 LLGEDVLNAREKQLRQWRgARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPdaVEVMSR 152
Cdd:COG4608 77 FDGQDITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLR--PEHADR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 153 YPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYA 232
Cdd:COG4608 154 YPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 233 GSVIESGGTADVIHHPRHPYTIGLLQCAPehgVP-----RQPLPaIPGTVPNLTHLPDGCAFRDRCYAAGAQCA-----L 302
Cdd:COG4608 234 GKIVEIAPRDELYARPLHPYTQALLSAVP---VPdperrRERIV-LEGDVPSPLNPPSGCRFHTRCPYAQDRCAteeppL 309
|
330
....*....|....*...
gi 446115686 303 TACGDNnqHCT-CWYPQQ 319
Cdd:COG4608 310 REVGPG--HQVaCHLAEE 325
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-300 |
3.18e-90 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 272.55 E-value: 3.18e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 4 PVLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTgSYCVHRGQISLLGEDVLNARE 83
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD-NWHVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 KQLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQP----ISRREARAK-AIALLEEMQIPDAVEVMSRYPFELS 158
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFkgkwWQRFKWRKKrAIELLHRVGIKDHKDIMNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 159 GGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIES 238
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115686 239 GGTADVIHHPRHPYTIGLLQCAPEHGVP---RQPLPAIPGTVPNLTHLPDGCAFRDRCYAAGAQC 300
Cdd:COG4170 241 GPTEQILKSPHHPYTKALLRSMPDFRQPlphKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKC 305
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-300 |
9.68e-90 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 271.23 E-value: 9.68e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYcVHRGQISLLGEDVLNAREK 84
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGR-VMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 QLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPFELSGGMRQR 164
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 165 VMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADV 244
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446115686 245 IHHPRHPYTIGLLQCAPEHGVPRQPLPAIPGTVPNLTHLPDGCAFRDRCYAAGAQC 300
Cdd:PRK11022 242 FRAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRC 297
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-262 |
3.28e-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: 263.47 E-value: 3.28e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 4 PVLDIQQLHLSFP---GF----NGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGsycvhrGQISLLGE 76
Cdd:COG4172 274 PLLEARDLKVWFPikrGLfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE------GEIRFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 77 DVLNAREKQLRQWRgARVAMIFQEPMTALNPTRRIGlqmmDVIR-----HHQPISRREARAKAIALLEEMQIPDavEVMS 151
Cdd:COG4172 348 DLDGLSRRALRPLR-RRMQVVFQDPFGSLSPRMTVG----QIIAeglrvHGPGLSAAERRARVAEALEEVGLDP--AARH 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 152 RYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:COG4172 421 RYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMK 500
|
250 260 270
....*....|....*....|....*....|.
gi 446115686 232 AGSVIESGGTADVIHHPRHPYTIGLLQCAPE 262
Cdd:COG4172 501 DGKVVEQGPTEQVFDAPQHPYTRALLAAAPL 531
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-280 |
5.07e-83 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 260.41 E-value: 5.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLN 80
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 81 AREKQLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPFELSGG 160
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 161 MRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGG 240
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446115686 241 TADVIHHPRHPYTIGLLQCAPEHgvprQPLPAIPGTVPNL 280
Cdd:PRK15134 241 AATLFSAPTHPYTQKLLNSEPSG----DPVPLPEPASPLL 276
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-274 |
6.53e-80 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 254.78 E-value: 6.53e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 2 TQPVLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLL--GEDVL 79
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRrrSRQVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 80 NARE---KQLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPFE 156
Cdd:PRK10261 89 ELSEqsaAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 157 LSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVI 236
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446115686 237 ESGGTADVIHHPRHPYTIGLLQCAPEHG------VPRQ-PLPAIP 274
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAVPQLGamkgldYPRRfPLISLE 293
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-266 |
5.65e-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: 5.65e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQ 85
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLER-----PWSGEVTFDGRPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 LRqwrgARVAMIFQEPMTALNPTRRIGLQMMDVIRHHqpiSRREARAKAIALLEEMQIPDavEVMSRYPFELSGGMRQRV 165
Cdd:COG1124 77 FR----RRVQMVFQDPYASLHPRHTVDRILAEPLRIH---GLPDREERIAELLEQVGLPP--SFLDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 166 MIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVI 245
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250 260
....*....|....*....|.
gi 446115686 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 |
3.90e-73 |
|
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: 225.33 E-value: 3.90e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 27 NVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVhRGQISLLGEDVLNARekqlrqWRGARVAMIFQEPMTALN 106
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQT-SGEILLDGRPLLPLS------IRGRHIATIMQNPRTAFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 107 PTRRIGLQMMDVIRHHQPISRrEARAKAIALLEEMQIPDAVEVMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTA 186
Cdd:TIGR02770 77 PLFTMGNHAIETLRSLGKLSK-QARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115686 187 LDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHHPRHPYTIGLL 257
Cdd:TIGR02770 156 LDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLL 226
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-317 |
3.43e-69 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 218.90 E-value: 3.43e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 4 PVLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLlPTGSYCVHRGQISLLGEDVLNARE 83
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 KQLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVI-------RHHQPISRREARAkaIALLEEMQIPDAVEVMSRYPFE 156
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgwtykgRWWQRFGWRKRRA--IELLHRVGIKDHKDAMRSFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 157 LSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVI 236
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 237 ESGGTADVIHHPRHPYTIGLLQCAPEHGVP---RQPLPAIPGTVPNLTHLPDGCAFRDRCYAAGAQCALTA--CGDNNQH 311
Cdd:PRK15093 239 ETAPSKELVTTPHHPYTQALIRAIPDFGSAmphKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIETPrlTGAKNHL 318
|
....*.
gi 446115686 312 CTCWYP 317
Cdd:PRK15093 319 YACHFP 324
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-300 |
4.58e-68 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 215.60 E-value: 4.58e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFP---GF---NGDVHALNNVSLQINRGEIVGLVGESGSGKSVTA-MLIMRLLPTGsycvhrGQISL 73
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPvkrGLfkpERLVKALDGVSFTLERGKTLAVVGESGCGKSTLArLLTMIETPTG------GELYY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 74 LGEDVLNA---REKQLRQwrgaRVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQI-PdavEV 149
Cdd:PRK11308 75 QGQDLLKAdpeAQKLLRQ----KIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrP---EH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 150 MSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYV 229
Cdd:PRK11308 148 YDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMV 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115686 230 MYAGSVIESGGTADVIHHPRHPYTIGLLQCAPE-HGVPRQPLPAIPGTVPNLTHLPDGCAFRDRCYAAGAQC 300
Cdd:PRK11308 228 MYLGRCVEKGTKEQIFNNPRHPYTQALLSATPRlNPDDRRERIKLTGELPSPLNPPPGCAFNARCPRAFGRC 299
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-303 |
6.44e-68 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 215.34 E-value: 6.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 24 ALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQlrqWRGAR--VAMIFQEP 101
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATD-----GEVAWLGKDLLGMKDDE---WRAVRsdIQMIFQDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 102 MTALNPTRRIGLQMMDVIRHHQP-ISRREARAKAIALLeeMQIPDAVEVMSRYPFELSGGMRQRVMIAPAFSCEPQLIIA 180
Cdd:PRK15079 108 LASLNPRMTIGEIIAEPLRTYHPkLSRQEVKDRVKAMM--LKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 181 GEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHHPRHPYTIGLLQCA 260
Cdd:PRK15079 186 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAV 265
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446115686 261 PehgVPRQPLPA------IPGTVPNLTHLPDGCAFRDRCYAAGAQCALT 303
Cdd:PRK15079 266 P---IPDPDLERnktiqlLEGELPSPINPPSGCVFRTRCPIAGPECAKT 311
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-260 |
8.67e-56 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 189.15 E-value: 8.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 2 TQPVLDIQQLHLSFPGFNG-------DVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTgsycvhRGQISLL 74
Cdd:PRK15134 272 ASPLLDVEQLQVAFPIRKGilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS------QGEIWFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 75 GEDVLNAREKQLRQWRgARVAMIFQEPMTALNPTrrigLQMMDVI----RHHQP-ISRREARAKAIALLEEMQIpDAvEV 149
Cdd:PRK15134 346 GQPLHNLNRRQLLPVR-HRIQVVFQDPNSSLNPR----LNVLQIIeeglRVHQPtLSAAQREQQVIAVMEEVGL-DP-ET 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 150 MSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYV 229
Cdd:PRK15134 419 RHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIV 498
|
250 260 270
....*....|....*....|....*....|.
gi 446115686 230 MYAGSVIESGGTADVIHHPRHPYTIGLLQCA 260
Cdd:PRK15134 499 LRQGEVVEQGDCERVFAAPQQEYTRQLLALS 529
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-266 |
6.27e-54 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 179.50 E-value: 6.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 8 IQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSvTamLImRLL-----PTgsycvhRGQISLLGEDVLNAR 82
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS-T--LI-RCInllerPT------SGSVLVDGVDLTALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 83 EKQLRQWRgARVAMIFQ-----EPMTAL-N---PTRRIGlqmmdvirhhqpISRREARAKAIALLEEMQIPDAVEvmsRY 153
Cdd:COG1135 74 ERELRAAR-RKIGMIFQhfnllSSRTVAeNvalPLEIAG------------VPKAEIRKRVAELLELVGLSDKAD---AY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 154 PFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALD-VTVQlQVLRLLKhKARAS-GTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:COG1135 138 PSQLSGGQKQRVGIARALANNPKVLLCDEATSALDpETTR-SILDLLK-DINRElGLTIVLITHEMDVVRRICDRVAVLE 215
|
250 260 270
....*....|....*....|....*....|....*
gi 446115686 232 AGSVIESGGTADVIHHPRHPYTIGLLQCAPEHGVP 266
Cdd:COG1135 216 NGRIVEQGPVLDVFANPQSELTRRFLPTVLNDELP 250
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
5-258 |
8.00e-54 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 176.81 E-value: 8.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSfpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHrGQISLLGEDVLNArek 84
Cdd:PRK10418 4 QIELRNIALQ-----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTA-GRVLLDGKPVAPC--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 qlrQWRGARVAMIFQEPMTALNPTRriglqmmdVIRHH-----QPISRREARAKAIALLEEMQIPDAVEVMSRYPFELSG 159
Cdd:PRK10418 75 ---ALRGRKIATIMQNPRSAFNPLH--------TMHTHaretcLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 160 GMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:PRK10418 144 GMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQG 223
|
250
....*....|....*....
gi 446115686 240 GTADVIHHPRHPYTIGLLQ 258
Cdd:PRK10418 224 DVETLFNAPKHAVTRSLVS 242
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-237 |
1.12e-53 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 175.23 E-value: 1.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 3 QPVLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSvTAMLIMRLL--PTGsycvhrGQISLLGEDVLN 80
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGLdrPTS------GEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 81 AREKQLRQWRGARVAMIFQEP-----MTAL-NptrrIGLQMMdvIRHhqpISRREARAKAIALLEEMQIPDaveVMSRYP 154
Cdd:COG1136 75 LSERELARLRRRHIGFVFQFFnllpeLTALeN----VALPLL--LAG---VSRKERRERARELLERVGLGD---RLDHRP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 155 FELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQlCDSVYVMYAGS 234
Cdd:COG1136 143 SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGR 221
|
...
gi 446115686 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 |
3.47e-53 |
|
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: 173.83 E-value: 3.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSvTAMLIMRLL--PTgsycvhRGQISLLGEDVLNARE 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGLdrPT------SGEVRVDGTDISKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 KQLRQWRGARVAMIFQEP-----MTAL-NptrrIGLQMMdvirhHQPISRREARAKAIALLEEMQIPDAvevMSRYPFEL 157
Cdd:cd03255 74 KELAAFRRRHIGFVFQSFnllpdLTALeN----VELPLL-----LAGVPKKERRERAEELLERVGLGDR---LNHYPSEL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115686 158 SGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSqLCDSVYVM 230
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIEL 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-246 |
1.32e-51 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 170.24 E-value: 1.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTGsycvhrGQISLLGEDVlnarEK 84
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLrPTS------GEVRVLGEDV----AR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 QLRQWRgARVAMIFQEPmtALNPTRRiGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAvevMSRYPFELSGGMRQR 164
Cdd:COG1131 67 DPAEVR-RRIGYVPQEP--ALYPDLT-VRENLRFFARLYGLPRKEARERIDELLELFGLTDA---ADRKVGTLSGGMKQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 165 VMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADV 244
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDPEARRELWELLR-ELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
..
gi 446115686 245 IH 246
Cdd:COG1131 219 KA 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-249 |
2.74e-50 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 166.74 E-value: 2.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPGfngDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAREK 84
Cdd:COG1122 1 IELENLSFSYPG---GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLkPT------SGEVLVDGKDITKKNLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 QLRQwrgaRVAMIFQEPMTAL-NPT---------RRIGLqmmdvirhhqpiSRREARAKAIALLEEMQIPDaveVMSRYP 154
Cdd:COG1122 72 ELRR----KVGLVFQNPDDQLfAPTveedvafgpENLGL------------PREEIRERVEEALELVGLEH---LADRPP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 155 FELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGS 234
Cdd:COG1122 133 HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLK-RLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
250
....*....|....*
gi 446115686 235 VIESGGTADVIHHPR 249
Cdd:COG1122 212 IVADGTPREVFSDYE 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-252 |
3.32e-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: 166.69 E-value: 3.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVL 79
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLrPD------SGEILVDGQDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 80 NAREKQLRQWRgARVAMIFQEP-----MTAL-NptrrIGLQMmdviRHHQPISRREARAKAIALLEEMQIPDAVEvmsRY 153
Cdd:COG1127 71 GLSEKELYELR-RRIGMLFQGGalfdsLTVFeN----VAFPL----REHTDLSEAEIRELVLEKLELVGLPGAAD---KM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 154 PFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALD-VTVQlQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYA 232
Cdd:COG1127 139 PSELSGGMRKRVALARALALDPEILLYDEPTAGLDpITSA-VIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLAD 217
|
250 260
....*....|....*....|
gi 446115686 233 GSVIESgGTADVIHHPRHPY 252
Cdd:COG1127 218 GKIIAE-GTPEELLASDDPW 236
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-248 |
5.77e-49 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 164.47 E-value: 5.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 12 HLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRL-LPTGsycvhrGQISLLGEDVLNAREKQLRQWR 90
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLeSPSQ------GNVSWRGEPLAKLNRAQRKAFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 91 GArVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDavEVMSRYPFELSGGMRQRVMIAPA 170
Cdd:PRK10419 89 RD-IQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDD--SVLDKRPPQLSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 171 FSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIH--HP 248
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTfsSP 245
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-249 |
4.07e-48 |
|
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: 161.21 E-value: 4.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSvTAMLIMRLLPTGSycvhRGQISLLGEDVLNAREK 84
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLERPT----SGSVLVDGTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 QLRQWRgARVAMIFQ-----EPMTALN----PtrrigLQMmdvirHHQPISRREARAKAiaLLEEMQIPDAVEvmsRYPF 155
Cdd:cd03258 76 ELRKAR-RRIGMIFQhfnllSSRTVFEnvalP-----LEI-----AGVPKAEIEERVLE--LLELVGLEDKAD---AYPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 156 ELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:cd03258 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
250
....*....|....
gi 446115686 236 IESGGTADVIHHPR 249
Cdd:cd03258 220 VEEGTVEEVFANPQ 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-261 |
2.36e-47 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 168.50 E-value: 2.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 3 QPVLDIQQLHLSFPGFNG-------DVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLG 75
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG-----GEIIFNG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 76 EDVLNAREKQLRQWRgARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDavEVMSRYPF 155
Cdd:PRK10261 386 QRIDTLSPGKLQALR-RDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLP--EHAWRYPH 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 156 ELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:PRK10261 463 EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
250 260
....*....|....*....|....*.
gi 446115686 236 IESGGTADVIHHPRHPYTIGLLQCAP 261
Cdd:PRK10261 543 VEIGPRRAVFENPQHPYTRKLMAAVP 568
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-253 |
1.26e-46 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 160.74 E-value: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 7 DIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRL-LPTGsycvhrGQISLLGEDVLNAREKQ 85
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLeRPTS------GRVLVDGQDLTALSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 LRQWRgARVAMIFQE---------------PMTALNptrriglqmmdvirhhqpISRREARAKAIALLEEMQIPDAvevM 150
Cdd:PRK11153 77 LRKAR-RQIGMIFQHfnllssrtvfdnvalPLELAG------------------TPKAEIKARVTELLELVGLSDK---A 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 151 SRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVM 230
Cdd:PRK11153 135 DRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVI 214
|
250 260
....*....|....*....|...
gi 446115686 231 YAGSVIESGGTADVIHHPRHPYT 253
Cdd:PRK11153 215 DAGRLVEQGTVSEVFSHPKHPLT 237
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-230 |
6.28e-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: 156.40 E-value: 6.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQ--PVLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSvTamlIMRLL-----PTgsycvhRGQISL 73
Cdd:COG1116 1 MSAaaPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS-T---LLRLIaglekPT------SGEVLV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 74 LGEDVLNArekqlrqwrGARVAMIFQEPmtALNPTRRI------GLQMMDVirhhqpiSRREARAKAIALLEEMQIPDAv 147
Cdd:COG1116 71 DGKPVTGP---------GPDRGVVFQEP--ALLPWLTVldnvalGLELRGV-------PKAERRERARELLELVGLAGF- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 148 evMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDV----TVQLQVLRLLkhkaRASGTAVLFISHDM--AVVs 221
Cdd:COG1116 132 --EDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQDELLRLW----QETGKTVLFVTHDVdeAVF- 204
|
....*....
gi 446115686 222 qLCDSVYVM 230
Cdd:COG1116 205 -LADRVVVL 212
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-251 |
7.82e-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: 155.54 E-value: 7.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVlNAREK 84
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEE-----PDSGTITVDGEDL-TDSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 QLRQWRgARVAMIFQE----P-MTAL-NPTrrIGLqmmdviRHHQPISRREARAKAIALLEEMQIPDaveVMSRYPFELS 158
Cdd:COG1126 71 DINKLR-RKVGMVFQQfnlfPhLTVLeNVT--LAP------IKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 159 GGMRQRVMIAPAFSCEPQLIIAGEPTTALD---VTVQLQVLRLLkhkaRASGTAVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:COG1126 139 GGQQQRVAIARALAMEPKVMLFDEPTSALDpelVGEVLDVMRDL----AKEGMTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
250
....*....|....*.
gi 446115686 236 IESGGTADVIHHPRHP 251
Cdd:COG1126 215 VEEGPPEEFFENPQHE 230
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
4-258 |
2.49e-44 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 152.30 E-value: 2.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 4 PVLDIQQLHLSFPGFNG-----DVHALNNVSLQINRGEIVGLVGESGSGKSVTA-MLIMRLLPTGsycvhrGQISLLGED 77
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAkMLAGIIEPTS------GEILINGHK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 78 VlnarEKQLRQWRGARVAMIFQEPMTALNPTRRIGlQMMDV-IRHHQPISRREARAKAIALLEemQIPDAVEVMSRYPFE 156
Cdd:COG4167 77 L----EYGDYKYRCKHIRMIFQDPNTSLNPRLNIG-QILEEpLRLNTDLTAEEREERIFATLR--LVGLLPEHANFYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 157 LSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVI 236
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
250 260
....*....|....*....|..
gi 446115686 237 ESGGTADVIHHPRHPYTIGLLQ 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 |
1.01e-43 |
|
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: 149.96 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAREK 84
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLrPD------SGEVLIDGEDISGLSEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 QLRQWRgARVAMIFQEPmtALnptrrigLQMMDV-------IRHHQPISRREARAKAIALLEEMQIPDAVEvmsRYPFEL 157
Cdd:cd03261 71 ELYRLR-RRMGMLFQSG--AL-------FDSLTVfenvafpLREHTRLSEEEIREIVLEKLEAVGLRGAED---LYPAEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 158 SGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIE 237
Cdd:cd03261 138 SGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
|
250
....*....|....*
gi 446115686 238 SgGTADVIHHPRHPY 252
Cdd:cd03261 218 E-GTPEELRASDDPL 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-244 |
1.19e-42 |
|
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: 147.31 E-value: 1.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVlnarE 83
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLkPD------SGSILIDGEDV----R 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 KQLRQWRgARVAMIFQEPMTALNPTRRiglqmmDVIRHH---QPISRREARAKAIALLEEMQIPDaveVMSRYPFELSGG 160
Cdd:COG4555 67 KEPREAR-RQIGVLPDERGLYDRLTVR------ENIRYFaelYGLFDEELKKRIEELIELLGLEE---FLDRRVGELSTG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 161 MRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGG 240
Cdd:COG4555 137 MKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILR-ALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
....
gi 446115686 241 TADV 244
Cdd:COG4555 216 LDEL 219
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
12-256 |
3.27e-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: 147.21 E-value: 3.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 12 HLSF---PGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAREKQLR 87
Cdd:TIGR04521 5 NVSYiyqPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLkPT------SGTVTIDGRDITAKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 88 QWRgARVAMIFQEP------MT-----ALNPtRRIGLqmmdvirhhqpiSRREARAKAIALLEEMQIPDavEVMSRYPFE 156
Cdd:TIGR04521 79 DLR-KKVGLVFQFPehqlfeETvykdiAFGP-KNLGL------------SEEEAEERVKEALELVGLDE--EYLERSPFE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 157 LSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVI 236
Cdd:TIGR04521 143 LSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIV 222
|
250 260
....*....|....*....|
gi 446115686 237 ESGGTADVIHHPRHPYTIGL 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 |
3.46e-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: 145.31 E-value: 3.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSvTamlIMRLL-----PTgsycvhRGQISLLGEDVln 80
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS-T---LLRIIaglerPT------SGEVLVDGEPV-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 81 arekqlrQWRGARVAMIFQEPmtALNPTRRI------GLQMmdvirhhQPISRREARAKAIALLEEMQIPDAVevmSRYP 154
Cdd:cd03293 69 -------TGPGPDRGYVFQQD--ALLPWLTVldnvalGLEL-------QGVPKAEARERAEELLELVGLSGFE---NAYP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 155 FELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDV----TVQLQVLRLLKHkaraSGTAVLFISHDM--AVVsqLCDSVY 228
Cdd:cd03293 130 HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRE----TGKTVLLVTHDIdeAVF--LADRVV 203
|
..
gi 446115686 229 VM 230
Cdd:cd03293 204 VL 205
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-233 |
4.79e-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: 144.92 E-value: 4.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 8 IQQLHLSFPgfNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQLR 87
Cdd:cd03225 2 LKNLSFSYP--DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTS-----GEVLVDGKDLTKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 88 QwrgaRVAMIFQEPMTAL-NPTRR----IGLQmmdvirhHQPISRREARAKAIALLEEMQIPDaveVMSRYPFELSGGMR 162
Cdd:cd03225 75 R----KVGLVFQNPDDQFfGPTVEeevaFGLE-------NLGLPEEEIEERVEEALELVGLEG---LRDRSPFTLSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115686 163 QRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLK-KLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-245 |
2.80e-41 |
|
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: 144.03 E-value: 2.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSvTAM-LIMRLLPtgsycVHRGQISLLGEDVLNARE 83
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKS-TLLrALAGLLK-----PSSGEVLLDGRDLASLSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 KQLRQwrgaRVAMIFQEPMTALnptrriGLQMMDVIR-----HHQPISR--REARAKAIALLEEMQIPDAVEvmsRYPFE 156
Cdd:COG1120 71 RELAR----RIAYVPQEPPAPF------GLTVRELVAlgrypHLGLFGRpsAEDREAVEEALERTGLEHLAD---RPVDE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 157 LSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVI 236
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
....*....
gi 446115686 237 ESGGTADVI 245
Cdd:COG1120 218 AQGPPEEVL 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-237 |
3.66e-41 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 143.34 E-value: 3.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRL-LPTGsycvhrGQISLLGEDVL 79
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLdRPTS------GTVRLAGQDLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 80 NAREKQLRQWRGARVAMIFQE----P-MTAL-NptrriglQMMdvirhhqPI---SRREARAKAIALLEemqipdAVEVM 150
Cdd:COG4181 78 ALDEDARARLRARHVGFVFQSfqllPtLTALeN-------VML-------PLelaGRRDARARARALLE------RVGLG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 151 SR---YPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQlCDSV 227
Cdd:COG4181 138 HRldhYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRV 216
|
250
....*....|
gi 446115686 228 YVMYAGSVIE 237
Cdd:COG4181 217 LRLRAGRLVE 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-235 |
3.71e-40 |
|
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: 138.68 E-value: 3.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTGsycvhrGQISLLGEDVLNAREK 84
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPDS------GEIKVLGKDIKKEPEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 QLRqwrgaRVAMIFQEPMtalnptrriglqmmdvirhhqpisrrearakaiaLLEEMQIPDAVEvmsrypfeLSGGMRQR 164
Cdd:cd03230 71 VKR-----RIGYLPEEPS----------------------------------LYENLTVRENLK--------LSGGMKQR 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115686 165 VMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:cd03230 104 LALAQALLHDPELLILDEPTSGLDPESRREFWELLR-ELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-244 |
4.26e-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: 140.78 E-value: 4.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPGfngDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQ 85
Cdd:cd03256 1 IEVENLSKTYPN---GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTS-----GSVLIDGTDINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 LRQWRgARVAMIFQ-----EPMTALN----------PTRRIGLQMMDvirhhqpisrREARAKAIALLEEMQIPDAVEVM 150
Cdd:cd03256 73 LRQLR-RQIGMIFQqfnliERLSVLEnvlsgrlgrrSTWRSLFGLFP----------KEEKQRALAALERVGLLDKAYQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 151 SRypfELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVM 230
Cdd:cd03256 142 AD---QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGL 218
|
250
....*....|....
gi 446115686 231 YAGSVIESGGTADV 244
Cdd:cd03256 219 KDGRIVFDGPPAEL 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-253 |
9.73e-40 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 140.06 E-value: 9.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKS-VTAMLIMRLLPTGSYCVHRGQISLLgEDVL 79
Cdd:PRK11701 2 MDQPLLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTtLLNALSARLAPDAGEVHYRMRDGQL-RDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 80 NAREKQLRQWRGARVAMIFQEPMTALNPT----RRIGLQMMDV-IRHHQPIsrreaRAKAIALLEEMQIPdaVEVMSRYP 154
Cdd:PRK11701 77 ALSEAERRRLLRTEWGFVHQHPRDGLRMQvsagGNIGERLMAVgARHYGDI-----RATAGDWLERVEID--AARIDDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 155 FELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGS 234
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
250
....*....|....*....
gi 446115686 235 VIESGGTADVIHHPRHPYT 253
Cdd:PRK11701 230 VVESGLTDQVLDDPQHPYT 248
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-249 |
1.73e-39 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 139.40 E-value: 1.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 2 TQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSvTAM-LImrllpTGSYCVHRGQISLLGEDVLN 80
Cdd:COG0411 1 SDPLLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKT-TLFnLI-----TGFYRPTSGRILFDGRDITG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 81 arekqLRQWRGAR--VAMIFQEP------------MTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDa 146
Cdd:COG0411 71 -----LPPHRIARlgIARTFQNPrlfpeltvlenvLVAAHARLGRGLLAALLRLPRARREEREARERAEELLERVGLAD- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 147 veVMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDS 226
Cdd:COG0411 145 --RADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADR 222
|
250 260
....*....|....*....|...
gi 446115686 227 VYVMYAGSVIESGGTADVIHHPR 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 |
3.20e-39 |
|
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: 138.34 E-value: 3.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSvTAM-LIMRLLPTGSycvhrGQISLLGEDVLNAREK 84
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKT-TLFnLISGFLRPTS-----GSVLFDGEDITGLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 QLRQwRGarVAMIFQEP-----MTALNpTRRIGLQMmdviRHHQPI-------SRREARAKAIALLEEMQIPDaveVMSR 152
Cdd:cd03219 71 EIAR-LG--IGRTFQIPrlfpeLTVLE-NVMVAAQA----RTGSGLllararrEEREARERAEELLERVGLAD---LADR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 153 YPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYA 232
Cdd:cd03219 140 PAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIR-ELRERGITVLLVEHDMDVVMSLADRVTVLDQ 218
|
250
....*....|....*..
gi 446115686 233 GSVIESGGTADVIHHPR 249
Cdd:cd03219 219 GRVIAEGTPDEVRNNPR 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-244 |
7.77e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 140.54 E-value: 7.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 2 TQPVLDIQQLHLSFPGfngdVHALNNVSLQINRGEIVGLVGESGSGKSvTAMLIMrllpTGSYCVHRGQISLLGEDV--L 79
Cdd:COG1129 1 AEPLLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKS-TLMKIL----SGVYQPDSGEILLDGEPVrfR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 80 NAREKQlrqwrGARVAMIFQEPMTALNptrriglqmMDV---------IRHHQPISRREARAKAIALLEEMQI---PDA- 146
Cdd:COG1129 72 SPRDAQ-----AAGIAIIHQELNLVPN---------LSVaeniflgrePRRGGLIDWRAMRRRARELLARLGLdidPDTp 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 147 VEvmsrypfELSGGMRQRVMIAPAFSCEPQLIIAGEPTTAL---DVTVQLQVLRLLKhkarASGTAVLFISHDMAVVSQL 223
Cdd:COG1129 138 VG-------DLSVAQQQLVEIARALSRDARVLILDEPTASLterEVERLFRIIRRLK----AQGVAIIYISHRLDEVFEI 206
|
250 260
....*....|....*....|.
gi 446115686 224 CDSVYVMYAGSVIESGGTADV 244
Cdd:COG1129 207 ADRVTVLRDGRLVGTGPVAEL 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-252 |
9.33e-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: 137.54 E-value: 9.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLN 80
Cdd:COG3842 1 MAMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFET-----PDSGRILLDGRDVTG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 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 446115686 152 RYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHD----MAvvsqLCDSV 227
Cdd:COG3842 131 RYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRI 206
|
250 260
....*....|....*....|....*
gi 446115686 228 YVMYAGSVIESGGTADVIHHPRHPY 252
Cdd:COG3842 207 AVMNDGRIEQVGTPEEIYERPATRF 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-245 |
1.47e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.06 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSvTAM-LIMRLLPtgsycVHRGQISLLGEDVL 79
Cdd:COG1121 2 MMMPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKS-TLLkAILGLLP-----PTSGTVRLFGKPPR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 80 NAREK-----QLRQwrgarVAMIFqePMTALnptrriglqmmDVIR----HHQPISRR---EARAKAIALLEEMQIPDav 147
Cdd:COG1121 72 RARRRigyvpQRAE-----VDWDF--PITVR-----------DVVLmgryGRRGLFRRpsrADREAVDEALERVGLED-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 148 evMSRYPF-ELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDS 226
Cdd:COG1121 132 --LADRPIgELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELL-RELRREGKTILVVTHDLGAVREYFDR 208
|
250
....*....|....*....
gi 446115686 227 VYVMyAGSVIESGGTADVI 245
Cdd:COG1121 209 VLLL-NRGLVAHGPPEEVL 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-260 |
1.66e-37 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 136.82 E-value: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPGFngdvHALNNVSLQINRGEIVGLVGESGSGKSvtamLIMRLL-----PTgsycvhRGQISLLGEDVLN 80
Cdd:COG1118 3 IEVRNISKRFGSF----TLLDDVSLEIASGELVALLGPSGSGKT----TLLRIIagletPD------SGRIVLNGRDLFT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 81 AREKQLRqwrgaRVAMIFQEPmtALNPTrriglqmMDVIRH------HQPISRREARAKAIALLEEMQIPDAVEvmsRYP 154
Cdd:COG1118 69 NLPPRER-----RVGFVFQHY--ALFPH-------MTVAENiafglrVRPPSKAEIRARVEELLELVQLEGLAD---RYP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 155 FELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGS 234
Cdd:COG1118 132 SQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGR 211
|
250 260
....*....|....*....|....*.
gi 446115686 235 VIESGGTADVIHHPRHPYTIGLLQCA 260
Cdd:COG1118 212 IEQVGTPDEVYDRPATPFVARFLGCV 237
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-185 |
2.66e-37 |
|
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: 130.46 E-value: 2.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAREKQLRQwrgaRVAMIFQEPmt 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLsPT------EGTILLDGQDLTDDERKSLRK----EIGYVFQDP-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 104 ALNPTRRIGLQMMDViRHHQPISRREARAKAIALLEEMQIPD-AVEVMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGE 182
Cdd:pfam00005 69 QLFPRLTVRENLRLG-LLLKGLSKREKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
...
gi 446115686 183 PTT 185
Cdd:pfam00005 148 PTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-239 |
4.90e-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: 4.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNaREKQ 85
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLER-----PDSGEILIDGRDVTG-VPPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 LRqwrgaRVAMIFQEPmtALNPTRRI------GLQMMDVirhhqpiSRREARAKAIALLEEMQIPDaveVMSRYPFELSG 159
Cdd:cd03259 71 RR-----NIGMVFQDY--ALFPHLTVaeniafGLKLRGV-------PKAEIRARVRELLELVGLEG---LLNRYPHELSG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 160 GMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03259 134 GQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-239 |
1.78e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 130.56 E-value: 1.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSFPGfngDVHALNNVSLQINRGEIVGLVGESGSGKSvTAM-LIMRLL-PTgsycvhRGQISLLGEDVLNAR 82
Cdd:COG2884 1 MIRFENVSKRYPG---GREALSDVSLEIEKGEFVFLTGPSGAGKS-TLLkLLYGEErPT------SGQVLVNGQDLSRLK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 83 EKQLRQWRgARVAMIFQEP-----MTAL-N---PTRRIGLqmmdvirhhqpiSRREARAKAIALLEEMQIPDAvevMSRY 153
Cdd:COG2884 71 RREIPYLR-RRIGVVFQDFrllpdRTVYeNvalPLRVTGK------------SRKEIRRRVREVLDLVGLSDK---AKAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 154 PFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:COG2884 135 PHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLE-EINRRGTTVLIATHDLELVDRMPKRVLELEDG 213
|
....*.
gi 446115686 234 SVIESG 239
Cdd:COG2884 214 RLVRDE 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
20-233 |
4.44e-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: 128.07 E-value: 4.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVlnAREKQLRQWRGARVAMIF 98
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEePD------SGSILIDGEDL--TDLEDELPPLRRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 99 QEPmtALNPTrriglqmMDVirhhqpisrrearakaialLEEMQIPdavevmsrypfeLSGGMRQRVMIAPAFSCEPQLI 178
Cdd:cd03229 83 QDF--ALFPH-------LTV-------------------LENIALG------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446115686 179 IAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-241 |
5.01e-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: 129.61 E-value: 5.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAREKQ 85
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 LrqWRGARVAMIFQEPmtalNPTR-------RIGLqmmdviRHHQPISRREARAKAIALLEEMQIPDavEVMSR-YPFEL 157
Cdd:cd03260 77 L--ELRRRVGMVFQKP----NPFPgsiydnvAYGL------RLHGIKLKEELDERVEEALRKAALWD--EVKDRlHALGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 158 SGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARAsgTAVLFISHDMAVVSQLCDSVYVMYAGSVIE 237
Cdd:cd03260 143 SGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
....
gi 446115686 238 SGGT 241
Cdd:cd03260 221 FGPT 224
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-253 |
6.17e-36 |
|
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: 130.34 E-value: 6.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 3 QPVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAR 82
Cdd:TIGR02323 1 KPLLQVSGLSKSY----GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 83 EKQLRQWRGARVAMIFQEPMTALNPT----RRIGLQMMDV-IRHHQPIsrreaRAKAIALLEEMQIPDAVevMSRYPFEL 157
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQNPRDGLRMRvsagANIGERLMAIgARHYGNI-----RATAQDWLEEVEIDPTR--IDDLPRAF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 158 SGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIE 237
Cdd:TIGR02323 150 SGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVE 229
|
250
....*....|....*.
gi 446115686 238 SGGTADVIHHPRHPYT 253
Cdd:TIGR02323 230 SGLTDQVLDDPQHPYT 245
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-244 |
2.20e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 129.84 E-value: 2.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSvTAM-LIMRLL-PTGsycvhrGQISLLGEDVlnaR 82
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKT-TTIrIILGILaPDS------GEVLWDGEPL---D 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 83 EKQLRQW------RGarvamifqepmtaLNPTRRIGLQMMDVIRHHQpISRREARAKAIALLEEMQIPDA----VEvmsr 152
Cdd:COG4152 67 PEDRRRIgylpeeRG-------------LYPKMKVGEQLVYLARLKG-LSKAEAKRRADEWLERLGLGDRankkVE---- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 153 ypfELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALD-VTVQL--QVLRLLKhkarASGTAVLFISHDMAVVSQLCDSVYV 229
Cdd:COG4152 129 ---ELSKGNQQKVQLIAALLHDPELLILDEPFSGLDpVNVELlkDVIRELA----AKGTTVIFSSHQMELVEELCDRIVI 201
|
250
....*....|....*
gi 446115686 230 MYAGSVIESGGTADV 244
Cdd:COG4152 202 INKGRKVLSGSVDEI 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-239 |
2.26e-35 |
|
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: 126.40 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 7 DIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQL 86
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSS-----GEILLDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 87 RQwrgaRVAMIFQepmtalnptrriglqmmdvirhhqpisrrearakaiaLLEEMQIPDAVEvmsRYPFELSGGMRQRVM 166
Cdd:cd03214 72 AR----KIAYVPQ-------------------------------------ALELLGLAHLAD---RPFNELSGGERQRVL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115686 167 IAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-252 |
3.80e-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: 128.53 E-value: 3.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAREKQLRQWRGARVAMIF 98
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIePT------SGKVLIDGQDIAAMSRKELRELRRKKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 99 QEpmTALNPTRRI------GLQMmdvirhhQPISRREARAKAIALLEEMQIPDAVEvmsRYPFELSGGMRQRVMIAPAFS 172
Cdd:cd03294 109 QS--FALLPHRTVlenvafGLEV-------QGVPRAEREERAAEALELVGLEGWEH---KYPDELSGGMQQRVGLARALA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 173 CEPQLIIAGEPTTALDVTV----QLQVLRLlkhkARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHHP 248
Cdd:cd03294 177 VDPDILLMDEAFSALDPLIrremQDELLRL----QAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
....
gi 446115686 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 |
5.49e-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: 127.42 E-value: 5.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 18 FNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAREKQLRQwrgaRVAM 96
Cdd:cd03295 10 YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIePT------SGEIFIDGEDIREQDPVELRR----KIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 97 IFQEpmTALNPTRRIgLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAvEVMSRYPFELSGGMRQRVMIAPAFSCEPQ 176
Cdd:cd03295 80 VIQQ--IGLFPHMTV-EENIALVPKLLKWPKEKIRERADELLALVGLDPA-EFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 177 LIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHHPRHPYTIGL 256
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEF 235
|
...
gi 446115686 257 LQC 259
Cdd:cd03295 236 VGA 238
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-233 |
1.30e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 125.31 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPGFNGdvhaLNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVlnaREKQ 85
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDP-----PTSGEIYLDGKPL---SAMP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 LRQWRgARVAMIFQEPmtalnptrriglQMM-DVIRHH-----QPISRREARAKAIALLEEMQIPDavEVMSRYPFELSG 159
Cdd:COG4619 69 PPEWR-RQVAYVPQEP------------ALWgGTVRDNlpfpfQLRERKFDRERALELLERLGLPP--DILDKPVERLSG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115686 160 GMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:COG4619 134 GERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-233 |
3.29e-34 |
|
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: 122.74 E-value: 3.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 8 IQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQLR 87
Cdd:cd00267 2 IENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-----PTSGEILIDGKDIAKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 88 QwrgaRVAMIFQepmtalnptrriglqmmdvirhhqpisrrearakaialleemqipdavevmsrypfeLSGGMRQRVMI 167
Cdd:cd00267 73 R----RIGYVPQ---------------------------------------------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115686 168 APAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLR-ELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-233 |
1.07e-33 |
|
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: 123.02 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVlNAREKQ 85
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDS-----GTIIIDGLKL-TDDKKN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 LRQWRgARVAMIFQ-----EPMTALNptrRIGLQMMDVirhhQPISRREARAKAIALLEEMQIPDaveVMSRYPFELSGG 160
Cdd:cd03262 71 INELR-QKVGMVFQqfnlfPHLTVLE---NITLAPIKV----KGMSKAEAEERALELLEKVGLAD---KADAYPAQLSGG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115686 161 MRQRVMIAPAFSCEPQLIIAGEPTTALD---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 |
4.17e-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: 4.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRL-LPTgsycvhRGQISLLGEDV--LNAREKQlrqwrgarVAM 96
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLeRPD------SGTILFGGEDAtdVPVQERN--------VGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 97 IFQ-----EPMTALNPTRrIGLQMmdvirhhQPISRR----EARAKAIALLEEMQIpDAVEvmSRYPFELSGGMRQRVMI 167
Cdd:cd03296 79 VFQhyalfRHMTVFDNVA-FGLRV-------KPRSERppeaEIRAKVHELLKLVQL-DWLA--DRYPAQLSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 168 APAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHH 247
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
250
....*....|
gi 446115686 248 PRHPYTIGLL 257
Cdd:cd03296 228 PASPFVYSFL 237
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-253 |
2.00e-32 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 121.44 E-value: 2.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 22 VHALNNVSLQINRGEIVGLVGESGSGKSVTA-MLIMRLLPTGsycvhrgqisllGEDVLNAREKQL--RQWRGARVAMIF 98
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAkMLAGMIEPTS------------GELLIDDHPLHFgdYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 99 QEPMTALNPTRRIGlQMMDV-IRHHQPISRrEARAKAI--ALLEEMQIPDAVevmSRYPFELSGGMRQRVMIAPAFSCEP 175
Cdd:PRK15112 94 QDPSTSLNPRQRIS-QILDFpLRLNTDLEP-EQREKQIieTLRQVGLLPDHA---SYYPHMLAPGQKQRLGLARALILRP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115686 176 QLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHHPRHPYT 253
Cdd:PRK15112 169 KVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELT 246
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-230 |
3.27e-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: 119.18 E-value: 3.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTgsycvHRGQISLLGEDVLNAREkqlrqwrgaRVAMIFQ 99
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP-----TSGSIRVFGKPLEKERK---------RIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 100 E-------PMTALNptrrigLQMMDVIRH--HQPISRREARAKAIALLEEMQIPDavevMSRYPF-ELSGGMRQRVMIAP 169
Cdd:cd03235 76 RrsidrdfPISVRD------VVLMGLYGHkgLFRRLSKADKAKVDEALERVGLSE----LADRQIgELSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115686 170 AFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVM 230
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLR-ELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-236 |
8.15e-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: 116.37 E-value: 8.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPGfngdVHALNNVSLQINRGEIVGLVGESGSGKSvTAMLIMrllpTGSYCVHRGQISLLGEDVlnarekq 85
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKS-TLMKIL----SGLYKPDSGEILVDGKEV------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 lrqwrgarvamifqepmtalnptrriglqmmdvirhhQPISRREARAKAIALLeemqipdavevmsrypFELSGGMRQRV 165
Cdd:cd03216 65 -------------------------------------SFASPRDARRAGIAMV----------------YQLSVGERQMV 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115686 166 MIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVI 236
Cdd:cd03216 92 EIARALARNARLLILDEPTAALTPAEVERLFKVIR-RLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-244 |
2.43e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 122.83 E-value: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 4 PVLDIQqlHLSFPGFNGdVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNARE 83
Cdd:COG3845 256 VVLEVE--NLSVRDDRG-VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP-----PASGSIRLDGEDITGLSP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 KQLRQwrgARVAMIFQEPM-TALNPTrriglqmMDVI------RHHQP-------ISRREARAKAIALLEEMQI-PDAVE 148
Cdd:COG3845 328 RERRR---LGVAYIPEDRLgRGLVPD-------MSVAenlilgRYRRPpfsrggfLDRKAIRAFAEELIEEFDVrTPGPD 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 149 VMSRypfELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVY 228
Cdd:COG3845 398 TPAR---SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLL-ELRDAGAAVLLISEDLDEILALSDRIA 473
|
250
....*....|....*.
gi 446115686 229 VMYAGSVIESGGTADV 244
Cdd:COG3845 474 VMYEGRIVGEVPAAEA 489
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
20-248 |
1.27e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 115.96 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVL--NAREKQLRQWRGarvaMI 97
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEE-----ITSGDLIVDGLKVNdpKVDERLIRQEAG----MV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 98 FQE----P-MTALN-----PTRRIGLqmmdvirhhqpiSRREARAKAIALLEEMQIPdavEVMSRYPFELSGGMRQRVMI 167
Cdd:PRK09493 83 FQQfylfPhLTALEnvmfgPLRVRGA------------SKEEAEKQARELLAKVGLA---ERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 168 APAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLfISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHH 247
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
.
gi 446115686 248 P 248
Cdd:PRK09493 227 P 227
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
21-237 |
1.54e-30 |
|
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: 115.14 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 21 DVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRL-LPTGsycvhrGQISLLGEDVLNAREKQLRQWRGARVAMIFQ 99
Cdd:TIGR02211 17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLdNPTS------GEVLFNGQSLSKLSSNERAKLRNKKLGFIYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 100 -----EPMTALNPTrriglqMMDVIRHHQpiSRREARAKAIALLEEMQIPDAvevMSRYPFELSGGMRQRVMIAPAFSCE 174
Cdd:TIGR02211 91 fhhllPDFTALENV------AMPLLIGKK--SVKEAKERAYEMLEKVGLEHR---INHRPSELSGGERQRVAIARALVNQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115686 175 PQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLcDSVYVMYAGSVIE 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 |
2.16e-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: 114.27 E-value: 2.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSFPGfngDVHALNNVSLQINRGEIVGLVGESGSGKS-VTAMLIMRLLPTgsycvhRGQISLLGEDVLNARE 83
Cdd:TIGR02673 1 MIEFHNVSKAYPG---GVAALHDVSLHIRKGEFLFLTGPSGAGKTtLLKLLYGALTPS------RGQVRIAGEDVNRLRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 KQLRQWRgARVAMIFQEPMTALNPT--RRIGLQMmdvirHHQPISRREARAKAIALLEEMQIPDAvevMSRYPFELSGGM 161
Cdd:TIGR02673 72 RQLPLLR-RRIGVVFQDFRLLPDRTvyENVALPL-----EVRGKKEREIQRRVGAALRQVGLEHK---ADAFPEQLSGGE 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115686 162 RQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQ 222
Cdd:TIGR02673 143 QQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLL-KRLNKRGTTVIVATHDLSLVDR 202
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-251 |
2.17e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.84 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSvTAMLIMRLLPTGSycvhRGQISLLGEDVLN 80
Cdd:PRK10619 1 MSENKLNVIDLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLEKPS----EGSIVVNGQTINL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 81 ARE----------KQLRQWRgARVAMIFQE-----PMTALNPTRRIGLQMMDvirhhqpISRREARAKAIALLEEMQIPD 145
Cdd:PRK10619 72 VRDkdgqlkvadkNQLRLLR-TRLTMVFQHfnlwsHMTVLENVMEAPIQVLG-------LSKQEARERAVKYLAKVGIDE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 146 AVEvmSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLfISHDMAVVSQLCD 225
Cdd:PRK10619 144 RAQ--GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSS 220
|
250 260
....*....|....*....|....*.
gi 446115686 226 SVYVMYAGSVIESGGTADVIHHPRHP 251
Cdd:PRK10619 221 HVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-230 |
7.29e-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: 111.71 E-value: 7.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPGfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQ 85
Cdd:cd03228 1 IEFKNVSFSYPG--RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD-----PTSGEILIDGVDLRDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 LRQwrgaRVAMIFQEP----MTalnptrriglqMMDVIrhhqpisrrearakaialleemqipdavevmsrypfeLSGGM 161
Cdd:cd03228 74 LRK----NIAYVPQDPflfsGT-----------IRENI-------------------------------------LSGGQ 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446115686 162 RQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLkhKARASGTAVLFISHDMAVVsQLCDSVYVM 230
Cdd:cd03228 102 RQRIAIARALLRDPPILILDEATSALDPETEALILEAL--RALAKGKTVIVIAHRLSTI-RDADRIIVL 167
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-244 |
8.67e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.21 E-value: 8.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFPGfngdVHALNNVSLQINRGEIVGLVGESGSGKSvTAMLIMrllpTGSYCVHRGQISLLGEDVln 80
Cdd:COG3845 1 MMPPALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKS-TLMKIL----YGLYQPDSGEILIDGKPV-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 81 arekQLRQWRGAR---VAMIFQ-----EPMTAL------NPTRRIGLqmmdvirhhqpISRREARAKAIALLEE--MQI- 143
Cdd:COG3845 70 ----RIRSPRDAIalgIGMVHQhfmlvPNLTVAenivlgLEPTKGGR-----------LDRKAARARIRELSERygLDVd 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 144 PDA-VEvmsrypfELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALdvTVQ-----LQVLRLLKhkarASGTAVLFISHDM 217
Cdd:COG3845 135 PDAkVE-------DLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeadelFEILRRLA----AEGKSIIFITHKL 201
|
250 260
....*....|....*....|....*..
gi 446115686 218 AVVSQLCDSVYVMYAGSVIESGGTADV 244
Cdd:COG3845 202 REVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
20-241 |
1.22e-29 |
|
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: 114.79 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVT-AMLIMRLLPTGsycvhrGQISLLGEDVLnaRE-KQLRQwrgaRVAMI 97
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTiRMLTTLLRPTS------GTARVAGYDVV--REpRKVRR----SIGIV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 98 FQEPMTALNPTRRIGLQMMDVIrhhQPISRREARAKAIALLEEMQIPDAVEVMSRYpfeLSGGMRQRVMIAPAFSCEPQL 177
Cdd:TIGR01188 72 PQYASVDEDLTGRENLEMMGRL---YGLPKDEAEERAEELLELFELGEAADRPVGT---YSGGMRRRLDIAASLIHQPDV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115686 178 IIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGT 241
Cdd:TIGR01188 146 LFLDEPTTGLDPRTRRAIWDYIR-ALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTP 208
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-216 |
1.92e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 113.03 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 4 PVLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVlnare 83
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSS-----GEITLDGVPV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 kqlrQWRGARVAMIFQEpmTALNPTRR------IGLQMmdvirhhQPISRREARAKAIALLEEMQIPDAVEvmsRYPFEL 157
Cdd:COG4525 72 ----TGPGADRGVVFQK--DALLPWLNvldnvaFGLRL-------RGVPKAERRARAEELLALVGLADFAR---RRIWQL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115686 158 SGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTV--QLQVLrLLKHKARaSGTAVLFISHD 216
Cdd:COG4525 136 SGGMRQRVGIARALAADPRFLLMDEPFGALDALTreQMQEL-LLDVWQR-TGKGVFLITHS 194
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
12-256 |
6.65e-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: 6.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 12 HLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNarEKQLRQWR 90
Cdd:TIGR04520 5 NVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLlPT------SGKVTVDGLDTLD--EENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 91 gARVAMIFQepmtalNPTRRI-----------GLQMMDVIRhhqpisrrearakaiallEEMQ--IPDAVEV--MSRY-- 153
Cdd:TIGR04520 77 -KKVGMVFQ------NPDNQFvgatveddvafGLENLGVPR------------------EEMRkrVDEALKLvgMEDFrd 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 154 --PFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDM--AVvsqLCDSVYV 229
Cdd:TIGR04520 132 rePHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMeeAV---LADRVIV 208
|
250 260
....*....|....*....|....*..
gi 446115686 230 MYAGSVIESGGTADVIHHPRHPYTIGL 256
Cdd:TIGR04520 209 MNKGKIVAEGTPREIFSQVELLKEIGL 235
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-247 |
1.30e-28 |
|
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: 115.63 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 2 TQPVLDIQQLHLSFPGfngDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNA 81
Cdd:COG4988 333 GPPSIELEDVSFSYPG---GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP-----PYSGSILINGVDLSDL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 82 REKQLRQwrgaRVAMIFQEP------------MTALNPTRRiglQMMDVIRhhqpisrreaRAKAIALLEEMqiPDAVEV 149
Cdd:COG4988 405 DPASWRR----QIAWVPQNPylfagtirenlrLGRPDASDE---ELEAALE----------AAGLDEFVAAL--PDGLDT 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 150 M-----SRypfeLSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLkhKARASGTAVLFISHDMAVVSQlC 224
Cdd:COG4988 466 PlgeggRG----LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL--RRLAKGRTVILITHRLALLAQ-A 538
|
250 260
....*....|....*....|...
gi 446115686 225 DSVYVMYAGSVIESGGTADVIHH 247
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLAK 561
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-245 |
2.02e-28 |
|
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: 114.90 E-value: 2.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLP--TGSYCVhrgqisLLGEDVLNAREKQ-LRQWRGAR-VA 95
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEptSGEVNV------RVGDEWVDMTKPGpDGRGRAKRyIG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 96 MIFQEpmTALNPTRRIGLQMMDVIRHHQPisRREARAKAIALLEEMQIPD--AVEVMSRYPFELSGGMRQRVMIAPAFSC 173
Cdd:TIGR03269 369 ILHQE--YDLYPHRTVLDNLTEAIGLELP--DELARMKAVITLKMVGFDEekAEEILDKYPDELSEGERHRVALAQVLIK 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115686 174 EPQLIIAGEPTTALDVTVQLQVLRLLkHKARAS-GTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVI 245
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVDVTHSI-LKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-239 |
4.78e-28 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 108.36 E-value: 4.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPgfNGDVHALNNVSLQINRGEIVGLVGESGSGKSVT-AMLIMRLLPTGsycvhrGQISLLGEDVLNAREK 84
Cdd:cd03263 1 LQIRNLTKTYK--KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTlKMLTGELRPTS------GTAYINGYSIRTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 QLRqwrgaRVAMIFQEPMTALNPTRRIGLQMMDVIRHHqpiSRREARAKAIALLEEMQIPDAVEVMSRypfELSGGMRQR 164
Cdd:cd03263 73 ARQ-----SLGYCPQFDALFDELTVREHLRFYARLKGL---PKSEIKEEVELLLRVLGLTDKANKRAR---TLSGGMKRK 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115686 165 VMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARasGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-248 |
4.80e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 111.33 E-value: 4.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDV--LNARE 83
Cdd:PRK10851 3 IEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTS-----GHIRFHGTDVsrLHARD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 KQlrqwrgarVAMIFQ-----EPMTALNPTRrIGLQMMDviRHHQPiSRREARAKAIALLEEMQIPDAVEvmsRYPFELS 158
Cdd:PRK10851 74 RK--------VGFVFQhyalfRHMTVFDNIA-FGLTVLP--RRERP-NAAAIKAKVTQLLEMVQLAHLAD---RYPAQLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 159 GGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIES 238
Cdd:PRK10851 139 GGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQA 218
|
250
....*....|
gi 446115686 239 GGTADVIHHP 248
Cdd:PRK10851 219 GTPDQVWREP 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-234 |
5.05e-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: 108.68 E-value: 5.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTqPVLDIQQLHLSFP--GFNG-DVHALNNVSLQINRGEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGE- 76
Cdd:COG4778 1 MT-TLLEVENLSKTFTlhLQGGkRLPVLDGVSFSVAAGECVALTGPSGAGKST----LLKCI-YGNYLPDSGSILVRHDg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 77 ---DVLNAREKQlrqwrgarvamifqepMTALnptRR--IG-----LQMM------DVIRH---HQPISRREARAKAIAL 137
Cdd:COG4778 75 gwvDLAQASPRE----------------ILAL---RRrtIGyvsqfLRVIprvsalDVVAEpllERGVDREEARARAREL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 138 LEEMQIPDavEVMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDM 217
Cdd:COG4778 136 LARLNLPE--RLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELI-EEAKARGTAIIGIFHDE 212
|
250
....*....|....*..
gi 446115686 218 AVVSQLCDSVYVMYAGS 234
Cdd:COG4778 213 EVREAVADRVVDVTPFS 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-253 |
5.27e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 109.23 E-value: 5.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 3 QPVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAR 82
Cdd:PRK14247 1 MNKIEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 83 EKQLRQwrgaRVAMIFQEPmtalNPTRRI--------GLQMMDVIRhhqpiSRREARAKAIALLEEMQIPDAVEVMSRYP 154
Cdd:PRK14247 77 VIELRR----RVQMVFQIP----NPIPNLsifenvalGLKLNRLVK-----SKKELQERVRWALEKAQLWDEVKDRLDAP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 155 F-ELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDV--TVQLQVLRL-LKHKarasgTAVLFISHDMAVVSQLCDSVYVM 230
Cdd:PRK14247 144 AgKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPenTAKIESLFLeLKKD-----MTIVLVTHFPQQAARISDYVAFL 218
|
250 260
....*....|....*....|...
gi 446115686 231 YAGSVIESGGTADVIHHPRHPYT 253
Cdd:PRK14247 219 YKGQIVEWGPTREVFTNPRHELT 241
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-239 |
5.27e-28 |
|
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: 108.23 E-value: 5.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVT-AMLIMRLLPTGsycvhrGQISLLGEDVLnareKQLRQWRgARVAMIF 98
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTiKMLTTLLKPTS------GRATVAGHDVV----REPREVR-RRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 99 QEPMTALNPTRRIGLQMMDVIrhhQPISRREARAKAIALLEEMQIPDAVEVMSRYpfeLSGGMRQRVMIAPAFSCEPQLI 178
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARL---YGVPGAERRERIDELLDFVGLLEAADRLVKT---YSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115686 179 IAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-248 |
6.50e-28 |
|
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: 108.58 E-value: 6.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPGFNgdvhaLNNVSLQINRGEIVGLVGESGSGKSVTAMLIMrllptGSYCVHRGQISLLGEDVLNAR-EK 84
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIA-----GFIKPDSGKILLNGKDITNLPpEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 QlrqwrgaRVAMIFQEpmTALNPTrriglqmMDVIRH------HQPISRREARAKAIALLEEMQIPdavEVMSRYPFELS 158
Cdd:cd03299 71 R-------DISYVPQN--YALFPH-------MTVYKNiayglkKRKVDKKEIERKVLEIAEMLGID---HLLNRKPETLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 159 GGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIES 238
Cdd:cd03299 132 GGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV 211
|
250
....*....|
gi 446115686 239 GGTADVIHHP 248
Cdd:cd03299 212 GKPEEVFKKP 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-235 |
1.22e-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: 105.98 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 4 PVLDIQQLHLSfpgfngdvHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVlnaRE 83
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP-----PASGEITLDGKPV---TR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 KQLRQWRGARVAMIFQEpmtalnptrriglqmmdviRHHQpisrrearakaiALLEEMQIPDAVeVMSRYpfeLSGGMRQ 163
Cdd:cd03215 67 RSPRDAIRAGIAYVPED-------------------RKRE------------GLVLDLSVAENI-ALSSL---LSGGNQQ 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115686 164 RVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLI-RELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
18-248 |
1.77e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 107.41 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 18 FNGDVHALNNVSLQINRGEIVGLVGESGSGKSvTAMLIMRLLPTGSycvhRGQISLLGEDV-----LNAREKQ-LRQwrg 91
Cdd:COG4161 11 FYGSHQALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLETPD----SGQLNIAGHQFdfsqkPSEKAIRlLRQ--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 92 aRVAMIFQE----P-MTALN-----PTRRIGLqmmdvirhhqpiSRREARAKAIALLEEMQIPDAVEvmsRYPFELSGGM 161
Cdd:COG4161 83 -KVGMVFQQynlwPhLTVMEnlieaPCKVLGL------------SKEQAREKAMKLLARLRLTDKAD---RFPLHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 162 RQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLfISHDMAVVSQLCDSVYVMYAGSVIESgGT 241
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVI-VTHEVEFARKVASQVVYMEKGRIIEQ-GD 224
|
....*..
gi 446115686 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 |
1.80e-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: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSvTamLImRLL-----PTgsycvhRGQISLLGEDVLNAREKQLRQWRGARV 94
Cdd:COG4175 38 GQTVGVNDASFDVEEGEIFVIMGLSGSGKS-T--LV-RCLnrliePT------AGEVLIDGEDITKLSKKELRELRRKKM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 95 AMIFQEpmTALNPTRRI------GLQMmdvirhhQPISRREARAKAIALLE-------EmqipdavevmSRYPFELSGGM 161
Cdd:COG4175 108 SMVFQH--FALLPHRTVlenvafGLEI-------QGVPKAERRERAREALElvglagwE----------DSYPDELSGGM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115686 162 RQRVMIAPAFSCEPQLIIAGEPTTALD--VTVQLQ--VLRLLK--HKarasgTaVLFISHD 216
Cdd:COG4175 169 QQRVGLARALATDPDILLMDEAFSALDplIRREMQdeLLELQAklKK-----T-IVFITHD 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-248 |
2.73e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 107.02 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 8 IQQLHLSFpgFNGDVHALNNVSLQINRGEIVGLVGESGSGKSvTAMLIMRLLPTGSycvhRGQISLLGEDV---LNAREK 84
Cdd:PRK11124 3 IQLNGINC--FYGAHQALFDITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLEMPR----SGTLNIAGNHFdfsKTPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 QLRQWRgARVAMIFQE----P-MTALN-----PTRRIGLqmmdvirhhqpiSRREARAKAIALLEEMQIPDAVEvmsRYP 154
Cdd:PRK11124 76 AIRELR-RNVGMVFQQynlwPhLTVQQnlieaPCRVLGL------------SKDQALARAEKLLERLRLKPYAD---RFP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 155 FELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLfISHDMAVVSQLCDSVYVMYAGS 234
Cdd:PRK11124 140 LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVI-VTHEVEVARKTASRVVYMENGH 218
|
250
....*....|....
gi 446115686 235 VIESgGTADVIHHP 248
Cdd:PRK11124 219 IVEQ-GDASCFTQP 231
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
20-227 |
5.76e-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: 105.00 E-value: 5.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSvTAMLIMRLLPTGSycvhRGQISLLGEDVLNAREKQLRQWRGARVAMIFQ 99
Cdd:TIGR03608 9 GDKVILDDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLLEKFD----SGQVYLNGQETPPLNSKKASKFRREKLGYLFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 100 EpmTALNPTRRIgLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEvmsRYPFELSGGMRQRVMIAPAFSCEPQLII 179
Cdd:TIGR03608 84 N--FALIENETV-EENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLK---QKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446115686 180 AGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQlCDSV 227
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLL-ELNDEGKTIIIVTHDPEVAKQ-ADRV 203
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-244 |
7.54e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 106.67 E-value: 7.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 24 ALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKqLRQWRgARVAMIFQEPM- 102
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTS-----GKIIIDGVDITDKKVK-LSDIR-KKVGLVFQYPEy 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 103 ----------TALNPtRRIGLQmmdvirhHQPISRREARAKAIALLEEMQIPDavevmsRYPFELSGGMRQRVMIAPAFS 172
Cdd:PRK13637 95 qlfeetiekdIAFGP-INLGLS-------EEEIENRVKRAMNIVGLDYEDYKD------KSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115686 173 CEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADV 244
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-248 |
1.07e-26 |
|
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: 105.01 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLImrllpTGSYCVHRGQISLLGEDVLN--AREKQlrqwrgarVAMI 97
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLI-----AGFETPTSGEILLDGKDITNlpPHKRP--------VNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 98 FQEpmTALNP----TRRI--GLQMmdvirhhQPISRREARAKAIALLEEMQIPdavEVMSRYPFELSGGMRQRVMIAPAF 171
Cdd:cd03300 78 FQN--YALFPhltvFENIafGLRL-------KKLPKAEIKERVAEALDLVQLE---GYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446115686 172 SCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHHP 248
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-237 |
1.36e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.07 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 16 PGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVtamlIMR-----LLPTgsycvhRGQISLLGEDV-LNAREKQLRQW 89
Cdd:PRK13641 14 PGTPMEKKGLDNISFELEEGSFVALVGHTGSGKST----LMQhfnalLKPS------SGTITIAGYHItPETGNKNLKKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 90 RgARVAMIFQEPMTALnpTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDavEVMSRYPFELSGGMRQRVMIAP 169
Cdd:PRK13641 84 R-KKVSLVFQFPEAQL--FENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSE--DLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115686 170 AFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARAsGTAVLFISHDMAVVSQLCDSVYVMYAGSVIE 237
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-239 |
2.83e-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: 109.15 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPGfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVlnaREK 84
Cdd:COG2274 474 IELENVSFRYPG--DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYePT------SGRILIDGIDL---RQI 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 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 446115686 157 -LSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLkhKARASGTAVLFISHDMAVVsQLCDSVYVMYAGSV 235
Cdd:COG2274 611 nLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL--RRLLKGRTVIIIAHRLSTI-RLADRIIVLDKGRI 687
|
....
gi 446115686 236 IESG 239
Cdd:COG2274 688 VEDG 691
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-239 |
3.02e-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: 103.60 E-value: 3.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLnarekq 85
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDA-----GFATVDGFDVV------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 lRQWRGARVAMIFQEPMTALNPtRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPdavEVMSRYPFELSGGMRQRV 165
Cdd:cd03266 71 -KEPAEARRRLGFVSDSTGLYD-RLTARENLEYFAGLYGLKGDELTARLEELADRLGME---ELLDRRVGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115686 166 MIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKaRASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-220 |
3.50e-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: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPGfngDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRL-LPTgsycvhRGQISLLGEDVLNAREK 84
Cdd:cd03292 1 IEFINVTKTYPN---GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPT------SGTIRVNGQDVSDLRGR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 QLRQWRgARVAMIFQEpmTALNPTRRIGLQM---MDVIRHhqpiSRREARAKAIALLEEMQIPDAVEVMsryPFELSGGM 161
Cdd:cd03292 72 AIPYLR-RKIGVVFQD--FRLLPDRNVYENVafaLEVTGV----PPREIRKRVPAALELVGLSHKHRAL---PAELSGGE 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446115686 162 RQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVV 220
Cdd:cd03292 142 QQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLK-KINKAGTTVVVATHAKELV 199
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
24-256 |
6.64e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 104.33 E-value: 6.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 24 ALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLlGEDVLNA--REKQLRQWRgARVAMIFQE 100
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqPT------SGTVTI-GERVITAgkKNKKLKPLR-KKVGIVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 101 PMTAL---NPTRRIGLQMMDVirhhqPISRREARAKAIALLEEMQIPDavEVMSRYPFELSGGMRQRVMIAPAFSCEPQL 177
Cdd:PRK13634 94 PEHQLfeeTVEKDICFGPMNF-----GVSEEDAKQKAREMIELVGLPE--ELLARSPFELSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446115686 178 IIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHHPRHPYTIGL 256
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEAIGL 245
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-252 |
7.40e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 106.27 E-value: 7.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 24 ALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAREKQLRQWRGARVAMIFQE-- 100
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePT------RGQVLIDGVDIAKISDAELREVRRKKIAMVFQSfa 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 101 ---PMTALNPTRrIGLQMMDvirhhqpISRREARAKAIALLEEMQIPDAVEvmsRYPFELSGGMRQRVMIAPAFSCEPQL 177
Cdd:PRK10070 117 lmpHMTVLDNTA-FGMELAG-------INAEERREKALDALRQVGLENYAH---SYPDELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115686 178 IIAGEPTTALDVTVQLQVL-RLLKHKARASGTaVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHHPRHPY 252
Cdd:PRK10070 186 LLMDEAFSALDPLIRTEMQdELVKLQAKHQRT-IVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
20-239 |
8.13e-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: 101.97 E-value: 8.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQ---LRQWRGarvam 96
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS-----GEVLFDGKPLDIAARNRigyLPEERG----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 97 ifqepmtaLNPTRRIGLQMMDVIRHHQpISRREARAKAIALLEEMQIPDAVEVMSRypfELSGGMRQRVMIAPAFSCEPQ 176
Cdd:cd03269 81 --------LYPKMKVIDQLVYLAQLKG-LKKEEARRRIDEWLERLELSEYANKRVE---ELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115686 177 LIIAGEPTTALD-VTVQL--QVLRLLkhkaRASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03269 149 LLILDEPFSGLDpVNVELlkDVIREL----ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-250 |
2.10e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 104.00 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTamliMRLL-----PTGsycvhrGQISLLGEDVLN 80
Cdd:COG3839 4 LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRMIagledPTS------GEILIGGRDVTD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 81 AREKQlrqwRGarVAMIFQEPmtALNPT---RR---IGLQMMDVirhhqpiSRREARAKAIALLEEMQIPDaveVMSRYP 154
Cdd:COG3839 70 LPPKD----RN--IAMVFQSY--ALYPHmtvYEniaFPLKLRKV-------PKAEIDRRVREAAELLGLED---LLDRKP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 155 FELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALD----VTVQLQVLRLLkhkaRASGTAVLFISHD----MAvvsqLCDS 226
Cdd:COG3839 132 KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLH----RRLGTTTIYVTHDqveaMT----LADR 203
|
250 260
....*....|....*....|....
gi 446115686 227 VYVMYAGSVIESGGTADVIHHPRH 250
Cdd:COG3839 204 IAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
24-239 |
2.53e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.55 E-value: 2.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 24 ALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLN-AREKQLRQWRgARVAMIFQEP 101
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLkPT------TGTVTVDDITITHkTKDKYIRPVR-KRIGMVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 102 MTAL---NPTRRIGLQ----MMDVirhhqpisrREARAKAIALLEEMQIPDavEVMSRYPFELSGGMRQRVMIAPAFSCE 174
Cdd:PRK13646 95 ESQLfedTVEREIIFGpknfKMNL---------DEVKNYAHRLLMDLGFSR--DVMSQSPFQMSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115686 175 PQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
20-239 |
2.64e-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: 100.79 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRL-LPTGsycvhrGQISLLGEDVLNAREKQlrqwRGarVAMIF 98
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLeEPTS------GRIYIGGRDVTDLPPKD----RD--IAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 99 QEpmTALNPTRRI------GLQMmdvirHHQPISRREARAKAIAllEEMQIPdavEVMSRYPFELSGGMRQRVMIAPAFS 172
Cdd:cd03301 79 QN--YALYPHMTVydniafGLKL-----RKVPKDEIDERVREVA--ELLQIE---HLLDRKPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446115686 173 CEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-266 |
3.35e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.77 E-value: 3.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 4 PVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTamliMRLLpTGSYCVHRGQISLLGedvlnare 83
Cdd:PRK13548 1 AMLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTL----LRAL-SGELSPDSGEVRLNG-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 KQLRQWRGA----RVAMIFQE-----PMTALnptrriglqmmDVI---RHHQPISRREARAkaiALLEEMQIPDAVEVMS 151
Cdd:PRK13548 64 RPLADWSPAelarRRAVLPQHsslsfPFTVE-----------EVVamgRAPHGLSRAEDDA---LVAAALAQVDLAHLAG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 152 R-YPfELSGGMRQRVMIAPAF------SCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLC 224
Cdd:PRK13548 130 RdYP-QLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYA 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446115686 225 DSVYVMYAGSVIESGGTADVIHHP--RHPYTIGLL-QCAPEHGVP 266
Cdd:PRK13548 209 DRIVLLHQGRLVADGTPAEVLTPEtlRRVYGADVLvQPHPETGAP 253
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-252 |
4.35e-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: 105.23 E-value: 4.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 2 TQPVLDIQQLHLSFPGfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNA 81
Cdd:COG4987 330 GGPSLELEDVSFRYPG--AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD-----PQSGSITLGGVDLRDL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 82 REKQLRQwrgaRVAMIFQEP----MTalnptrriglqMMDVIRhhqpISRREA-RAKAIALLEEMQIPDAVEvmsRYP-- 154
Cdd:COG4987 403 DEDDLRR----RIAVVPQRPhlfdTT-----------LRENLR----LARPDAtDEELWAALERVGLGDWLA---ALPdg 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 155 ---------FELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLkhKARASGTAVLFISHDMAVVSQlCD 225
Cdd:COG4987 461 ldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL--LEALAGRTVLLITHRLAGLER-MD 537
|
250 260
....*....|....*....|....*..
gi 446115686 226 SVYVMYAGSVIESGGTADVIHHPRHPY 252
Cdd:COG4987 538 RILVLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
18-253 |
4.77e-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: 4.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 18 FNGDVhALNNVSLQINRGEIVGLVGESGSGKSvTAMLIMRLL--PTGSYcVHRGQISLLGEDVLNAREKQLRQWRgARVA 95
Cdd:PRK11264 13 FHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLeqPEAGT-IRVGDITIDTARSLSQQKGLIRQLR-QHVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 96 MIFQEpmTALNPTRRIglqmMDVIRHHQPISRREARAKAIALLEEMQIPDAVE-VMSRYPFELSGGMRQRVMIAPAFSCE 174
Cdd:PRK11264 89 FVFQN--FNLFPHRTV----LENIIEGPVIVKGEPKEEATARARELLAKVGLAgKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446115686 175 PQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLfISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHHPRHPYT 253
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRT 240
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-256 |
6.42e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 101.25 E-value: 6.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQqlHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLN 80
Cdd:PRK13635 1 MKEEIIRVE--HISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 81 AREKqlrqwrgarVAMIFQepmtalNPTRR-IGLQMMDVIR---HHQPISRREARAKAIALLEE--MQipdavEVMSRYP 154
Cdd:PRK13635 79 VRRQ---------VGMVFQ------NPDNQfVGATVQDDVAfglENIGVPREEMVERVDQALRQvgME-----DFLNREP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 155 FELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQlCDSVYVMYAGS 234
Cdd:PRK13635 139 HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGE 217
|
250 260
....*....|....*....|..
gi 446115686 235 VIESGGTADVIHHPRHPYTIGL 256
Cdd:PRK13635 218 ILEEGTPEEIFKSGHMLQEIGL 239
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-253 |
7.55e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 101.33 E-value: 7.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 17 GFNGDVhALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAREkqLRQWRgARVAM 96
Cdd:PRK14271 30 GFAGKT-VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRD--VLEFR-RRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 97 IFQEPmtalNPtrrIGLQMMDVI----RHHQPISRREARAKAIALLEEMQIPDAV-EVMSRYPFELSGGMRQRVMIAPAF 171
Cdd:PRK14271 106 LFQRP----NP---FPMSIMDNVlagvRAHKLVPRKEFRGVAQARLTEVGLWDAVkDRLSDSPFRLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 172 SCEPQLIIAGEPTTALDVTVQLQVLRLLkhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHHPRHP 251
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFI--RSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
..
gi 446115686 252 YT 253
Cdd:PRK14271 257 ET 258
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-255 |
7.62e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 104.24 E-value: 7.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFPGfngdVHALNNVSLQINRGEIVGLVGESGSGKSVtamlIMRLL----PTGSYcvhRGQISLLGE 76
Cdd:PRK13549 1 MMEYLLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKST----LMKVLsgvyPHGTY---EGEIIFEGE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 77 DVlnaREKQLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQ--IPDAVEVMsryp 154
Cdd:PRK13549 70 EL---QASNIRDTERAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKldINPATPVG---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 155 fELSGGMRQRVMIAPAFSCEPQLIIAGEPTTAL---DVTVQLQVLRLLKHKarasGTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:PRK13549 143 -NLGLGQQQLVEIAKALNKQARLLILDEPTASLtesETAVLLDIIRDLKAH----GIACIYISHKLNEVKAISDTICVIR 217
|
250 260 270
....*....|....*....|....*....|....*....
gi 446115686 232 AGSVI-----ESGGTADVIH----------HPRHPYTIG 255
Cdd:PRK13549 218 DGRHIgtrpaAGMTEDDIITmmvgreltalYPREPHTIG 256
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-239 |
9.46e-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: 99.19 E-value: 9.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPGfngdVHALNNVSLQINRGeIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKq 85
Cdd:cd03264 1 LQLENLTKRYGK----KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSS-----GTIRIDGQDVLKQPQK- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 LRQwrgaRVAMIFQEPMTALNPTRRIGLQMMDVIRHhqpISRREARAKAIALLEEMQIPDaveVMSRYPFELSGGMRQRV 165
Cdd:cd03264 70 LRR----RIGYLPQEFGVYPNFTVREFLDYIAWLKG---IPSKEVKARVDEVLELVNLGD---RAKKKIGSLSGGMRRRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115686 166 MIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHkaRASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSE--LGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-249 |
1.27e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 102.61 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 4 PVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNARE 83
Cdd:PRK09536 2 PMIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA-----GTVLVAGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 KQLrqwrGARVAMIFQEPMTALNPTRRiglQMMDVIRH-HQPISRREARAKAIALLEEMQIPDAVEVMSRYPFELSGGMR 162
Cdd:PRK09536 73 RAA----SRRVASVPQDTSLSFEFDVR---QVVEMGRTpHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 163 QRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFIsHDMAVVSQLCDSVYVMYAGSVIESGGTA 242
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPA 224
|
....*..
gi 446115686 243 DVIHHPR 249
Cdd:PRK09536 225 DVLTADT 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-236 |
1.49e-24 |
|
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: 98.48 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 12 HLSFpGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTgsycvHRGQISLLGEDVLNARekqlrqwRG 91
Cdd:cd03226 4 NISF-SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE-----SSGSILLNGKPIKAKE-------RR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 92 ARVAMIFQEPMTAL---NPTRRIGLQMMDvirhhqpISRREARAKAIalLEEMQIPDAVEvmsRYPFELSGGMRQRVMIA 168
Cdd:cd03226 71 KSIGYVMQDVDYQLftdSVREELLLGLKE-------LDAGNEQAETV--LKDLDLYALKE---RHPLSLSGGQKQRLAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115686 169 PAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARAsGTAVLFISHDMAVVSQLCDSVYVMYAGSVI 236
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-222 |
1.51e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 104.04 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTqPVLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSvTAMLIMRLL--PT-GSYCVhrgqislLGED 77
Cdd:PRK10535 1 MT-ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS-TLMNILGCLdkPTsGTYRV-------AGQD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 78 VLNAREKQLRQWRGARVAMIFQ--EPMTALNptrriGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVmsrYPF 155
Cdd:PRK10535 72 VATLDADALAQLRREHFGFIFQryHLLSHLT-----AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEY---QPS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446115686 156 ELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQ 222
Cdd:PRK10535 144 QLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAIL-HQLRDRGHTVIIVTHDPQVAAQ 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-239 |
1.60e-24 |
|
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: 98.44 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQ 85
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDS-----GEITFDGKSYQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 lrqwrgARVAMIFQEP-----MTALNPTRRIGLQMMdvirhhqpisRREARAKAIALLEEMQIPDAVEVMSrypfeLSGG 160
Cdd:cd03268 72 ------RRIGALIEAPgfypnLTARENLRLLARLLG----------IRKKRIDEVLDVVGLKDSAKKKVKG-----FSLG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446115686 161 MRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03268 131 MKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELI-LSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-239 |
1.61e-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: 99.33 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 21 DVHALNNVSLQINRGEIVGLVGESGSGKSVT-AMLIMRLLPTGsycvhrGQISLLGEDVLNAREKQLRqwrgaRVAMIF- 98
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTlKILSGLLQPTS------GEVRVAGLVPWKRRKKFLR-----RIGVVFg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 99 QEPMTALNPTRRIGLQMMdviRHHQPISRREARAKAIALLEEMQIPDAVEVMSRypfELSGGMRQRVMIAPAFSCEPQLI 178
Cdd:cd03267 102 QKTQLWWDLPVIDSFYLL---AAIYDLPPARFKKRLDELSELLDLEELLDTPVR---QLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115686 179 IAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
10-248 |
2.32e-24 |
|
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: 101.33 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 10 QLHLSFPGFngdvhALNnVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTgsycvHRGQISLLGEDVLNAREkqlRQW 89
Cdd:COG4148 6 DFRLRRGGF-----TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERP-----DSGRIRLGGEVLQDSAR---GIF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 90 RGA---RVAMIFQEPmtALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEemqIPDaveVMSRYPFELSGGMRQRVM 166
Cdd:COG4148 72 LPPhrrRIGYVFQEA--RLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLG---IGH---LLDRRPATLSGGERQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 167 IAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIH 246
Cdd:COG4148 144 IGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
..
gi 446115686 247 HP 248
Cdd:COG4148 224 RP 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-244 |
4.64e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 98.91 E-value: 4.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 3 QPVLDIQQLHLSFPgfNGDVHALNNVSLQINRGEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGEDVLNAR 82
Cdd:PRK13632 5 SVMIKVENVSFSYP--NSENNALKNVSFEINEGEYVAILGHNGSGKST----ISKIL-TGLLKPQSGEIKIDGITISKEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 83 EKQLRQwrgaRVAMIFQepmtalNPTRR-IGLQMMDVIR---HHQPISRREARAKAIALLEEMQIPDAVEvmsRYPFELS 158
Cdd:PRK13632 78 LKEIRK----KIGIIFQ------NPDNQfIGATVEDDIAfglENKKVPPKKMKDIIDDLAKKVGMEDYLD---KEPQNLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 159 GGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSqLCDSVYVMYAGSVIES 238
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQ 223
|
....*.
gi 446115686 239 GGTADV 244
Cdd:PRK13632 224 GKPKEI 229
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
236-300 |
5.26e-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: 92.85 E-value: 5.26e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115686 236 IESGGTADVIHHPRHPYTIGLLQCAPEHGVPRQPLPAIPGTVPNLTHLPDGCAFRDRCYAAGAQC 300
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-239 |
8.01e-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: 8.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 12 HLSFpGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGEDVlnaREKQLRQWRg 91
Cdd:COG1132 344 NVSF-SYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF-----YDPTSGRILIDGVDI---RDLTLESLR- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 92 ARVAMIFQEP----MTAlnptrriglqmMDVIRhhqpISRREA------RAKAIALLEE--MQIPDAVE-------VMsr 152
Cdd:COG1132 414 RQIGVVPQDTflfsGTI-----------RENIR----YGRPDAtdeeveEAAKAAQAHEfiEALPDGYDtvvgergVN-- 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 153 ypfeLSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARasGTAVLFISHDMAVVsQLCDSVYVMYA 232
Cdd:COG1132 477 ----LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTI-RNADRILVLDD 549
|
....*..
gi 446115686 233 GSVIESG 239
Cdd:COG1132 550 GRIVEQG 556
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-216 |
9.24e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 97.16 E-value: 9.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 2 TQPVLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSvTAMLIMRLLPTGSycvhRGQISLLGEDVLNA 81
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKS-TLLAILAGLDDGS----SGEVSLVGQPLHQM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 82 REKQLRQWRGARVAMIFQEPMtaLNPTRRI--GLQMMDVIRHHqpiSRREARAKAIALLEEMQIPDAVEVMsryPFELSG 159
Cdd:PRK10584 78 DEEARAKLRAKHVGFVFQSFM--LIPTLNAleNVELPALLRGE---SSRQSRNGAKALLEQLGLGKRLDHL---PAQLSG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446115686 160 GMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHD 216
Cdd:PRK10584 150 GEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-256 |
1.08e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 98.24 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSFPGfNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAREK 84
Cdd:PRK13642 4 ILEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 qlrqwrgarVAMIFQEPmtalnPTRRIGLQMMDVI---RHHQPISRREARAKaiaLLEEMQIPDAVEVMSRYPFELSGGM 161
Cdd:PRK13642 83 ---------IGMVFQNP-----DNQFVGATVEDDVafgMENQGIPREEMIKR---VDEALLAVNMLDFKTREPARLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 162 RQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESGGT 241
Cdd:PRK13642 146 KQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAP 224
|
250
....*....|....*
gi 446115686 242 ADVIHHPRHPYTIGL 256
Cdd:PRK13642 225 SELFATSEDMVEIGL 239
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
24-247 |
1.16e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 97.89 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 24 ALNNVSLQINRGEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGEDVLN-AREKQLRQWRgARVAMIFQEPM 102
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKST----IMQLL-NGLHVPTQGSVRVDDTLITStSKNKDIKQIR-KKVGLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 103 TAL-NPTrriglQMMDVIRHHQP--ISRREARAKAIALLEEMQIPDavEVMSRYPFELSGGMRQRVMIAPAFSCEPQLII 179
Cdd:PRK13649 96 SQLfEET-----VLKDVAFGPQNfgVSQEEAEALAREKLALVGISE--SLFEKNPFELSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115686 180 AGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHH 247
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFK-KLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-236 |
2.24e-23 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 100.08 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 2 TQPVLDIQQLHLSFPGfngdVHALNNVSLQINRGEIVGLVGESGSGKSvTAMLIMrllpTGSYCVHRGQISLLGEDVLNA 81
Cdd:PRK10762 1 MQALLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKS-TMMKVL----TGIYTRDAGSILYLGKEVTFN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 82 REKQLRQwrgARVAMIFQEpmtaLN----------------PTRRIGLqmmdvirhhqpISRREARAKAIALLEEMQIPD 145
Cdd:PRK10762 72 GPKSSQE---AGIGIIHQE----LNlipqltiaeniflgreFVNRFGR-----------IDWKKMYAEADKLLARLNLRF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 146 AvevmSRYPF-ELSGGMRQRVMIAPAFSCEPQLIIAGEPTTAL-DV-TVQL-QVLRLLkhkaRASGTAVLFISHDMAVVS 221
Cdd:PRK10762 134 S----SDKLVgELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTeTESLfRVIREL----KSQGRGIVYISHRLKEIF 205
|
250
....*....|....*
gi 446115686 222 QLCDSVYVMYAGSVI 236
Cdd:PRK10762 206 EICDDVTVFRDGQFI 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-239 |
3.19e-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: 95.76 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 17 GFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGEDVLNAREKQLRQwrgaRVAM 96
Cdd:cd03254 11 SYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRF-----YDPQKGQILIDGIDIRDISRKSLRS----MIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 97 IFQEPmTALNPTrriglqMMDVIRHHQPISRRE---ARAKAIALLEE-MQIPDAVE-VMSRYPFELSGGMRQRVMIAPAF 171
Cdd:cd03254 82 VLQDT-FLFSGT------IMENIRLGRPNATDEeviEAAKEAGAHDFiMKLPNGYDtVLGENGGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115686 172 SCEPQLIIAGEPTTALDV----TVQLQVLRLLKhkarasGTAVLFISHDMAVVsQLCDSVYVMYAGSVIESG 239
Cdd:cd03254 155 LRDPKILILDEATSNIDTetekLIQEALEKLMK------GRTSIIIAHRLSTI-KNADKILVLDDGKIIEEG 219
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-245 |
3.30e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 96.34 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSvTamlIMRLLpTGSYCVHRGQISLLGedvlnareKQ 85
Cdd:COG4559 2 LEAENLSVRL----GGRTLLDDVSLTLRPGELTAIIGPNGAGKS-T---LLKLL-TGELTPSSGEVRLNG--------RP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 LRQWRGARVAMI-----------FqePMTALnptrriglqmmDVI---RHHQPISRREARAKAIALLEEMQIPDAVEvmS 151
Cdd:COG4559 65 LAAWSPWELARRravlpqhsslaF--PFTVE-----------EVValgRAPHGSSAAQDRQIVREALALVGLAHLAG--R 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 152 RYPfELSGGMRQRVMIA-------PAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARAsGTAVLFISHDMAVVSQLC 224
Cdd:COG4559 130 SYQ-TLSGGEQQRVQLArvlaqlwEPVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYA 207
|
250 260
....*....|....*....|.
gi 446115686 225 DSVYVMYAGSVIESGGTADVI 245
Cdd:COG4559 208 DRILLLHQGRLVAQGTPEEVL 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-239 |
3.30e-23 |
|
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: 95.05 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 27 NVSLQINrGEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGEdVLNAREKQLR---QWRgaRVAMIFQEpmT 103
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKST----LLRCI-AGLEKPDGGTIVLNGT-VLFDSRKKINlppQQR--KIGLVFQQ--Y 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 104 ALNPTRRIGLQMMDVIRHHqpiSRREARAKAIALLEEMQIPdavEVMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEP 183
Cdd:cd03297 85 ALFPHLNVRENLAFGLKRK---RNREDRISVDELLDLLGLD---HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446115686 184 TTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-236 |
5.67e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.94 E-value: 5.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 4 PVLDIQqlHLSFPGfngdvhALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVlnaRE 83
Cdd:COG1129 255 VVLEVE--GLSVGG------VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADP-----ADSGEIRLDGKPV---RI 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 KQLRQWRGARVAMIfqeP----MTALNPTRRIG----LQMMDVIRHHQPISRREARAKAIALLEEMQI----PDAvEVMS 151
Cdd:COG1129 319 RSPRDAIRAGIAYV---PedrkGEGLVLDLSIRenitLASLDRLSRGGLLDRRRERALAEEYIKRLRIktpsPEQ-PVGN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 152 rypfeLSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:COG1129 395 -----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLI-RELAAEGKAVIVISSELPELLGLSDRILVMR 468
|
....*
gi 446115686 232 AGSVI 236
Cdd:COG1129 469 EGRIV 473
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-267 |
6.54e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.34 E-value: 6.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 24 ALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGedvlNAREKQLRQWRgARVAMIFQEPMT 103
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSS----TSKQKEIKPVR-KKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 104 ALnpTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIpdAVEVMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEP 183
Cdd:PRK13643 96 QL--FEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGL--ADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 184 TTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHHprhpytIGLLQcAPEH 263
Cdd:PRK13643 172 TAGLDPKARIEMMQLFE-SIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE------VDFLK-AHEL 243
|
....
gi 446115686 264 GVPR 267
Cdd:PRK13643 244 GVPK 247
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-253 |
7.27e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 95.29 E-value: 7.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAREKQLRQWRgaRVAMIFQ 99
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEVRR--EVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 100 EPmtalNP--------TRRIGLQMMDVIRHHQPISRR-EARAKAIALLEEMQipdavEVMSRYPFELSGGMRQRVMIAPA 170
Cdd:PRK14267 93 YP----NPfphltiydNVAIGVKLNGLVKSKKELDERvEWALKKAALWDEVK-----DRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 171 FSCEPQLIIAGEPTTALDVTVQLQVLRLLkHKARASGTAVLfISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHHPRH 250
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELL-FELKKEYTIVL-VTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
...
gi 446115686 251 PYT 253
Cdd:PRK14267 242 ELT 244
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
25-249 |
9.13e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 94.71 E-value: 9.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNarekqLRQWRGARVAMIF--QEP- 101
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK-----PDSGRIFLDGEDITH-----LPMHKRARLGIGYlpQEAs 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 102 ----MTALNPTRRIgLQMmdvirhhQPISRREARAKAIALLEEMQIpdaVEVMSRYPFELSGGMRQRVMIAPAFSCEPQL 177
Cdd:COG1137 89 ifrkLTVEDNILAV-LEL-------RKLSKKEREERLEELLEEFGI---THLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115686 178 IIAGEPTTALD-VTVQ-LQ-VLRLLKHKarasGTAVLFISHDmavVS---QLCDSVYVMYAGSVIESGGTADVIHHPR 249
Cdd:COG1137 158 ILLDEPFAGVDpIAVAdIQkIIRHLKER----GIGVLITDHN---VRetlGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-253 |
1.43e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 94.33 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 2 TQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNA 81
Cdd:COG1117 8 LEPKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIYDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 82 REK--QLRqwrgARVAMIFQEPmtalNP-TRRI------GLqmmdviRHHQPISRREARAKAIALLEEMQIPDavEV--- 149
Cdd:COG1117 84 DVDvvELR----RRVGMVFQKP----NPfPKSIydnvayGL------RLHGIKSKSELDEIVEESLRKAALWD--EVkdr 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 150 MSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQV---LRLLKHKarasgTAVLFISHDMAVVSQLCDS 226
Cdd:COG1117 148 LKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIeelILELKKD-----YTIVIVTHNMQQAARVSDY 222
|
250 260
....*....|....*....|....*..
gi 446115686 227 VYVMYAGSVIESGGTADVIHHPRHPYT 253
Cdd:COG1117 223 TAFFYLGELVEFGPTEQIFTNPKDKRT 249
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
27-245 |
1.88e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 93.80 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 27 NVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLP--TGSYCVHRGQISLLGedvLNAREKqlrqwRGarVAMIFQEPmta 104
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPrdAGNIIIDDEDISLLP---LHARAR-----RG--IGYLPQEA--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 105 lNPTRRIGL--QMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRypfELSGGMRQRVMIAPAFSCEPQLIIAGE 182
Cdd:PRK10895 88 -SIFRRLSVydNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQ---SLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115686 183 PTTALDVTVQLQVLRLLKHkARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVI 245
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-239 |
1.88e-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: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 12 HLSFpGFNGD-VHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGEDVlnaREKQLRQWR 90
Cdd:cd03251 5 NVTF-RYPGDgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRF-----YDVDSGRILIDGHDV---RDYTLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 91 gARVAMIFQEPMTaLNPTrriglqMMDVIRHHQP-ISRREARAKA-IALLEE--MQIPDAVE-VMSRYPFELSGGMRQRV 165
Cdd:cd03251 76 -RQIGLVSQDVFL-FNDT------VAENIAYGRPgATREEVEEAArAANAHEfiMELPEGYDtVIGERGVKLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115686 166 MIAPAFSCEPQLIIAGEPTTALDVT----VQLQVLRLLKHKarasgtAVLFISHDMAVVSQlCDSVYVMYAGSVIESG 239
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTEserlVQAALERLMKNR------TTFVIAHRLSTIEN-ADRIVVLEDGKIVERG 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-247 |
2.57e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 95.15 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 22 VHALNNVSLQINRGEIVGLVGESGSGKSVT-AMLIMRLLPTGsycvhrGQISLLGEDVlNAREKQLRqwrgarvamifqe 100
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTiKMLTGILVPTS------GEVRVLGYVP-FKRRKEFA------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 101 pmtalnptRRIGLQM---------------MDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRypfELSGGMRQRV 165
Cdd:COG4586 95 --------RRIGVVFgqrsqlwwdlpaidsFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVR---QLSLGQRMRC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 166 MIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVI 245
Cdd:COG4586 164 ELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELK 243
|
..
gi 446115686 246 HH 247
Cdd:COG4586 244 ER 245
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-240 |
2.61e-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: 93.45 E-value: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 12 HLSFpGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGEDVLNAREKQLRQwrg 91
Cdd:cd03253 5 NVTF-AYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRF-----YDVSSGSILIDGQDIREVTLDSLRR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 92 aRVAMIFQEpmTAL-NPTrriglqMMDVIRHHQPISRRE---ARAKAIALLEE-MQIPDAVE-VMSRYPFELSGGMRQRV 165
Cdd:cd03253 76 -AIGVVPQD--TVLfNDT------IGYNIRYGRPDATDEeviEAAKAAQIHDKiMRFPDGYDtIVGERGLKLSGGEKQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115686 166 MIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLkhKARASGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESGG 240
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAAL--RDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-253 |
5.69e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.92 E-value: 5.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLN 80
Cdd:PRK14239 1 MTEPILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 81 AREK--QLRQwrgaRVAMIFQEPmtalNP-------TRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQipdavEVMS 151
Cdd:PRK14239 77 PRTDtvDLRK----EIGMVFQQP----NPfpmsiyeNVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVK-----DRLH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 152 RYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQV---LRLLKHKarasgTAVLFISHDMAVVSQLCDSVY 228
Cdd:PRK14239 144 DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIeetLLGLKDD-----YTMLLVTRSMQQASRISDRTG 218
|
250 260
....*....|....*....|....*
gi 446115686 229 VMYAGSVIESGGTADVIHHPRHPYT 253
Cdd:PRK14239 219 FFLDGDLIEYNDTKQMFMNPKHKET 243
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-244 |
6.34e-22 |
|
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: 91.73 E-value: 6.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAR-EK 84
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP-----PRSGSIRFDGRDITGLPpHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 QLRqwRGarVAMIFQEpmtalnptRRI--GLQMMDVIRHHQPISRREARAKAIALLEEMqIPDAVEVMSRYPFELSGGMR 162
Cdd:cd03224 72 RAR--AG--IGYVPEG--------RRIfpELTVEENLLLGAYARRRAKRKARLERVYEL-FPRLKERRKQLAGTLSGGEQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 163 QRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTA 242
Cdd:cd03224 139 QMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIR-ELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAA 217
|
..
gi 446115686 243 DV 244
Cdd:cd03224 218 EL 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-255 |
7.47e-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: 95.66 E-value: 7.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYcvhRGQISLLGEDVlnaREKQLRQWRGARVAMIFQ 99
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTW---DGEIYWSGSPL---KASNIRDTERAGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 100 EPMTALNPTRRIGLQMMDVIRHHQPISRREARA-KAIALLEEMQIPDavEVMSRYPFELSGGMRQRVMIAPAFSCEPQLI 178
Cdd:TIGR02633 86 ELTLVPELSVAENIFLGNEITLPGGRMAYNAMYlRAKNLLRELQLDA--DNVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 179 IAGEPTTAL---DVTVQLQVLRLLKhkarASGTAVLFISHDMAVVSQLCDSVYVMYAGSVI-----ESGGTADVIH---- 246
Cdd:TIGR02633 164 ILDEPSSSLtekETEILLDIIRDLK----AHGVACVYISHKLNEVKAVCDTICVIRDGQHVatkdmSTMSEDDIITmmvg 239
|
250
....*....|....*
gi 446115686 247 ------HPRHPYTIG 255
Cdd:TIGR02633 240 reitslYPHEPHEIG 254
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-239 |
7.85e-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: 92.22 E-value: 7.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 21 DVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGEDVlnaREKQLRQWRgARVAMIFQE 100
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERF-----YDPTSGEILLDGVDI---RDLNLRWLR-SQIGLVSQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 101 PMTaLNPTrriglqMMDVIRH--HQPISRREARAKAIALLEE--MQIPDAVE-VMSRYPFELSGGMRQRVMIAPAFSCEP 175
Cdd:cd03249 86 PVL-FDGT------IAENIRYgkPDATDEEVEEAAKKANIHDfiMSLPDGYDtLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115686 176 QLIIAGEPTTALDVTVQLQVLRLLKhKARAsGTAVLFISHDMAVVsQLCDSVYVMYAGSVIESG 239
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALD-RAMK-GRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQG 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-242 |
8.68e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.87 E-value: 8.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 19 NGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLG-----EDVLNAREKqlrqwrgar 93
Cdd:PRK13650 17 DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES-----GQIIIDGdllteENVWDIRHK--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 94 VAMIFQEPmtalnPTRRIGLQMMDVIR---HHQPISRREARAKaiaLLEEMQIPDAVEVMSRYPFELSGGMRQRVMIAPA 170
Cdd:PRK13650 83 IGMVFQNP-----DNQFVGATVEDDVAfglENKGIPHEEMKER---VNEALELVGMQDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115686 171 FSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSqLCDSVYVMYAGSViESGGTA 242
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV-ESTSTP 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
24-239 |
1.12e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 92.76 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 24 ALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQiSLLGEDVLNAREKQLRQWRGAR--VAMIFQEP 101
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISET-----GQ-TIVGDYAIPANLKKIKEVKRLRkeIGLVFQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 102 MTALnptrriglqMMDVIRH-------HQPISRREARAKAIALLEEMQIPDavEVMSRYPFELSGGMRQRVMIAPAFSCE 174
Cdd:PRK13645 100 EYQL---------FQETIEKdiafgpvNLGENKQEAYKKVPELLKLVQLPE--DYVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115686 175 PQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
23-248 |
1.35e-21 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 91.45 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 23 HALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVlnareKQLRQWRGARVAMIF--QE 100
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS-----GKILLDGQDI-----TKLPMHKRARLGIGYlpQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 101 P-----MTAlnptrrigLQMMDVIRHHQPISRREARAKAIALLEEMQIpdaVEVMSRYPFELSGGMRQRVMIAPAFSCEP 175
Cdd:cd03218 84 AsifrkLTV--------EENILAVLEIRGLSKKEREEKLEELLEEFHI---THLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115686 176 QLIIAGEPTTALD-VTVQLqvLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHHP 248
Cdd:cd03218 153 KFLLLDEPFAGVDpIAVQD--IQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
12-256 |
1.74e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.17 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 12 HLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycVHRGQISLLG-----EDVLNAREKql 86
Cdd:PRK13640 10 HVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD--NPNSKITVDGitltaKTVWDIREK-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 87 rqwrgarVAMIFQEPmtalnPTRRIGLQMMDVIR---HHQPISRREARAKAIALLEEMqipDAVEVMSRYPFELSGGMRQ 163
Cdd:PRK13640 86 -------VGIVFQNP-----DNQFVGATVGDDVAfglENRAVPRPEMIKIVRDVLADV---GMLDYIDSEPANLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 164 RVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESGGTAD 243
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVE 229
|
250
....*....|...
gi 446115686 244 VIHHPRHPYTIGL 256
Cdd:PRK13640 230 IFSKVEMLKEIGL 242
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-239 |
2.28e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 90.28 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 13 LSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGedvlnarekqlrqwrga 92
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKST----LLRLL-AGIYPPDSGTVTVRG----------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 93 RVAMIFqEPMTALNP-------TRRIGLqMMDvirhhqpISRREARAKAIALLEEMQIPDAVEV-MSRYpfelSGGMRQR 164
Cdd:cd03220 84 RVSSLL-GLGGGFNPeltgrenIYLNGR-LLG-------LSRKEIDEKIDEIIEFSELGDFIDLpVKTY----SSGMKAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115686 165 VMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKaRASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-251 |
2.46e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 90.58 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 29 SLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREkqlrqwrGAR-VAMIFQEP-----M 102
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDS-----GRILWNGQDLTALPP-------AERpVSMLFQENnlfphL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 103 T-------ALNPTRRIglqmmdvirhhqpisRREARAKAIALLEEMQIPDaveVMSRYPFELSGGMRQRVMIAPAFSCEP 175
Cdd:COG3840 87 TvaqniglGLRPGLKL---------------TAEQRAQVEQALERVGLAG---LLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115686 176 QLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHHPRHP 251
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-239 |
4.33e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.84 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 19 NGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPT--GSYCV---HRGQISLLGEDVLNAREKQLRQWRGAR 93
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSkyGTIQVgdiYIGDKKNNHELITNPYSKKIKNFKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 94 --VAMIFQEPMTALNPTrRIGLQMMdvirhHQPI----SRREARAKAIALLEEMQIPDAveVMSRYPFELSGGMRQRVMI 167
Cdd:PRK13631 116 rrVSMVFQFPEYQLFKD-TIEKDIM-----FGPValgvKKSEAKKLAKFYLNKMGLDDS--YLERSPFGLSGGQKRRVAI 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115686 168 APAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKGEHEMMQLIL-DAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-239 |
4.90e-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: 89.85 E-value: 4.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 24 ALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGEDVLNAREKQLRqwrgARVAMIFQEPmT 103
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF-----YVPENGRVLVDGHDLALADPAWLR----RQVGVVLQEN-V 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 104 ALNPTRRIGLQMMDvirHHQPISRREARAK-AIALLEEMQIPDAVE-VMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAG 181
Cdd:cd03252 87 LFNRSIRDNIALAD---PGMSMERVIEAAKlAGAHDFISELPEGYDtIVGEQGAGLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446115686 182 EPTTALDVTVQLQVLRLLkhKARASGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESG 239
Cdd:cd03252 164 EATSALDYESEHAIMRNM--HDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-252 |
6.30e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 91.93 E-value: 6.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGEDVLN 80
Cdd:PRK09452 10 SLSPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTT----VLRLI-AGFETPDSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 81 AREKQlRQwrgarVAMIFQEpmTALNPTRRI------GLQMMDVirHHQPISRREARAKAIALLEEMQipdavevmSRYP 154
Cdd:PRK09452 81 VPAEN-RH-----VNTVFQS--YALFPHMTVfenvafGLRMQKT--PAAEITPRVMEALRMVQLEEFA--------QRKP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 155 FELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGs 234
Cdd:PRK09452 143 HQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG- 221
|
250
....*....|....*...
gi 446115686 235 VIESGGTadvihhPRHPY 252
Cdd:PRK09452 222 RIEQDGT------PREIY 233
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-249 |
6.63e-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: 89.27 E-value: 6.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 4 PVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNARE 83
Cdd:COG0410 2 PMLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP-----PRSGSIRFDGEDITGLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 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 446115686 154 PFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALD-VTVQlQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYA 232
Cdd:COG0410 134 AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLApLIVE-EIFEIIR-RLNREGVTILLVEQNARFALEIADRAYVLER 211
|
250
....*....|....*..
gi 446115686 233 GSVIESGGTADVIHHPR 249
Cdd:COG0410 212 GRIVLEGTAAELLADPE 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-247 |
6.86e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.76 E-value: 6.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSvTamlIMRLL-----PTgsycvhRGQISLLGedvlnarekqlrqwrgaRV 94
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKS-T---LLKLIagilePT------SGRVEVNG-----------------RV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 95 AMIFqEPMTALNPT---R---RIGLQMMDvirhhqpISRREARAKaialleemqIPDAVEV----------MSRYpfelS 158
Cdd:COG1134 90 SALL-ELGAGFHPEltgReniYLNGRLLG-------LSRKEIDEK---------FDEIVEFaelgdfidqpVKTY----S 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 159 GGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKaRASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIES 238
Cdd:COG1134 149 SGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
....*....
gi 446115686 239 GGTADVIHH 247
Cdd:COG1134 228 GDPEEVIAA 236
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-216 |
1.05e-20 |
|
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: 88.30 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 4 PVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSvTAM-LIMRLLPtgsycVHRGQISLLGEDVLNAR 82
Cdd:COG4133 1 MMLEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKT-TLLrILAGLLP-----PSAGEVLWNGEPIRDAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 83 EkqlrQWRgARVAMIFQEP-----MTALnptrriglqmmDVIRHHQPISRREARAKAI-ALLEEMQIPDAVEVMSRYpfe 156
Cdd:COG4133 71 E----DYR-RRLAYLGHADglkpeLTVR-----------ENLRFWAALYGLRADREAIdEALEAVGLAGLADLPVRQ--- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 157 LSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHkARASGTAVLFISHD 216
Cdd:COG4133 132 LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-245 |
1.83e-20 |
|
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: 88.60 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 3 QPVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhRGQISLLGEDV--LN 80
Cdd:COG1119 1 DPLLELRNVTVRR----GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTY----GNDVRLFGERRggED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 81 AREkqLRQ---WRGARVAMIFQEPMTALNptrriglqmM------DVIRHHQPISRREaRAKAIALLEEMQIpdaVEVMS 151
Cdd:COG1119 73 VWE--LRKrigLVSPALQLRFPRDETVLD---------VvlsgffDSIGLYREPTDEQ-RERARELLELLGL---AHLAD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 152 RYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:COG1119 138 RPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLK 217
|
250
....*....|....
gi 446115686 232 AGSVIESGGTADVI 245
Cdd:COG1119 218 DGRVVAAGPKEEVL 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-239 |
2.02e-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: 86.60 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPgfNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLImrllpTGSYCVHRGQISLLGEDVLNArEKQ 85
Cdd:cd03247 1 LSINNVSFSYP--EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLL-----TGDLKPQQGEITLDGVPVSDL-EKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 LRQwrgaRVAMIFQEPMTaLNPTRRiglqmmdvirhhQPISRRearakaialleemqipdavevmsrypfeLSGGMRQRV 165
Cdd:cd03247 73 LSS----LISVLNQRPYL-FDTTLR------------NNLGRR----------------------------FSGGERQRL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115686 166 MIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARasGTAVLFISHDMAVVSQLcDSVYVMYAGSVIESG 239
Cdd:cd03247 108 ALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-217 |
3.35e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.83 E-value: 3.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPGfngdVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVlnarekq 85
Cdd:PRK11248 2 LQISHLYADYGG----KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQH-----GSITLDGKPV------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 lrQWRGARVAMIFQEpmTALNPTRRI------GLQMMDVirhhqpiSRREARAKAIALLEEMqipDAVEVMSRYPFELSG 159
Cdd:PRK11248 66 --EGPGAERGVVFQN--EGLLPWRNVqdnvafGLQLAGV-------EKMQRLEIAHQMLKKV---GLEGAEKRYIWQLSG 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446115686 160 GMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDM 217
Cdd:PRK11248 132 GQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-241 |
5.05e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.02 E-value: 5.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFPgfNGDVhALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLN 80
Cdd:PRK15056 2 MQQAGIVVNDVTVTWR--NGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLAS-----GKISILGQPTRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 81 AREKQLrqwrgarVAMIFQ-EPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIaLLEEMQIPDAVEVMSRYPFELSG 159
Cdd:PRK15056 74 ALQKNL-------VAYVPQsEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQI-VTAALARVDMVEFRHRQIGELSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 160 GMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVyVMYAGSVIESG 239
Cdd:PRK15056 146 GQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLR-ELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASG 223
|
..
gi 446115686 240 GT 241
Cdd:PRK15056 224 PT 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-221 |
5.53e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.75 E-value: 5.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGqisllgedvlnarekqlrqwRGARVAMIFQ 99
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA--------------------GGARVAYVPQ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 100 EpmTALN---PTRRIGLQMMDVIRHHQPISR--REARAKAIALLEEMQIPDavevMSRYPF-ELSGGMRQRVMIAPAFSC 173
Cdd:NF040873 63 R--SEVPdslPLTVRDLVAMGRWARRGLWRRltRDDRAAVDDALERVGLAD----LAGRQLgELSGGQRQRALLAQGLAQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446115686 174 EPQLIIAGEPTTALDVTVQLQVLRLLKHkARASGTAVLFISHDMAVVS 221
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAE-EHARGATVVVVTHDLELVR 183
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-253 |
5.91e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.41 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 3 QPVLDIQQLHLsfpgFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPT-GSYCVHRGQISLLGEDVLNA 81
Cdd:PRK14246 8 EDVFNISRLYL----YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSKIKVDGKVLYFGKDIFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 82 REKQLRQwrgaRVAMIFQEPmtalNPTRRIGL--QMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPF-ELS 158
Cdd:PRK14246 84 DAIKLRK----EVGMVFQQP----NPFPHLSIydNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPAsQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 159 GGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARAsgTAVLFISHDMAVVSQLCDSVYVMYAGSVIES 238
Cdd:PRK14246 156 GGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEW 233
|
250
....*....|....*
gi 446115686 239 GGTADVIHHPRHPYT 253
Cdd:PRK14246 234 GSSNEIFTSPKNELT 248
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-240 |
8.72e-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: 8.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMrllptG--SYCVHRGQISLLGEDVLNArE 83
Cdd:cd03217 1 LEIKDLHVSV----GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIM-----GhpKYEVTEGEILFKGEDITDL-P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 KQLRQWRGarVAMIFQEPMtalnptrRI-GLQMMDVIrhhqpisrrearakaialleemqipdavevmsRYPFE-LSGGM 161
Cdd:cd03217 71 PEERARLG--IFLAFQYPP-------EIpGVKNADFL--------------------------------RYVNEgFSGGE 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 162 RQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQL-CDSVYVMYAGSVIESGG 240
Cdd:cd03217 110 KKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVIN-KLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-244 |
9.38e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 87.06 E-value: 9.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSFPGfngDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PT-GSYCVHRGQISLLGEDVLNAR 82
Cdd:PRK13639 1 ILETRDLKYSYPD---GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkPTsGEVLIKGEPIKYDKKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 83 EKqlrqwrgarVAMIFQEPMTAL-NPTRR---------IGLQMMDVirhhqpisrrEARAKaialleemqipDAVEV--M 150
Cdd:PRK13639 78 KT---------VGIVFQNPDDQLfAPTVEedvafgplnLGLSKEEV----------EKRVK-----------EALKAvgM 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 151 SRY----PFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDS 226
Cdd:PRK13639 128 EGFenkpPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLL-YDLNKEGITIIISTHDVDLVPVYADK 206
|
250
....*....|....*...
gi 446115686 227 VYVMYAGSVIESGGTADV 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 |
9.73e-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: 89.48 E-value: 9.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVtamLIMRLLPTGSYCVHRGQI----------------SLLGE------- 76
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSV---LMHVLRGMDQYEPTSGRIiyhvalcekcgyverpSKVGEpcpvcgg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 77 -------DVLNAREKQLRQWRgARVAMIFQEPMtALNPTRRIglqMMDVIRHHQPI--SRREARAKAIALLEEMQIPDAV 147
Cdd:TIGR03269 88 tlepeevDFWNLSDKLRRRIR-KRIAIMLQRTF-ALYGDDTV---LDNVLEALEEIgyEGKEAVGRAVDLIEMVQLSHRI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 148 EVMSRypfELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSV 227
Cdd:TIGR03269 163 THIAR---DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*...
gi 446115686 228 YVMYAGSVIESGGTADVI 245
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVV 257
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
234-301 |
1.06e-19 |
|
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: 82.02 E-value: 1.06e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115686 234 SVIESGGTADVIHHPRHPYTIGLLQCAPEHGVPRQPLPAIPGTVPNLTHLPDGCAFRDRCYAAGAQCA 301
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECR 68
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-240 |
1.17e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 86.71 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSFPGfngDVHALNNVSLQINRGEIVGLVGESGSGKSVtamLIMRLlpTGSYCVHRGQISLLGEDVLNAREK 84
Cdd:PRK13647 4 IIEVEDLHFRYKD---GTKALKGLSLSIPEGSKTALLGPNGAGKST---LLLHL--NGIYLPQRGRVKVMGREVNAENEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 QLRqwrgARVAMIFQEP------MT-----ALNPtRRIGLQMMDVIRhhqpisRREARAKAIalleEMQipdavEVMSRY 153
Cdd:PRK13647 76 WVR----SKVGLVFQDPddqvfsSTvwddvAFGP-VNMGLDKDEVER------RVEEALKAV----RMW-----DFRDKP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 154 PFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:PRK13647 136 PYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILD-RLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
....*..
gi 446115686 234 SVIESGG 240
Cdd:PRK13647 215 RVLAEGD 221
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-245 |
1.23e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 86.29 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 7 DIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQL 86
Cdd:COG4604 3 EIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLP-----PDSGEVLVDGLDVATTPSREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 87 RQwrgaRVAMIFQEPMTALNPTRRiglqmmDVIR-----HHQpiSR-----REARAKAIALLEEMQIPDavevmsRYPFE 156
Cdd:COG4604 74 AK----RLAILRQENHINSRLTVR------ELVAfgrfpYSK--GRltaedREIIDEAIAYLDLEDLAD------RYLDE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 157 LSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVI 236
Cdd:COG4604 136 LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVV 215
|
....*....
gi 446115686 237 ESGGTADVI 245
Cdd:COG4604 216 AQGTPEEII 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-253 |
1.26e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 88.35 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFPGfngdVHALNNVSLQINRGEIVGLVGESGSGKSVtamlIMRLL-----PTgsycvhRGQISLLG 75
Cdd:PRK11607 15 ALTPLLEIRNLTKSFDG----QHAVDDVSLTIYKGEIFALLGASGCGKST----LLRMLagfeqPT------AGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 76 EDVLNAREKQlrqwrgARVAMIFQE----PMTALNPTRRIGLQmmdvirhHQPISRREARAKAIALLE--EMQipdavEV 149
Cdd:PRK11607 81 VDLSHVPPYQ------RPINMMFQSyalfPHMTVEQNIAFGLK-------QDKLPKAEIASRVNEMLGlvHMQ-----EF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 150 MSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTV----QLQVLRLLKhkaRASGTAVLfISHDMAVVSQLCD 225
Cdd:PRK11607 143 AKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILE---RVGVTCVM-VTHDQEEAMTMAG 218
|
250 260
....*....|....*....|....*...
gi 446115686 226 SVYVMYAGSVIESGGTADVIHHPRHPYT 253
Cdd:PRK11607 219 RIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
6-244 |
1.42e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.05 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSfpgfngdvHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycvHRGQISLLGEDVLNAREKQ 85
Cdd:COG4138 1 LQLNDVAVA--------GRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP------GQGEILLNGRPLSDWSAAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 LRQWRgarvAMIFQEPMTALnptrriglqMMDV---IRHHQP-ISRREARAKAIA-LLEEMQIPDAvevMSRYPFELSGG 160
Cdd:COG4138 67 LARHR----AYLSQQQSPPF---------AMPVfqyLALHQPaGASSEAVEQLLAqLAEALGLEDK---LSRPLTQLSGG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 161 MRQRVMIA-------PAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLfISHDMAVVSQLCDSVYVMYAG 233
Cdd:COG4138 131 EWQRVRLAavllqvwPTINPEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVM-SSHDLNHTLRHADRVWLLKQG 209
|
250
....*....|.
gi 446115686 234 SVIESGGTADV 244
Cdd:COG4138 210 KLVASGETAEV 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-238 |
1.62e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.81 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 2 TQPVLDIQQLHLSFPGfngdVHALNNVSLQINRGEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGEDVL-- 79
Cdd:PRK11288 1 SSPYLSFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKST----LLKIL-SGNYQPDAGSILIDGQEMRfa 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 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 446115686 145 DAvevmsryPF-ELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQL 223
Cdd:PRK11288 135 DT-------PLkYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIR-ELRAEGRVILYVSHRMEEIFAL 206
|
250
....*....|....*
gi 446115686 224 CDSVYVMYAGSVIES 238
Cdd:PRK11288 207 CDAITVFKDGRYVAT 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
11-252 |
2.01e-19 |
|
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: 87.47 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 11 LHLSFPGFNGDvHALNnVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTGsycvhrGQISLLGEDVLNAREKQLRQW 89
Cdd:TIGR02142 1 LSARFSKRLGD-FSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTrPDE------GEIVLNGRTLFDSRKGIFLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 90 RGARVAMIFQE----PMTALNPTRRIGLQMMDvirhhqPISRREARAKAIALLeemqipdAVE-VMSRYPFELSGGMRQR 164
Cdd:TIGR02142 73 EKRRIGYVFQEarlfPHLSVRGNLRYGMKRAR------PSERRISFERVIELL-------GIGhLLGRLPGRLSGGEKQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 165 VMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADV 244
Cdd:TIGR02142 140 VAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
....*...
gi 446115686 245 IHHPRHPY 252
Cdd:TIGR02142 220 WASPDLPW 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-244 |
2.13e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.44 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFPGfngDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQIsLLGEDVLN 80
Cdd:PRK13636 1 MEDYILKVEELNYNYSD---GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSS-----GRI-LFDGKPID 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 81 AREKQLRQWRGArVAMIFQEPMTAL---NPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQipdavevmSRYPFEL 157
Cdd:PRK13636 72 YSRKGLMKLRES-VGMVFQDPDNQLfsaSVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLK--------DKPTHCL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 158 SGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIE 237
Cdd:PRK13636 143 SFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVIL 222
|
....*..
gi 446115686 238 SGGTADV 244
Cdd:PRK13636 223 QGNPKEV 229
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-223 |
2.44e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.25 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRL-LPTGSYCVHRGQiSLlgeDVL 79
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQ-PM---SKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 80 NAREKQlrQWRGARVAMIFQ-----EPMTALNptrriGLQMMDVIRHHQPisrREARAKAIALLEemqipdAVEVMSR-- 152
Cdd:PRK11629 77 SSAAKA--ELRNQKLGFIYQfhhllPDFTALE-----NVAMPLLIGKKKP---AEINSRALEMLA------AVGLEHRan 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115686 153 -YPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQL 223
Cdd:PRK11629 141 hRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM 212
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-244 |
3.78e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.92 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFPGfngdVHALNNVSLQINRGEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGEDvLN 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKST----LMKVL-SGIHEPTKGTITINNIN-YN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 81 AREKQLRQWRGarVAMIFQE-----PMTALN-------PTRRI-GLQMMDVirhhqpisrREARAKAIALLEEMQIPDAV 147
Cdd:PRK09700 71 KLDHKLAAQLG--IGIIYQElsvidELTVLEnlyigrhLTKKVcGVNIIDW---------REMRVRAAMMLLRVGLKVDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 148 EVMSRypfELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALdVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSV 227
Cdd:PRK09700 140 DEKVA---NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRY 215
|
250
....*....|....*..
gi 446115686 228 YVMYAGSVIESGGTADV 244
Cdd:PRK09700 216 TVMKDGSSVCSGMVSDV 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
24-239 |
4.70e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.14 E-value: 4.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 24 ALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTGsycvhrGQISLLGEDVLNarEKQLRQWRgARVAMIFQEPM 102
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLiPSE------GKVYVDGLDTSD--EENLWDIR-NKAGMVFQNPD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 103 TALNPT----------RRIGLQMmDVIRhhqpiSRREARAKAIALLEEMQIPdavevmsryPFELSGGMRQRVMIAPAFS 172
Cdd:PRK13633 96 NQIVATiveedvafgpENLGIPP-EEIR-----ERVDESLKKVGMYEYRRHA---------PHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446115686 173 CEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESG 239
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-230 |
5.32e-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: 87.34 E-value: 5.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 4 PVLDIQQLHLSFPGFNgdvHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNARE 83
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD-----PTEGSIAVNGVPLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 KQLRQwrgaRVAMIFQEPmTALNPTrriglqMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPF-----ELS 158
Cdd:TIGR02857 392 DSWRD----QIAWVPQHP-FLFAGT------IAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIgeggaGLS 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115686 159 GGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLkhKARASGTAVLFISHDMAVVsQLCDSVYVM 230
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEAL--RALAQGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
13-239 |
7.92e-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: 83.47 E-value: 7.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 13 LSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrgqiSLLGEDVLNAREKQLRQWRgA 92
Cdd:cd03234 11 LKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGG--------TTSGQILFNGQPRKPDQFQ-K 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 93 RVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPiSRREARAKAIALLEEMQIPDAVeVMSRYPFELSGGMRQRVMIAPAFS 172
Cdd:cd03234 82 CVAYVRQDDILLPGLTVRETLTYTAILRLPRK-SSDAIRKKRVEDVLLRDLALTR-IGGNLVKGISGGERRRVSIAVQLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446115686 173 CEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-248 |
1.15e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.08 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 18 FNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQLRQWrgarVAMI 97
Cdd:PRK13652 13 YSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTS-----GSVLIRGEPITKENIREVRKF----VGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 98 FQEPMTAL-NPT--RRIGLQMMDVIRHHQPISRREARAKAIALLEEMQipdavevmSRYPFELSGGMRQRVMIAPAFSCE 174
Cdd:PRK13652 84 FQNPDDQIfSPTveQDIAFGPINLGLDEETVAHRVSSALHMLGLEELR--------DRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115686 175 PQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHHP 248
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-216 |
1.16e-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: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 4 PVLDIQQLHLSFPGfngDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTgsycvHRGQISLLGEDVLNARE 83
Cdd:TIGR02868 333 PTLELRDLSAGYPG---APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP-----LQGEVTLDGVPVSSLDQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 KQLRqwrgARVAMIFQEPM---TALNPTRRIGL------QMMDVIRhhqpisrreaRAKAIALLEEMqiPDAVE-VMSRY 153
Cdd:TIGR02868 405 DEVR----RRVSVCAQDAHlfdTTVRENLRLARpdatdeELWAALE----------RVGLADWLRAL--PDGLDtVLGEG 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115686 154 PFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLkhKARASGTAVLFISHD 216
Cdd:TIGR02868 469 GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-247 |
1.16e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.86 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVT-AMLIMRLLPTGsycvhrGQISLLGEDVl 79
Cdd:PRK13537 3 MSVAPIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTlRMLLGLTHPDA------GSISLCGEPV- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 80 NAREKQLRQwrgaRVAMIFQepMTALNP--TRRIGLQmmdVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRypfEL 157
Cdd:PRK13537 72 PSRARHARQ----RVGVVPQ--FDNLDPdfTVRENLL---VFGRYFGLSAAAARALVPPLLEFAKLENKADAKVG---EL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 158 SGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVtvqlQVLRLLKHKAR---ASGTAVLFISHDMAVVSQLCDSVYVMYAGS 234
Cdd:PRK13537 140 SGGMKRRLTLARALVNDPDVLVLDEPTTGLDP----QARHLMWERLRsllARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
250
....*....|...
gi 446115686 235 VIESGGTADVIHH 247
Cdd:PRK13537 216 KIAEGAPHALIES 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-245 |
2.70e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.11 E-value: 2.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMrllptGSYCVHRGQISLLGEDVlnarEKQLRQWRgARVAMIFQ 99
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIL-----GMTSPDAGKITVLGVPV----PARARLAR-ARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 100 EPMTALNPTRRIGLQmmdVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRypfELSGGMRQRVMIAPAFSCEPQLII 179
Cdd:PRK13536 122 FDNLDLEFTVRENLL---VFGRYFGMSTREIEAVIPSLLEFARLESKADARVS---DLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115686 180 AGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVI 245
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLR-SLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
24-245 |
2.71e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 83.60 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 24 ALNNVSLQINRGEIVGLVGESGSGKSV-TAMLIMRLLPTgsycvhRGQISLLGEDVLNAREKQLRQWRGARVAM---IFQ 99
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTfIEHLNALLLPD------TGTIEWIFKDEKNKKKTKEKEKVLEKLVIqktRFK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 100 EPMTALNPTRRIGL-------QMM------DVIrhHQPIS----RREARAKAIALLEEMQIPdaVEVMSRYPFELSGGMR 162
Cdd:PRK13651 96 KIKKIKEIRRRVGVvfqfaeyQLFeqtiekDII--FGPVSmgvsKEEAKKRAAKYIELVGLD--ESYLQRSPFELSGGQK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 163 QRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTA 242
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIF-DNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTY 250
|
...
gi 446115686 243 DVI 245
Cdd:PRK13651 251 DIL 253
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-238 |
4.28e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.46 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 14 SFPGfngdVHALNNVSLQINRGEIVGLVGESGSGKSVtamlIMRLL----PTGSYcvhRGQISLLGEdvlnarekqLRQW 89
Cdd:NF040905 10 TFPG----VKALDDVNLSVREGEIHALCGENGAGKST----LMKVLsgvyPHGSY---EGEILFDGE---------VCRF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 90 RGAR------VAMIFQEpmTAL-------------NPTRRIGLqmmdvirhhqpISRREARAKAIALLEE--MQIPDAVE 148
Cdd:NF040905 70 KDIRdsealgIVIIHQE--LALipylsiaeniflgNERAKRGV-----------IDWNETNRRARELLAKvgLDESPDTL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 149 VMsrypfELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHkARASGTAVLFISHDMAVVSQLCDSVY 228
Cdd:NF040905 137 VT-----DIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLE-LKAQGITSIIISHKLNEIRRVADSIT 210
|
250
....*....|
gi 446115686 229 VMYAGSVIES 238
Cdd:NF040905 211 VLRDGRTIET 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-245 |
5.00e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.98 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQ 85
Cdd:PRK11231 3 LRTENLTVGY----GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQS-----GTVFLGDKPISMLSSRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 LRQwrgaRVAMIFQEPMTALNPTRRiglQMMDVIR-----HHQPISRREaRAKAIALLEEMQIpdaVEVMSRYPFELSGG 160
Cdd:PRK11231 74 LAR----RLALLPQHHLTPEGITVR---ELVAYGRspwlsLWGRLSAED-NARVNQAMEQTRI---NHLADRRLTDLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 161 MRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGG 240
Cdd:PRK11231 143 QRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMR-ELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
....*
gi 446115686 241 TADVI 245
Cdd:PRK11231 222 PEEVM 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-250 |
2.10e-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: 79.82 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRL-LPT-GSYCVHRGQISLLGEDVLNA-REKQLRQWRGARvamifqep 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTsGGVILEGKQITEPGPDRMVVfQNYSLLPWLTVR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 102 mtalnptRRIGLQMmDVIRHHQPISRREARAKaiallEEMQIPDAVEVMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAG 181
Cdd:TIGR01184 73 -------ENIALAV-DRVLPDLSKSERRAIVE-----EHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLD 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 182 EPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADV-IHHPRH 250
Cdd:TIGR01184 140 EPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-239 |
2.62e-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: 79.17 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 14 SFPgfNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDvlnarekqLRQWRGA 92
Cdd:cd03245 11 SYP--NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYkPT------SGSVLLDGTD--------IRQLDPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 93 RVamifqepmtalnpTRRIGLQMMDV------IRHHQPISRREARAKAIalLEEMQIPDAVEVMSRYP-----------F 155
Cdd:cd03245 75 DL-------------RRNIGYVPQDVtlfygtLRDNITLGAPLADDERI--LRAAELAGVTDFVNKHPngldlqigergR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 156 ELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLkhKARASGTAVLFISHDMAVVsQLCDSVYVMYAGSV 235
Cdd:cd03245 140 GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERL--RQLLGDKTLIIITHRPSLL-DLVDRIIVMDSGRI 216
|
....
gi 446115686 236 IESG 239
Cdd:cd03245 217 VADG 220
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-249 |
6.22e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.88 E-value: 6.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLImrllpTGSYCVHRGQISLLGEDV-- 78
Cdd:PRK11300 1 MSQPLLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCL-----TGFYKPTGGTILLRGQHIeg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 79 ----LNAREKQLRQWRGARvamIFQEpMTALnptrriglQMMDVIRHHQ------------PISRR---EARAKAIALLE 139
Cdd:PRK11300 72 lpghQIARMGVVRTFQHVR---LFRE-MTVI--------ENLLVAQHQQlktglfsgllktPAFRRaesEALDRAATWLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 140 EMQIpdaVEVMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDV--TVQLQVL-RLLKhkaRASGTAVLFISHD 216
Cdd:PRK11300 140 RVGL---LEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPkeTKELDELiAELR---NEHNVTVLLIEHD 213
|
250 260 270
....*....|....*....|....*....|...
gi 446115686 217 MAVVSQLCDSVYVMYAGSVIESGGTADVIHHPR 249
Cdd:PRK11300 214 MKLVMGISDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-248 |
7.81e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 80.15 E-value: 7.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVtamlIMRLL-----PTGsycvhrGQISLLGEDVLNaREKQLRQwrgarV 94
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTT----VLRLVaglekPTE------GQIFIDGEDVTH-RSIQQRD-----I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 95 AMIFQEpmTALNPTRRI------GLQMMDVirhhqPISRREARAKaiallEEMQIPDAVEVMSRYPFELSGGMRQRVMIA 168
Cdd:PRK11432 81 CMVFQS--YALFPHMSLgenvgyGLKMLGV-----PKEERKQRVK-----EALELVDLAGFEDRYVDQISGGQQQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 169 PAFSCEPQLIIAGEPTTALDVTVQlqvlRLLKHKAR----ASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADV 244
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLR----RSMREKIRelqqQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
....
gi 446115686 245 IHHP 248
Cdd:PRK11432 225 YRQP 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-239 |
1.89e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.09 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 23 HALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrgQISllGEDVLNAREKQLRQWRgARVAMIFQEPM 102
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGV------KGS--GSVLLNGMPIDAKEMR-AISAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 103 TALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEM----------QIPDAVEVmsrypfeLSGGMRQRVmiapAFS 172
Cdd:TIGR00955 110 FIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALglrkcantriGVPGRVKG-------LSGGERKRL----AFA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115686 173 CE----PQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:TIGR00955 179 SElltdPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLG 249
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-233 |
2.06e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.71 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 3 QPVLDIQQLhlSFPGFNgdvhalnNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVlNAR 82
Cdd:PRK15439 266 APVLTVEDL--TGEGFR-------NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARG-----GRIMLNGKEI-NAL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 83 EKQLRQWRGArVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIalLEE------MQIPDAVEVMSRypfe 156
Cdd:PRK15439 331 STAQRLARGL-VYLPEDRQSSGLYLDAPLAWNVCALTHNRRGFWIKPARENAV--LERyrralnIKFNHAEQAART---- 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446115686 157 LSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKArASGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-218 |
2.39e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 76.37 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKS-VTAMLIMRLLPTGSYcvhRGQISLLGEDvLNAREKQLRqwrgaRVAMIFQEPMt 103
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKStLLAAIAGTLSPAFSA---SGEVLLNGRR-LTALPAEQR-----RIGILFQDDL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 104 aLNPTRRIGLQMMDVIRHHqpISRREARAKAIALLEEMQIPDaveVMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEP 183
Cdd:COG4136 87 -LFPHLSVGENLAFALPPT--IGRAQRRARVEQALEEAGLAG---FADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190
....*....|....*....|....*....|....*
gi 446115686 184 TTALDVTVQLQVLRLLKHKARASGTAVLFISHDMA 218
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-239 |
2.84e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.48 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 2 TQPVLDIQQLHLSFPgfNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRllptgSYCVHRGQISLLGEDVLNA 81
Cdd:PRK11160 335 DQVSLTLNNVSFTYP--DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTR-----AWDPQQGEILLNGQPIADY 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 82 REKQLRQwrgarvAMIF--QEPMTaLNPTRRIGLQMmdvirhhqpisrrearAKAIALLEEMqipdaVEVMSRYPFE--- 156
Cdd:PRK11160 408 SEAALRQ------AISVvsQRVHL-FSATLRDNLLL----------------AAPNASDEAL-----IEVLQQVGLEkll 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 157 ----------------LSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARasGTAVLFISHDMAVV 220
Cdd:PRK11160 460 eddkglnawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGL 537
|
250
....*....|....*....
gi 446115686 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 |
2.94e-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: 79.38 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 7 DIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRL-LPTGsycvhrGQISLLGEDVLNAREKQ 85
Cdd:TIGR02203 330 DVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFyEPDS------GQILLDGHDLADYTLAS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 LRqwrgARVAMIFQEpMTALNPTrriglqMMDVIRHHQP--ISRREA-RAKAIALLEEM--QIPDAVE-VMSRYPFELSG 159
Cdd:TIGR02203 404 LR----RQVALVSQD-VVLFNDT------IANNIAYGRTeqADRAEIeRALAAAYAQDFvdKLPLGLDtPIGENGVLLSG 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 160 GMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARasGTAVLFISHDMAVVsQLCDSVYVMYAGSVIESG 239
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTI-EKADRIVVMDDGRIVERG 549
|
....*...
gi 446115686 240 GTADVIHH 247
Cdd:TIGR02203 550 THNELLAR 557
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-227 |
4.28e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.91 E-value: 4.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 11 LHLSFPGFN-GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLLGEDVLNAREKQLRQ 88
Cdd:PRK10247 8 LQLQNVGYLaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPT------SGTLLFEGEDISTLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 89 wrgaRVAMIFQEPMTaLNPTRRIGLQMMDVIRHHQPisrreARAKAIALLEEMQIPDavEVMSRYPFELSGGMRQRVMIA 168
Cdd:PRK10247 82 ----QVSYCAQTPTL-FGDTVYDNLIFPWQIRNQQP-----DPAIFLDDLERFALPD--TILTKNIAELSGGEKQRISLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446115686 169 PAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQlCDSV 227
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-239 |
4.47e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.00 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSFPGfNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTGsycvhrGQISLLGEDVLNARE 83
Cdd:TIGR00958 478 LIEFQDVSFSYPN-RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYqPTG------GQVLLDGVPLVQYDH 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 KQLRQwrgaRVAMIFQEPM---------TALNPTRRIGLQMMDVIRhhqpisrreaRAKAIALLEEMQIPDAVEVMSRYP 154
Cdd:TIGR00958 551 HYLHR----QVALVGQEPVlfsgsvrenIAYGLTDTPDEEIMAAAK----------AANAHDFIMEFPNGYDTEVGEKGS 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 155 FeLSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQlqvlRLLKHKARASGTAVLFISHDMAVVSQlCDSVYVMYAGS 234
Cdd:TIGR00958 617 Q-LSGGQKQRIAIARALVRKPRVLILDEATSALDAECE----QLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGS 690
|
....*
gi 446115686 235 VIESG 239
Cdd:TIGR00958 691 VVEMG 695
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-245 |
5.79e-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: 78.25 E-value: 5.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPGfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAmlimRLLpTGSYCVHRGQISLLGEDvlnarekq 85
Cdd:COG4618 331 LSVENLTVVPPG--SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLA----RLL-VGVWPPTAGSVRLDGAD-------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 LRQWRGARVAmifqepmtalnptRRIGLQMMDV------IRhhQPISR-REARAKAIalLEEMQIPDAVEVMSRYP---- 154
Cdd:COG4618 396 LSQWDREELG-------------RHIGYLPQDVelfdgtIA--ENIARfGDADPEKV--VAAAKLAGVHEMILRLPdgyd 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 155 -------FELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHkARASGTAVLFISHDMAVVSQlCDSV 227
Cdd:COG4618 459 trigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRA-LKARGATVVVITHRPSLLAA-VDKL 536
|
250
....*....|....*...
gi 446115686 228 YVMYAGSVIESGGTADVI 245
Cdd:COG4618 537 LVLRDGRVQAFGPRDEVL 554
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-235 |
6.49e-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: 75.59 E-value: 6.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSFPGfNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGEDVLNAREK 84
Cdd:cd03248 11 IVKFQNVTFAYPT-RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENF-----YQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 QLRQwrgaRVAMIFQEP-MTALNPTRRIGLQMMDVirHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPfELSGGMRQ 163
Cdd:cd03248 85 YLHS----KVSLVGQEPvLFARSLQDNIAYGLQSC--SFECVKEAAQKAHAHSFISELASGYDTEVGEKGS-QLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115686 164 RVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARAsgTAVLFISHDMAVVSQlCDSVYVMYAGSV 235
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-222 |
6.51e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.30 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRL-LPTGsycvhrGQISLLGEDVLNAREKQLRQWRgARVAMIF 98
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIeRPSA------GKIWFSGHDITRLKNREVPFLR-RQIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 99 QEPMTALNPTRRIGLQMMDVIrhhQPISRREARAKAIALLEEMQIPDAVEvmsRYPFELSGGMRQRVMIAPAFSCEPQLI 178
Cdd:PRK10908 86 QDHHLLMDRTVYDNVAIPLII---AGASGDDIRRRVSAALDKVGLLDKAK---NFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446115686 179 IAGEPTTALDVTVQLQVLRLLKHKARAsGTAVLFISHDMAVVSQ 222
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISR 202
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
12-256 |
6.75e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 76.33 E-value: 6.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 12 HLSFPgFNGDV-HALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMrllptGSYCVHRGQISLLGEDVLNAREKQLRQwr 90
Cdd:PRK13648 12 NVSFQ-YQSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMI-----GIEKVKSGEIFYNNQAITDDNFEKLRK-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 91 gaRVAMIFQEPMTALnptrrIG-LQMMDVI--RHHQPISRREARAKAIALLEEMqipDAVEVMSRYPFELSGGMRQRVMI 167
Cdd:PRK13648 84 --HIGIVFQNPDNQF-----VGsIVKYDVAfgLENHAVPYDEMHRRVSEALKQV---DMLERADYEPNALSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 168 APAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESGGTADVIHH 247
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
....*....
gi 446115686 248 PRHPYTIGL 256
Cdd:PRK13648 233 AEELTRIGL 241
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
25-235 |
9.08e-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: 73.79 E-value: 9.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQLRQwrgarvamifqepmta 104
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTS-----GRVRLDGADISQWDPNELGD---------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 105 lnptrRIGLQMMDVIrhhqpisrrearakaialLEEMQIPDAVevmsrypfeLSGGMRQRVMIAPAFSCEPQLIIAGEPT 184
Cdd:cd03246 77 -----HVGYLPQDDE------------------LFSGSIAENI---------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446115686 185 TALDVTVQLQVLRLLKHkARASGTAVLFISHDMAVVSQlCDSVYVMYAGSV 235
Cdd:cd03246 125 SHLDVEGERALNQAIAA-LKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-239 |
2.11e-15 |
|
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: 73.68 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 29 SLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVlNAREKQLRQwrgarVAMIFQEP--MTALN 106
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQS-----GRVLINGVDV-TAAPPADRP-----VSMLFQENnlFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 107 PTRRIGLQMMDVIRhhqpiSRREARAKAIALLEEMQIPdavEVMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTA 186
Cdd:cd03298 87 VEQNVGLGLSPGLK-----LTAEDRQAIEVALARVGLA---GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446115686 187 LDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
20-251 |
2.66e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.42 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTgsycvHRGQISLLGEDVLNAREKQLRQWRgARVAMIFQ 99
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAP-----DHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 100 EP--MTALNPTRRIGLQMmdviRHHQPISRREARAKAIALLEEMQIPDAVEVMsryPFELSGGMRQRVMIAPAFSCEPQL 177
Cdd:PRK11831 92 SGalFTDMNVFDNVAYPL----REHTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115686 178 IIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMyAGSVIESGGTADVIHHPRHP 251
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIV-ADKKIVAHGSAQALQANPDP 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-247 |
3.79e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 75.77 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 7 DIQQLHLSFpGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTGsycvhrGQISLLGEDVLNAREKQ 85
Cdd:PRK13657 334 AVEFDDVSF-SYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFdPQS------GRILIDGTDIRTVTRAS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 LRQwrgaRVAMIFQEPMTaLNptRRIGlqmmDVIRhhqpisrreaRAKAIALLEEM----QIPDAVEVMSRYP--FE--- 156
Cdd:PRK13657 407 LRR----NIAVVFQDAGL-FN--RSIE----DNIR----------VGRPDATDEEMraaaERAQAHDFIERKPdgYDtvv 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 157 ------LSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVlfISHDMAVVSQlCDSVYVM 230
Cdd:PRK13657 466 gergrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI--IAHRLSTVRN-ADRILVF 542
|
250
....*....|....*..
gi 446115686 231 YAGSVIESGGTADVIHH 247
Cdd:PRK13657 543 DNGRVVESGSFDELVAR 559
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-216 |
4.39e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.49 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 8 IQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSvTamlIMRLLpTGSYCVHRGQISLLgedvlnarekqlr 87
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKS-T---LLKIL-AGELEPDSGEVSIP------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 88 qwRGARVAMIFQEP------------MTALNPTRRIGLQM-----------MDVIRHHQPISR--------REARAKAIa 136
Cdd:COG0488 59 --KGLRIGYLPQEPpldddltvldtvLDGDAELRALEAELeeleaklaepdEDLERLAELQEEfealggweAEARAEEI- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 137 lLEEMQIPDAV--EVMSrypfELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDV-TVQ-LQvlRLLKhkaRASGTaVLF 212
Cdd:COG0488 136 -LSGLGFPEEDldRPVS----ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIEwLE--EFLK---NYPGT-VLV 204
|
....
gi 446115686 213 ISHD 216
Cdd:COG0488 205 VSHD 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-241 |
6.90e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.10 E-value: 6.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 4 PVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSvTamlIMRLLpTGSYCVHRGQISlLGEDVlnare 83
Cdd:COG0488 314 KVLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKS-T---LLKLL-AGELEPDSGTVK-LGETV----- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 kqlrqwrgaRVAMIFQEpMTALNPTRRIglqmMDVIRHHQP-ISRREARakaiALLEEMQIP--DA---VEVmsrypfeL 157
Cdd:COG0488 379 ---------KIGYFDQH-QEELDPDKTV----LDELRDGAPgGTEQEVR----GYLGRFLFSgdDAfkpVGV-------L 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 158 SGGMRQRVMIAPAFSCEPQLIIAGEPTTALDV-TvqLQVL-RLLKHkarASGTaVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeT--LEALeEALDD---FPGT-VLLVSHDRYFLDRVATRILEFEDGGV 507
|
....*.
gi 446115686 236 IESGGT 241
Cdd:COG0488 508 REYPGG 513
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-244 |
7.60e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.50 E-value: 7.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 21 DVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTgsycvHRGQISLLGEdVLNAREKQLRQWRgARVAMIFQE 100
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRP-----QKGAVLWQGK-PLDYSKRGLLALR-QQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 101 PMTALNPT---RRIGLQMMDVIRHHQPISRRearakaiaLLEEMQIPDAvEVMSRYPFE-LSGGMRQRVMIAPAFSCEPQ 176
Cdd:PRK13638 86 PEQQIFYTdidSDIAFSLRNLGVPEAEITRR--------VDEALTLVDA-QHFRHQPIQcLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115686 177 LIIAGEPTTALDVTVQLQVLRLLKHKArASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADV 244
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIV-AQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
14-247 |
9.84e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 74.67 E-value: 9.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 14 SFPGfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGEDVLNAREKQLRQwrgaR 93
Cdd:PRK11176 350 TYPG--KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRF-----YDIDEGEILLDGHDLRDYTLASLRN----Q 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 94 VAMIFQEpMTALNPT--RRIGLQMMDVIRHHQpISRREARAKAIALLEEMqiPDAVE-VMSRYPFELSGGMRQRVMIAPA 170
Cdd:PRK11176 419 VALVSQN-VHLFNDTiaNNIAYARTEQYSREQ-IEEAARMAYAMDFINKM--DNGLDtVIGENGVLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 171 FSCEPQLIIAGEPTTALDV----TVQLQVLRLLKHKarasgtAVLFISHDMAVVSQlCDSVYVMYAGSVIESGGTADVIH 246
Cdd:PRK11176 495 LLRDSPILILDEATSALDTeserAIQAALDELQKNR------TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567
|
.
gi 446115686 247 H 247
Cdd:PRK11176 568 Q 568
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-248 |
1.81e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.95 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPGfngDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVlNAREKQ 85
Cdd:PRK11650 4 LKLQAVRKSYDG---KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITS-----GEIWIGGRVV-NELEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 LRQwrgarVAMIFQEpmTALNP--TRR----IGLQMMDVIRHHqpISRREARAKAIALLEEMqipdavevMSRYPFELSG 159
Cdd:PRK11650 75 DRD-----IAMVFQN--YALYPhmSVRenmaYGLKIRGMPKAE--IEERVAEAARILELEPL--------LDRKPRELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 160 GMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQvLRL-LKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGsVIES 238
Cdd:PRK11650 138 GQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ-MRLeIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGG-VAEQ 215
|
250
....*....|.
gi 446115686 239 GGT-ADVIHHP 248
Cdd:PRK11650 216 IGTpVEVYEKP 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-244 |
3.35e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.12 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 28 VSLQINRGEIVGLVGESGSGKSvTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQLRQWRgarvAMIFQEPMTALNp 107
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKS-TLLARMAGLLPGS-----GSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFA- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 108 trriglqmMDVIRH---HQPISRREA-RAKAIALLEEM-QIPDAVEVMSRypfELSGGMRQRVMIA-------PAFSCEP 175
Cdd:PRK03695 84 --------MPVFQYltlHQPDKTRTEaVASALNEVAEAlGLDDKLGRSVN---QLSGGEWQRVRLAavvlqvwPDINPAG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446115686 176 QLIIAGEPTTALDVTVQLQVLRLLKHKARAsGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADV 244
Cdd:PRK03695 153 QLLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-265 |
4.44e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.17 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 24 ALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTgsycvHRGQISLLGEDVLNAREKQlrqwrGAR--VAMIFQEP 101
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRP-----QKGKVLVSGIDTGDFSKLQ-----GIRklVGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 102 MTAL---NPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQipdavevmSRYPFELSGGMRQRVMIAPAFSCEPQLI 178
Cdd:PRK13644 87 ETQFvgrTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYR--------HRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 179 IAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVsQLCDSVYVMYAGSVIESGGTADVIHHPR-------HP 251
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIK-KLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSlqtlgltPP 236
|
250
....*....|....
gi 446115686 252 YTIGLLQCAPEHGV 265
Cdd:PRK13644 237 SLIELAENLKMHGV 250
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-248 |
5.46e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.84 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAREKQLRQWRgaRVAMIFQEP--- 101
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLNRLRR--QVSMVHPKPnlf 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 102 -MTALNPT----RRIG----LQMMDVIrhhqpisrrEARAKAIALLEEMQipdavEVMSRYPFELSGGMRQRVMIAPAFS 172
Cdd:PRK14258 101 pMSVYDNVaygvKIVGwrpkLEIDDIV---------ESALKDADLWDEIK-----HKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 173 CEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYA-----GSVIESGGTADVIHH 247
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNS 246
|
.
gi 446115686 248 P 248
Cdd:PRK14258 247 P 247
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
24-239 |
8.26e-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: 69.44 E-value: 8.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 24 ALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQLRQwrgaRVAMIFQEPmT 103
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSS-----GSILIDGVDISKIGLHDLRS----RISIIPQDP-V 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 104 ALNPTRRIGLqmmDVIRHHQPisrrEARAKAialLEEMQIPDAVEVMS---RYPFE-----LSGGMRQRVMIAPAFSCEP 175
Cdd:cd03244 89 LFSGTIRSNL---DPFGEYSD----EELWQA---LERVGLKEFVESLPgglDTVVEeggenLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115686 176 QLIIAGEPTTALDVTVQLQVLRLLKHKarASGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESG 239
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREA--FKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-245 |
1.42e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.63 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPV--LDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDV 78
Cdd:PRK10253 1 MTESVarLRGEQLTLGY----GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAH-----GHVWLDGEHI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 79 LNAREKQLRQwrgaRVAMIFQEPMTALNPTRRiglQMMDVIRH-HQPISRREARAKAIALLEEMQIPDAVEVMSRYPFEL 157
Cdd:PRK10253 72 QHYASKEVAR----RIGLLAQNATTPGDITVQ---ELVARGRYpHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 158 SGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIE 237
Cdd:PRK10253 145 SGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVA 224
|
....*...
gi 446115686 238 SGGTADVI 245
Cdd:PRK10253 225 QGAPKEIV 232
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
20-257 |
1.70e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.44 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQIsLLGEDVLNAREKQLRQwrgarVAMIFQ 99
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITS-----GDL-FIGEKRMNDVPPAERG-----VGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 100 EpmTALNPTRRI------GLQMMDVIRhhqpiSRREARAKAIAllEEMQIPDAVEvmsRYPFELSGGMRQRVMIAPAFSC 173
Cdd:PRK11000 83 S--YALYPHLSVaenmsfGLKLAGAKK-----EEINQRVNQVA--EVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 174 EPQLIIAGEPTTALD----VTVQLQVLRLlkHKARasGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHHPR 249
Cdd:PRK11000 151 EPSVFLLDEPLSNLDaalrVQMRIEISRL--HKRL--GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
....*...
gi 446115686 250 HPYTIGLL 257
Cdd:PRK11000 227 NRFVAGFI 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-242 |
2.51e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 68.37 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVtamlimrLLPT--GSYCVHRGQISLLGEDV 78
Cdd:PRK11614 1 MEKVMLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTT-------LLGTlcGDPRATSGRIVFDGKDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 79 lnarekqlRQWRGARvamIFQEPMTALNPTRRI--------GLQMMDVIRHHQPISRREARAKAIalleemqIPDAVEVM 150
Cdd:PRK11614 70 --------TDWQTAK---IMREAVAIVPEGRRVfsrmtveeNLAMGGFFAERDQFQERIKWVYEL-------FPRLHERR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 151 SRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQLCDSVYVM 230
Cdd:PRK11614 132 IQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIE-QLREQGMTIFLVEQNANQALKLADRGYVL 210
|
250
....*....|...
gi 446115686 231 YAGSVI-ESGGTA 242
Cdd:PRK11614 211 ENGHVVlEDTGDA 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
24-239 |
4.27e-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: 67.05 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 24 ALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQLRQwrgaRVAMIFQEPmT 103
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLE-----AEEGKIEIDGIDISTIPLEDLRS----SLTIIPQDP-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 104 ALNPTRRIGLqmmDVIRHHqpisrrearakaiallEEMQIPDAVEVmSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEP 183
Cdd:cd03369 93 LFSGTIRSNL---DPFDEY----------------SDEEIYGALRV-SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446115686 184 TTALDVTVQLQVLRLLKHKarASGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESG 239
Cdd:cd03369 153 TASIDYATDALIQKTIREE--FTNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-247 |
5.71e-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: 69.08 E-value: 5.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIMrllptGSY-CVHRGQISLLGEDVlNAREKQlrQWRGARVAMIFQE-PM 102
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALF-----GAYpGKFEGNVFINGKPV-DIRNPA--QAIRAGIAMVPEDrKR 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 103 TALNPTRRIGLQM-MDVIRHHQPISRREARAKAIALLEEMQipdAVEVMSRYPF----ELSGGMRQRVMIAPAFSCEPQL 177
Cdd:TIGR02633 348 HGIVPILGVGKNItLSVLKSFCFKMRIDAAAELQIIGSAIQ---RLKVKTASPFlpigRLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 178 IIAGEPTTALDVTVQLQVLRLLKHKARaSGTAVLFISHDMAVVSQLCDSVYVMYAGSViesggTADVIHH 247
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKL-----KGDFVNH 488
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
25-245 |
6.81e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.51 E-value: 6.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrgqisllGEDVLNarEKQLRQWRG---AR-VAMIFQE 100
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSE-----------GEILLD--AQPLESWSSkafARkVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 101 PMTALNPTRRiglQMMDVIRH--HQPISR-----REARAKAIALLeemqipDAVEVMSRYPFELSGGMRQRVMIAPAFSC 173
Cdd:PRK10575 94 LPAAEGMTVR---ELVAIGRYpwHGALGRfgaadREKVEEAISLV------GLKPLAHRLVDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115686 174 EPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVI 245
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-236 |
1.23e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.22 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 14 SFPGfngdVHALNNVSLQINRGEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGEDVLNAREKQLRQwrgAR 93
Cdd:PRK10982 7 SFPG----VKALDNVNLKVRPHSIHALMGENGAGKST----LLKCL-FGIYQKDSGSILFQGKEIDFKSSKEALE---NG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 94 VAMIFQEpmtaLNPTRRigLQMMDVI---RHHQP---ISRREARAKAIALLEEMQIP-DAVEVMSrypfELSGGMRQRVM 166
Cdd:PRK10982 75 ISMVHQE----LNLVLQ--RSVMDNMwlgRYPTKgmfVDQDKMYRDTKAIFDELDIDiDPRAKVA----TLSVSQMQMIE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115686 167 IAPAFSCEPQLIIAGEPTTAL---DVTVQLQVLRLLKHKarasGTAVLFISHDMAVVSQLCDSVYVMYAGSVI 236
Cdd:PRK10982 145 IAKAFSYNAKIVIMDEPTSSLtekEVNHLFTIIRKLKER----GCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
9-245 |
1.29e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.14 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 9 QQLHLSFpgfngdvhalnnvSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQlrq 88
Cdd:PRK10771 12 HHLPMRF-------------DLTVERGERVAILGPSGAGKSTLLNLIAGFLT-----PASGSLTLNGQDHTTTPPSR--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 89 wrgaR-VAMIFQEP--MTALNPTRRIGLQMMDVIR--HHQpisrreaRAKAIALLEEMQIPDaveVMSRYPFELSGGMRQ 163
Cdd:PRK10771 71 ----RpVSMLFQENnlFSHLTVAQNIGLGLNPGLKlnAAQ-------REKLHAIARQMGIED---LLARLPGQLSGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 164 RVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTAD 243
Cdd:PRK10771 137 RVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
..
gi 446115686 244 VI 245
Cdd:PRK10771 217 LL 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
25-239 |
1.51e-12 |
|
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: 65.26 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSvTAM--LIMRLLPTGsycvhrgqisLLGEDVLNAREKQLRQWRgARVAMIFQEPM 102
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKS-TLLnaLAGRRTGLG----------VSGEVLINGRPLDKRSFR-KIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 103 talnptrriglqmmdvirHHQPISRREArakaialleeMQIpdAVEVMSrypfeLSGGMRQRVMIAPAFSCEPQLIIAGE 182
Cdd:cd03213 93 ------------------LHPTLTVRET----------LMF--AAKLRG-----LSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446115686 183 PTTALDVTVQLQVLRLLKHKARaSGTAVLFISHDM-AVVSQLCDSVYVMYAGSVIESG 239
Cdd:cd03213 138 PTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-237 |
2.73e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 21 DVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDV-----LNAREKQL------RQW 89
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG-----GEIRLNGKDIsprspLDAVKKGMayitesRRD 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 90 RGARVAMIFQEPMTALNPTRRIGLQ-MMDVIRHHQPISRREARAKAIALleemqipdAVEVMSRYPFELSGGMRQRVMIA 168
Cdd:PRK09700 350 NGFFPNFSIAQNMAISRSLKDGGYKgAMGLFHEVDEQRTAENQRELLAL--------KCHSVNQNITELSGGNQQKVLIS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446115686 169 PAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARaSGTAVLFISHDMAVVSQLCDSVYVMYAGSVIE 237
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-240 |
2.75e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.43 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 1 MTQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLImrllpTG--SYCVHRGQISLLGEDV 78
Cdd:CHL00131 3 KNKPILEIKNLHASV----NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI-----AGhpAYKILEGDILFKGESI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 79 LNArEKQLRQWRGARVAmiFQEP------------MTALNpTRRIGLQMMDVirhhQPISRREARAKAIALLEEMQIpda 146
Cdd:CHL00131 74 LDL-EPEERAHLGIFLA--FQYPieipgvsnadflRLAYN-SKRKFQGLPEL----DPLEFLEIINEKLKLVGMDPS--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 147 veVMSRYPFE-LSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVqLQVLRLLKHKARASGTAVLFISHDMAVVSQLC- 224
Cdd:CHL00131 143 --FLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDA-LKIIAEGINKLMTSENSIILITHYQRLLDYIKp 219
|
250
....*....|....*.
gi 446115686 225 DSVYVMYAGSVIESGG 240
Cdd:CHL00131 220 DYVHVMQNGKIIKTGD 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-230 |
7.79e-12 |
|
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: 62.08 E-value: 7.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSvtamlimRLLptgsycvhrgQIsLLGEdvlnarekq 85
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKS-------TLL----------KL-IAGE--------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 lrqwrgarvamifqepmtaLNPTRRIglqmmdvIRHHQPISrrearakaIALLEEmqipdavevmsrypfeLSGGMRQRV 165
Cdd:cd03221 50 -------------------LEPDEGI-------VTWGSTVK--------IGYFEQ----------------LSGGEKMRL 79
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115686 166 MIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARasgtAVLFISHDMAVVSQLCDSVYVM 230
Cdd:cd03221 80 ALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIEL 140
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
20-235 |
1.04e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.93 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVtamlIMRLL-----PTGsycvhrGQIsLLGEDVLNAREKQLRqwrgarv 94
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKST----LLRLLagletPSA------GEL-LAGTAPLAEAREDTR------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 95 aMIFQEpmTALNPTRRI----GLQMmdvirhhqpisRREARAKAIALLEEMQIPD-AVEvmsrYPFELSGGMRQRVMIAP 169
Cdd:PRK11247 85 -LMFQD--ARLLPWKKVidnvGLGL-----------KGQWRDAALQALAAVGLADrANE----WPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115686 170 AFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
20-239 |
1.12e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 64.76 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAmlimrlLPTgsycvhrgqiSLLGEDVlNAREKQLRQW----RGARVA 95
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA------LPA----------HV*GPDA-GRRPWRF*TWcanrRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 96 MIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVevmSRYPFELSGGMRQRVMIAPAFSCEP 175
Cdd:NF000106 87 IG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAA---GRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115686 176 QLIIAGEPTTALDVTVQLQVLRLLKHKARaSGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-241 |
1.52e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.49 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 3 QPVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSvTAMLIMRLLPTGSYCVHrGQISLLGEDVLNAR 82
Cdd:PRK09984 2 QTIIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKS-TLLRHLSGLITGDKSAG-SHIELLGRTVQREG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 83 E--KQLRQWRgARVAMIFQEpmtaLNPTRRIGLqMMDVI---RHHQPISRrearaKAIALLEEMQIPDAVEVMSRYPF-- 155
Cdd:PRK09984 76 RlaRDIRKSR-ANTGYIFQQ----FNLVNRLSV-LENVLigaLGSTPFWR-----TCFSWFTREQKQRALQALTRVGMvh 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 156 -------ELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVY 228
Cdd:PRK09984 145 fahqrvsTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIV 224
|
250
....*....|...
gi 446115686 229 VMYAGSVIESGGT 241
Cdd:PRK09984 225 ALRQGHVFYDGSS 237
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-233 |
1.78e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 12 HLSFPGfngdvhaLNNVSLQINRGEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGEDVlNAREKQL----- 86
Cdd:PRK10762 262 NLSGPG-------VNDVSFTLRKGEILGVSGLMGAGRTE----LMKVL-YGALPRTSGYVTLDGHEV-VTRSPQDglang 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 87 -------RQWRGARVAMIFQEPM--TALNPTRRIGLQmmdvIRHHQpisRREARAKAIALLEeMQIPDavevMSRYPFEL 157
Cdd:PRK10762 329 ivyisedRKRDGLVLGMSVKENMslTALRYFSRAGGS----LKHAD---EQQAVSDFIRLFN-IKTPS----MEQAIGLL 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115686 158 SGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLI-NQFKAEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-239 |
2.18e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.35 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 7 DIQQLHLSFpGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMrllptGSYCVHRGQISLLGEDVLNAREKQL 86
Cdd:PRK10790 340 RIDIDNVSF-AYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLM-----GYYPLTEGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 87 RQwrgaRVAMIFQEPMTalnptrriglqMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPF--------ELS 158
Cdd:PRK10790 414 RQ----GVAMVQQDPVV-----------LADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYtplgeqgnNLS 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 159 GGMRQRVMIAPAFSCEPQLIIAGEPTTALDV----TVQlQVLRLLKHKarasgTAVLFISHDMAVVSQlCDSVYVMYAGS 234
Cdd:PRK10790 479 VGQKQLLALARVLVQTPQILILDEATANIDSgteqAIQ-QALAAVREH-----TTLVVIAHRLSTIVE-ADTILVLHRGQ 551
|
....*
gi 446115686 235 VIESG 239
Cdd:PRK10790 552 AVEQG 556
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-239 |
6.24e-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: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 12 HLSFpGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLlptgsYCVHRGQISLLGEDVLNAREKQLRqwrg 91
Cdd:COG5265 362 NVSF-GYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF-----YDVTSGRILIDGQDIRDVTQASLR---- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 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 446115686 165 VMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARasGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESG 239
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
150-248 |
7.54e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.20 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 150 MSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYV 229
Cdd:PRK11144 122 LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVV 201
|
90
....*....|....*....
gi 446115686 230 MYAGSVIESGGTADVIHHP 248
Cdd:PRK11144 202 LEQGKVKAFGPLEEVWASS 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-227 |
1.34e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.51 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISllgedvlnaREKQLRQwrGARVAMIFQ 99
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDE-----GVIK---------RNGKLRI--GYVPQKLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 100 EPMTALNPTR----RIGLQMMDVIrhhqPISRRearAKAIALLEE-MQipdavevmsrypfELSGGMRQRVMIAPAFSCE 174
Cdd:PRK09544 79 DTTLPLTVNRflrlRPGTKKEDIL----PALKR---VQAGHLIDApMQ-------------KLSGGETQRVLLARALLNR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446115686 175 PQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSV 227
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-233 |
1.44e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.73 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIMrllptG-SYcvhrGQ-ISllGEDVLNAREKQLRQWRGARVAMIfqepM 102
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVF-----GrSY----GRnIS--GTVFKDGKEVDVSTVSDAIDAGL----A 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 103 TALNPTRRIGLQMMDVIRHH------QPISRR----EARAKAIAllEE----MQI--PDAVEVMSRypfeLSGGMRQRVM 166
Cdd:NF040905 341 YVTEDRKGYGLNLIDDIKRNitlanlGKVSRRgvidENEEIKVA--EEyrkkMNIktPSVFQKVGN----LSGGNQQKVV 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446115686 167 IAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKArASGTAVLFISHDMAVVSQLCDSVYVMYAG 233
Cdd:NF040905 415 LSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELA-AEGKGVIVISSELPELLGMCDRIYVMNEG 480
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-230 |
1.63e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.97 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 23 HALNNVSLQINRGEIVGLVGESGSGKSVtamlIMRLLptgsycvhrgqisllgedvlnarekqLRQWRGARVAMIFQEPM 102
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKST----LLRLL--------------------------AGALKGTPVAGCVDVPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 103 TALNPTRRIglqmmdvIRHhqpISRREARAKAIALLEEMQIPDAVEVMSRYPfELSGGMRQRVMIAPAFSCEPQLIIAGE 182
Cdd:COG2401 94 NQFGREASL-------IDA---IGRKGDFKDAVELLNAVGLSDAVLWLRRFK-ELSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446115686 183 PTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVM 230
Cdd:COG2401 163 FCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-247 |
2.32e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.44 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 19 NGDVH-ALNNVSLQINRGEIVGLVGESGSGKSVTAMLImrllpTGSYCVHRGQISLLGEDVLNAREKQLrqwrgarvami 97
Cdd:PRK13545 33 DGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLI-----AGVTMPNKGTVDIKGSAALIAISSGL----------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 98 fQEPMTALNPTRRIGLqMMDVIRhhqpisrrearakaiallEEMQ--IPDAVEVMSRYPF------ELSGGMRQRVMIAP 169
Cdd:PRK13545 97 -NGQLTGIENIELKGL-MMGLTK------------------EKIKeiIPEIIEFADIGKFiyqpvkTYSSGMKSRLGFAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115686 170 AFSCEPQLIIAGEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHH 247
Cdd:PRK13545 157 SVHINPDILVIDEALSVGDQTFTKKCLDKM-NEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-231 |
2.37e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 60.07 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 35 GEIVGLVGESGSGKSvTAMLIM--RLLPtgSYCVHRGQISLlgEDVLNArekqlrqWRGARVamifQEPMTALNPTRrig 112
Cdd:cd03236 26 GQVLGLVGPNGIGKS-TALKILagKLKP--NLGKFDDPPDW--DEILDE-------FRGSEL----QNYFTKLLEGD--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 113 lqmMDVIRHHQPISR--REARAKAIALLEEM-------QIPDAVE---VMSRYPFELSGGMRQRVMIAPAFSCEPQLIIA 180
Cdd:cd03236 87 ---VKVIVKPQYVDLipKAVKGKVGELLKKKdergkldELVDQLElrhVLDRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446115686 181 GEPTTALDVTVQLQVLRLLKHKARaSGTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:cd03236 164 DEPSSYLDIKQRLNAARLIRELAE-DDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
24-234 |
3.36e-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: 58.63 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 24 ALNNVSLQINRGEIVGLVGESGSGKSvtaMLIMRLLptGSYCVHRGQISLLGedvlnarekqlrqwrgaRVAMIFQEPMt 103
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKS---SLLSALL--GELEKLSGSVSVPG-----------------SIAYVSQEPW- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 104 ALNPTRRiglqmmDVIRHHQPI-SRREARA-KAIALLEEMQI-P--DAVEVMSRyPFELSGGMRQRVMIAPAFSCEPQLI 178
Cdd:cd03250 77 IQNGTIR------ENILFGKPFdEERYEKViKACALEPDLEIlPdgDLTEIGEK-GINLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446115686 179 IAGEPTTALDVTVQLQVL-RLLKHKARASGTAVLfISHDMAVVSQlCDSVYVMYAGS 234
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRIL-VTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-225 |
3.79e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 59.41 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 2 TQPVLDIQQLHLSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNA 81
Cdd:PRK14243 7 TETVLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 82 REKQLRQWRgaRVAMIFQEPmtalNP------------TRRIGLQM-MD--VIRhhqpiSRREArakaiALLEEMQipda 146
Cdd:PRK14243 83 DVDPVEVRR--RIGMVFQKP----NPfpksiydniaygARINGYKGdMDelVER-----SLRQA-----ALWDEVK---- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446115686 147 vEVMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARAsgTAVLFISHDMAVVSQLCD 225
Cdd:PRK14243 143 -DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSD 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-239 |
4.07e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.91 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTamliMRLLpTGSYCVHRGQISLLGEDVlNAREKQLRqwrgarvamifq 99
Cdd:NF033858 277 GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTT----MKML-TGLLPASEGEAWLFGQPV-DAGDIATR------------ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 100 epmtalnptRRIG--------------LQMMDVirH----HQPISRREARAKaiALLEEMqipDAVEVMSRYPFELSGGM 161
Cdd:NF033858 339 ---------RRVGymsqafslygeltvRQNLEL--HarlfHLPAAEIAARVA--EMLERF---DLADVADALPDSLPLGI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 162 RQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVlFIS-HDM--AvvsQLCDSVYVMYAGSVIES 238
Cdd:NF033858 403 RQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTI-FIStHFMneA---ERCDRISLMHAGRVLAS 478
|
.
gi 446115686 239 G 239
Cdd:NF033858 479 D 479
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-229 |
9.24e-10 |
|
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: 58.19 E-value: 9.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 32 INRGEIVGLVGESGSGKSVTA-MLIMRLLPTGsycvhrGQISLLGEDVlnarekqlrQWRGARVAMIFQEPMTALnptrr 110
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIkMLAGVLKPDE------GDIEIELDTV---------SYKPQYIKADYEGTVRDL----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 111 iglqMMDVIRHH--QPISRREarakaiaLLEEMQIPDaveVMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALD 188
Cdd:cd03237 82 ----LSSITKDFytHPYFKTE-------IAKPLQIEQ---ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446115686 189 VTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYV 229
Cdd:cd03237 148 VEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-245 |
1.56e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.74 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIMrllptgsycvhrGQI---SLLGEDVLNARE--KQLRQwrgaRVAMIFQ 99
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALA------------GRIqgnNFTGTILANNRKptKQILK----RTGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 100 EPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPF--ELSGGMRQRVMIAPAFSCEPQL 177
Cdd:PLN03211 148 DDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFirGISGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115686 178 IIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVI 245
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAM 295
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-239 |
2.42e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 58.32 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycvHRGQISLLGEDVlnaREKQLRQWRgARVAMIFQEPMTa 104
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP------YQGSLKINGIEL---RELDPESWR-KHLSWVGQNPQL- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 105 LNPTRRIGLQMMDVIRHHQPISRREARAKAIALLEEM------QIPDAvevMSRypfeLSGGMRQRVMIAPAFSCEPQLI 178
Cdd:PRK11174 435 PHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLpqgldtPIGDQ---AAG----LSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115686 179 IAGEPTTALDVTVQLQVLRLLKHKARasGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESG 239
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQG 565
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-243 |
2.69e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.14 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 4 PVLDIQQLHLSFPGfngdVHALNNVSLQINRGEIVGLVGESGSGKSvTAMLIMR-LLPTGSycvhrGQISLLGEDVLNAR 82
Cdd:PRK15439 10 PLLCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKS-TLMKIIAgIVPPDS-----GTLEIGGNPCARLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 83 EKQLRQWRgarVAMIFQEPMTALNPTRR----IGLQmmdvirhhqpiSRREARAKAIALLEEMQI---PDA----VEVMS 151
Cdd:PRK15439 80 PAKAHQLG---IYLVPQEPLLFPNLSVKenilFGLP-----------KRQASMQKMKQLLAALGCqldLDSsagsLEVAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 152 RYPFE-LSGGMRqrvmiapafscEPQLIIAGEPTTALdvtVQLQVLRLLKH--KARASGTAVLFISHDMAVVSQLCDSVY 228
Cdd:PRK15439 146 RQIVEiLRGLMR-----------DSRILILDEPTASL---TPAETERLFSRirELLAQGVGIVFISHKLPEIRQLADRIS 211
|
250
....*....|....*
gi 446115686 229 VMYAGSVIESGGTAD 243
Cdd:PRK15439 212 VMRDGTIALSGKTAD 226
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
137-229 |
3.26e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 137 LLEEMQIPDaveVMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHD 216
Cdd:PRK13409 437 IIKPLQLER---LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD 513
|
90
....*....|...
gi 446115686 217 MAVVSQLCDSVYV 229
Cdd:PRK13409 514 IYMIDYISDRLMV 526
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
156-229 |
3.50e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 3.50e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115686 156 ELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYV 229
Cdd:COG1245 455 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-235 |
5.08e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.23 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 28 VSLQINRGEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQISLLGEDVlnarekQLRQWRGARVAMIfqepmtALNP 107
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSE----LMKLL-YGATRRTAGQVYLDGKPI------DIRSPRDAIRAGI------MLCP 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 108 TRR-----IGLQ-MMDVI-----RHHQP----ISRREARAKAIALLEEMQI--PDAVEVMSrypfELSGGMRQRVMIAPA 170
Cdd:PRK11288 335 EDRkaegiIPVHsVADNInisarRHHLRagclINNRWEAENADRFIRSLNIktPSREQLIM----NLSGGNQQKAILGRW 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115686 171 FSCEPQLIIAGEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:PRK11288 411 LSEDMKVILLDEPTRGIDVGAKHEIYNVI-YELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
156-231 |
5.79e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 5.79e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115686 156 ELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHkaRASGTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRE--LAEGKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-231 |
6.50e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.10 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 34 RGEIVGLVGESGSGKSvTAMLIM--RLLPTgsycvhrgqislLGE-DVLNAREKQLRQWRGARVAMIFQ-----EPMTAL 105
Cdd:COG1245 98 KGKVTGILGPNGIGKS-TALKILsgELKPN------------LGDyDEEPSWDEVLKRFRGTELQDYFKklangEIKVAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 106 NPtrriglQMMDVIRhhqpisrREARAKAIALL----EEMQIPDAVE------VMSRYPFELSGGMRQRVMIAPAFSCEP 175
Cdd:COG1245 165 KP------QYVDLIP-------KVFKGTVRELLekvdERGKLDELAEklglenILDRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446115686 176 QLIIAGEPTTALDVTVQLQVLRLLKHKARaSGTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:COG1245 232 DFYFFDEPSSYLDIYQRLNVARLIRELAE-EGKYVLVVEHDLAILDYLADYVHILY 286
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-215 |
7.60e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 56.74 E-value: 7.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSFPgfNGDVhALNNVSLQINRGEIVGLVGESGSGKSvtamLIMR----LLPTGSycvhrGQISLLgedvlna 81
Cdd:COG4178 363 LALEDLTLRTP--DGRP-LLEDLSLSLKPGERLLITGPSGSGKS----TLLRaiagLWPYGS-----GRIARP------- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 82 rekqlrqwRGARVAMIFQEPMTALNPTRriglqmmDVI---RHHQPISRREARAkaiaLLEEMQIPDAVEVM------SR 152
Cdd:COG4178 424 --------AGARVLFLPQRPYLPLGTLR-------EALlypATAEAFSDAELRE----ALEAVGLGHLAERLdeeadwDQ 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115686 153 ypfELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHkaRASGTAVLFISH 215
Cdd:COG4178 485 ---VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-240 |
1.14e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.80 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSFPgfngDVHALNNVSLQINRGEIVGLVGESGSGKS-VTAMLIMRllptGSYCVHRGQISLLGEDVLnarE 83
Cdd:PRK09580 1 MLSIKDLHVSVE----DKAILRGLNLEVRPGEVHAIMGPNGSGKStLSATLAGR----EDYEVTGGTVEFKGKDLL---E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 84 KQLRQWRGARVAMIFQEPM------------TALNPTRRiglqmmdvIRHHQPISRREARAKAIALLEEMQIPDavEVMS 151
Cdd:PRK09580 70 LSPEDRAGEGIFMAFQYPVeipgvsnqfflqTALNAVRS--------YRGQEPLDRFDFQDLMEEKIALLKMPE--DLLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 152 R-YPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVqLQVLRLLKHKARASGTAVLFISHDMAVVSQL-CDSVYV 229
Cdd:PRK09580 140 RsVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDA-LKIVADGVNSLRDGKRSFIIVTHYQRILDYIkPDYVHV 218
|
250
....*....|.
gi 446115686 230 MYAGSVIESGG 240
Cdd:PRK09580 219 LYQGRIVKSGD 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-247 |
2.83e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 26 NNVSLQINRGEIVGLVGESGSGKSVTAMLIMrllptGSYcvhRGQISllGEDVLNAREKQLRQWRGARVAMIfqepmtAL 105
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLF-----GAY---PGRWE--GEIFIDGKPVKIRNPQQAIAQGI------AM 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 106 NPT--RRIGL-QMMDVIrhhQPIS----RREARAKAI-ALLEEMQIPDAVE---VMSRYPF----ELSGGMRQRVMIAPA 170
Cdd:PRK13549 343 VPEdrKRDGIvPVMGVG---KNITlaalDRFTGGSRIdDAAELKTILESIQrlkVKTASPElaiaRLSGGNQQKAVLAKC 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446115686 171 FSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARaSGTAVLFISHDMAVVSQLCDSVYVMYAGSViesggTADVIHH 247
Cdd:PRK13549 420 LLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKL-----KGDLINH 490
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-237 |
3.37e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.98 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 6 LDIQQLHLSF-PGFNGDVHALnnvSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREK 84
Cdd:PLN03232 1235 IKFEDVHLRYrPGLPPVLHGL---SFFVSPSEKVGVVGRTGAGKSSMLNALFRIVE-----LEKGRIMIDDCDVAKFGLT 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 QLRqwrgaRVAMIFQEPMTALNPTRRIGLqmmDVIRHHQPISRREArakaialLEEMQIPDAVevmSRYPFEL------- 157
Cdd:PLN03232 1307 DLR-----RVLSIIPQSPVLFSGTVRFNI---DPFSEHNDADLWEA-------LERAHIKDVI---DRNPFGLdaevseg 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 158 ----SGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARAsgTAVLFISHDMAVVSQlCDSVYVMYAG 233
Cdd:PLN03232 1369 genfSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS--CTMLVIAHRLNTIID-CDKILVLSSG 1445
|
....
gi 446115686 234 SVIE 237
Cdd:PLN03232 1446 QVLE 1449
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-245 |
1.05e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.14 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSY---CVHRGQISLLGEDVLNAREKQLRQWRgarvAMIFQ-- 99
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAprgARVTGDVTLNGEPLAAIDAPRLARLR----AVLPQaa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 100 EPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIALleemQIPDAVEVMSRYPFELSGGMRQRVMIA---------PA 170
Cdd:PRK13547 93 QPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQAL----ALAGATALVGRDVTTLSGGELARVQFArvlaqlwppHD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115686 171 FSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVI 245
Cdd:PRK13547 169 AAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
153-215 |
1.56e-07 |
|
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: 50.23 E-value: 1.56e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115686 153 YPF--ELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhkarASGTAVLFISH 215
Cdd:cd03223 86 YPWddVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-247 |
1.65e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.74 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 19 NGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHR-GQISLLGEDV-LNAREKQLRQWRGARVAM 96
Cdd:PRK13546 34 NKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRnGEVSVIAISAgLSGQLTGIENIEFKMLCM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 97 IF-QEPMTALNPTRRIGLQMMDVIrhHQPISRrearakaialleemqipdavevmsrypfeLSGGMRQRVMIAPAFSCEP 175
Cdd:PRK13546 114 GFkRKEIKAMTPKIIEFSELGEFI--YQPVKK-----------------------------YSSGMRAKLGFSINITVNP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115686 176 QLIIAGEPTTALDVTVQLQVLRLLkHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGGTADVIHH 247
Cdd:PRK13546 163 DILVIDEALSVGDQTFAQKCLDKI-YEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-234 |
1.79e-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: 51.18 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 21 DVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAREKQlrqwRGArVAMIFQE 100
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRN----RYS-VAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 101 PMTaLNPTrriglqMMDVIRHHQPISRREARA--KAIALLEEMQI---PDAVEVMSRyPFELSGGMRQRVMIAPAFSCEP 175
Cdd:cd03290 88 PWL-LNAT------VEENITFGSPFNKQRYKAvtDACSLQPDIDLlpfGDQTEIGER-GINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115686 176 QLIIAGEPTTALDV-----TVQLQVLRLLKHKARasgtAVLFISHDMAVVSQlCDSVYVMYAGS 234
Cdd:cd03290 160 NIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAMKDGS 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-239 |
2.06e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 52.71 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 24 ALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKqLRQWRGarvamifqepmt 103
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTS-----GTVLVGGKDIETNLDA-VRQSLG------------ 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 104 aLNPTRRIGLQMMDVIRHH------QPISRREARAKAIALLEEMQIPDAVEVMSRypfELSGGMRQRVMIAPAFSCEPQL 177
Cdd:TIGR01257 1007 -MCPQHNILFHHLTVAEHIlfyaqlKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQ---DLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115686 178 IIAGEPTTALDVTVQLQVLR-LLKHKaraSGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESG 239
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDlLLKYR---SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-222 |
3.85e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.80 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 27 NVSLQINRGEIVGLVGESGSGKsvTAMLimRLL-----PTGsycvhrGQISLLGEDVLNAREKQLRQ--WRGaRVAMIFQ 99
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGK--TSLL--RILaglarPDA------GEVLWQGEPIRRQRDEYHQDllYLG-HQPGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 100 EpMTAL-NptrrigLQMMdvIRHHQPISRrEARAKAIA---LLEEMQIPDAVevmsrypfeLSGGMRQRVMIAPAFSCEP 175
Cdd:PRK13538 88 E-LTALeN------LRFY--QRLHGPGDD-EALWEALAqvgLAGFEDVPVRQ---------LSAGQQRRVALARLWLTRA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446115686 176 QLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQ 222
Cdd:PRK13538 149 PLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVASD 195
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
156-231 |
6.02e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.72 E-value: 6.02e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115686 156 ELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
18-220 |
6.61e-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: 49.92 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 18 FNGDVHALNNVSLQINRGEIVGLVGESGSGKSVtamLIMRLL-PTGSYCVHRGQISLLGEDVLNAREKQlrqwrgARVAM 96
Cdd:cd03271 4 KGARENNLKNIDVDIPLGVLTCVTGVSGSGKSS---LINDTLyPALARRLHLKKEQPGNHDRIEGLEHI------DKVIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 97 IFQEPM---TALNPTRRIGLqmMDVIR------------HHQPISRReARAKAIALLEEMQIPDAVEVMSRYP------- 154
Cdd:cd03271 75 IDQSPIgrtPRSNPATYTGV--FDEIRelfcevckgkryNRETLEVR-YKGKSIADVLDMTVEEALEFFENIPkiarklq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 155 ----------------FELSGGMRQRVMIAPAFS---CEPQLIIAGEPTTAL---DVTVQLQVLrllkHKARASGTAVLF 212
Cdd:cd03271 152 tlcdvglgyiklgqpaTTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLhfhDVKKLLEVL----QRLVDKGNTVVV 227
|
....*...
gi 446115686 213 ISHDMAVV 220
Cdd:cd03271 228 IEHNLDVI 235
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-244 |
6.78e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 21 DVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-PTgsycvhRGQISLlgEDVLNAREKQLRQWRgARVAMIFQ 99
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPT------EGDIII--NDSHNLKDINLKWWR-SKIGVVSQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 100 EPMTALNPTRR------IGLQMMDVIRHH----------QPISRREARAKAIALLEEM---------------------- 141
Cdd:PTZ00265 468 DPLLFSNSIKNnikyslYSLKDLEALSNYynedgndsqeNKNKRNSCRAKCAGDLNDMsnttdsneliemrknyqtikds 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 142 ----------------QIPDAVEVM-SRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKAR 204
Cdd:PTZ00265 548 evvdvskkvlihdfvsALPDKYETLvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKG 627
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446115686 205 ASGTAVLFISHDMAVVsQLCDSVYVMyagSVIESGGTADV 244
Cdd:PTZ00265 628 NENRITIIIAHRLSTI-RYANTIFVL---SNRERGSTVDV 663
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-78 |
7.50e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 50.57 E-value: 7.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 2 TQPVLDIQQLHL-----SFPGFNGDVH-ALNNVSLQINRGEIVGLVGESGSGKSVTAMLImrllpTGSYCVHRGQISLLG 75
Cdd:COG4615 319 PPAPADFQTLELrgvtyRYPGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLL-----TGLYRPESGEILLDG 393
|
...
gi 446115686 76 EDV 78
Cdd:COG4615 394 QPV 396
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
25-230 |
8.76e-07 |
|
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: 48.78 E-value: 8.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVtamlimrLLPTGSYCVHRGQISllGEDVLNAREKQlrqwrgarvaMIFQepmta 104
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTT-------LLDVLAGRKTAGVIT--GEILINGRPLD----------KNFQ----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 105 lnptRRIG-LQMMDVirhHQPISR-REArakaialLEemqipdavevMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGE 182
Cdd:cd03232 79 ----RSTGyVEQQDV---HSPNLTvREA-------LR----------FSALLRGLSVEQRKRLTIGVELAAKPSILFLDE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446115686 183 PTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVM 230
Cdd:cd03232 135 PTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLL 182
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-211 |
9.88e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.29 E-value: 9.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTgsycvhRGQISLlgeDVLNAREKQLRQWRGArVAMIFQEpMTA 104
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST------EGEIQI---DGVSWNSVTLQTWRKA-FGVIPQK-VFI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 105 LNPTRRIGL----QMMDvirhhQPISRREARAKAIALLEemQIPDAVE-VMSRYPFELSGGMRQRVMIAPAFSCEPQLII 179
Cdd:TIGR01271 1304 FSGTFRKNLdpyeQWSD-----EEIWKVAEEVGLKSVIE--QFPDKLDfVLVDGGYVLSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190
....*....|....*....|....*....|..
gi 446115686 180 AGEPTTALDvTVQLQVLRLLKHKARASGTAVL 211
Cdd:TIGR01271 1377 LDEPSAHLD-PVTLQIIRKTLKQSFSNCTVIL 1407
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-188 |
1.01e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.12 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLImrllpTGSYCVHRGQISLLGEDVLNAREkqlRQWRGARVAMIFQ 99
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-----AGARKIQQGRVEVLGGDMADARH---RRAVCPRIAYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 100 EPMTALNPT-----------RRIGLqmmdvirhhqpiSRREARAKAIALLEEMQIpdavevmsrYPF------ELSGGMR 162
Cdd:NF033858 84 GLGKNLYPTlsvfenldffgRLFGQ------------DAAERRRRIDELLRATGL---------APFadrpagKLSGGMK 142
|
170 180
....*....|....*....|....*.
gi 446115686 163 QRVMIAPAFSCEPQLIIAGEPTTALD 188
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-243 |
2.10e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.26 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSFPgfngDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLL-------------PTG--------- 62
Cdd:PTZ00265 1168 IMDVNFRYISRP----NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfkneHTNdmtneqdyq 1243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 63 -------------------------SYCVHR--GQISLLGEDVLNAREKQLRQWrgarVAMIFQEPMTalnptrrIGLQM 115
Cdd:PTZ00265 1244 gdeeqnvgmknvnefsltkeggsgeDSTVFKnsGKILLDGVDICDYNLKDLRNL----FSIVSQEPML-------FNMSI 1312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 116 MDVIRHHQPISRRE--ARAKAIALLEEM--QIPDAVEV-MSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVT 190
Cdd:PTZ00265 1313 YENIKFGKEDATREdvKRACKFAAIDEFieSLPNKYDTnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1392
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446115686 191 VQLQVLR-LLKHKARASGTaVLFISHDMAVVSQlCDSVYVM----YAGSVIESGGTAD 243
Cdd:PTZ00265 1393 SEKLIEKtIVDIKDKADKT-IITIAHRIASIKR-SDKIVVFnnpdRTGSFVQAHGTHE 1448
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-129 |
2.37e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.60 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 34 RGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCV--------HRGQISLLGEDVLNAREKQLRQWRGARVAM--------- 96
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgediLEEVLDQLLLIIVGGKKASGSGELRLRLALalarklkpd 80
|
90 100 110
....*....|....*....|....*....|....*
gi 446115686 97 --IFQEPMTALNPTRRIGLQMMDVIRHHQPISRRE 129
Cdd:smart00382 81 vlILDEITSLLDAEQEALLLLLEELRLLLLLKSEK 115
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-239 |
2.84e-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: 49.17 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 14 SFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKS--VTAMLimrllptGSYCVHRGQISLLGEdVLNAREKQLRQWRG 91
Cdd:TIGR00957 643 TFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSslLSALL-------AEMDKVEGHVHMKGS-VAYVPQQAWIQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 92 ARVAMIFQEPmtaLNPtrriglqmmdvirhhqpiSRREARAKAIALLEEMQI-P--DAVEVMSRyPFELSGGMRQRVMIA 168
Cdd:TIGR00957 715 LRENILFGKA---LNE------------------KYYQQVLEACALLPDLEIlPsgDRTEIGEK-GVNLSGGQKQRVSLA 772
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446115686 169 PAFSCEPQLIIAGEPTTALDVTVQLQVLR-------LLKHKARasgtavLFISHDMAVVSQLcDSVYVMYAGSVIESG 239
Cdd:TIGR00957 773 RAVYSNADIYLFDDPLSAVDAHVGKHIFEhvigpegVLKNKTR------ILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
13-222 |
6.13e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.78 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 13 LSFPGFNgdVHALNNVSLQINRGEIVGLVGESGSGKSvtamlimrllptgsycvhrgqiSLLGEDVLNAREKQLRQWRga 92
Cdd:cd03238 1 LTVSGAN--VHNLQNLDVSIPLNVLVVVTGVSGSGKS----------------------TLVNEGLYASGKARLISFL-- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 93 rvamifqePMTALNPTRRIG-LQ-MMDVIRHHQPISRrearakaialleEMQipdavevmsrypfELSGGMRQRVMIAP- 169
Cdd:cd03238 55 --------PKFSRNKLIFIDqLQfLIDVGLGYLTLGQ------------KLS-------------TLSGGELQRVKLASe 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446115686 170 -AFSCEPQLIIAGEPTTALDVTVQLQVLRLLKhKARASGTAVLFISHDMAVVSQ 222
Cdd:cd03238 102 lFSEPPGTLFILDEPSTGLHQQDINQLLEVIK-GLIDLGNTVILIEHNLDVLSS 154
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-239 |
6.94e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQLRQwrgaRVAMIFQEPM-- 102
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVE-----VCGGEIRVNGREIGAYGLRELRR----QFSMIPQDPVlf 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 103 ---TALNPTRRIGLQMMDVIRHHQPISRREARAKaiallEEMQIPDAV-EVMSRYpfelSGGMRQRVMIAPA-FSCEPQL 177
Cdd:PTZ00243 1397 dgtVRQNVDPFLEASSAEVWAALELVGLRERVAS-----ESEGIDSRVlEGGSNY----SVGQRQLMCMARAlLKKGSGF 1467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446115686 178 IIAGEPTT----ALDVTVQLQVLRLLkhkaraSGTAVLFISHDMAVVSQlCDSVYVMYAGSVIESG 239
Cdd:PTZ00243 1468 ILMDEATAnidpALDRQIQATVMSAF------SAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMG 1526
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-239 |
9.66e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 9.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKS--VTAMLimRLLPT--GSYCVHRGQISLLgedvlnarekqlrqwrgARVA 95
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTslISAML--GELPPrsDASVVIRGTVAYV-----------------PQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 96 MIFqepmtalNPTRRiglqmmDVIRHHQPI--SRREARAKAIALLEEMQI-P--DAVEVMSRyPFELSGGMRQRVMIAPA 170
Cdd:PLN03130 689 WIF-------NATVR------DNILFGSPFdpERYERAIDVTALQHDLDLlPggDLTEIGER-GVNISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115686 171 FSCEPQLIIAGEPTTALDVTVQLQVL-----RLLKHKARASGTAVL-FISHdmavvsqlCDSVYVMYAGSVIESG 239
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHVGRQVFdkcikDELRGKTRVLVTNQLhFLSQ--------VDRIILVHEGMIKEEG 821
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
25-254 |
1.02e-05 |
|
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: 46.06 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQLRqwrgARVAMIFQEPMT- 103
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVD-----IFDGKIVIDGIDISKLPLHTLR----SRLSIILQDPILf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 104 ------ALNPTRRIglqmmdvirhhqpISRREARAKAIALLEEM--QIPDAVEVMSRYPFE-LSGGMRQRVMIAPAFSCE 174
Cdd:cd03288 108 sgsirfNLDPECKC-------------TDDRLWEALEIAQLKNMvkSLPGGLDAVVTEGGEnFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 175 PQLIIAGEPTTALDVTVQlQVLRLLKHKARASGTaVLFISHDMAVVSQlCDSVYVMYAGSVIESGGTADVIHHPRHPYTI 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 |
1.39e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 46.00 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTgsycvhRGQISLlgeDVLNAREKQLRQWRGArVAMIFQEPMTA 104
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT------EGDIQI---DGVSWNSVPLQKWRKA-FGVIPQKVFIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 105 LNPTRriglQMMDVIRHH--QPISRREARAKAIALLEemQIPDAVE-VMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAG 181
Cdd:cd03289 90 SGTFR----KNLDPYGKWsdEEIWKVAEEVGLKSVIE--QFPGQLDfVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190
....*....|....*....|....*....|
gi 446115686 182 EPTTALDvTVQLQVLRLLKHKARASGTAVL 211
Cdd:cd03289 164 EPSAHLD-PITYQVIRKTLKQAFADCTVIL 192
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
16-88 |
1.76e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.12 E-value: 1.76e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446115686 16 PGFngdvhALNNVSLQINRGEIVGLVGESGSGKSVTAMLImrllpTGSYCVHRGQISLLGEDVLNAREKQLRQ 88
Cdd:PRK10522 335 NGF-----SVGPINLTIKRGELLFLIGGNGSGKSTLAMLL-----TGLYQPQSGEILLDGKPVTAEQPEDYRK 397
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-216 |
2.33e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 13 LSFpgfnGDVHALNNVSLQINRGEIVGLVGESGSGKSVtamlIMRLLpTGSYCVHRGQIsLLGEDVLNAREKQ--LRQWR 90
Cdd:PRK11147 11 LSF----SDAPLLDNAELHIEDNERVCLVGRNGAGKST----LMKIL-NGEVLLDDGRI-IYEQDLIVARLQQdpPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 91 G---ARVAMIFQEPMTALNPTRRIGLQMMdvirhHQPISRREAR-AKAIALLE-------EMQIPDAVEVMSRYP----F 155
Cdd:PRK11147 81 GtvyDFVAEGIEEQAEYLKRYHDISHLVE-----TDPSEKNLNElAKLQEQLDhhnlwqlENRINEVLAQLGLDPdaalS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115686 156 ELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHkarASGtAVLFISHD 216
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT---FQG-SIIFISHD 212
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-234 |
2.74e-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: 44.85 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIM-RLLPTGSYCVHRGQISLlgedvlnarekqlrqwrGARVAMIFqePMT 103
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIKHSGRISF-----------------SSQFSWIM--PGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 104 aLNPTRRIGLQmMDVIRHHQPIsrrearaKAIALLEEM-QIPDAVE-VMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAG 181
Cdd:cd03291 114 -IKENIIFGVS-YDEYRYKSVV-------KACQLEEDItKFPEKDNtVLGEGGITLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446115686 182 EPTTALDVTVQLQVLRLLKHKARASGTAVLFISHdmavVSQL--CDSVYVMYAGS 234
Cdd:cd03291 185 SPFGYLDVFTEKEIFESCVCKLMANKTRILVTSK----MEHLkkADKILILHEGS 235
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-245 |
4.33e-05 |
|
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: 45.32 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGsycvhRGQISLLGEDVLNAREKQLRqwrgARVAMIFQEPMTa 104
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESA-----EGEIIIDGLNIAKIGLHDLR----FKITIIPQDPVL- 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 105 LNPTRRIGLqmmdvirhhQPISRREARAKAIAlLEEMQIPDAVEVM-SRYPFE-------LSGGMRQRVMIAPAFSCEPQ 176
Cdd:TIGR00957 1372 FSGSLRMNL---------DPFSQYSDEEVWWA-LELAHLKTFVSALpDKLDHEcaeggenLSVGQRQLVCLARALLRKTK 1441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446115686 177 LIIAGEPTTALDvtvqLQVLRLLKHKARAS--GTAVLFISHDMAVVSQLCdSVYVMYAGSVIESGGTADVI 245
Cdd:TIGR00957 1442 ILVLDEATAAVD----LETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLL 1507
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
24-215 |
5.60e-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: 43.50 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 24 ALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSycvhrGQISLLGEDVLNAREKQLRQ--WRGARVAMifqep 101
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDS-----GEVRWNGTPLAEQRDEPHENilYLGHLPGL----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 102 MTALNPTRRIglqmmdviRHHQPISRREARAkAIALLEEMQIPDAVEVMSRYpfeLSGGMRQRVMIAPAFSCEPQLIIAG 181
Cdd:TIGR01189 85 KPELSALENL--------HFWAAIHGGAQRT-IEDALAAVGLTGFEDLPAAQ---LSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|....*
gi 446115686 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 |
7.05e-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: 44.52 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIM-RLLPTGSYCVHRGQISLlgedvlnarekqlrqwrGARVAMIFqePMT 103
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMgELEPSEGKIKHSGRISF-----------------SPQTSWIM--PGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 104 aLNPTRRIGLQmMDVIRHHQPIsrrearaKAIALLEEMQI-PDAVE-VMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAG 181
Cdd:TIGR01271 503 -IKDNIIFGLS-YDEYRYTSVI-------KACQLEEDIALfPEKDKtVLGEGGITLSGGQRARISLARAVYKDADLYLLD 573
|
170 180 190
....*....|....*....|....*....|...
gi 446115686 182 EPTTALDVTVQLQVLRLLKHKARASGTAVLFIS 214
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFESCLCKLMSNKTRILVTS 606
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
157-235 |
1.46e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 1.46e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446115686 157 LSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARaSGTAVLFISHDMAVVSQLCDSVYVMYAGSV 235
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-237 |
2.06e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.19 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPtgsycVHRGQISLLGEDVLNAREKQLRQwrgaRVAMIFQEPMTa 104
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVE-----LERGRILIDGCDISKFGLMDLRK----VLGIIPQAPVL- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 105 LNPTRRIGLqmmDVIRHHQPISRREArakaialLEEMQIPDAVEvmsRYPFEL-----------SGGMRQRVMIAPAFSC 173
Cdd:PLN03130 1325 FSGTVRFNL---DPFNEHNDADLWES-------LERAHLKDVIR---RNSLGLdaevseagenfSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446115686 174 EPQLIIAGEPTTALDVTVQLQVLRLLKHKARAsgTAVLFISHDMAVVSQlCDSVYVMYAGSVIE 237
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIREEFKS--CTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-248 |
2.89e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.84 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVtamLIMRLLptGSYCVHRGqisllgedvlnarekqlRQWRGARVAMIFQEPMTa 104
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKST---LLQSLL--SQFEISEG-----------------RVWAERSIAYVPQQAWI- 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 105 LNPTRRIGLQMMDvirhhqpiSRREAR-AKAIAL--LEE--MQIPDAVEV-MSRYPFELSGGMRQRVMIAPAFSCEPQLI 178
Cdd:PTZ00243 733 MNATVRGNILFFD--------EEDAARlADAVRVsqLEAdlAQLGGGLETeIGEKGVNLSGGQKARVSLARAVYANRDVY 804
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 179 IAGEPTTALDVTVQLQVLRLLKHKARASGTAVLfISHDMAVVSqLCDSVYVMYAGSVIESGGTADVIHHP 248
Cdd:PTZ00243 805 LLDDPLSALDAHVGERVVEECFLGALAGKTRVL-ATHQVHVVP-RADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
157-227 |
3.25e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 3.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446115686 157 LSGGMRQRVMIA---PAFSCEPQLIIAGEPTTAL---DVTVQLQVLRLLKHKarasGTAVLFISHDMAVVsQLCDSV 227
Cdd:PRK00635 810 LSGGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLhthDIKALIYVLQSLTHQ----GHTVVIIEHNMHVV-KVADYV 881
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
158-239 |
3.29e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.40 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 158 SGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLfishdMAVV--SQ----LCDSVYVMY 231
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPL-----VAIYqcSQdayeLFDKVIVLY 285
|
....*...
gi 446115686 232 AGSVIESG 239
Cdd:TIGR00956 286 EGYQIYFG 293
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
25-216 |
3.81e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVtamlIMRLLptgsycvhRGQISLLGEDVLNAREKQLrqwrgarvAMIFQE---- 100
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKST----LLALL--------KNEISADGGSYTFPGNWQL--------AWVNQEtpal 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 101 PMTALNptrriglQMMDVIRHHQPISRREARAK------AIALLE-EMQIPDAVEVMSRYPFEL---------------- 157
Cdd:PRK10636 77 PQPALE-------YVIDGDREYRQLEAQLHDANerndghAIATIHgKLDAIDAWTIRSRAASLLhglgfsneqlerpvsd 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 158 -SGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHkarASGTAVLfISHD 216
Cdd:PRK10636 150 fSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKS---YQGTLIL-ISHD 205
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-234 |
5.65e-04 |
|
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: 41.92 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 5 VLDIQQLHLSFPGFNGDvhALNNVSLQINRGEIVGLVGESGSGKSVTAMLImrllpTGSYCVHRGQISLLGEDVLNAREK 84
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKML-----TGDTTVTSGDATVAGKSILTNISD 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 85 qlrqwrgARVAMIFQEPMTALNptrriglQMMDVIRHHQPISR-REARAKAIALLEEMQIPDAVevMSRYPFEL----SG 159
Cdd:TIGR01257 2010 -------VHQNMGYCPQFDAID-------DLLTGREHLYLYARlRGVPAEEIEKVANWSIQSLG--LSLYADRLagtySG 2073
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115686 160 GMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARaSGTAVLFISHDMAVVSQLCDSVYVMYAGS 234
Cdd:TIGR01257 2074 GNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
25-189 |
7.21e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSV----TAMLIMRLLPTGSYCVHRGQiSLLGED------VLNA---------REKQ 85
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTflryMAMHAIDGIPKNCQILHVEQ-EVVGDDttalqcVLNTdiertqlleEEAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 86 L-RQWRGARVAMIFQEPMTALNPTRR---IGLQMMDVIRHHQPISRREARAKAIALLEEMQIPDAVEVMSRYPFelSGGM 161
Cdd:PLN03073 272 LvAQQRELEFETETGKGKGANKDGVDkdaVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQVKATKTF--SGGW 349
|
170 180
....*....|....*....|....*...
gi 446115686 162 RQRVMIAPAFSCEPQLIIAGEPTTALDV 189
Cdd:PLN03073 350 RMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
157-222 |
7.82e-04 |
|
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: 41.15 E-value: 7.82e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446115686 157 LSGGMRQRVMIAPAFSCE---PQLIIAGEPTTAL---DVTVQLQVLRLLKHKarasGTAVLFISHDMAVVSQ 222
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIKKLLEVLQRLVDK----GNTVVVIEHNLDVIKT 897
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-215 |
4.28e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 38.94 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 25 LNNVSLQINRGEIVGLVGESGSGKSVtamlimrLLPTGSYCVHRGQISlLGEDVLNAREKQLRQWRgaRVAMIFQEPMTA 104
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTT-------LLNVLAERVTTGVIT-GGDRLVNGRPLDSSFQR--SIGYVQQQDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 105 LNPTRRIGLQMMDVIRHHQPISRREARA---KAIALLEEMQIPDAVEVMsryPFE-LSGGMRQRVMIAPAFSCEPQLII- 179
Cdd:TIGR00956 849 PTSTVRESLRFSAYLRQPKSVSKSEKMEyveEVIKLLEMESYADAVVGV---PGEgLNVEQRKRLTIGVELVAKPKLLLf 925
|
170 180 190
....*....|....*....|....*....|....*.
gi 446115686 180 AGEPTTALDVTVQLQVLRLLKHKARAsGTAVLFISH 215
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIH 960
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
155-241 |
4.83e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.69 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 155 FELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALD---VTVQLQVLRLLKhkarasgTAVLFISHDMAVVSQLCDSVYVMY 231
Cdd:PLN03073 626 YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDldaVEALIQGLVLFQ-------GGVLMVSHDEHLISGSVDELWVVS 698
|
90
....*....|
gi 446115686 232 AGSVIESGGT 241
Cdd:PLN03073 699 EGKVTPFHGT 708
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
157-220 |
5.09e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 38.39 E-value: 5.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446115686 157 LSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVtvqlQVLRLLKHK-ARASGTaVLFISHDMAVV 220
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELlDSYQGT-VLLVSHDRQFV 500
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
135-215 |
6.31e-03 |
|
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: 38.19 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 135 IALLEEMQIPDAVE------VMSRYPFELSGGMRQRVMIAPAFSCEPQLIIAGEPTTALDVTVQLQVLRLLKHKarasGT 208
Cdd:TIGR00954 555 EQILDNVQLTHILEreggwsAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF----GI 630
|
....*..
gi 446115686 209 AVLFISH 215
Cdd:TIGR00954 631 TLFSVSH 637
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
22-53 |
6.84e-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: 37.24 E-value: 6.84e-03
10 20 30
....*....|....*....|....*....|..
gi 446115686 22 VHALNNVSLQINRGEIVGLVGESGSGKSVTAM 53
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSLAF 39
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-215 |
7.98e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 37.69 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 20 GDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGsYCVH-------RGQisllGEDVLNAreKQLRQWRGA 92
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQG-YSNDltlfgrrRGS----GETIWDI--KKHIGYVSS 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446115686 93 RVAMIFQEPMTALNPtrrIGLQMMDVIRHHQPISRREaRAKAIALLEEMQIPDAvevMSRYPFE-LSGGMRQRVMIAPAF 171
Cdd:PRK10938 344 SLHLDYRVSTSVRNV---ILSGFFDSIGIYQAVSDRQ-QKLAQQWLDILGIDKR---TADAPFHsLSWGQQRLALIVRAL 416
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446115686 172 SCEPQLIIAGEPTTALDVTVQLQVLRLLKHKARASGTAVLFISH 215
Cdd:PRK10938 417 VKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| |
