|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-323 |
4.73e-177 |
|
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: 492.26 E-value: 4.73e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTLIEGGMTVDGHDIMSLSNRAL 87
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 SDLRGAVVSMVFQEPRLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIPSPERRLSNYPHEMSGGMLQRAM 167
Cdd:COG0444 81 RKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 168 IAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIR 247
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523689182 248 NPRHPYTKGLLGARVELAEGRDRLVTIPGAPPDLAAMPPGCAFAPRCVQVSDLCQKQIPPLLPLSGGAGVACLFPD 323
Cdd:COG0444 241 NPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGPGHRVACHLYE 316
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-283 |
3.22e-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: 386.73 E-value: 3.22e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 3 MQNDAMIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTLIEGG-MTVDGHDIMS 81
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGsILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 82 LSNRALSDLRGAVVSMVFQEPRLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIPSPERRLSNYPHEMSGG 161
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 162 MLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGL 241
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 523689182 242 VGDIIRNPRHPYTKGLLGARVElaegRDRLVTIPGAPPDLAA 283
Cdd:COG4172 241 TAELFAAPQHPYTRKLLAAEPR----GDPRPVPPDAPPLLEA 278
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
4-322 |
5.60e-112 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 327.84 E-value: 5.60e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 4 QNDAMIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTLIEGGMTVDGHDIMSLS 83
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 84 NRALSDLRGAVVSMVFQEPRLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIPSPERRLSNYPHEMSGGML 163
Cdd:PRK09473 88 EKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 164 QRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVG 243
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNAR 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523689182 244 DIIRNPRHPYTKGLLGARVELAEGRDRLVTIPGAPPDLAAMPPGCAFAPRCVQVSDLCQkQIPPLLPLSGGAGVACLFP 322
Cdd:PRK09473 248 DVFYQPSHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICS-SAPPLEEFGPGRLRACFKP 325
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-240 |
1.23e-111 |
|
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: 323.30 E-value: 1.23e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgtlIEGGMTVDGHDIMSLSNRAL 87
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKP---TSGSIIFDGKDLLKLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 SdLRGAVVSMVFQEPRLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALfQKVRIPSPERRLSNYPHEMSGGMLQRAM 167
Cdd:cd03257 78 K-IRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLL-LLVGVGLPEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523689182 168 IAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-323 |
3.34e-104 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 307.81 E-value: 3.34e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 3 MQNDAMIDISNLSVTF-------RRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgTliEGGMTVD 75
Cdd:COG4608 2 AMAEPLLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEP-T--SGEILFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 76 GHDIMSLSNRALSDLRgAVVSMVFQEPRLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIPsPERrLSNYP 155
Cdd:COG4608 79 GQDITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLR-PEH-ADRYP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 156 HEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGR 235
Cdd:COG4608 156 HEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 236 IVEEGLVGDIIRNPRHPYTKGLLGA--RVELAEGRDRLVtIPGAPPDLAAMPPGCAFAPRCVQVSDLCQKQIPPLLPLSG 313
Cdd:COG4608 236 IVEIAPRDELYARPLHPYTQALLSAvpVPDPERRRERIV-LEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLREVGP 314
|
330
....*....|
gi 523689182 314 GAGVACLFPD 323
Cdd:COG4608 315 GHQVACHLAE 324
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
7-322 |
8.24e-104 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 307.05 E-value: 8.24e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 7 AMIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRL--HPkGTLIEGGMTVDGHDIMSLSN 84
Cdd:PRK11022 2 ALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYP-GRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 85 RALSDLRGAVVSMVFQEPRLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIPSPERRLSNYPHEMSGGMLQ 164
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 165 RAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGD 244
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523689182 245 IIRNPRHPYTKGLLGARVELAEGRDRLVTIPGAPPDLAAMPPGCAFAPRCVQVSDLCQKQIPPLLPLsGGAGVACLFP 322
Cdd:PRK11022 241 IFRAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNML-AGRQSKCHYP 317
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-260 |
4.37e-97 |
|
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: 296.04 E-value: 4.37e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 6 DAMIDISNLSVTFR-RGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtLIEGGMTVDGHDIMSLSN 84
Cdd:COG1123 258 EPLLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR---PTSGSILFDGKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 85 RALSDLRGAVvSMVFQEPRLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIPspERRLSNYPHEMSGGMLQ 164
Cdd:COG1123 335 RSLRELRRRV-QMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP--PDLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 165 RAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGD 244
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
250
....*....|....*.
gi 523689182 245 IIRNPRHPYTKGLLGA 260
Cdd:COG1123 492 VFANPQHPYTRALLAA 507
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-281 |
2.02e-94 |
|
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: 289.11 E-value: 2.02e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 6 DAMIDISNLSVTFRRGgkAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTLIEGGMTVDGHDIMSLSNR 85
Cdd:COG1123 2 TPLLEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 alsdLRGAVVSMVFQEPRLALDPVyTVGRQIEETImRHEKVSRGLAAERALALFQKVRIpspERRLSNYPHEMSGGMLQR 165
Cdd:COG1123 80 ----LRGRRIGMVFQDPMTQLNPV-TVGDQIAEAL-ENLGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 166 AMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDI 245
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 523689182 246 IRNPRhpytkgLLGARVELAEGRDRLVTIPGAPPDL 281
Cdd:COG1123 231 LAAPQ------ALAAVPRLGAARGRAAPAAAAAEPL 260
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-260 |
6.47e-87 |
|
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: 260.89 E-value: 6.47e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTlieGGMTVDGHDImslSNRAL 87
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWS---GEVTFDGRPV---TRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 SDLRGAVvSMVFQEPRLALDPVYTVGRQIEETIMRHEkvsRGLAAERALALFQKVRIPspERRLSNYPHEMSGGMLQRAM 167
Cdd:COG1124 75 KAFRRRV-QMVFQDPYASLHPRHTVDRILAEPLRIHG---LPDREERIAELLEQVGLP--PSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 168 IAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIR 247
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
250
....*....|...
gi 523689182 248 NPRHPYTKGLLGA 260
Cdd:COG1124 229 GPKHPYTRELLAA 241
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
7-322 |
4.32e-82 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 251.75 E-value: 4.32e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 7 AMIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTLIEGG-MTVDGHDIMSLSNR 85
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADrFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 ALSDLRGAVVSMVFQEPRLALDPVYTVGRQIEETIMRHE-KVS----RGLAAERALALFQKVRIPSPERRLSNYPHEMSG 160
Cdd:COG4170 82 ERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTfKGKwwqrFKWRKKRAIELLHRVGIKDHKDIMNSYPHELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 161 GMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 241 LVGDIIRNPRHPYTKGLLGA----RVELAEgRDRLVTIPGAPPDLAAMPPGCAFAPRCVQVSDLCQKQiPPLLPLSGGAg 316
Cdd:COG4170 242 PTEQILKSPHHPYTKALLRSmpdfRQPLPH-KSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVET-PRLRKIKGHE- 318
|
....*.
gi 523689182 317 VACLFP 322
Cdd:COG4170 319 FACHFP 324
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
27-261 |
2.03e-81 |
|
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: 246.51 E-value: 2.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 27 AVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTLI-EGGMTVDGHDIMSLSnralsdLRGAVVSMVFQEPRLA 105
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQtSGEILLDGRPLLPLS------IRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 106 LDPVYTVGRQIEETIMRHEKVSRGlAAERALALFQKVRIPSPERRLSNYPHEMSGGMLQRAMIAMALACNPKVLLADEPT 185
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSLGKLSKQ-ARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523689182 186 TALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNPRHPYTKGLLGAR 261
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSAH 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-266 |
1.98e-80 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 256.32 E-value: 1.98e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 3 MQNDAMIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRL--HPKGTLIEGGMTVDGH--- 77
Cdd:PRK10261 7 LDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLleQAGGLVQCDKMLLRRRsrq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 78 --DIMSLSNRALSDLRGAVVSMVFQEPRLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIPSPERRLSNYP 155
Cdd:PRK10261 87 viELSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 156 HEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGR 235
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250 260 270
....*....|....*....|....*....|.
gi 523689182 236 IVEEGLVGDIIRNPRHPYTKGLLGARVELAE 266
Cdd:PRK10261 247 AVETGSVEQIFHAPQHPYTRALLAAVPQLGA 277
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-260 |
2.55e-78 |
|
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: 248.06 E-value: 2.55e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTF-------RRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgtliEGGMTVDGHDIMS 81
Cdd:COG4172 276 LEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS----EGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 82 LSNRALSDLRgAVVSMVFQEPRLALDPVYTVGRQIEETIMRHE-KVSRGLAAERALALFQKVRIPsPERRlSNYPHEMSG 160
Cdd:COG4172 352 LSRRALRPLR-RRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLD-PAAR-HRYPHEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 161 GMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQG 508
|
250 260
....*....|....*....|
gi 523689182 241 LVGDIIRNPRHPYTKGLLGA 260
Cdd:COG4172 509 PTEQVFDAPQHPYTRALLAA 528
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-319 |
5.91e-78 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 241.02 E-value: 5.91e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 20 RGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLlrlhpkgTLIE----GGMTVDGHDIMSLSNRALSDLRGAVv 95
Cdd:PRK11308 23 KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLL-------TMIEtptgGELYYQGQDLLKADPEAQKLLRQKI- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 96 SMVFQEPRLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIpSPERrLSNYPHEMSGGMLQRAMIAMALACN 175
Cdd:PRK11308 95 QIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGL-RPEH-YDRYPHMFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 176 PKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNPRHPYTK 255
Cdd:PRK11308 173 PDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQ 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523689182 256 GLLGARVELAEGRDRL-VTIPGAPPDLAAMPPGCAFAPRCVQVSDLCQKQIPPLLPLsGGAGVAC 319
Cdd:PRK11308 253 ALLSATPRLNPDDRRErIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDY-DGRLVAC 316
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-260 |
7.13e-77 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 244.61 E-value: 7.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 1 MTMqndAMIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTLI--EGGMTVDGHD 78
Cdd:PRK15134 1 MTQ---PLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVypSGDIRFHGES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 79 IMSLSNRALSDLRGAVVSMVFQEPRLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIPSPERRLSNYPHEM 158
Cdd:PRK15134 78 LLHASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 159 SGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVE 238
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
250 260
....*....|....*....|..
gi 523689182 239 EGLVGDIIRNPRHPYTKGLLGA 260
Cdd:PRK15134 238 QNRAATLFSAPTHPYTQKLLNS 259
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
1-254 |
2.14e-70 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 219.30 E-value: 2.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 1 MTMQNDAMIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSL-LRLHP-KGTLIEGGMTVDGHD 78
Cdd:COG4107 1 MTNEEQPLLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLyFDLAPtSGSVYYRDRDGGPRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 79 IMSLSNRALSDLRGAVVSMVFQEPRLALDPVYTVGRQIEETIM----RHEKVSRglaaERALALFQKVRIPSpeRRLSNY 154
Cdd:COG4107 81 LFALSEAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAERLMaageRHYGDIR----ARALEWLERVEIPL--ERIDDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 155 PHEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAG 234
Cdd:COG4107 155 PRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNG 234
|
250 260
....*....|....*....|
gi 523689182 235 RIVEEGLVGDIIRNPRHPYT 254
Cdd:COG4107 235 RVVESGLTDQVLEDPQHPYT 254
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
8-322 |
6.88e-68 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 215.44 E-value: 6.88e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTLIEGG-MTVDGHDIMSLSNRA 86
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADrMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSDLRGAVVSMVFQEPRLALDPVYTVGRQIEETIMRHEKVSR-----GLAAERALALFQKVRIPSPERRLSNYPHEMSGG 161
Cdd:PRK15093 83 RRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGWTYKGRwwqrfGWRKRRAIELLHRVGIKDHKDAMRSFPYELTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 162 MLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGL 241
Cdd:PRK15093 163 ECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 242 VGDIIRNPRHPYTKGLLGARVELAEG---RDRLVTIPGAPPDLAAMPPGCAFAPRCVQVSDLCQkQIPPLLPLSGGAgVA 318
Cdd:PRK15093 243 SKELVTTPHHPYTQALIRAIPDFGSAmphKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECI-ETPRLTGAKNHL-YA 320
|
....
gi 523689182 319 CLFP 322
Cdd:PRK15093 321 CHFP 324
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-320 |
2.45e-67 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 213.80 E-value: 2.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 1 MTMQNDAMIDISNLSVTFR-RGGKA--------VKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgtlIEGG 71
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDiKDGKQwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKA---TDGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 72 MTVDGHDIMSLSNRALSDLRGAVvSMVFQEPRLALDPVYTVGRQIEETI-MRHEKVSRGLAAERALALFQKVRI-PSPER 149
Cdd:PRK15079 78 VAWLGKDLLGMKDDEWRAVRSDI-QMIFQDPLASLNPRMTIGEIIAEPLrTYHPKLSRQEVKDRVKAMMLKVGLlPNLIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 150 RlsnYPHEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIA 229
Cdd:PRK15079 157 R---YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 230 VMYAGRIVEEGLVGDIIRNPRHPYTKGLLGA------------RVELAEGRdrlVTIPGAPPDlaamppGCAFAPRCVQV 297
Cdd:PRK15079 234 VMYLGHAVELGTYDEVYHNPLHPYTKALMSAvpipdpdlernkTIQLLEGE---LPSPINPPS------GCVFRTRCPIA 304
|
330 340
....*....|....*....|...
gi 523689182 298 SDLCQKQiPPLLPLSGGAGVACL 320
Cdd:PRK15079 305 GPECAKT-RPVLEGSFRHAVSCL 326
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-274 |
5.26e-67 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 213.40 E-value: 5.26e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRL-----HPkgTliEGGMTVDGHDIMSL 82
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS----TLIRCinlleRP--T--SGSVLVDGVDLTAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 83 SNRALSDLRGAVvSMVFQEPRLaLDpvytvGRQIEETI---MRHEKVSRGLAAERALALFQKVRIpspERRLSNYPHEMS 159
Cdd:COG1135 73 SERELRAARRKI-GMIFQHFNL-LS-----SRTVAENValpLEIAGVPKAEIRKRVAELLELVGL---SDKADAYPSQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 160 GGMLQRAMIAMALACNPKVLLADEPTTALD-ATVQiQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVE 238
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDpETTR-SILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVE 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 523689182 239 EGLVGDIIRNPRHPYTKGLLG------------ARVELAEGRDRLVTI 274
Cdd:COG1135 222 QGPVLDVFANPQSELTRRFLPtvlndelpeellARLREAAGGGRLVRL 269
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
9-264 |
4.97e-64 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 203.01 E-value: 4.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTfrrggKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKG-TLIEGGMTVDGHDImslsnrAL 87
Cdd:PRK10418 5 IELRNIALQ-----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvRQTAGRVLLDGKPV------AP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 SDLRGAVVSMVFQEPRLALDPVYTVGRQIEETIMrhekvSRGLAAERA--LALFQKVRIPSPERRLSNYPHEMSGGMLQR 165
Cdd:PRK10418 74 CALRGRKIATIMQNPRSAFNPLHTMHTHARETCL-----ALGKPADDAtlTAALEAVGLENAARVLKLYPFEMSGGMLQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 166 AMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDI 245
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
250
....*....|....*....
gi 523689182 246 IRNPRHPYTKGLLGARVEL 264
Cdd:PRK10418 229 FNAPKHAVTRSLVSAHLAL 247
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
9-236 |
1.18e-63 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 200.79 E-value: 1.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSvTMRSLLrlhpkGTLI---EGGMTVDGHDIMSLSNR 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNIL-----GGLDrptSGEVRVDGTDISKLSEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 ALSDLRGAVVSMVFQEPRLAldPVYTVGRQIEeTIMRHEKVSRGLAAERALALFQKVRIpspERRLSNYPHEMSGGMLQR 165
Cdd:cd03255 75 ELAAFRRRHIGFVFQSFNLL--PDLTALENVE-LPLLLAGVPKKERRERAEELLERVGL---GDRLNHYPSELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523689182 166 AMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEvADRIAVMYAGRI 236
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-239 |
8.56e-62 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 196.03 E-value: 8.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 6 DAMIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSvTMRSLLrlhpkGTLI---EGGMTVDGHDIMSL 82
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNIL-----GGLDrptSGEVLIDGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 83 SNRALSDLRGAVVSMVFQEPRLalDPVYTVGRQIEeTIMRHEKVSRGLAAERALALFQKVRIpspERRLSNYPHEMSGGM 162
Cdd:COG1136 76 SERELARLRRRHIGFVFQFFNL--LPELTALENVA-LPLLLAGVSRKERRERARELLERVGL---GDRLDHRPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523689182 163 LQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEvADRIAVMYAGRIVEE 239
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-250 |
4.07e-59 |
|
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: 189.71 E-value: 4.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRsLLRLHPKGTliEGGMTVDGHDIMSLSNRAL 87
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLERPT--SGSVLVDGTDLTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 SDLRgAVVSMVFQEPRLaLDpvytvGRQIEETI---MRHEKVSRGLAAERALALFQKVRIpspERRLSNYPHEMSGGMLQ 164
Cdd:cd03258 78 RKAR-RRIGMIFQHFNL-LS-----SRTVFENValpLEIAGVPKAEIEERVLELLELVGL---EDKADAYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 165 RAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGD 244
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
....*.
gi 523689182 245 IIRNPR 250
Cdd:cd03258 228 VFANPQ 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
8-255 |
2.12e-58 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 187.89 E-value: 2.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFrrGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtlIEGG-MTVDGHDImSLSNRA 86
Cdd:COG1126 1 MIEIENLHKSF--GDLEV--LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEE----PDSGtITVDGEDL-TDSKKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSDLRgAVVSMVFQepRLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIPSperRLSNYPHEMSGGMLQRA 166
Cdd:COG1126 72 INKLR-RKVGMVFQ--QFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 167 MIAMALACNPKVLLADEPTTALD-ATVQiQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDI 245
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDpELVG-EVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
250
....*....|
gi 523689182 246 IRNPRHPYTK 255
Cdd:COG1126 224 FENPQHERTR 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-255 |
3.67e-57 |
|
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: 184.80 E-value: 3.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 4 QNDAMIDISNLsvTFRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHP--KGTlieggMTVDGHDIMS 81
Cdd:COG1127 1 MSEPMIEVRNL--TKSFGDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRpdSGE-----ILVDGQDITG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 82 LSNRALSDLRgAVVSMVFQEPRL--ALdpvyTVgrqiEETIM----RHEKVSRGLAAERALALFQKVRIPSPERRlsnYP 155
Cdd:COG1127 72 LSEKELYELR-RRIGMLFQGGALfdSL----TV----FENVAfplrEHTDLSEAEIRELVLEKLELVGLPGAADK---MP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 156 HEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGR 235
Cdd:COG1127 140 SELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGK 219
|
250 260
....*....|....*....|
gi 523689182 236 IVEEGLVGDiIRNPRHPYTK 255
Cdd:COG1127 220 IIAEGTPEE-LLASDDPWVR 238
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-287 |
5.25e-55 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 182.61 E-value: 5.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 1 MTMqndAMIDISNLSVTFrrggKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtLIEGGMTVDGHDIM 80
Cdd:COG3842 1 MAM---PALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFET---PDSGRILLDGRDVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 81 SLS-NRalsdlRGavVSMVFQepRLALDPVYTVgrqiEETIM---RHEKVSRGLAAERALALFQKVRIPSPERRlsnYPH 156
Cdd:COG3842 71 GLPpEK-----RN--VGMVFQ--DYALFPHLTV----AENVAfglRMRGVPKAEIRARVAELLELVGLEGLADR---YPH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 157 EMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRI 236
Cdd:COG3842 135 QLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 523689182 237 VEEGLVGDIIRNPRHPYTKGLLGA----RVELAEGRDRLVTIPGAP---PDLAAMPPG 287
Cdd:COG3842 215 EQVGTPEEIYERPATRFVADFIGEanllPGTVLGDEGGGVRTGGRTlevPADAGLAAG 272
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
8-246 |
8.34e-55 |
|
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: 179.08 E-value: 8.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSvtFRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtLIEGGMTVDGHDIMSLSNRAL 87
Cdd:COG1120 1 MLEAENLS--VGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK---PSSGEVLLDGRDLASLSRREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 SdlrgAVVSMVFQEPRLALDpvYTVgrqiEETIMR----HEKVSRGL------AAERALALFQ--KVRipspERRLsnyp 155
Cdd:COG1120 74 A----RRIAYVPQEPPAPFG--LTV----RELVALgrypHLGLFGRPsaedreAVEEALERTGleHLA----DRPV---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 156 HEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGR 235
Cdd:COG1120 136 DELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGR 215
|
250
....*....|.
gi 523689182 236 IVEEGLVGDII 246
Cdd:COG1120 216 IVAQGPPEEVL 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-278 |
1.34e-54 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 181.54 E-value: 1.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRL-----HP-KGTLIeggmtVDGHDIMS 81
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS----TLIRCinlleRPtSGRVL-----VDGQDLTA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 82 LSNRALSDLRGAVvSMVFQEPRLAldpvytVGRQIEETI---MRHEKVSRGLAAERALALFQKVRIPSPERRlsnYPHEM 158
Cdd:PRK11153 72 LSEKELRKARRQI-GMIFQHFNLL------SSRTVFDNValpLELAGTPKAEIKARVTELLELVGLSDKADR---YPAQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 159 SGGMLQRAMIAMALACNPKVLLADEPTTALD-ATVQiQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIV 237
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDpATTR-SILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 523689182 238 EEGLVGDIIRNPRHPYTKGLLGA--RVELAEGRDRLVTIPGAP 278
Cdd:PRK11153 221 EQGTVSEVFSHPKHPLTREFIQStlHLDLPEDYLARLQAEPTT 263
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-260 |
5.28e-54 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 186.21 E-value: 5.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 18 FRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMSLSNRALSDLRGAVvSM 97
Cdd:PRK10261 330 LNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ---GGEIIFNGQRIDTLSPGKLQALRRDI-QF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 98 VFQEPRLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIpSPERRLsNYPHEMSGGMLQRAMIAMALACNPK 177
Cdd:PRK10261 406 IFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGL-LPEHAW-RYPHEFSGGQRQRICIARALALNPK 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 178 VLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNPRHPYTKGL 257
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKL 563
|
...
gi 523689182 258 LGA 260
Cdd:PRK10261 564 MAA 566
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-247 |
6.68e-54 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 176.02 E-value: 6.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRggkaVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMSLSNRALs 88
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT---SGEVRVLGEDVARDPAEVR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 dlrgAVVSMVFQEPrlALDPVYTVgRQIEETIMRHEKVSRGLAAERALALFQKVRI-PSPERRLSNYphemSGGMLQRAM 167
Cdd:COG1131 73 ----RRIGYVPQEP--ALYPDLTV-RENLRFFARLYGLPRKEARERIDELLELFGLtDAADRKVGTL----SGGMKQRLG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 168 IAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIR 247
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-239 |
9.11e-54 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 176.43 E-value: 9.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 1 MTMqNDAMIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRL-----HPkgtlIEGGMTVD 75
Cdd:COG1116 1 MSA-AAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS----TLLRLiagleKP----TSGEVLVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 76 GHDIMSLSNRalsdlrgavVSMVFQEPRL-----ALDPVyTVGrqieetiMRHEKVSRGLAAERALALFQKVRIpspERR 150
Cdd:COG1116 72 GKPVTGPGPD---------RGVVFQEPALlpwltVLDNV-ALG-------LELRGVPKAERRERARELLELVGL---AGF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 151 LSNYPHEMSGGMLQRAMIAMALACNPKVLLADEPTTALDA-T-VQIQILLLirELQREYGLSVIFVTHDIGVAAEVADRI 228
Cdd:COG1116 132 EDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAlTrERLQDELL--RLWQETGKTVLFVTHDVDEAVFLADRV 209
|
250
....*....|...
gi 523689182 229 AVMYA--GRIVEE 239
Cdd:COG1116 210 VVLSArpGRIVEE 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
15-264 |
2.00e-51 |
|
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: 170.17 E-value: 2.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 15 SVTFRRGGKAvKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRL-HPKgtliEGGMTVDGHDIMSLSnraLSDLRGA 93
Cdd:cd03295 5 NVTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLiEPT----SGEIFIDGEDIREQD---PVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 94 VvSMVFQEprLALDPVYTVGRQIEeTIMRHEKVSRGLAAERALALFQKVRIPsPERRLSNYPHEMSGGMLQRAMIAMALA 173
Cdd:cd03295 77 I-GYVIQQ--IGLFPHMTVEENIA-LVPKLLKWPKEKIRERADELLALVGLD-PAEFADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 174 CNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNPRHPY 253
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDF 231
|
250
....*....|.
gi 523689182 254 TKGLLGARVEL 264
Cdd:cd03295 232 VAEFVGADRLL 242
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-239 |
2.19e-51 |
|
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: 169.19 E-value: 2.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRL-----HPKgtliEGGMTVDGHDIMSLS 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS----TLLRIiagleRPT----SGEVLVDGEPVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 84 NRalsdlrgavVSMVFQEPRLAldPVYTVgrqiEETIM---RHEKVSRGLAAERALALFQKVRIPSPERRlsnYPHEMSG 160
Cdd:cd03293 73 PD---------RGYVFQQDALL--PWLTV----LDNVAlglELQGVPKAEARERAEELLELVGLSGFENA---YPHQLSG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 161 GMLQRAMIAMALACNPKVLLADEPTTALDA-T-VQIQILLLirELQREYGLSVIFVTHDIGVAAEVADRIAVMYA--GRI 236
Cdd:cd03293 135 GMRQRVALARALAVDPDVLLLDEPFSALDAlTrEQLQEELL--DIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRI 212
|
...
gi 523689182 237 VEE 239
Cdd:cd03293 213 VAE 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-255 |
4.23e-51 |
|
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: 168.83 E-value: 4.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFrrGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRL-HPKGtlieGGMTVDGHDIMSLSNRAL 87
Cdd:cd03261 1 IELRGLTKSF--GGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLlRPDS----GEVLIDGEDISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 SDLRgAVVSMVFQEPrlALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIPSPERRlsnYPHEMSGGMLQRAM 167
Cdd:cd03261 73 YRLR-RRMGMLFQSG--ALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDL---YPAELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 168 IAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDiIR 247
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE-LR 225
|
....*...
gi 523689182 248 NPRHPYTK 255
Cdd:cd03261 226 ASDDPLVR 233
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-240 |
3.30e-50 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 165.77 E-value: 3.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRrggkAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHpkgTLIEGGMTVDGHDIMSLSNRals 88
Cdd:cd03259 1 LELKGLSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLE---RPDSGEILIDGRDVTGVPPE--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 dLRGavVSMVFQEPrlALDPVYTVgrqiEETI---MRHEKVSRGLAAERALALFQKVRIPSPERRlsnYPHEMSGGMLQR 165
Cdd:cd03259 71 -RRN--IGMVFQDY--ALFPHLTV----AENIafgLKLRGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGGQQQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523689182 166 AMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:cd03259 139 VALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
9-291 |
7.66e-50 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 169.17 E-value: 7.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFrrggKAVKAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRL-----HP-KGTLIeggmtVDGHDIMSl 82
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKT----TLLRIiagleTPdSGRIV-----LNGRDLFT- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 83 sNRALSDLRgavVSMVFQEPrlALDPVYTVgrqiEETI---MRHEKVSRGLAAERALALFQKVRIPSPERRlsnYPHEMS 159
Cdd:COG1118 69 -NLPPRERR---VGFVFQHY--ALFPHMTV----AENIafgLRVRPPSKAEIRARVEELLELVQLEGLADR---YPSQLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 160 GGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEE 239
Cdd:COG1118 136 GGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQV 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 523689182 240 GLVGDIIRNPRHPYTKGLLGA----RVELAEGRDRLVTIPgaPPDLAAMPPGCAFA 291
Cdd:COG1118 216 GTPDEVYDRPATPFVARFLGCvnvlRGRVIGGQLEADGLT--LPVAEPLPDGPAVA 269
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-239 |
1.09e-46 |
|
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: 157.60 E-value: 1.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 1 MTMQNDAMIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRL-----HPKgtliEGGMTVD 75
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS----TLLGLlagldRPT----SGTVRLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 76 GHDIMSLSNRALSDLRGAVVSMVFQE----PRL-ALDPVytvgrqieetIMRHEKVSRGLAAERALALFQKVRIpspERR 150
Cdd:COG4181 73 GQDLFALDEDARARLRARHVGFVFQSfqllPTLtALENV----------MLPLELAGRRDARARARALLERVGL---GHR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 151 LSNYPHEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEvADRIAV 230
Cdd:COG4181 140 LDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLR 218
|
....*....
gi 523689182 231 MYAGRIVEE 239
Cdd:COG4181 219 LRAGRLVED 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
9-250 |
1.56e-46 |
|
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: 157.11 E-value: 1.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGgkaVKAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLR-----LHPKgtliEGGMTVDGHDImslS 83
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKS----TLLRllnglLKPT----SGEVLVDGKDI---T 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 84 NRALSDLRgAVVSMVFQEPRLALdpvytVGRQIEETIM---RHEKVSRGLAAERALALFQKVRIPSPERRlsnYPHEMSG 160
Cdd:COG1122 67 KKNLRELR-RKVGLVFQNPDDQL-----FAPTVEEDVAfgpENLGLPREEIRERVEEALELVGLEHLADR---PPHELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 161 GMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:COG1122 138 GQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADG 216
|
250
....*....|
gi 523689182 241 LVGDIIRNPR 250
Cdd:COG1122 217 TPREVFSDYE 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
9-236 |
4.48e-46 |
|
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: 155.38 E-value: 4.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFrrGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtlIEGG-MTVDGHDImSLSNRAL 87
Cdd:cd03262 1 IEIKNLHKSF--GDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEE----PDSGtIIIDGLKL-TDDKKNI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 SDLRgAVVSMVFQepRLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIPSperRLSNYPHEMSGGMLQRAM 167
Cdd:cd03262 72 NELR-QKVGMVFQ--QFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLAD---KADAYPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523689182 168 IAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRI 236
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
13-238 |
6.47e-46 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 155.20 E-value: 6.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 13 NLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSvTMrsllrLHPKGTL---IEGGMTVDGHDIMSLSNRALSD 89
Cdd:TIGR02211 6 NLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKS-TL-----LHLLGGLdnpTSGEVLFNGQSLSKLSSNERAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 90 LRGAVVSMVFQEPRLALDpvYTVgrqIEETIMRH--EKVSRGLAAERALALFQKVRIpspERRLSNYPHEMSGGMLQRAM 167
Cdd:TIGR02211 80 LRNKKLGFIYQFHHLLPD--FTA---LENVAMPLliGKKSVKEAKERAYEMLEKVGL---EHRINHRPSELSGGERQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523689182 168 IAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEvADRIAVMYAGRIVE 238
Cdd:TIGR02211 152 IARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKK-LDRVLEMKDGQLFN 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-240 |
8.13e-46 |
|
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: 153.36 E-value: 8.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 10 DISNLSvtFRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtLIEGGMTVDGHDIMSLSNRALSD 89
Cdd:cd03214 1 EVENLS--VGYGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK---PSSGEILLDGKDLASLSPKELAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 90 LRgAVVSMVfqeprlaldpvytvgrqIEETIMRHekvsrglaaeraLAlfqkvripspERRLSnyphEMSGGMLQRAMIA 169
Cdd:cd03214 74 KI-AYVPQA-----------------LELLGLAH------------LA----------DRPFN----ELSGGERQRVLLA 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523689182 170 MALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:cd03214 110 RALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
24-257 |
1.82e-45 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 155.08 E-value: 1.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 24 AVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSL-LRLHP-KGTLIEGGMTVDGHDIMSLSN---RALSDLRGAVVSmv 98
Cdd:PRK11701 18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALsARLAPdAGEVHYRMRDGQLRDLYALSEaerRRLLRTEWGFVH-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 99 fQEPRLALDPVYTVGRQIEETIM----RHEKVSRglaaERALALFQKVRIPSpeRRLSNYPHEMSGGMLQRAMIAMALAC 174
Cdd:PRK11701 96 -QHPRDGLRMQVSAGGNIGERLMavgaRHYGDIR----ATAGDWLERVEIDA--ARIDDLPTTFSGGMQQRLQIARNLVT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 175 NPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNPRHPYT 254
Cdd:PRK11701 169 HPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYT 248
|
...
gi 523689182 255 KGL 257
Cdd:PRK11701 249 QLL 251
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
7-260 |
2.61e-45 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 154.96 E-value: 2.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 7 AMIDISNLSVTFRRGG----KAVKAV-NGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMS 81
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGGlfgaKQRAPVlTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPA---QGTVSFRGQDLYQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 82 LSNRALSDLRgAVVSMVFQEPRLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIPSPERRlsNYPHEMSGG 161
Cdd:TIGR02769 78 LDRKQRRAFR-RDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDAD--KLPRQLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 162 MLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGL 241
Cdd:TIGR02769 155 QLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECD 234
|
250
....*....|....*....
gi 523689182 242 VGDIIrNPRHPYTKGLLGA 260
Cdd:TIGR02769 235 VAQLL-SFKHPAGRNLQSA 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-258 |
3.50e-45 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 161.03 E-value: 3.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTF-------RRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgtliEGGMTVDGHDIM 80
Cdd:PRK15134 275 LLDVEQLQVAFpirkgilKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS----QGEIWFDGQPLH 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 81 SLSNRALSDLRGAVvSMVFQEPRLALDPVYTVGRQIEETIMRHEKVSRGLAAE-RALALFQKVRIpSPERRlSNYPHEMS 159
Cdd:PRK15134 351 NLNRRQLLPVRHRI-QVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREqQVIAVMEEVGL-DPETR-HRYPAEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 160 GGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEE 239
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQ 507
|
250
....*....|....*....
gi 523689182 240 GLVGDIIRNPRHPYTKGLL 258
Cdd:PRK15134 508 GDCERVFAAPQQEYTRQLL 526
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-260 |
9.51e-45 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 153.69 E-value: 9.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 18 FRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLH-PKGtlieGGMTVDGHDIMSLSNRALSDLRGAVvS 96
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLEsPSQ----GNVSWRGEPLAKLNRAQRKAFRRDI-Q 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 97 MVFQEPRLALDPVYTVGRQIEETiMRH-EKVSRGLAAERALALFQKVRIPspERRLSNYPHEMSGGMLQRAMIAMALACN 175
Cdd:PRK10419 93 MVFQDSISAVNPRKTVREIIREP-LRHlLSLDKAERLARASEMLRAVDLD--DSVLDKRPPQLSGGQLQRVCLARALAVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 176 PKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNpRHPYTK 255
Cdd:PRK10419 170 PKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTF-SSPAGR 248
|
....*
gi 523689182 256 GLLGA 260
Cdd:PRK10419 249 VLQNA 253
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-235 |
1.23e-44 |
|
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: 151.47 E-value: 1.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 16 VTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgtlIEGGMTVDGHDIMSLSNRALSdlrgAVV 95
Cdd:cd03225 5 LSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP---TSGEVLVDGKDLTKLSLKELR----RKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 96 SMVFQEPRLALdpvytVGRQIEETI---MRHEKVSRGLAAERALALFQKVRIPSPERRlsnYPHEMSGGMLQRAMIAMAL 172
Cdd:cd03225 78 GLVFQNPDDQF-----FGPTVEEEVafgLENLGLPEEEIEERVEEALELVGLEGLRDR---SPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523689182 173 ACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGR 235
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
8-260 |
2.76e-44 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 153.32 E-value: 2.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFrrgGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLhpkgtlIE---GGMTVDGHDIMSLSn 84
Cdd:COG1125 1 MIEFENVTKRY---PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRL------IEptsGRILIDGEDIRDLD- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 85 raLSDLR---GAVVsmvfQEPrlALDPVYTVGRQIEeTIMRHEKVSRGLAAERALALFQKVRIPsPERRLSNYPHEMSGG 161
Cdd:COG1125 71 --PVELRrriGYVI----QQI--GLFPHMTVAENIA-TVPRLLGWDKERIRARVDELLELVGLD-PEEYRDRYPHELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 162 MLQRAMIAMALACNPKVLLADEPTTALDATV--QIQILLLirELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEE 239
Cdd:COG1125 141 QQQRVGVARALAADPPILLMDEPFGALDPITreQLQDELL--RLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQY 218
|
250 260
....*....|....*....|.
gi 523689182 240 GLVGDIIRNPRHPYTKGLLGA 260
Cdd:COG1125 219 DTPEEILANPANDFVADFVGA 239
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
9-240 |
4.74e-44 |
|
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: 151.84 E-value: 4.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGK-AVKAVNGVSLSVKPGEVVALLGESGSGKSvTMRSLLR--LHP-KGTLieggmTVDGHDIMSLSN 84
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPfEKKALDDVSLTIEDGEFVAIIGHTGSGKS-TLIQHLNglLKPtSGTV-----TIDGRDITAKKK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 85 RALSDLRgAVVSMVFQEPRlaldpvytvgRQI-EETIM-------RHEKVSRGLAAERALALFQKVRIPspERRLSNYPH 156
Cdd:TIGR04521 75 KKLKDLR-KKVGLVFQFPE----------HQLfEETVYkdiafgpKNLGLSEEEAEERVKEALELVGLD--EEYLERSPF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 157 EMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRI 236
Cdd:TIGR04521 142 ELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKI 221
|
....
gi 523689182 237 VEEG 240
Cdd:TIGR04521 222 VLDG 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-262 |
5.90e-44 |
|
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: 151.64 E-value: 5.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 23 KAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLhpkgtlIE---GGMTVDGHDIMSLSNRALSDLRGAVVSMVF 99
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRL------IEptsGKVLIDGQDIAAMSRKELRELRRKKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 100 QEprLALDPVYTVGRQIEETI-MRHekVSRGLAAERALALFQKVRIpspERRLSNYPHEMSGGMLQRAMIAMALACNPKV 178
Cdd:cd03294 109 QS--FALLPHRTVLENVAFGLeVQG--VPRAEREERAAEALELVGL---EGWEHKYPDELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 179 LLADEPTTALDATV--QIQILLLirELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNPRHPY--- 253
Cdd:cd03294 182 LLMDEAFSALDPLIrrEMQDELL--RLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYvre 259
|
250
....*....|
gi 523689182 254 -TKGLLGARV 262
Cdd:cd03294 260 fFRGVDRAKV 269
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-240 |
7.94e-44 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 150.41 E-value: 7.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGKAVKavnGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHpkgTLIEGGMTVDGHDIMSLSNRALS 88
Cdd:cd03256 1 IEVENLSKTYPNGKKALK---DVSLSINPGEFVALIGPSGAGKSTLLRCLNGLV---EPTSGSVLIDGTDINKLKGKALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 DLRGAVvSMVFQEPRLaldpvytVGRQ--IEETIM----RHEKVsRGLAA-------ERALALFQKVRI-PSPERRLSny 154
Cdd:cd03256 75 QLRRQI-GMIFQQFNL-------IERLsvLENVLSgrlgRRSTW-RSLFGlfpkeekQRALAALERVGLlDKAYQRAD-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 155 phEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAG 234
Cdd:cd03256 144 --QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
....*.
gi 523689182 235 RIVEEG 240
Cdd:cd03256 222 RIVFDG 227
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
21-269 |
8.03e-44 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 153.85 E-value: 8.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 21 GGKavKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLhpkgtlIE---GGMTVDGHDIMSLSNRALSDLRGAVVSM 97
Cdd:TIGR01186 4 GGK--KGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRL------IEptaGQIFIDGENIMKQSPVELREVRRKKIGM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 98 VFQEprLALDPVYTVGRQIEeTIMRHEKVSRGLAAERALALFQKVRIPSPERRlsnYPHEMSGGMLQRAMIAMALACNPK 177
Cdd:TIGR01186 76 VFQQ--FALFPHMTILQNTS-LGPELLGWPEQERKEKALELLKLVGLEEYEHR---YPDELSGGMQQRVGLARALAAEPD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 178 VLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNPRHPYTKGL 257
Cdd:TIGR01186 150 ILLMDEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEF 229
|
250
....*....|..
gi 523689182 258 LGaRVELAEGRD 269
Cdd:TIGR01186 230 IG-KVDLSQVFD 240
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-249 |
1.24e-43 |
|
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: 149.69 E-value: 1.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFrrGGKavKAVNGVSLSVKPGEVVALLGESGSGKSVTMRsllrlhpkgtLIEGGMTVDGHDIMsLSNRALS 88
Cdd:cd03300 1 IELENVSKFY--GGF--VALDGVSLDIKEGEFFTLLGPSGCGKTTLLR----------LIAGFETPTSGEIL-LDGKDIT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 DL----RGavVSMVFQEprLALDPVYTVGRQIEETiMRHEKVSRGLAAERALALFQKVRIPSPERRlsnYPHEMSGGMLQ 164
Cdd:cd03300 66 NLpphkRP--VNTVFQN--YALFPHLTVFENIAFG-LRLKKLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 165 RAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGD 244
Cdd:cd03300 138 RVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
....*
gi 523689182 245 IIRNP 249
Cdd:cd03300 218 IYEEP 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-240 |
2.64e-43 |
|
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: 148.48 E-value: 2.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSvtFRRGGKavKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHP--KGTLIEGGMTVDGHDIMSLSNRA 86
Cdd:cd03260 1 IELRDLN--VYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDliPGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSdLRgAVVSMVFQEPRLALDPVY---TVG---RQIEETIMRHEKVSRGLaaERAlALFQKVripspERRLSnyPHEMSG 160
Cdd:cd03260 77 LE-LR-RRVGMVFQKPNPFPGSIYdnvAYGlrlHGIKLKEELDERVEEAL--RKA-ALWDEV-----KDRLH--ALGLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 161 GMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYglSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
7-260 |
4.08e-43 |
|
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: 148.83 E-value: 4.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 7 AMIDISNLSVTFRRGgkavKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLL-RLHPK-GTLIEGGMTVDGHDIMSLSN 84
Cdd:TIGR02323 2 PLLQVSGLSKSYGGG----KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAgRLAPDhGTATYIMRSGAELELYQLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 85 RALSDLRGAVVSMVFQEPRLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIPspERRLSNYPHEMSGGMLQ 164
Cdd:TIGR02323 78 AERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEID--PTRIDDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 165 RAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGD 244
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQ 235
|
250
....*....|....*.
gi 523689182 245 IIRNPRHPYTKGLLGA 260
Cdd:TIGR02323 236 VLDDPQHPYTQLLVSS 251
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-260 |
4.85e-43 |
|
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: 148.26 E-value: 4.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRggkaVKAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRL-----HP-KGTLIEGGMTVDGHDImsl 82
Cdd:cd03296 3 IEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKT----TLLRLiagleRPdSGTILFGGEDATDVPV--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 83 snralsdlRGAVVSMVFQEprLALDPVYTVGRQIE---ETIMRHEKVSRGLAAERALALFQKVRIPSPERRlsnYPHEMS 159
Cdd:cd03296 72 --------QERNVGFVFQH--YALFRHMTVFDNVAfglRVKPRSERPPEAEIRAKVHELLKLVQLDWLADR---YPAQLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 160 GGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEE 239
Cdd:cd03296 139 GGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQV 218
|
250 260
....*....|....*....|.
gi 523689182 240 GLVGDIIRNPRHPYTKGLLGA 260
Cdd:cd03296 219 GTPDEVYDHPASPFVYSFLGE 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-258 |
4.87e-43 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 148.74 E-value: 4.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 7 AMIDISNLSVTFRrgGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRS--LLRLHPKGTLIEGGMTVDGHDIMSLSN 84
Cdd:PRK11264 2 SAIEVKNLVKKFH--GQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQPEAGTIRVGDITIDTARSLSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 85 RALSDLRGAVvSMVFQEprLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIPSPErrlSNYPHEMSGGMLQ 164
Cdd:PRK11264 78 GLIRQLRQHV-GFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKE---TSYPRRLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 165 RAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIfVTHDIGVAAEVADRIAVMYAGRIVEEGLVGD 244
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
|
250
....*....|....
gi 523689182 245 IIRNPRHPYTKGLL 258
Cdd:PRK11264 231 LFADPQQPRTRQFL 244
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-255 |
1.11e-42 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 147.88 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 1 MTMQNDAM---IDISNLSVTFrrGGKavKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLH---PkGTLIEGGMTV 74
Cdd:COG1117 1 MTAPASTLepkIEVRNLNVYY--GDK--QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdliP-GARVEGEILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 75 DGHDIMSlSNRALSDLRgAVVSMVFQEP---------------RLaldpvytvgrqieetimrHEKVSRGLAA---ERAL 136
Cdd:COG1117 76 DGEDIYD-PDVDVVELR-RRVGMVFQKPnpfpksiydnvayglRL------------------HGIKSKSELDeivEESL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 137 ---ALFQKVRipspeRRLSNYPHEMSGGMLQRAMIAMALACNPKVLLADEPTTALD--ATVQIQilLLIRELQREYglSV 211
Cdd:COG1117 136 rkaALWDEVK-----DRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpiSTAKIE--ELILELKKDY--TI 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 523689182 212 IFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNPRHPYTK 255
Cdd:COG1117 207 VIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-236 |
4.05e-42 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 143.69 E-value: 4.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGgkavKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHP--KGTLieggmTVDGHDIMSLSNRA 86
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKpdSGEI-----KVLGKDIKKEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSDlrgavVSMVFQEPRLalDPVYTVgrqiEETImrhekvsrglaaeralalfqkvripsperrlsnyphEMSGGMLQRA 166
Cdd:cd03230 72 KRR-----IGYLPEEPSL--YENLTV----RENL------------------------------------KLSGGMKQRL 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 167 MIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRI 236
Cdd:cd03230 105 ALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-245 |
4.88e-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: 145.77 E-value: 4.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFrrggKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLR-LHPKgtliEGGMTVDGHDIMSLSNRA 86
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGlLKPD----SGSILIDGEDVRKEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSDLrgavvSMVFQEPrlALDPVYTVGRQIEETIMRHeKVSRGLAAERALALFQKVRIPSP-ERRLsnypHEMSGGMLQR 165
Cdd:COG4555 73 RRQI-----GVLPDER--GLYDRLTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEFlDRRV----GELSTGMKKK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 166 AMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELqREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDI 245
Cdd:COG4555 141 VALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-235 |
1.01e-41 |
|
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: 142.71 E-value: 1.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFrrggKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHpkgTLIEGGMTVDGHDIMSLsNRALS 88
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE---EPDSGSILIDGEDLTDL-EDELP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 DLRgAVVSMVFQEPRLaldpvytvgrqieetiMRHekvsrglaaeraLALFQKVRIPsperrlsnypheMSGGMLQRAMI 168
Cdd:cd03229 73 PLR-RRIGMVFQDFAL----------------FPH------------LTVLENIALG------------LSGGQQQRVAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523689182 169 AMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGR 235
Cdd:cd03229 112 ARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-243 |
2.16e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 140.96 E-value: 2.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFRRGgkaVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLR-LHPKgtliEGGMTVDGHDIMSLSNRA 86
Cdd:COG2884 1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERPT----SGQVLVNGQDLSRLKRRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSDLR---GavvsMVFQEPRLaLDpvytvGRQIEETI---MRHEKVSRGLAAERALALFQKVRIpspERRLSNYPHEMSG 160
Cdd:COG2884 74 IPYLRrriG----VVFQDFRL-LP-----DRTVYENValpLRVTGKSRKEIRRRVREVLDLVGL---SDKAKALPHELSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 161 GMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:COG2884 141 GEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
...
gi 523689182 241 LVG 243
Cdd:COG2884 220 ARG 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-258 |
4.39e-40 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 140.61 E-value: 4.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFrrggKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHP--KGTLIEGGMTVDGHdimSLSNR 85
Cdd:PRK09493 1 MIEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEitSGDLIVDGLKVNDP---KVDER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 ALSDLRGavvsMVFQE----PRL-ALDPVYTVGRQIEetimrheKVSRGLAAERALALFQKVRIpspERRLSNYPHEMSG 160
Cdd:PRK09493 74 LIRQEAG----MVFQQfylfPHLtALENVMFGPLRVR-------GASKEEAEKQARELLAKVGL---AERAHHYPSELSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 161 GMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:PRK09493 140 GQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
|
250
....*....|....*...
gi 523689182 241 LVGDIIRNPRHPYTKGLL 258
Cdd:PRK09493 219 DPQVLIKNPPSQRLQEFL 236
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
9-260 |
8.00e-40 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 139.93 E-value: 8.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRggkaVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRL-HPKgtliEGGMTVDGHDIMSLsnral 87
Cdd:TIGR00968 1 IEIANISKRFGS----FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLeQPD----SGRIRLNGQDATRV----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 sDLRGAVVSMVFQEprLALDPVYTVGRQIE--ETIMRHEKVSRGLAAERALALFQKvripspERRLSNYPHEMSGGMLQR 165
Cdd:TIGR00968 68 -HARDRKIGFVFQH--YALFKHLTVRDNIAfgLEIRKHPKAKIKARVEELLELVQL------EGLGDRYPNQLSGGQRQR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 166 AMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDI 245
Cdd:TIGR00968 139 VALARALAVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEV 218
|
250
....*....|....*
gi 523689182 246 IRNPRHPYTKGLLGA 260
Cdd:TIGR00968 219 YDHPANPFVMSFLGE 233
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-262 |
3.54e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 138.51 E-value: 3.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 7 AMIDISNLSVTFrrggKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMR---SLLRLHPKGTlIEGGMTVDGHDIMSLS 83
Cdd:PRK14247 2 NKIEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnRLIELYPEAR-VSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 84 nraLSDLRGAVvSMVFQEPrlalDPVYTVgrQIEETIMRHEKVSRgLAAERAlALFQKVRIP--------SPERRLSNYP 155
Cdd:PRK14247 77 ---VIELRRRV-QMVFQIP----NPIPNL--SIFENVALGLKLNR-LVKSKK-ELQERVRWAlekaqlwdEVKDRLDAPA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 156 HEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREygLSVIFVTHDIGVAAEVADRIAVMYAGR 235
Cdd:PRK14247 145 GKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQ 222
|
250 260
....*....|....*....|....*..
gi 523689182 236 IVEEGLVGDIIRNPRHPYTKGLLGARV 262
Cdd:PRK14247 223 IVEWGPTREVFTNPRHELTEKYVTGRL 249
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-247 |
3.82e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.60 E-value: 3.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 3 MQNDAMIDISNLSVTFRRggkaVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtLIEGGMTVDGHDIMSL 82
Cdd:COG1121 1 MMMMPAIELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP---PTSGTVRLFGKPPRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 83 SNRalsdlrgavVSMVFQepRLALD---PVyTVgrqiEETIM----RHEKVSRGL------AAERALAL-----FQKVRI 144
Cdd:COG1121 74 RRR---------IGYVPQ--RAEVDwdfPI-TV----RDVVLmgryGRRGLFRRPsradreAVDEALERvgledLADRPI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 145 psperrlsnypHEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEV 224
Cdd:COG1121 138 -----------GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREY 205
|
250 260
....*....|....*....|...
gi 523689182 225 ADRIAVMyAGRIVEEGLVGDIIR 247
Cdd:COG1121 206 FDRVLLL-NRGLVAHGPPEEVLT 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-186 |
8.20e-38 |
|
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: 131.62 E-value: 8.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 28 VNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgtlIEGGMTVDGHDIMSLSNRALsdlrGAVVSMVFQEPRLalD 107
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP---TEGTILLDGQDLTDDERKSL----RKEIGYVFQDPQL--F 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 108 PVYTVGRQIEETiMRHEKVSRGLAAERALALFQKVRIPS-PERRLSNYPHEMSGGMLQRAMIAMALACNPKVLLADEPTT 186
Cdd:pfam00005 72 PRLTVRENLRLG-LLLKGLSKREKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-287 |
9.96e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 137.51 E-value: 9.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 7 AMIDISNLSVTFrrggKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHpkgTLIEGGMTVDGHDIMSLSNRA 86
Cdd:COG3839 2 ASLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLE---DPTSGEILIGGRDVTDLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 lsdlRGavVSMVFQEPrlALDPVYTVgrqiEETI---MRHEKVSRGLAAERALALFQKVRIpspERRLSNYPHEMSGGML 163
Cdd:COG3839 75 ----RN--IAMVFQSY--ALYPHMTV----YENIafpLKLRKVPKAEIDRRVREAAELLGL---EDLLDRKPKQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 164 QRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDigvAAEV---ADRIAVMYAGRIVEEG 240
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHD---QVEAmtlADRIAVMNDGRIQQVG 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 523689182 241 LVGDIIRNPRHPYTKGLLGA------RVELAEGRDRL--VTIPgAPPDLAAMPPG 287
Cdd:COG3839 217 TPEELYDRPANLFVAGFIGSppmnllPGTVEGGGVRLggVRLP-LPAALAAAAGG 270
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
9-237 |
3.49e-37 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 132.45 E-value: 3.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSvTMRSL---LRlhpkgTLIEGGMTVDGHDIMSLSNR 85
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKT-TLLTLiggLR-----SVQEGSLKVLGQELHGASKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 ALSDLRGAVvSMVFQEPRLAldPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIpspERRLSNYPHEMSGGMLQR 165
Cdd:TIGR02982 76 QLVQLRRRI-GYIFQAHNLL--GFLTARQNVQMALELQPNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSGGQKQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523689182 166 AMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVaAEVADRIAVMYAGRIV 237
Cdd:TIGR02982 150 VAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRI-LDVADRILQMEDGKLL 220
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
24-253 |
3.78e-37 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 135.93 E-value: 3.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 24 AVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHpkgTLIEGGMTVDGHDIMSLSNRAlsdlRGavVSMVFQEpr 103
Cdd:TIGR03265 16 AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLE---RQTAGTIYQGGRDITRLPPQK----RD--YGIVFQS-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 104 LALDPVYTVGRQIEETiMRHEKVSRGLAAERALALFQKVRIPSPERRlsnYPHEMSGGMLQRAMIAMALACNPKVLLADE 183
Cdd:TIGR03265 85 YALFPNLTVADNIAYG-LKNRGMGRAEVAERVAELLDLVGLPGSERK---YPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 184 PTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNPRHPY 253
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPF 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
30-262 |
7.82e-37 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 132.07 E-value: 7.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 30 GVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgtlIEGGMTVDGHDIMSLSnralSDLRGavVSMVFQEprLALDPV 109
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKP---DSGKILLNGKDITNLP----PEKRD--ISYVPQN--YALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 110 YTVGRQIEETiMRHEKVSRGLAAERALALFQKVRIpspERRLSNYPHEMSGGMLQRAMIAMALACNPKVLLADEPTTALD 189
Cdd:cd03299 86 MTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGI---DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523689182 190 ATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNPRHPYTKGLLGARV 262
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNN 234
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-245 |
9.18e-37 |
|
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: 131.34 E-value: 9.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLsvTFRRGGkaVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTlieGGMTVDGHDIMslsnRALS 88
Cdd:cd03265 1 IEVENL--VKKYGD--FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTS---GRATVAGHDVV----REPR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 DLRgAVVSMVFQEPrlALDPVYTvGRQIEETIMRHEKVSRGLAAERALALFQKVRI-PSPERRLSNYphemSGGMLQRAM 167
Cdd:cd03265 70 EVR-RRIGIVFQDL--SVDDELT-GWENLYIHARLYGVPGAERRERIDELLDFVGLlEAADRLVKTY----SGGMRRRLE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523689182 168 IAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDI 245
Cdd:cd03265 142 IARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
16-236 |
1.17e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 130.71 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 16 VTFRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMSLSnraLSDLRGAVv 95
Cdd:COG4619 6 LSFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT---SGEIYLDGKPLSAMP---PPEWRRQV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 96 SMVFQEPRLALDpvyTVGRQIEET-IMRHEKVSRglaaERALALFQKVRIPspERRLSNYPHEMSGGMLQRAMIAMALAC 174
Cdd:COG4619 77 AYVPQEPALWGG---TVRDNLPFPfQLRERKFDR----ERALELLERLGLP--PDILDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523689182 175 NPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRI 236
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
7-235 |
2.81e-36 |
|
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: 130.25 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 7 AMIDISNLSVTFR---RGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLR--LHPKGTLI---EGGMTvdghD 78
Cdd:COG4778 3 TLLEVENLSKTFTlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnyLPDSGSILvrhDGGWV----D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 79 IMSLSNRALSDLRGAVVSMVFQ----EPRL-ALDPVytvgrqIEEtiMRHEKVSRGLAAERALALFQKVRIPspERRLSN 153
Cdd:COG4778 79 LAQASPREILALRRRTIGYVSQflrvIPRVsALDVV------AEP--LLERGVDREEARARARELLARLNLP--ERLWDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 154 YPHEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYA 233
Cdd:COG4778 149 PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTP 227
|
..
gi 523689182 234 GR 235
Cdd:COG4778 228 FS 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
27-240 |
3.20e-36 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 130.52 E-value: 3.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 27 AVNGVSLSVKPGEVVALLGESGSGKSVTMR--SLLRLHPKGTLIEGGMTVDGHDimSLSNRALSDLRGAVvSMVFQEPRL 104
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRvlNLLETPDSGQLNIAGHQFDFSQ--KPSEKAIRLLRQKV-GMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 105 AldPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIPSPERRlsnYPHEMSGGMLQRAMIAMALACNPKVLLADEP 184
Cdd:COG4161 94 W--PHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADR---FPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 523689182 185 TTALDATVQIQILLLIRELQrEYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:COG4161 169 TAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
31-240 |
3.51e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 130.52 E-value: 3.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 31 VSLSVKPGEVVALLGESGSGKSVTMR--SLLRLHPKGTLIEGGMTVDghdimsLSN----RALSDLRGAVvSMVFQEPRL 104
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRvlNLLEMPRSGTLNIAGNHFD------FSKtpsdKAIRELRRNV-GMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 105 AldPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRI-PSPERrlsnYPHEMSGGMLQRAMIAMALACNPKVLLADE 183
Cdd:PRK11124 94 W--PHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLkPYADR----FPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 523689182 184 PTTALDATVQIQILLLIRELQrEYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:PRK11124 168 PTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-250 |
3.51e-36 |
|
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: 130.25 E-value: 3.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFrrGGkaVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHP--KGTLIeggmtVDGHDIMSLSNRA 86
Cdd:cd03219 1 LEVRGLTKRF--GG--LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRptSGSVL-----FDGEDITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSDLRgavVSMVFQEPRL-----ALDPVYTVGRQIEETIMRHEKVSRGLAA--ERALALFQKVRIpspERRLSNYPHEMS 159
Cdd:cd03219 72 IARLG---IGRTFQIPRLfpeltVLENVMVAAQARTGSGLLLARARREEREarERAEELLERVGL---ADLADRPAGELS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 160 GGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELqREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEE 239
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
250
....*....|.
gi 523689182 240 GLVGDIIRNPR 250
Cdd:cd03219 225 GTPDEVRNNPR 235
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-258 |
1.26e-35 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 129.91 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 6 DAMIDISNLSVTFR-RGG----KAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTlieGGMTVDGHDIm 80
Cdd:PRK15112 2 ETLLEVRNLSKTFRyRTGwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTS---GELLIDDHPL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 81 slsnrALSD--LRGAVVSMVFQEPRLALDPVYTVGRQIEETIMRHEKVSrglAAERALALFQKVRIPS--PERrLSNYPH 156
Cdd:PRK15112 78 -----HFGDysYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLE---PEQREKQIIETLRQVGllPDH-ASYYPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 157 EMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRI 236
Cdd:PRK15112 149 MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
250 260
....*....|....*....|..
gi 523689182 237 VEEGLVGDIIRNPRHPYTKGLL 258
Cdd:PRK15112 229 VERGSTADVLASPLHELTKRLI 250
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-249 |
1.99e-35 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 131.36 E-value: 1.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRggkaVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMSLSNRals 88
Cdd:PRK10851 3 IEIANIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT---SGHIRFHGTDVSRLHAR--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 DLRgavVSMVFQEprLALDPVYTVGRQIE---ETIMRHEKVSRGLAAERALALFQKVRIPsperRLSN-YPHEMSGGMLQ 164
Cdd:PRK10851 73 DRK---VGFVFQH--YALFRHMTVFDNIAfglTVLPRRERPNAAAIKAKVTQLLEMVQLA----HLADrYPAQLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 165 RAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGD 244
Cdd:PRK10851 144 RVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQ 223
|
....*
gi 523689182 245 IIRNP 249
Cdd:PRK10851 224 VWREP 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
11-235 |
3.42e-35 |
|
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: 125.05 E-value: 3.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 11 ISNLSVTFrrggKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMSLSNRALSDL 90
Cdd:cd00267 2 IENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT---SGEILIDGKDIAKLPLEELRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 91 rgavVSMVFQeprlaldpvytvgrqieetimrhekvsrglaaeralalfqkvripsperrlsnypheMSGGMLQRAMIAM 170
Cdd:cd00267 75 ----IGYVPQ---------------------------------------------------------LSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523689182 171 ALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGR 235
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
25-240 |
4.10e-35 |
|
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: 126.60 E-value: 4.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 25 VKAVNGVSLSVKPGEVVALLGESGSGKSVTMRsllrlhpkgtLIEGGMTVDGHDImSLSNRALSDL----RGavVSMVFQ 100
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLR----------MIAGLEEPTSGRI-YIGGRDVTDLppkdRD--IAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 101 EprLALDPVYTVGRQIEETiMRHEKVSRGLAAERALALFQKVRIpspERRLSNYPHEMSGGMLQRAMIAMALACNPKVLL 180
Cdd:cd03301 80 N--YALYPHMTVYDNIAFG-LKLRKVPKDEIDERVREVAELLQI---EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 181 ADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-240 |
8.11e-35 |
|
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: 126.08 E-value: 8.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGKavKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTlieGGMTVDGHDIMSLSNRALS 88
Cdd:cd03263 1 LQIRNLTKTYKKGTK--PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTS---GTAYINGYSIRTDRKAARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 dlrgaVVSMVFQEprLALDPVYTVgrqiEETIMRHEKVsRGL----AAERALALFQKVRIPSPERRLSnypHEMSGGMLQ 164
Cdd:cd03263 76 -----SLGYCPQF--DALFDELTV----REHLRFYARL-KGLpkseIKEEVELLLRVLGLTDKANKRA---RTLSGGMKR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523689182 165 RAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-240 |
1.36e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 126.81 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 7 AMIDISNLSVtfRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLL-RLHPkgtlIEGGMTVDGHDIMSLSNR 85
Cdd:PRK13548 1 AMLEARNLSV--RLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgELSP----DSGEVRLNGRPLADWSPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 ALSDLRgAVVSmvfQEPRLALDpvYTVgrqieetimrHEKVSRGLA------------AERALALfqkVRIPSPERRLsn 153
Cdd:PRK13548 73 ELARRR-AVLP---QHSSLSFP--FTV----------EEVVAMGRAphglsraeddalVAAALAQ---VDLAHLAGRD-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 154 YPhEMSGGMLQRAMIAMALA------CNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADR 227
Cdd:PRK13548 132 YP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADR 210
|
250
....*....|...
gi 523689182 228 IAVMYAGRIVEEG 240
Cdd:PRK13548 211 IVLLHQGRLVADG 223
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-247 |
1.61e-34 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 126.35 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFrrGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSvTMRSLL-RLHPKGtliEGGMTVDGHDIMSLSNRA 86
Cdd:COG4604 1 MIEIKNVSKRY--GGKVV--LDDVSLTIPKGGITALIGPNGAGKS-TLLSMIsRLLPPD---SGEVLVDGLDVATTPSRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSdlrgAVVSMVFQEPRLAL-----DPV------YTVGRQIEETimrHEKVsrglaaERALALFQkvripsperrLSNYP 155
Cdd:COG4604 73 LA----KRLAILRQENHINSrltvrELVafgrfpYSKGRLTAED---REII------DEAIAYLD----------LEDLA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 156 H----EMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVM 231
Cdd:COG4604 130 DryldELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAM 209
|
250
....*....|....*.
gi 523689182 232 YAGRIVEEGLVGDIIR 247
Cdd:COG4604 210 KDGRVVAQGTPEEIIT 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-245 |
1.95e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 131.29 E-value: 1.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 5 NDAMIDISNLSVTFrrGGkaVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMSLSN 84
Cdd:COG1129 1 AEPLLEMRGISKSF--GG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPD---SGEILLDGEPVRFRSP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 85 RalsDLRGAVVSMVFQEPRLALDpvytvgRQIEETI-MRHEKVSRGL-----AAERALALFQKVRIP-SPERRLSNYPhe 157
Cdd:COG1129 74 R---DAQAAGIAIIHQELNLVPN------LSVAENIfLGREPRRGGLidwraMRRRARELLARLGLDiDPDTPVGDLS-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 158 msggMLQRAM--IAMALACNPKVLLADEPTTALDATvQIQILL-LIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAG 234
Cdd:COG1129 143 ----VAQQQLveIARALSRDARVLILDEPTASLTER-EVERLFrIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDG 216
|
250
....*....|.
gi 523689182 235 RIVEEGLVGDI 245
Cdd:COG1129 217 RLVGTGPVAEL 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-240 |
5.56e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.51 E-value: 5.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 16 VTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLlrlhpKGTLI--EGGMTVDGhdiMSLSNRALSDLRgA 93
Cdd:PRK13635 11 ISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLL-----NGLLLpeAGTITVGG---MVLSEETVWDVR-R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 94 VVSMVFQEPrlalDPVYtVGRQIEETI---MRHEKVSRGLAAERALALFQKVRIpspERRLSNYPHEMSGGMLQRAMIAM 170
Cdd:PRK13635 82 QVGMVFQNP----DNQF-VGATVQDDVafgLENIGVPREEMVERVDQALRQVGM---EDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 171 ALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEvADRIAVMYAGRIVEEG 240
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-240 |
1.79e-33 |
|
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: 129.95 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNlsVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtLIEGGMTVDGHDIMSLSnraLS 88
Cdd:COG2274 474 IELEN--VSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE---PTSGRILIDGIDLRQID---PA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 DLRGAvVSMVFQEPRL---------AL-DPVYTVGR--------QIEETIMRHEKvsrGLA---AERALALfqkvripsp 147
Cdd:COG2274 546 SLRRQ-IGVVLQDVFLfsgtireniTLgDPDATDEEiieaarlaGLHDFIEALPM---GYDtvvGEGGSNL--------- 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 148 errlsnyphemSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIGVAAEvADR 227
Cdd:COG2274 613 -----------SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADR 678
|
250
....*....|...
gi 523689182 228 IAVMYAGRIVEEG 240
Cdd:COG2274 679 IIVLDKGRIVEDG 691
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
9-248 |
2.04e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 124.39 E-value: 2.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGK-AVKAVNGVSLSVKPGEVVALLGESGSGKSVtmrslLRLHPKGTL--IEGGMTVDGHDIMSlSNR 85
Cdd:PRK13637 3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKST-----LIQHLNGLLkpTSGKIIIDGVDITD-KKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 ALSDLRGAVvSMVFQEPRLALdpvytvgrqIEETImrhEK------VSRGLAAE----RALALFQKVRIpSPERRLSNYP 155
Cdd:PRK13637 77 KLSDIRKKV-GLVFQYPEYQL---------FEETI---EKdiafgpINLGLSEEeienRVKRAMNIVGL-DYEDYKDKSP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 156 HEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGR 235
Cdd:PRK13637 143 FELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
250
....*....|...
gi 523689182 236 IVEEGLVGDIIRN 248
Cdd:PRK13637 223 CELQGTPREVFKE 235
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-231 |
7.33e-33 |
|
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: 120.72 E-value: 7.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 11 ISNLSVTFRRggkaVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgtlIEGGMTVDGHDIMSLSNRalsdl 90
Cdd:cd03235 2 VEDLTVSYGG----HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP---TSGSIRVFGKPLEKERKR----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 91 rgavVSMVFQepRLALDPVYTVgrQIEETIM----RHEKVSRGLAAE---RALALFQKVRIPS-PERRLSnyphEMSGGM 162
Cdd:cd03235 70 ----IGYVPQ--RRSIDRDFPI--SVRDVVLmglyGHKGLFRRLSKAdkaKVDEALERVGLSElADRQIG----ELSGGQ 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523689182 163 LQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVM 231
Cdd:cd03235 138 QQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-240 |
5.94e-32 |
|
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: 118.62 E-value: 5.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLrlhpkgTLIE---GGMTVDGHDimslsn 84
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLA------GLLEpdaGFATVDGFD------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 85 rALSDLRGAVVSMVFQEPRLALDPVYTVGRQIEETIMRHekvsrGLAAERALA----LFQKVRI-PSPERRLSnyphEMS 159
Cdd:cd03266 69 -VVKEPAEARRRLGFVSDSTGLYDRLTARENLEYFAGLY-----GLKGDELTArleeLADRLGMeELLDRRVG----GFS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 160 GGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELqREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEE 239
Cdd:cd03266 139 TGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
.
gi 523689182 240 G 240
Cdd:cd03266 218 G 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-235 |
1.44e-31 |
|
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: 115.94 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 16 VTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLH-PKgtliEGGMTVDGHDIMSLSnraLSDLRGAv 94
Cdd:cd03228 6 VSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPT----SGEILIDGVDLRDLD---LESLRKN- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 95 VSMVFQEPRLaldpvytVGRQIEETImrhekvsrglaaeralalfqkvripsperrlsnypheMSGGMLQRAMIAMALAC 174
Cdd:cd03228 78 IAYVPQDPFL-------FSGTIRENI-------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523689182 175 NPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIGvAAEVADRIAVMYAGR 235
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
6-254 |
1.52e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 118.34 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 6 DAMIDISNLSVTFRRGgkavKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLR---LHPKGTlIEGGMTVDGHDIMSL 82
Cdd:PRK14239 3 EPILQVSDLSVYYNKK----KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndLNPEVT-ITGSIVYNGHNIYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 83 SNRALsDLRGAVvSMVFQEPRLALDPVY---TVGRQIEETimrHEKVSRGLAAERAL---ALFQKVRipspeRRLSNYPH 156
Cdd:PRK14239 78 RTDTV-DLRKEI-GMVFQQPNPFPMSIYenvVYGLRLKGI---KDKQVLDEAVEKSLkgaSIWDEVK-----DRLHDSAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 157 EMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYglSVIFVTHDIGVAAEVADRIAVMYAGRI 236
Cdd:PRK14239 148 GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDL 225
|
250
....*....|....*...
gi 523689182 237 VEEGLVGDIIRNPRHPYT 254
Cdd:PRK14239 226 IEYNDTKQMFMNPKHKET 243
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
235-321 |
1.69e-31 |
|
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: 113.23 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 235 RIVEEGLVGDIIRNPRHPYTKGLLGARVELAEGRDRLVTIPGAPPDLAAMPPGCAFAPRCVQVSDLCQKQIPPLLPLSGG 314
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVEIAEG 80
|
....*..
gi 523689182 315 AGVACLF 321
Cdd:TIGR01727 81 HRVACHL 87
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
27-255 |
2.48e-31 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 121.29 E-value: 2.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 27 AVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgtlIEGGMTVDGHDIMSLSNRALSDLRGAVVSMVFQEprLAL 106
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP---TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 107 DPVYTVgrqIEETIMRHEkVSRGLAAERALALFQKVRIPSPERRLSNYPHEMSGGMLQRAMIAMALACNPKVLLADEPTT 186
Cdd:PRK10070 118 MPHMTV---LDNTAFGME-LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523689182 187 ALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNPRHPYTK 255
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-238 |
4.03e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 117.66 E-value: 4.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 7 AMIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLrlhpkgTLIEGGMTVDGHDIMsLSNRA 86
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT----TLL------NLIAGFLAPSSGEIT-LDGVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSDlRGAVVSMVFQEPrlALDPVYTVGRQIEETiMRHEKVSRGLAAERALALFQKVRIPSPERRlsnYPHEMSGGMLQRA 166
Cdd:COG4525 71 VTG-PGADRGVVFQKD--ALLPWLNVLDNVAFG-LRLRGVPKAERRARAEELLALVGLADFARR---RIWQLSGGMRQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523689182 167 MIAMALACNPKVLLADEPTTALDATV--QIQILLLirELQREYGLSVIFVTHDIGVAAEVADRIAVM--YAGRIVE 238
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALTreQMQELLL--DVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
26-252 |
5.88e-31 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 116.99 E-value: 5.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 26 KAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDI---------MSLSNRALSDLRGAVVS 96
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPS---EGSIVVNGQTInlvrdkdgqLKVADKNQLRLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 97 MVFQEprLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIPspERRLSNYPHEMSGGMLQRAMIAMALACNP 176
Cdd:PRK10619 96 MVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGID--ERAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523689182 177 KVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNPRHP 252
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
26-269 |
1.36e-30 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 117.11 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 26 KAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLlrlhpkGTLI---EGGMTVDGHDIMslsnRALSDLRgAVVSMVFQEP 102
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRML------TTLLrptSGTARVAGYDVV----REPRKVR-RSIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 103 rlALDPVYTvGRQIEETIMRHEKVSRGLAAERALALFQKVRIPSPERRLSNYpheMSGGMLQRAMIAMALACNPKVLLAD 182
Cdd:TIGR01188 76 --SVDEDLT-GRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGT---YSGGMRRRLDIAASLIHQPDVLFLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 183 EPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIirnprhpytKGLLGARV 262
Cdd:TIGR01188 150 EPTTGLDPRTRRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL---------KRRLGKDT 219
|
....*..
gi 523689182 263 ELAEGRD 269
Cdd:TIGR01188 220 LESRPRD 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-250 |
1.43e-30 |
|
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: 115.46 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 6 DAMIDISNLSVtfRRGGkaVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtLIEGGMTVDGHDIMSLSNR 85
Cdd:COG0410 1 MPMLEVENLHA--GYGG--IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP---PRSGSIRFDGEDITGLPPH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 ALSDlRGavVSMVFQeprlaldpvytvGRQI------EETIM-----RHEKVSRGLAAERALALFqkvriPSPERRLSNY 154
Cdd:COG0410 74 RIAR-LG--IGYVPE------------GRRIfpsltvEENLLlgayaRRDRAEVRADLERVYELF-----PRLKERRRQR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 155 PHEMSGGmlQRAM--IAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMY 232
Cdd:COG0410 134 AGTLSGG--EQQMlaIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLE 210
|
250
....*....|....*...
gi 523689182 233 AGRIVEEGLVGDIIRNPR 250
Cdd:COG0410 211 RGRIVLEGTAAELLADPE 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-259 |
1.66e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 118.51 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 2 TMQNDAMIDISNLSVTFrrGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHpkgTLIEGGMTVDGHDIMS 81
Cdd:PRK09452 8 PSSLSPLVELRGISKSF--DGKEV--ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFE---TPDSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 82 LS--NRAlsdlrgavVSMVFQEprLALDPVYTVgrqiEETI---MRHEKVSRGLAAERALALFQKVRIPS-PERRlsnyP 155
Cdd:PRK09452 81 VPaeNRH--------VNTVFQS--YALFPHMTV----FENVafgLRMQKTPAAEITPRVMEALRMVQLEEfAQRK----P 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 156 HEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGR 235
Cdd:PRK09452 143 HQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
250 260
....*....|....*....|....
gi 523689182 236 IVEEGLVGDIIRNPRHPYTKGLLG 259
Cdd:PRK09452 223 IEQDGTPREIYEEPKNLFVARFIG 246
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
9-240 |
1.74e-30 |
|
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: 114.84 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVtfrrGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtLIEGGMTVDGHDIMSLSNRALS 88
Cdd:cd03224 1 LEVENLNA----GYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP---PRSGSIRFDGRDITGLPPHERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 DlRGavVSMVFQEPRLAldPVYTVgrqiEETIM------RHEKVSRGLaaERALALFqkvriPSPERRLSNYPHEMSGGm 162
Cdd:cd03224 74 R-AG--IGYVPEGRRIF--PELTV----EENLLlgayarRRAKRKARL--ERVYELF-----PRLKERRKQLAGTLSGG- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 163 lQRAM--IAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:cd03224 137 -EQQMlaIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEG 214
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
43-259 |
2.08e-30 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 117.21 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 43 LLGESGSGKSVTMRSLLRLHpkgTLIEGGMTVDGHDImslSNRAlSDLRGavVSMVFQEprLALDPVYTVgrqiEETI-- 120
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFE---QPDSGSIMLDGEDV---TNVP-PHLRH--INMVFQS--YALFPHMTV----EENVaf 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 121 -MRHEKVSRGLAAERALALFQKVRIpspERRLSNYPHEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLL 199
Cdd:TIGR01187 66 gLKMRKVPRAEIKPRVLEALRLVQL---EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLE 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 200 IRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNPRHPYTKGLLG 259
Cdd:TIGR01187 143 LKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIG 202
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
5-240 |
2.49e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 115.96 E-value: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 5 NDAMIDISNLSVTFRRGGKAVK--AVNGVSLSVKPGEVVALLGESGSGKSvTMRSllrlHPKGTLI--EGGMTVDGHDIM 80
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKS-TIAK----HMNALLIpsEGKVYVDGLDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 81 SLSNraLSDLRGAVvSMVFQEPrlaldpvytvGRQIEETIMRhEKVSRGLaaeralalfQKVRIPSPERR---------- 150
Cdd:PRK13633 76 DEEN--LWDIRNKA-GMVFQNP----------DNQIVATIVE-EDVAFGP---------ENLGIPPEEIRervdeslkkv 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 151 -LSNY----PHEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEvA 225
Cdd:PRK13633 133 gMYEYrrhaPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-A 211
|
250
....*....|....*
gi 523689182 226 DRIAVMYAGRIVEEG 240
Cdd:PRK13633 212 DRIIVMDSGKVVMEG 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-260 |
2.68e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.47 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLsvTFRRGGKAVKAvngvSLSVKPGEVVALLGESGSGKSvTMRSLLR--LHPKGtlieGGMTVDGHDIMSLSnr 85
Cdd:COG3840 1 MLRLDDL--TYRYGDFPLRF----DLTIAAGERVAILGPSGAGKS-TLLNLIAgfLPPDS----GRILWNGQDLTALP-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 alSDLRGavVSMVFQE------------------PRLALDPvytvgrqiEEtimrHEKVsrglaaERALAlfqKVRIPSP 147
Cdd:COG3840 68 --PAERP--VSMLFQEnnlfphltvaqniglglrPGLKLTA--------EQ----RAQV------EQALE---RVGLAGL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 148 ERRLsnyPHEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADR 227
Cdd:COG3840 123 LDRL---PGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADR 199
|
250 260 270
....*....|....*....|....*....|...
gi 523689182 228 IAVMYAGRIVEEGLVGDIIRNPRHPYTKGLLGA 260
Cdd:COG3840 200 VLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-237 |
3.04e-30 |
|
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: 112.52 E-value: 3.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFrrGGkaVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDImslSNRALS 88
Cdd:cd03216 1 LELRGITKRF--GG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPD---SGEILVDGKEV---SFASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 DLRGAVVSMVFQeprlaldpvytvgrqieetimrhekvsrglaaeralalfqkvripsperrlsnypheMSGGMLQRAMI 168
Cdd:cd03216 71 DARRAGIAMVYQ---------------------------------------------------------LSVGERQMVEI 93
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 169 AMALACNPKVLLADEPTTALDATvQIQILL-LIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIV 237
Cdd:cd03216 94 ARALARNARLLILDEPTAALTPA-EVERLFkVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-259 |
3.64e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 115.58 E-value: 3.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 13 NLSVTFrrGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPK-------GTLIEGGMTV-DGHDIMSLSN 84
Cdd:PRK14271 26 NLTLGF--AGKTV--LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrysGDVLLGGRSIfNYRDVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 85 RalsdlrgavVSMVFQEPR---LALDPVYTVGRQIEETIMRHEkvSRGLAAER--ALALFQKVRipspeRRLSNYPHEMS 159
Cdd:PRK14271 102 R---------VGMLFQRPNpfpMSIMDNVLAGVRAHKLVPRKE--FRGVAQARltEVGLWDAVK-----DRLSDSPFRLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 160 GGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREygLSVIFVTHDIGVAAEVADRIAVMYAGRIVEE 239
Cdd:PRK14271 166 GGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
250 260
....*....|....*....|....
gi 523689182 240 GLVGDIIRNPRHP----YTKGLLG 259
Cdd:PRK14271 244 GPTEQLFSSPKHAetarYVAGLSG 267
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
8-246 |
4.95e-30 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 114.73 E-value: 4.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFrrGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHpkgTLIEGGMTVDGHDIMSLSNRAL 87
Cdd:PRK11231 2 TLRTENLTVGY--GTKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLL---TPQSGTVFLGDKPISMLSSRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 SDlrgavvsmvfqepRLALDPVYTVgrqIEETIMRHEKVSRG----------LAAE------RALALFQKVRIPspERRL 151
Cdd:PRK11231 75 AR-------------RLALLPQHHL---TPEGITVRELVAYGrspwlslwgrLSAEdnarvnQAMEQTRINHLA--DRRL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 152 SnyphEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVM 231
Cdd:PRK11231 137 T----DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVL 211
|
250
....*....|....*
gi 523689182 232 YAGRIVEEGLVGDII 246
Cdd:PRK11231 212 ANGHVMAQGTPEEVM 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-249 |
9.53e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 115.97 E-value: 9.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 3 MQNDAMIDISNLSVTFrrgGKAVkAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHpKGTliEGGMTVDGHDIM-- 80
Cdd:PRK11432 1 MTQKNFVVLKNITKRF---GSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLE-KPT--EGQIFIDGEDVThr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 81 SLSNRAlsdlrgavVSMVFQEprLALDPVYTVGRQIEETiMRHEKVSRGLAAER---ALALfqkVRIPSPERRlsnYPHE 157
Cdd:PRK11432 74 SIQQRD--------ICMVFQS--YALFPHMSLGENVGYG-LKMLGVPKEERKQRvkeALEL---VDLAGFEDR---YVDQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 158 MSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIV 237
Cdd:PRK11432 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
250
....*....|..
gi 523689182 238 EEGLVGDIIRNP 249
Cdd:PRK11432 217 QIGSPQELYRQP 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
37-240 |
1.45e-29 |
|
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: 112.00 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 37 PGEVVALLGESGSGKSvtmrSLLRLhpkgtlIEGGMTVDGHDImSLSNRALSDLRGAV--------VSMVFQEprLALDP 108
Cdd:cd03297 22 NEEVTGIFGASGAGKS----TLLRC------IAGLEKPDGGTI-VLNGTVLFDSRKKInlppqqrkIGLVFQQ--YALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 109 VYTVGRQIEETIMRHEKVSRGLAAERALALFQkvrIPSPERRlsnYPHEMSGGMLQRAMIAMALACNPKVLLADEPTTAL 188
Cdd:cd03297 89 HLNVRENLAFGLKRKRNREDRISVDELLDLLG---LDHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 523689182 189 DATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:cd03297 163 DRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-259 |
2.49e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 112.63 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGgkavKAVNGVSLSVKPGEVVALLGESGSGKSVTMRS---LLRLHPKGTlIEGGMTVDGHDIMSLSNR 85
Cdd:PRK14267 5 IETVNLRVYYGSN----HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEAR-VEGEVRLFGRNIYSPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 ALSDLRGavVSMVFQEP----RLALDPVYTVGRQIEETIMRHEKVSRGLA-AERALALFQKVRipspeRRLSNYPHEMSG 160
Cdd:PRK14267 80 PIEVRRE--VGMVFQYPnpfpHLTIYDNVAIGVKLNGLVKSKKELDERVEwALKKAALWDEVK-----DRLNDYPSNLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 161 GMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYglSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
250 260
....*....|....*....|...
gi 523689182 241 LVGDIIRNPRHP----YTKGLLG 259
Cdd:PRK14267 231 PTRKVFENPEHEltekYVTGALG 253
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
8-249 |
2.83e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 113.25 E-value: 2.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFRRGGKAVKavnGVSLSVKPGEVVALLGESGSGKSVTMrsllrLHPKGTL--IEGGMTVDGHDImSLSNR 85
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALK---GINFKAEKGEMVALLGPNGAGKSTLF-----LHFNGILkpTSGEVLIKGEPI-KYDKK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 ALSDLRgAVVSMVFQEPRlalDPVY--TVGRQIEETIMrHEKVSRGLAAERALALFQKVRIPSPERRLsnyPHEMSGGML 163
Cdd:PRK13639 72 SLLEVR-KTVGIVFQNPD---DQLFapTVEEDVAFGPL-NLGLSKEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 164 QRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVG 243
Cdd:PRK13639 144 KRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
|
....*.
gi 523689182 244 DIIRNP 249
Cdd:PRK13639 223 EVFSDI 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
7-237 |
5.98e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 116.75 E-value: 5.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 7 AMIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHpKGTliEGGMTVDGHDIMSLSNRA 86
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLD-KPT--SGTYRVAGQDVATLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSDLRGAVVSMVFQepRLALDPVYTVGRQIEETIMrHEKVSRGLAAERALALFQKVRIpspERRLSNYPHEMSGGMLQRA 166
Cdd:PRK10535 80 LAQLRREHFGFIFQ--RYHLLSHLTAAQNVEVPAV-YAGLERKQRLLRAQELLQRLGL---EDRVEYQPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523689182 167 MIAMALACNPKVLLADEPTTALDATVQIQILLLIRELqREYGLSVIFVTHDIGVAAEvADRIAVMYAGRIV 237
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-266 |
1.13e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 111.74 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFrrggKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLR-LHPKgtliEGGMTVDGHDImSLSNRA 86
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGiLAPD----SGEVLWDGEPL-DPEDRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 ----LSDLRGavvsmvfqeprlaLDPVYTVGRQIEETIMRHeKVSRGLAAERALALFQKVRIPS-PERRLsnypHEMSGG 161
Cdd:COG4152 72 rigyLPEERG-------------LYPKMKVGEQLVYLARLK-GLSKAEAKRRADEWLERLGLGDrANKKV----EELSKG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 162 MLQRAMIAMALACNPKVLLADEPTTALDAtVQIQILL-LIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDP-VNVELLKdVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
250 260
....*....|....*....|....*.
gi 523689182 241 LVGDiIRNpRHPYTKGLLGARVELAE 266
Cdd:COG4152 212 SVDE-IRR-QFGRNTLRLEADGDAGW 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-249 |
1.39e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 111.65 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 26 KAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRlHPKGTL--IEGGMTVDGHDIMS-LSNRALSDLRGAVvSMVFQEP 102
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKS----TLLQ-HLNGLLqpTSGTVTIGERVITAgKKNKKLKPLRKKV-GIVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 103 RLALdpvytvgrqIEETImrhEK----------VSRGLAAERALALFQKVRIPspERRLSNYPHEMSGGMLQRAMIAMAL 172
Cdd:PRK13634 95 EHQL---------FEETV---EKdicfgpmnfgVSEEDAKQKAREMIELVGLP--EELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523689182 173 ACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNP 249
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
8-259 |
1.48e-28 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 112.86 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSvtfrRGGKAVKaVNGVSLSVKPGEVVALLGESGSGKSVtmrsLLRLhpkgtlIEGGMTVDGHDIMsLSNRAL 87
Cdd:NF040840 1 MIRIENLS----KDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTV----LLEL------IAGIWPPDSGKIY-LDGKDI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 SDL----RGavVSMVFQEprLALDPVYTVGRQIEETiMRHEKVSRGLAAERALALFQKVRIpspERRLSNYPHEMSGGML 163
Cdd:NF040840 65 TNLppekRG--IAYVYQN--YMLFPHKTVFENIAFG-LKLRKVPKEEIERKVKEIMELLGI---SHLLHRKPRTLSGGEQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 164 QRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVG 243
Cdd:NF040840 137 QRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVR 216
|
250
....*....|....*.
gi 523689182 244 DIIRNPRHPYTKGLLG 259
Cdd:NF040840 217 EVFRRPKNEFVARFVG 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-248 |
2.81e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.47 E-value: 2.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 5 NDAMIDISNlsVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSvTMRSLLR--LHPKgtliEGGMTVDGHDImsl 82
Cdd:PRK13632 4 KSVMIKVEN--VSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKS-TISKILTglLKPQ----SGEIKIDGITI--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 83 SNRALSDLRGAVvSMVFQEPrlalDPVYtVGRQIEETI---MRHEKVSRGLAAERALALFQKVRIpspERRLSNYPHEMS 159
Cdd:PRK13632 74 SKENLKEIRKKI-GIIFQNP----DNQF-IGATVEDDIafgLENKKVPPKKMKDIIDDLAKKVGM---EDYLDKEPQNLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 160 GGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAeVADRIAVMYAGRIVEE 239
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQ 223
|
....*....
gi 523689182 240 GLVGDIIRN 248
Cdd:PRK13632 224 GKPKEILNN 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
7-249 |
3.53e-28 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 111.73 E-value: 3.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 7 AMIDISnlsVTFRRGGKAVKavngVSLSVKPGEVVALLGESGSGKSvtmrSLLRlhpkgtLIEGGMTVDGHDImSLSNRA 86
Cdd:COG4148 1 MMLEVD---FRLRRGGFTLD----VDFTLPGRGVTALFGPSGSGKT----TLLR------AIAGLERPDSGRI-RLGGEV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSDLRGAV--------VSMVFQEPRlaLDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQkvrIpspERRLSNYPHEM 158
Cdd:COG4148 63 LQDSARGIflpphrrrIGYVFQEAR--LFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLG---I---GHLLDRRPATL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 159 SGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVE 238
Cdd:COG4148 135 SGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVA 214
|
250
....*....|.
gi 523689182 239 EGLVGDIIRNP 249
Cdd:COG4148 215 SGPLAEVLSRP 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
8-283 |
1.12e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 111.09 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFrrGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLlrlhpKGTL--IEGGMTVDGHDIMSLSNR 85
Cdd:PRK09536 3 MIDVSDLSVEF--GDTTV--LDGVDLSVREGSLVGLVGPNGAGKTTLLRAI-----NGTLtpTAGTVLVAGDDVEALSAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 ALSDLrgavVSMVFQEPRLALDpvYTVgRQIEEtIMRHEKVSR--------GLAAERALALFQKVRIPspERRLSnyphE 157
Cdd:PRK09536 74 AASRR----VASVPQDTSLSFE--FDV-RQVVE-MGRTPHRSRfdtwtetdRAAVERAMERTGVAQFA--DRPVT----S 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 158 MSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIV 237
Cdd:PRK09536 140 LSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVR 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 523689182 238 EEGLVGDIIRNPRhpyTKGLLGARV----ELAEGRDRLVTIPGAPPDLAA 283
Cdd:PRK09536 219 AAGPPADVLTADT---LRAAFDARTavgtDPATGAPTVTPLPDPDRTEAA 265
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-240 |
1.56e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 112.57 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 16 VTFRRGGKAvKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtLIEGGMTVDGHDIMSLSnraLSDLRGAvV 95
Cdd:COG1132 345 VSFSYPGDR-PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD---PTSGRILIDGVDIRDLT---LESLRRQ-I 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 96 SMVFQEPRLALDPVY---TVGR---------------QIEETIMRHEKvsrGLAA---ERALALfqkvripsperrlsny 154
Cdd:COG1132 417 GVVPQDTFLFSGTIReniRYGRpdatdeeveeaakaaQAHEFIEALPD---GYDTvvgERGVNL---------------- 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 155 phemSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIGVAAEvADRIAVMYAG 234
Cdd:COG1132 478 ----SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDG 550
|
....*.
gi 523689182 235 RIVEEG 240
Cdd:COG1132 551 RIVEQG 556
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
9-260 |
3.84e-27 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 109.31 E-value: 3.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVtfRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLR-LHPKGtlIEGGMTVDGHDIMSLSNRAl 87
Cdd:TIGR03258 6 IRIDHLRV--AYGANTV--LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGfVKAAG--LTGRIAIADRDLTHAPPHK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 sdlRGavVSMVFQEprLALDPVYTVgrqiEETI---MRHEKVSRGLAAERALALFQKVRIPSPERRlsnYPHEMSGGMLQ 164
Cdd:TIGR03258 79 ---RG--LALLFQN--YALFPHLKV----EDNVafgLRAQKMPKADIAERVADALKLVGLGDAAAH---LPAQLSGGMQQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 165 RAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREY-GLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVG 243
Cdd:TIGR03258 145 RIAIARAIAIEPDVLLLDEPLSALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQ 224
|
250
....*....|....*..
gi 523689182 244 DIIRNPRHPYTKGLLGA 260
Cdd:TIGR03258 225 ALYDAPADGFAAEFLGA 241
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-239 |
3.87e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.89 E-value: 3.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 6 DAMIDISNLSVTFRRGGKAVKavnGVSLSVKPGEVVALLGESGSGKSVTMRSL--LRLHPKGTlieggMTVDGHDIMSLS 83
Cdd:COG3845 255 EVVLEVENLSVRDDRGVPALK---DVSLEVRAGEILGIAGVAGNGQSELAEALagLRPPASGS-----IRLDGEDITGLS 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 84 NRALSDLRGAVVSmvfqEPRL--ALDPVYTV------GRQIEETIMRHEKVSRGLAAERALALFQK--VRIPSPERRLSN 153
Cdd:COG3845 327 PRERRRLGVAYIP----EDRLgrGLVPDMSVaenlilGRYRRPPFSRGGFLDRKAIRAFAEELIEEfdVRTPGPDTPARS 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 154 ypheMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELqREYGLSVIFVTHDIGVAAEVADRIAVMYA 233
Cdd:COG3845 403 ----LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYE 477
|
....*.
gi 523689182 234 GRIVEE 239
Cdd:COG3845 478 GRIVGE 483
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-240 |
5.33e-27 |
|
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: 111.00 E-value: 5.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 5 NDAMIDISNLSVtfrRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtLIEGGMTVDGHDIMSLSN 84
Cdd:COG4988 333 GPPSIELEDVSF---SYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP---PYSGSILINGVDLSDLDP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 85 RALSDLrgavVSMVFQEPRL---------AL-DPVYTvgrqiEETIMRhekvsrglAAERA-LALFqkvrIPSPERRLSN 153
Cdd:COG4988 407 ASWRRQ----IAWVPQNPYLfagtirenlRLgRPDAS-----DEELEA--------ALEAAgLDEF----VAALPDGLDT 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 154 YPHE----MSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIGVAAEvADRIA 229
Cdd:COG4988 466 PLGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRIL 542
|
250
....*....|.
gi 523689182 230 VMYAGRIVEEG 240
Cdd:COG4988 543 VLDDGRIVEQG 553
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-249 |
5.86e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.19 E-value: 5.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 5 NDAMIDISNLSVTFRRGGKAvkAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTLIEGGMTVDGhdiMSLSN 84
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDSKKP--ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDG---ITLTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 85 RALSDLRGAVvSMVFQEPrlalDPVY---TVG---------RQIEETIMRheKVSRGLAAERALALFQKVRipsperrls 152
Cdd:PRK13640 77 KTVWDIREKV-GIVFQNP----DNQFvgaTVGddvafglenRAVPRPEMI--KIVRDVLADVGMLDYIDSE--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 153 nyPHEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGvAAEVADRIAVMY 232
Cdd:PRK13640 141 --PANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLD 217
|
250
....*....|....*..
gi 523689182 233 AGRIVEEGLVGDIIRNP 249
Cdd:PRK13640 218 DGKLLAQGSPVEIFSKV 234
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-235 |
6.36e-27 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 110.40 E-value: 6.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 24 AVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTLiEGGMTVDGHDimsLSNRALSDLRGAVVSMVFQEpr 103
Cdd:PRK13549 17 GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTY-EGEIIFEGEE---LQASNIRDTERAGIAIIHQE-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 104 LALDPVYTVGRQIeetIMRHEKVSRGLAA-----ERALALFQKVRIP-SPERRLSNYphemSGGMLQRAMIAMALACNPK 177
Cdd:PRK13549 91 LALVKELSVLENI---FLGNEITPGGIMDydamyLRAQKLLAQLKLDiNPATPVGNL----GLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 523689182 178 VLLADEPTTALDATvQIQILL-LIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGR 235
Cdd:PRK13549 164 LLILDEPTASLTES-ETAVLLdIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
8-267 |
8.31e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.38 E-value: 8.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFrrggKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgtlIEGGMTVDGHDIMSLSNRAL 87
Cdd:PRK11607 19 LLEIRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP---TAGQIMLDGVDLSHVPPYQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 SdlrgavVSMVFQEprLALDPVYTVGRQIEETiMRHEKVSRGLAAERALALFQKVRIPSPERRlsnYPHEMSGGMLQRAM 167
Cdd:PRK11607 92 P------INMMFQS--YALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKR---KPHQLSGGQRQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 168 IAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIR 247
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
250 260
....*....|....*....|
gi 523689182 248 NPRHPYTKGLLGArVELAEG 267
Cdd:PRK11607 240 HPTTRYSAEFIGS-VNVFEG 258
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-237 |
1.02e-26 |
|
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: 104.26 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 10 DISNLSVTFRRGGKAVKavnGVSLSVKPGEVVALLGESGSGKSVTMR---SLLRLHpKGTLIEGGmtvdghdimslSNRA 86
Cdd:cd03226 1 RIENISFSYKKGTEILD---DLSLDLYAGEIIALTGKNGAGKTTLAKilaGLIKES-SGSILLNG-----------KPIK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSDLRGAVvSMVFQEPRLAL--DPVYtvgrqiEETIMRHEKVSRGlaAERALALFQKVRIPSPERRlsnYPHEMSGGMLQ 164
Cdd:cd03226 66 AKERRKSI-GYVMQDVDYQLftDSVR------EELLLGLKELDAG--NEQAETVLKDLDLYALKER---HPLSLSGGQKQ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523689182 165 RAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIV 237
Cdd:cd03226 134 RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
9-240 |
2.02e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 105.63 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGK-AVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTlieGGMTVDGHDIMSLS-NRA 86
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTT---GTVTVDDITITHKTkDKY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSDLRGAVvSMVFQEPRLAL--DpvyTVGRQIE----ETIMRHEKVSrglaaERALALFqkVRIPSPERRLSNYPHEMSG 160
Cdd:PRK13646 80 IRPVRKRI-GMVFQFPESQLfeD---TVEREIIfgpkNFKMNLDEVK-----NYAHRLL--MDLGFSRDVMSQSPFQMSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 161 GMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-249 |
2.16e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 105.68 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 26 KAVNGVSLSVKPGEVVALLGESGSGKSVTMRsllrlHPKGTLI--EGGMTVDGHDIMS-LSNRALSDLRGAVvSMVFQEP 102
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQ-----HFNALLKpsSGTITIAGYHITPeTGNKNLKKLRKKV-SLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 103 RLALdpvytvgrqIEETIMRHEK-------VSRGLAAERALALFQKVRIPspERRLSNYPHEMSGGMLQRAMIAMALACN 175
Cdd:PRK13641 95 EAQL---------FENTVLKDVEfgpknfgFSEDEAKEKALKWLKKVGLS--EDLISKSPFELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523689182 176 PKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNP 249
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-313 |
2.17e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.58 E-value: 2.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 5 NDAMIDISNLSVTFrrGGkaVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGH--DIMSl 82
Cdd:COG3845 2 MPPALELRGITKRF--GG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPD---SGEILIDGKpvRIRS- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 83 SNRALSdlRGavVSMVFQEPRLAldPVYTVgrqIEETIMRHEKVSRGL-----AAERALALFQKVRIP-SPERRLsnypH 156
Cdd:COG3845 74 PRDAIA--LG--IGMVHQHFMLV--PNLTV---AENIVLGLEPTKGGRldrkaARARIRELSERYGLDvDPDAKV----E 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 157 EMSGGMLQRAMIAMALACNPKVLLADEPTTALdaTVQ-IQILL-LIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAG 234
Cdd:COG3845 141 DLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeADELFeILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 235 RIVEEGLVGDIIRNprhpytkgllgarvELAE---GRDRLVTIPGAPPdlaamPPGcafaPRCVQVSDLCQKQIPPLLPL 311
Cdd:COG3845 218 KVVGTVDTAETSEE--------------ELAElmvGREVLLRVEKAPA-----EPG----EVVLEVENLSVRDDRGVPAL 274
|
..
gi 523689182 312 SG 313
Cdd:COG3845 275 KD 276
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-237 |
2.46e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 104.78 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFRRG-GKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLlrlhpKGTLI--EGGMTVDGHDI--MSL 82
Cdd:COG1101 1 MLELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAI-----AGSLPpdSGSILIDGKDVtkLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 83 SNRAlsdlrgAVVSMVFQEPRLAldpvyTVGR-QIEETI----MRHEK--VSRGLAAERaLALFQKvRIPSPERRLSNYP 155
Cdd:COG1101 76 YKRA------KYIGRVFQDPMMG-----TAPSmTIEENLalayRRGKRrgLRRGLTKKR-RELFRE-LLATLGLGLENRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 156 HE----MSGGmlQRAMIA--MALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIA 229
Cdd:COG1101 143 DTkvglLSGG--QRQALSllMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLI 220
|
....*...
gi 523689182 230 VMYAGRIV 237
Cdd:COG1101 221 MMHEGRII 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-240 |
7.90e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 104.02 E-value: 7.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 6 DAMIDISNLSVTFRRGGKaVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgtlIEGGMTVDGHdimSLSNR 85
Cdd:PRK13642 2 NKILEVENLVFKYEKESD-VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE---FEGKVKIDGE---LLTAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 ALSDLRGAvVSMVFQEPRLALdpvytVGRQIEETI---MRHEKVSRGLAAERALALFQKVRIPSPERRlsnYPHEMSGGM 162
Cdd:PRK13642 75 NVWNLRRK-IGMVFQNPDNQF-----VGATVEDDVafgMENQGIPREEMIKRVDEALLAVNMLDFKTR---EPARLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523689182 163 LQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEvADRIAVMYAGRIVEEG 240
Cdd:PRK13642 146 KQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEA 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
16-240 |
1.79e-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: 106.39 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 16 VTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtLIEGGMTVDGHDIMSLSNRALSdlrgAVV 95
Cdd:COG4987 339 VSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD---PQSGSITLGGVDLRDLDEDDLR----RRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 96 SMVFQEPRLaldpvytvgrqIEETIMRHEKVSRGLAAERAL--ALfQKVRIpspERRLSNYPH-----------EMSGGM 162
Cdd:COG4987 412 AVVPQRPHL-----------FDTTLRENLRLARPDATDEELwaAL-ERVGL---GDWLAALPDgldtwlgeggrRLSGGE 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523689182 163 LQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIgVAAEVADRIAVMYAGRIVEEG 240
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRL-AGLERMDRILVLEDGRIVEQG 551
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
25-240 |
2.11e-25 |
|
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: 101.85 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 25 VKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHpkgTLIEGGMTVDGHDIMSLSNRALSDLrgavVSMVFQEPRL 104
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFY---DPTSGEILLDGVDIRDLNLRWLRSQ----IGLVSQEPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 105 -----ALDPVYTVGRQIEETIMRhekvsrglAAERALALFQKVRIPSP-ERRLSNYPHEMSGGMLQRAMIAMALACNPKV 178
Cdd:cd03249 89 fdgtiAENIRYGKPDATDEEVEE--------AAKKANIHDFIMSLPDGyDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523689182 179 LLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIGvAAEVADRIAVMYAGRIVEEG 240
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQG 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-240 |
2.54e-25 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 100.75 E-value: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFrrGGKavKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMSLSNrALS 88
Cdd:cd03268 1 LKTNDLTKTY--GKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD---SGEITFDGKSYQKNIE-ALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 DLrGAVVSM-VFQEPRLALDPVYTVGRQIeetIMRHEKVSR-----GLAAeralalfqkvripSPERRLSNYphemSGGM 162
Cdd:cd03268 73 RI-GALIEApGFYPNLTARENLRLLARLL---GIRKKRIDEvldvvGLKD-------------SAKKKVKGF----SLGM 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523689182 163 LQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELqREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:cd03268 132 KQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-239 |
2.92e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 101.01 E-value: 2.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 3 MQNDAMIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMSL 82
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS---SGEVSLVGQPLHQM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 83 SNRALSDLRGAVVSMVFQEprLALDPVYTVGRQIE-ETIMRHEkvSRGLAAERALALFQKVRIpspERRLSNYPHEMSGG 161
Cdd:PRK10584 78 DEEARAKLRAKHVGFVFQS--FMLIPTLNALENVElPALLRGE--SSRQSRNGAKALLEQLGL---GKRLDHLPAQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523689182 162 MLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEvADRIAVMYAGRIVEE 239
Cdd:PRK10584 151 EQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
26-240 |
3.91e-25 |
|
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: 100.77 E-value: 3.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 26 KAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHpkgTLIEGGMTVDGHDIMSLSnraLSDLRGAvVSMVFQEPRLA 105
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFY---DVSSGSILIDGQDIREVT---LDSLRRA-IGVVPQDTVLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 106 LDPV-YTV--GR---------------QIEETIMRHEKVSRGLAAERALALfqkvripsperrlsnyphemSGGMLQRAM 167
Cdd:cd03253 88 NDTIgYNIryGRpdatdeevieaakaaQIHDKIMRFPDGYDTIVGERGLKL--------------------SGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523689182 168 IAMALACNPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIGVAAEvADRIAVMYAGRIVEEG 240
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
25-236 |
5.56e-25 |
|
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: 100.17 E-value: 5.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 25 VKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLH-PKGTLIEggmtVDGHDIMSLSNRALSDLRGAVvSMVFQEPR 103
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEElPTSGTIR----VNGQDVSDLRGRAIPYLRRKI-GVVFQDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 104 LALDpvytvgRQIEETI---MRHEKVSRGLAAERALALFQKVRIPSPERrlsNYPHEMSGGMLQRAMIAMALACNPKVLL 180
Cdd:cd03292 89 LLPD------RNVYENVafaLEVTGVPPREIRKRVPAALELVGLSHKHR---ALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 523689182 181 ADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRI 236
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-249 |
8.93e-25 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 100.63 E-value: 8.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 15 SVTFRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMSLSNRALSDLRGAV 94
Cdd:PRK10575 16 NVSFRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS---EGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 95 VSMVFQEPRLALDPVYTVGRqieetIMRHEKVSRGLAAER-----ALALfqkVRIPSPERRLSNyphEMSGGMLQRAMIA 169
Cdd:PRK10575 91 PQQLPAAEGMTVRELVAIGR-----YPWHGALGRFGAADRekveeAISL---VGLKPLAHRLVD---SLSGGERQRAWIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 170 MALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNP 249
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-262 |
9.16e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 100.50 E-value: 9.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFrrggKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtlIEGGMTVDGHdiMSLSNRALS 88
Cdd:PRK14258 8 IKVNNLSFYY----DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE----LESEVRVEGR--VEFFNQNIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 DLRGAV------VSMVFQEPRLALDPVYTVGRQIEETIMRHEKVSRGLAAERALA---LFQKVRipspeRRLSNYPHEMS 159
Cdd:PRK14258 78 ERRVNLnrlrrqVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKdadLWDEIK-----HKIHKSALDLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 160 GGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYA-----G 234
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriG 232
|
250 260
....*....|....*....|....*...
gi 523689182 235 RIVEEGLVGDIIRNPRHPYTKGLLGARV 262
Cdd:PRK14258 233 QLVEFGLTKKIFNSPHDSRTREYVLSRL 260
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-239 |
9.87e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 99.89 E-value: 9.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 5 NDAMIDISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTmrsllrLHPKGTL---IEGGMTVDGHDIMS 81
Cdd:PRK11629 2 NKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTL------LHLLGGLdtpTSGDVIFNGQPMSK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 82 LSNRALSDLRGAVVSMVFQEPRLAldPVYTVgrqIEETIMRH--EKVSRGLAAERALALFQKVRIpspERRLSNYPHEMS 159
Cdd:PRK11629 76 LSSAAKAELRNQKLGFIYQFHHLL--PDFTA---LENVAMPLliGKKKPAEINSRALEMLAAVGL---EHRANHRPSELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 160 GGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVaDRIAVMYAGRIVEE 239
Cdd:PRK11629 148 GGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-240 |
9.88e-25 |
|
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: 99.28 E-value: 9.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRggkaVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMSLSNRALS 88
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD---SGEVLFDGKPLDIAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 DL---RGavvsmvfqeprlaLDPVYTVGRQieetiMRHEKVSRGL----AAERALALFQKVRI-PSPERRLSnyphEMSG 160
Cdd:cd03269 74 YLpeeRG-------------LYPKMKVIDQ-----LVYLAQLKGLkkeeARRRIDEWLERLELsEYANKRVE----ELSK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 161 GMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:cd03269 132 GNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
9-245 |
1.18e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.59 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGK-AVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHpkgTLIEGGMTVDGHDIMSLS-NRA 86
Cdd:PRK13649 3 INLQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH---VPTQGSVRVDDTLITSTSkNKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSDLRGAVvSMVFQEPRLALdpvytvgrqIEETIMR-------HEKVSRGLAAERALALFQKVRIPspERRLSNYPHEMS 159
Cdd:PRK13649 80 IKQIRKKV-GLVFQFPESQL---------FEETVLKdvafgpqNFGVSQEEAEALAREKLALVGIS--ESLFEKNPFELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 160 GGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEE 239
Cdd:PRK13649 148 GGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLS 226
|
....*.
gi 523689182 240 GLVGDI 245
Cdd:PRK13649 227 GKPKDI 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-240 |
1.18e-24 |
|
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: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGgkavKAVNGVSLSVKPGeVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMslsnRALS 88
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPS---SGTIRIDGQDVL----KQPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 DLRgAVVSMVFQEPRLalDPVYTVGRQIEeTIMRHEKVSRGLAAERALALFQKVRIpspERRLSNYPHEMSGGMLQRAMI 168
Cdd:cd03264 69 KLR-RRIGYLPQEFGV--YPNFTVREFLD-YIAWLKGIPSKEVKARVDEVLELVNL---GDRAKKKIGSLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523689182 169 AMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYglSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-246 |
1.56e-24 |
|
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: 99.77 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 6 DAMIDISNlsVTFRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRL----HPKGTliegGMTVD--GHDI 79
Cdd:COG1119 1 DPLLELRN--VTVRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKS----TLLSLitgdLPPTY----GNDVRlfGERR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 80 MSLSnraLSDLRG--AVVSmvfqePRLALD-PVYTVGRQI-----EETIMRHEKVSRgLAAERALALFQKVRIpspeRRL 151
Cdd:COG1119 69 GGED---VWELRKriGLVS-----PALQLRfPRDETVLDVvlsgfFDSIGLYREPTD-EQRERARELLELLGL----AHL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 152 SNYP-HEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAV 230
Cdd:COG1119 136 ADRPfGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLL 215
|
250
....*....|....*.
gi 523689182 231 MYAGRIVEEGLVGDII 246
Cdd:COG1119 216 LKDGRVVAAGPKEEVL 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-239 |
2.36e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 102.79 E-value: 2.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 26 KAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgtlIEGGMTVDGHDIMSLSNRALSDLRGAVVSmvfqEPR-- 103
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPA---DSGEIRLDGKPVRIRSPRDAIRAGIAYVP----EDRkg 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 104 --LALDpvytvgRQIEE--TIMRHEKVSRGL----AAERALA--LFQKVRI--PSPERRLSNypheMSGGMLQRAMIAMA 171
Cdd:COG1129 339 egLVLD------LSIREniTLASLDRLSRGGlldrRRERALAeeYIKRLRIktPSPEQPVGN----LSGGNQQKVVLAKW 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523689182 172 LACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEE 239
Cdd:COG1129 409 LATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGE 475
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-240 |
3.08e-24 |
|
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: 98.46 E-value: 3.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 15 SVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHpkgTLIEGGMTVDGHDIMSLSnraLSDLRgAV 94
Cdd:cd03251 5 NVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFY---DVDSGRILIDGHDVRDYT---LASLR-RQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 95 VSMVFQEPRLALDPV-----YTVGRQIEETIMRhekvsrglAAERALALFQKVRIPS------PERRLSnypheMSGGML 163
Cdd:cd03251 78 IGLVSQDVFLFNDTVaeniaYGRPGATREEVEE--------AARAANAHEFIMELPEgydtviGERGVK-----LSGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523689182 164 QRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIGvAAEVADRIAVMYAGRIVEEG 240
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKIVERG 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
15-279 |
3.38e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.98 E-value: 3.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 15 SVTFRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRL-HPK-GTLIEGgmtvdghdimslsNRALSDLRG 92
Cdd:PRK11247 17 AVSKRYGERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLeTPSaGELLAG-------------TAPLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 93 AVvSMVFQEPRLAldPVYTVgrqieetimrHEKVSRGL------AAERALAlfqKVRIpspERRLSNYPHEMSGGMLQRA 166
Cdd:PRK11247 82 DT-RLMFQDARLL--PWKKV----------IDNVGLGLkgqwrdAALQALA---AVGL---ADRANEWPAALSGGQKQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 167 MIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAvmyagrIVEEGLVG--- 243
Cdd:PRK11247 143 ALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVL------LIEEGKIGldl 216
|
250 260 270
....*....|....*....|....*....|....*...
gi 523689182 244 --DIIRnPRHPYTKGLlgARVElAEGRDRLVTIPGAPP 279
Cdd:PRK11247 217 tvDLPR-PRRRGSARL--AELE-AEVLQRVMSRGESEP 250
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-248 |
3.81e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 100.16 E-value: 3.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFR-----------------RGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLR-LHP-KGTLi 68
Cdd:COG4586 1 IIEVENLSKTYRvyekepglkgalkglfrREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVPtSGEV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 69 eggmTVDGHDIMSLSNRALSDlrgavVSMVF-QEPRLALDpvytvgrqieetimrhekvsrgLAAERALALFQKV-RIPS 146
Cdd:COG4586 80 ----RVLGYVPFKRRKEFARR-----IGVVFgQRSQLWWD----------------------LPAIDSFRLLKAIyRIPD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 147 PE--RRLsnypHEMSGgMLQ------------------RAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQRE 206
Cdd:COG4586 129 AEykKRL----DELVE-LLDlgelldtpvrqlslgqrmRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRE 203
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 523689182 207 YGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRN 248
Cdd:COG4586 204 RGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
21-244 |
4.28e-24 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 98.02 E-value: 4.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 21 GGKavKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTlieGGMTVDGHDIMSLSNRALSDLRGAVvSMVFQ 100
Cdd:PRK10908 13 GGR--QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSA---GKIWFSGHDITRLKNREVPFLRRQI-GMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 101 EPRLALD---------PVYTVGRQiEETIMRheKVSrglAAERALALFQKVRipsperrlsNYPHEMSGGMLQRAMIAMA 171
Cdd:PRK10908 87 DHHLLMDrtvydnvaiPLIIAGAS-GDDIRR--RVS---AALDKVGLLDKAK---------NFPIQLSGGEQQRVGIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523689182 172 LACNPKVLLADEPTTALDATVQIQILLLIRELQReYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVeEGLVGD 244
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH-GGVGGE 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
9-240 |
5.79e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 101.96 E-value: 5.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLS-------VTFRRGGKAvKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLH-PKGtlieGGMTVDGHDIM 80
Cdd:PRK13657 326 IDLGRVKgavefddVSFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFdPQS----GRILIDGTDIR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 81 SLSnraLSDLRGAvVSMVFQEPRLaldpvytVGRQIEETI------MRHEKVSRglAAERALAL-FQkvripspERRLSN 153
Cdd:PRK13657 401 TVT---RASLRRN-IAVVFQDAGL-------FNRSIEDNIrvgrpdATDEEMRA--AAERAQAHdFI-------ERKPDG 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 154 YP-------HEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIGVAAEvAD 226
Cdd:PRK13657 461 YDtvvgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-AD 537
|
250
....*....|....
gi 523689182 227 RIAVMYAGRIVEEG 240
Cdd:PRK13657 538 RILVFDNGRVVESG 551
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-240 |
8.42e-24 |
|
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: 97.56 E-value: 8.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 16 VTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMSLsnrALSDLRgAVV 95
Cdd:cd03252 6 VRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE---NGRVLVDGHDLALA---DPAWLR-RQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 96 SMVFQEPRLaldpvytVGRQIEETI------MRHEKVSRGLAAERALALFQKVRIpSPERRLSNYPHEMSGGMLQRAMIA 169
Cdd:cd03252 79 GVVLQENVL-------FNRSIRDNIaladpgMSMERVIEAAKLAGAHDFISELPE-GYDTIVGEQGAGLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523689182 170 MALACNPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIGvAAEVADRIAVMYAGRIVEEG 240
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQG 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-237 |
1.49e-23 |
|
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: 100.67 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 25 VKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTLiEGGMTVDGHDIMSlsnRALSDLRGAVVSMVFQEprL 104
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTW-DGEIYWSGSPLKA---SNIRDTERAGIVIIHQE--L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 105 ALDPVYTVgrqIEETIMRHEKVSRG------LAAERALALFQKVRIP-SPERRLSNyphEMSGGMLQRAMIAMALACNPK 177
Cdd:TIGR02633 88 TLVPELSV---AENIFLGNEITLPGgrmaynAMYLRAKNLLRELQLDaDNVTRPVG---DYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523689182 178 VLLADEPTTALDATvQIQILL-LIRELQReYGLSVIFVTHDIGVAAEVADRIAVMYAGRIV 237
Cdd:TIGR02633 162 LLILDEPSSSLTEK-ETEILLdIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-253 |
1.71e-23 |
|
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: 99.03 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 31 VSLSVKPGEVVALLGESGSGKSvtmrSLLRLhpkgtlIEGGMTVDGHDImSLSNRALSDLRGAV--------VSMVFQEP 102
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKT----TLIRL------IAGLTRPDEGEI-VLNGRTLFDSRKGIflppekrrIGYVFQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 103 RLAldPVYTVGRQIEETIMRHEKVSRGLAAERALALFqkvripSPERRLSNYPHEMSGGMLQRAMIAMALACNPKVLLAD 182
Cdd:TIGR02142 85 RLF--PHLSVRGNLRYGMKRARPSERRISFERVIELL------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523689182 183 EPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNPRHPY 253
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-236 |
2.59e-23 |
|
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: 94.42 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 5 NDAMIDISNLSVTfrrggkavKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtLIEGGMTVDGHDIMSLSN 84
Cdd:cd03215 1 GEPVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP---PASGEITLDGKPVTRRSP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 85 RALSDLRGAVVSmvfqeprlaldpvytvgrqiEEtimRHEkvsRGLAAERALAlfQKVRIPspeRRLSnyphemsGGMLQ 164
Cdd:cd03215 70 RDAIRAGIAYVP--------------------ED---RKR---EGLVLDLSVA--ENIALS---SLLS-------GGNQQ 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523689182 165 RAMIAMALACNPKVLLADEPTTALD-ATVQiQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRI 236
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVDvGAKA-EIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
27-240 |
2.95e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 96.84 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 27 AVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLR-LHP-KGTLIEGGMTVDghdimsLSNRALSDLRGAvVSMVFQEP-- 102
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGiLKPsSGRILFDGKPID------YSRKGLMKLRES-VGMVFQDPdn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 103 RLALDPVY------TVGRQIEETIMrHEKVSRGLAAERALALFQKvriPSperrlsnypHEMSGGMLQRAMIAMALACNP 176
Cdd:PRK13636 94 QLFSASVYqdvsfgAVNLKLPEDEV-RKRVDNALKRTGIEHLKDK---PT---------HCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523689182 177 KVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQG 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
8-279 |
3.11e-23 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 96.82 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVtFRRGGKAVKAVngvSLSVKPGEVVALLGESGSGKSVTMRSLL-----RLHPKGTLIEGGMTVDGHDIMSL 82
Cdd:PRK13547 1 MLTADHLHV-ARRHRAILRDL---SLRIEPGRVTALLGRNGAGKSTLLKALAgdltgGGAPRGARVTGDVTLNGEPLAAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 83 SNRALSDLRGAVVSMVFQEPRLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVriPSPERRLSNypheMSGGM 162
Cdd:PRK13547 77 DAPRLARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGAT--ALVGRDVTT----LSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 163 LQRAMIAMALA---------CNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYA 233
Cdd:PRK13547 151 LARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLAD 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 523689182 234 GRIVEEGLVGDIIRnPRHpyTKGLLGARVELAEGRDrlvtipGAPP 279
Cdd:PRK13547 231 GAIVAHGAPADVLT-PAH--IARCYGFAVRLVDAGD------GVPP 267
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-261 |
3.36e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 96.39 E-value: 3.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 4 QNDAMIDISNLSVTFrrgGKAVkAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHP--KGTLIEGGMTVDGHDIMS 81
Cdd:PRK14243 6 GTETVLRTENLNVYY---GSFL-AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFRVEGKVTFHGKNLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 82 lSNRALSDLRGAVvSMVFQEPrlaldpvYTVGRQIEETIM-----------RHEKVSRGLaaeRALALFQKVRIPSPERR 150
Cdd:PRK14243 82 -PDVDPVEVRRRI-GMVFQKP-------NPFPKSIYDNIAygaringykgdMDELVERSL---RQAALWDEVKDKLKQSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 151 LSnypheMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYglSVIFVTHDIGVAAEVADRIAV 230
Cdd:PRK14243 150 LS-----LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAF 222
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 523689182 231 MYA---------GRIVEEGLVGDIIRNPRHPYTKGLLGAR 261
Cdd:PRK14243 223 FNVeltegggryGYLVEFDRTEKIFNSPQQQATRDYVSGR 262
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-217 |
4.46e-23 |
|
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: 94.47 E-value: 4.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 7 AMIDISNLSVtfRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLR-----LHPkgtlIEGGMTVDGHDIms 81
Cdd:COG4133 1 MMLEAENLSC--RRGERLL--FSGLSFTLAAGEALALTGPNGSGKT----TLLRilaglLPP----SAGEVLWNGEPI-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 82 lsNRALSDLRGAvvsMVFQEPRLALDPVYTVGRQIEETIMRHEKVSRGLAAERALALFQkvripsPERRLSNYPHEMSGG 161
Cdd:COG4133 67 --RDAREDYRRR---LAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVG------LAGLADLPVRQLSAG 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 523689182 162 MLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRElQREYGLSVIFVTHD 217
Cdd:COG4133 136 QKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-240 |
8.38e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 95.57 E-value: 8.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 6 DAMIDISNLSVTFRRGGKAVKavnGVSLSVKPGEVVALLGESGSGKSVtmrslLRLHPKG--TLIEGGMTVDGHDImslS 83
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALK---GLSLSIPEGSKTALLGPNGAGKST-----LLLHLNGiyLPQRGRVKVMGREV---N 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 84 NRALSDLRGAVvSMVFQEPR-----------LALDPVyTVGRQIEETimrHEKVSRGLAAERALALFQKVripsperrls 152
Cdd:PRK13647 71 AENEKWVRSKV-GLVFQDPDdqvfsstvwddVAFGPV-NMGLDKDEV---ERRVEEALKAVRMWDFRDKP---------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 153 nyPHEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMY 232
Cdd:PRK13647 136 --PYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLK 212
|
....*...
gi 523689182 233 AGRIVEEG 240
Cdd:PRK13647 213 EGRVLAEG 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-240 |
1.16e-22 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 93.81 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 16 VTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMSLSnraLSDLRgAVV 95
Cdd:cd03245 8 VSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT---SGSVLLDGTDIRQLD---PADLR-RNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 96 SMVFQEPRLALDPVY---TVGRQI--EETIMRhekvsrglAAERA-LALFQKVRIPSPERRLSNYPHEMSGGMLQRAMIA 169
Cdd:cd03245 81 GYVPQDVTLFYGTLRdniTLGAPLadDERILR--------AAELAgVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523689182 170 MALACNPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIgVAAEVADRIAVMYAGRIVEEG 240
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-262 |
1.22e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 94.73 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 31 VSLSVKPGEVVALLGESGSGKSVTMRSLLRL---HPKGTLIEGGMTVDGHDIMSLSNRALSDlrgaVVSMVFQEPRL--A 105
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKIKVDGKVLYFGKDIFQIDAIKLRK----EVGMVFQQPNPfpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 106 LDPVYTVGRQIEETIMRHEKVSRGLAAE--RALALFQKVRipspeRRLSNYPHEMSGGMLQRAMIAMALACNPKVLLADE 183
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEEclRKVGLWKEVY-----DRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523689182 184 PTTALDATVQIQILLLIRELQREygLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRNPRHPYTKGLLGARV 262
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYVIGRI 256
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-236 |
1.41e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 96.45 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 7 AMIDISNLSVTFrrGGKaVKAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRLhpkgtlIEGGMTVDGHDImSLSNRA 86
Cdd:PRK11650 2 AGLKLQAVRKSY--DGK-TQVIKGIDLDVADGEFIVLVGPSGCGKS----TLLRM------VAGLERITSGEI-WIGGRV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSDL----RGavVSMVFQEprLALDPVYTVgRQIEETIMRHEKVSRGLAAERALALFQKVRI-PSPERRlsnyPHEMSGG 161
Cdd:PRK11650 68 VNELepadRD--IAMVFQN--YALYPHMSV-RENMAYGLKIRGMPKAEIEERVAEAARILELePLLDRK----PRELSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523689182 162 mlQRAMIAM--ALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRI 236
Cdd:PRK11650 139 --QRQRVAMgrAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
9-240 |
1.43e-22 |
|
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: 93.71 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtLIEGGMTVDGHDIMSLSnraLS 88
Cdd:cd03244 3 IEFKNVSLRYRPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE---LSSGSILIDGVDISKIG---LH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 DLRGAvVSMVFQEP-------RLALDPvytVGRQIEETIMrhekvsrglaaeRALALFQ-KVRIPSPERRLsNYPHEMSG 160
Cdd:cd03244 75 DLRSR-ISIIPQDPvlfsgtiRSNLDP---FGEYSDEELW------------QALERVGlKEFVESLPGGL-DTVVEEGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 161 GML---QRAMIAMALAC--NPKVLLADEPTTALDatvqIQILLLIRELQREY--GLSVIFVTHDIGVAAEvADRIAVMYA 233
Cdd:cd03244 138 ENLsvgQRQLLCLARALlrKSKILVLDEATASVD----PETDALIQKTIREAfkDCTVLTIAHRLDTIID-SDRILVLDK 212
|
....*..
gi 523689182 234 GRIVEEG 240
Cdd:cd03244 213 GRVVEFD 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-249 |
2.25e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 95.30 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 3 MQNDAMIDISNLSVTF-RRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKS--VTMRSLLRLHPKGTlIEGGMTVDGHDI 79
Cdd:PRK13631 16 LSDDIILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKStlVTHFNGLIKSKYGT-IQVGDIYIGDKK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 80 MSLSN---------RALSDLRgAVVSMVFQEPRLALdpvytVGRQIEETIMrHEKVSRGLAAERA--LALFQKVRIPSPE 148
Cdd:PRK13631 95 NNHELitnpyskkiKNFKELR-RRVSMVFQFPEYQL-----FKDTIEKDIM-FGPVALGVKKSEAkkLAKFYLNKMGLDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 149 RRLSNYPHEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRI 228
Cdd:PRK13631 168 SYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEV 246
|
250 260
....*....|....*....|.
gi 523689182 229 AVMYAGRIVEEGLVGDIIRNP 249
Cdd:PRK13631 247 IVMDKGKILKTGTPYEIFTDQ 267
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
6-236 |
2.28e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.41 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 6 DAMIDISNLsvTFRRGGKAVK-AVNGVSLSVKPGEVVALLGESGSGKSVTMRsllrlhpkgtLIEGGMTVDGHDIM---- 80
Cdd:PRK13650 2 SNIIEVKNL--TFKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVR----------LIDGLLEAESGQIIidgd 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 81 SLSNRALSDLRGAVvSMVFQEPrlalDPVYtVGRQIEETI---MRHEKVSRGLAAERALALFQKVRIPSPERRlsnYPHE 157
Cdd:PRK13650 70 LLTEENVWDIRHKI-GMVFQNP----DNQF-VGATVEDDVafgLENKGIPHEEMKERVNEALELVGMQDFKER---EPAR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 158 MSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGvaaEVA--DRIAVMYAGR 235
Cdd:PRK13650 141 LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLD---EVAlsDRVLVMKNGQ 217
|
.
gi 523689182 236 I 236
Cdd:PRK13650 218 V 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-249 |
4.16e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.71 E-value: 4.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFRrggKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRsllrlHPKGTL--IEGGMTVDGHDImslSNR 85
Cdd:PRK13652 3 LIETRDLCYSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFR-----HFNGILkpTSGSVLIRGEPI---TKE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 ALSDLRgAVVSMVFQEPRlalDPVY--TVGRQI----------EETImrHEKVSRGLaaeRALALfqkvripspERRLSN 153
Cdd:PRK13652 72 NIREVR-KFVGLVFQNPD---DQIFspTVEQDIafgpinlgldEETV--AHRVSSAL---HMLGL---------EELRDR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 154 YPHEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYA 233
Cdd:PRK13652 134 VPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDK 213
|
250
....*....|....*.
gi 523689182 234 GRIVEEGLVGDIIRNP 249
Cdd:PRK13652 214 GRIVAYGTVEEIFLQP 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
9-231 |
4.28e-22 |
|
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: 96.59 E-value: 4.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGKAVKavnGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMSLSnralS 88
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALR---PVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT---EGSIAVNGVPLADAD----A 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 DLRGAVVSMVFQEPrlaldpvYTVGRQIEETIMRHEKVSRGLAAERALAL-----FQKVRIPSPERRLSNYPHEMSGGML 163
Cdd:TIGR02857 392 DSWRDQIAWVPQHP-------FLFAGTIAENIRLARPDASDAEIREALERagldeFVAALPQGLDTPIGEGGAGLSGGQA 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523689182 164 QRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIGVAAEvADRIAVM 231
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
8-238 |
5.10e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 92.84 E-value: 5.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFrrGGKavKAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLrlhpkgTLIEGGMTVDGHDImSLSNRAL 87
Cdd:PRK11248 1 MLQISHLYADY--GGK--PALEDINLTLESGELLVVLGPSGCGKT----TLL------NLIAGFVPYQHGSI-TLDGKPV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 SDlRGAVVSMVFQEPRL-----ALDPVyTVGRQIEetimrheKVSRGLAAERALALFQKVRIPSPERRlsnYPHEMSGGM 162
Cdd:PRK11248 66 EG-PGAERGVVFQNEGLlpwrnVQDNV-AFGLQLA-------GVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGGQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 163 LQRAMIAMALACNPKVLLADEPTTALDATV--QIQILLLirELQREYGLSVIFVTHDIGVAAEVADRIAVMY--AGRIVE 238
Cdd:PRK11248 134 RQRVGIARALAANPQLLLLDEPFGALDAFTreQMQTLLL--KLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVE 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-251 |
5.41e-22 |
|
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: 92.53 E-value: 5.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 28 VNGVSLSVKPGEVVALLGESGSGKS--VTMRSLLRLHPKGTLIEGGMTVD--GHDIMSL-SNRALSDLRgavvsMVFQEP 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKStlLNLISGLAQPTSGGVILEGKQITepGPDRMVVfQNYSLLPWL-----TVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 103 RLALDPVYTVGRQIE-ETIMRH--EKVSRGLAAERalalfqkvripsperrlsnYPHEMSGGMLQRAMIAMALACNPKVL 179
Cdd:TIGR01184 76 ALAVDRVLPDLSKSErRAIVEEhiALVGLTEAADK-------------------RPGQLSGGMKQRVAIARALSIRPKVL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523689182 180 LADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDI-IRNPRH 251
Cdd:TIGR01184 137 LLDEPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-236 |
5.66e-22 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 92.15 E-value: 5.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 6 DAMIDISNLSVTFRRGgKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtLIEGGMTVDGHDIMSLSNR 85
Cdd:cd03248 9 KGIVKFQNVTFAYPTR-PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ---PQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 ALSdlrgAVVSMVFQEPRLaldpvytVGRQIEETImrhekvSRGLAA---ERALALFQKVRIPSPERRLSNYPHE----- 157
Cdd:cd03248 85 YLH----SKVSLVGQEPVL-------FARSLQDNI------AYGLQScsfECVKEAAQKAHAHSFISELASGYDTevgek 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 158 ---MSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIfvTHDIGVaAEVADRIAVMYAG 234
Cdd:cd03248 148 gsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVI--AHRLST-VERADQILVLDGG 224
|
..
gi 523689182 235 RI 236
Cdd:cd03248 225 RI 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3-248 |
6.28e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 93.61 E-value: 6.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 3 MQndamIDISNLSVTFRRGGK-AVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSL--LRLHPKGTLIEggMTVDGHDi 79
Cdd:PRK13651 1 MQ----IKVKNIVKIFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLnaLLLPDTGTIEW--IFKDEKN- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 80 mslsNRALSDLRGAVVSMVFQEPRL-ALDPVYTVGRQI------------EETImrhEK----------VSRGLAAERAL 136
Cdd:PRK13651 74 ----KKKTKEKEKVLEKLVIQKTRFkKIKKIKEIRRRVgvvfqfaeyqlfEQTI---EKdiifgpvsmgVSKEEAKKRAA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 137 ALFQKVRIPspERRLSNYPHEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTH 216
Cdd:PRK13651 147 KYIELVGLD--ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTH 223
|
250 260 270
....*....|....*....|....*....|..
gi 523689182 217 DIGVAAEVADRIAVMYAGRIVEEGLVGDIIRN 248
Cdd:PRK13651 224 DLDNVLEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
9-240 |
6.90e-22 |
|
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: 90.84 E-value: 6.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFrrGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSvTMRSLLR--LHPKgtliEGGMTVDGHDIMSLSNrA 86
Cdd:cd03247 1 LSINNVSFSY--PEQEQQVLKNLSLELKQGEKIALLGRSGSGKS-TLLQLLTgdLKPQ----QGEITLDGVPVSDLEK-A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSDLrgavVSMVFQEPRLaldpvytvgrqIEETIMrhekvsrglaaeralalfqkvripsperrlSNYPHEMSGGMLQRA 166
Cdd:cd03247 73 LSSL----ISVLNQRPYL-----------FDTTLR------------------------------NNLGRRFSGGERQRL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523689182 167 MIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYglSVIFVTHDIgVAAEVADRIAVMYAGRIVEEG 240
Cdd:cd03247 108 ALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1-248 |
7.99e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.15 E-value: 7.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 1 MTMQNDAMIDisNLSVTF-RRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSvTMRSLlrlhPKGTLI-EGGMTVDGhD 78
Cdd:PRK13645 1 FDFSKDIILD--NVSYTYaKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKS-TMIQL----TNGLIIsETGQTIVG-D 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 79 IMSLSN----RALSDLRGAVvSMVFQEPRLALdpvytvgrqIEETIMR-------HEKVSRGLAAERALALFQKVRIPsp 147
Cdd:PRK13645 73 YAIPANlkkiKEVKRLRKEI-GLVFQFPEYQL---------FQETIEKdiafgpvNLGENKQEAYKKVPELLKLVQLP-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 148 ERRLSNYPHEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADR 227
Cdd:PRK13645 141 EDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADE 220
|
250 260
....*....|....*....|.
gi 523689182 228 IAVMYAGRIVEEGLVGDIIRN 248
Cdd:PRK13645 221 VIVMHEGKVISIGSPFEIFSN 241
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-266 |
8.04e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.74 E-value: 8.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFRRGGKAVKAVNgvsLSVKPGEVVALLGESGSGKSVtmrslLRLHPKGTL--IEGGMTVDGHDIMSLSNr 85
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENIN---LVIKKGEYIGIIGKNGSGKST-----LALHLNGLLrpQKGKVLVSGIDTGDFSK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 aLSDLRgAVVSMVFQEPRLALdpvytVGRQIEET------------IMRHEKVSRGLAaERALalfQKVRIPSPErrlsn 153
Cdd:PRK13644 72 -LQGIR-KLVGIVFQNPETQF-----VGRTVEEDlafgpenlclppIEIRKRVDRALA-EIGL---EKYRHRSPK----- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 154 yphEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGvAAEVADRIAVMYA 233
Cdd:PRK13644 136 ---TLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLE-ELHDADRIIVMDR 210
|
250 260 270
....*....|....*....|....*....|...
gi 523689182 234 GRIVEEGLVGDIIRNPRHPYTKGLLGARVELAE 266
Cdd:PRK13644 211 GKIVLEGEPENVLSDVSLQTLGLTPPSLIELAE 243
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-240 |
1.10e-21 |
|
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: 91.63 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 18 FRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLR-LHPKgtliEGGMTVDGHDIMSLSNRALSDLrgavvS 96
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGlLQPT----SGEVRVAGLVPWKRRKKFLRRI-----G 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 97 MVF-QEPRLALD-PV---YTVGRQI-----EETIMRHEKVSRGLAAERALAlfqkvripSPERRLSNyphemsgGMLQRA 166
Cdd:cd03267 98 VVFgQKTQLWWDlPVidsFYLLAAIydlppARFKKRLDELSELLDLEELLD--------TPVRQLSL-------GQRMRA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523689182 167 MIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-238 |
1.17e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 95.24 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 25 VKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTLiEGGMTVDGhDIMSLSNRALSDLRGAVVsmVFQEprL 104
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSY-EGEILFDG-EVCRFKDIRDSEALGIVI--IHQE--L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 105 ALDPVYTvgrqIEETI-MRHEKVSRGL-----AAERALALFQKVRIP-SPERRLSNypheMSGGMLQRAMIAMALACNPK 177
Cdd:NF040905 88 ALIPYLS----IAENIfLGNERAKRGVidwneTNRRARELLAKVGLDeSPDTLVTD----IGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523689182 178 VLLADEPTTALDATVQIQILLLIRELqREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVE 238
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-250 |
1.76e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 91.24 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 7 AMIDISNLSVTFrrGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLrlhpkGtLI---EGGMTVDGHDI--MS 81
Cdd:COG1137 2 MTLEAENLVKSY--GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIV-----G-LVkpdSGRIFLDGEDIthLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 82 LSNRAlsdLRGavVSMVFQEP----RLaldpvyTVgrqiEETIM---RHEKVSRGLAAERALALFQKVRIpspERRLSNY 154
Cdd:COG1137 72 MHKRA---RLG--IGYLPQEAsifrKL------TV----EDNILavlELRKLSKKEREERLEELLEEFGI---THLRKSK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 155 PHEMSGGMLQRAMIAMALACNPKVLLADEPTTALD--ATVQIQilLLIRELqREYGLSVIFVTHDIGVAAEVADRIAVMY 232
Cdd:COG1137 134 AYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiAVADIQ--KIIRHL-KERGIGVLITDHNVRETLGICDRAYIIS 210
|
250
....*....|....*...
gi 523689182 233 AGRIVEEGLVGDIIRNPR 250
Cdd:COG1137 211 EGKVLAEGTPEEILNNPL 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
32-240 |
1.91e-21 |
|
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: 90.24 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 32 SLSVKPGEVVALLGESGSGKSvtmrSLLRLHPK-GTLIEGGMTVDGHDI--MSLSNRAlsdlrgavVSMVFQEPRLAldP 108
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKS----TLLNLIAGfETPQSGRVLINGVDVtaAPPADRP--------VSMLFQENNLF--A 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 109 VYTVGRQIEETI---MRHEKVSRGlAAERALAlfqKVRIPSPERRLsnyPHEMSGGMLQRAMIAMALACNPKVLLADEPT 185
Cdd:cd03298 84 HLTVEQNVGLGLspgLKLTAEDRQ-AIEVALA---RVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 523689182 186 TALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-249 |
2.05e-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: 90.68 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGgkavKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDI--MSLSNRA 86
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPD---SGKILLDGQDItkLPMHKRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 lsdLRGavVSMVFQEPrlaldpvyTVGRQ--IEETIM---RHEKVSRGLAAERALALFQKVRIPSPERRLSNYpheMSGG 161
Cdd:cd03218 74 ---RLG--IGYLPQEA--------SIFRKltVEENILavlEIRGLSKKEREEKLEELLEEFHITHLRKSKASS---LSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 162 MLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELqREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGL 241
Cdd:cd03218 138 ERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
....*...
gi 523689182 242 VGDIIRNP 249
Cdd:cd03218 217 PEEIAANE 224
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
237-301 |
2.29e-21 |
|
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: 85.92 E-value: 2.29e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523689182 237 VEEGLVGDIIRNPRHPYTKGLLGARVELAEGRDRLVTIPGAPPDLAAMPPGCAFAPRCVQVSDLC 301
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-240 |
2.59e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 90.41 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 32 SLSVKPGEVVALLGESGSGKSvTMRSLLR--LHPKGtlieGGMTVDG--HDIMSLSNRAlsdlrgavVSMVFQEPRLAld 107
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS-TLLNLIAgfLTPAS----GSLTLNGqdHTTTPPSRRP--------VSMLFQENNLF-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 108 PVYTVGRQIEETIMRHEKVSrglAAERAL--ALFQKVRIpspERRLSNYPHEMSGGMLQRAMIAMALACNPKVLLADEPT 185
Cdd:PRK10771 84 SHLTVAQNIGLGLNPGLKLN---AAQREKlhAIARQMGI---EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 523689182 186 TALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDG 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-245 |
8.98e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.81 E-value: 8.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 3 MQNDAMIDISNlsVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRsllrlhpkgtLIEGGMTV-DGHDIMS 81
Cdd:PRK13648 2 EDKNSIIVFKN--VSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAK----------LMIGIEKVkSGEIFYN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 82 ---LSNRALSDLRGAVvSMVFQEPR-------LALDPVYTVGRQIEETIMRHEKVSRGLAAERALAlfqkvripsperRL 151
Cdd:PRK13648 70 nqaITDDNFEKLRKHI-GIVFQNPDnqfvgsiVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLE------------RA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 152 SNYPHEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEvADRIAVM 231
Cdd:PRK13648 137 DYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVM 215
|
250
....*....|....
gi 523689182 232 YAGRIVEEGLVGDI 245
Cdd:PRK13648 216 NKGTVYKEGTPTEI 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
10-240 |
1.19e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 92.39 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 10 DISNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSvTMRSLL-RLHpkgTLIEGGMTVDGHDIMSLSnraLS 88
Cdd:PRK11176 341 DIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKS-TIANLLtRFY---DIDEGEILLDGHDLRDYT---LA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 DLRGAvVSMVFQEPRLALDpvyTVGRQIeeTIMRHEKVSRG---LAAERALAL-FqkvrIPSPERRLSNYPHE----MSG 160
Cdd:PRK11176 414 SLRNQ-VALVSQNVHLFND---TIANNI--AYARTEQYSREqieEAARMAYAMdF----INKMDNGLDTVIGEngvlLSG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 161 GMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYglSVIFVTHDIGvAAEVADRIAVMYAGRIVEEG 240
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEKADEILVVEDGEIVERG 560
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-247 |
1.61e-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: 91.79 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFRRGgkAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVD-GHDIMSLSNRA 86
Cdd:TIGR03269 282 VRNVSKRYISVDRG--VVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT---SGEVNVRvGDEWVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LsDLRGAV---VSMVFQEprLALDPVYTVGRQIEETIMRheKVSRGLAAERALALFQKVRIPSPERR--LSNYPHEMSGG 161
Cdd:TIGR03269 357 P-DGRGRAkryIGILHQE--YDLYPHRTVLDNLTEAIGL--ELPDELARMKAVITLKMVGFDEEKAEeiLDKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 162 MLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGL 241
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
....*.
gi 523689182 242 VGDIIR 247
Cdd:TIGR03269 512 PEEIVE 517
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
15-260 |
1.85e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.47 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 15 SVTFRRGGKA---VKAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRLhpkgtlIEGGMTVDGHDIMsLSNRALSDL- 90
Cdd:PRK11000 3 SVTLRNVTKAygdVVISKDINLDIHEGEFVVFVGPSGCGKS----TLLRM------IAGLEDITSGDLF-IGEKRMNDVp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 91 ---RGavVSMVFQEprLALDPVYTVGrqieetimrhEKVSRGLA------AERALALFQKVRIPSPERRLSNYPHEMSGG 161
Cdd:PRK11000 72 paeRG--VGMVFQS--YALYPHLSVA----------ENMSFGLKlagakkEEINQRVNQVAEVLQLAHLLDRKPKALSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 162 MLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGL 241
Cdd:PRK11000 138 QRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
|
250
....*....|....*....
gi 523689182 242 VGDIIRNPRHPYTKGLLGA 260
Cdd:PRK11000 218 PLELYHYPANRFVAGFIGS 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
11-248 |
2.07e-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: 87.20 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 11 ISNLSVtfRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSvTMRSLLRLHPKGTLIEGGMTVDGHDI--MSLSNRAls 88
Cdd:cd03217 3 IKDLHV--SVGGKEI--LKGVNLTIKKGEVHALMGPNGSGKS-TLAKTIMGHPKYEVTEGEILFKGEDItdLPPEERA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 dLRGavVSMVFQEPrlaldpvytvgrqieetimrhekvsrglaaeralalfqkVRIpsPERRLSNYPHEM----SGGMLQ 164
Cdd:cd03217 76 -RLG--IFLAFQYP---------------------------------------PEI--PGVKNADFLRYVnegfSGGEKK 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 165 RAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELqREYGLSVIFVTHDIGVAAEV-ADRIAVMYAGRIVEEG--- 240
Cdd:cd03217 112 RNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGdke 190
|
....*...
gi 523689182 241 LVGDIIRN 248
Cdd:cd03217 191 LALEIEKK 198
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
32-236 |
2.51e-20 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 87.22 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 32 SLSVKPGEVVALLGESGSGKSvTMRSLLR--LHPkgtlIEGGMTVDGHDIMSL--SNRAlsdlrgavVSMVFQEPRLAld 107
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKS-TLLNLIAgfIEP----ASGSIKVNDQSHTGLapYQRP--------VSMLFQENNLF-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 108 PVYTVGRQIEETIMRHEKVSrGLAAERALALFQKVRIPSPERRLsnyPHEMSGGMLQRAMIAMALACNPKVLLADEPTTA 187
Cdd:TIGR01277 83 AHLTVRQNIGLGLHPGLKLN-AEQQEKVVDAAQQVGIADYLDRL---PEQLSGGQRQRVALARCLVRPNPILLLDEPFSA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 523689182 188 LDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRI 236
Cdd:TIGR01277 159 LDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-246 |
2.71e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.50 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 22 GKAVKAVNgVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHpkgTLIEGGMTVDGHDIMSLSNRALSDLRGAV------- 94
Cdd:PRK10253 18 GKYTVAEN-LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM---TPAHGHVWLDGEHIQHYASKEVARRIGLLaqnattp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 95 ----VSMVFQEPRLALDPVYTVGRQIEEtimrhEKVSRGLAAERALAL-FQKVripsperrlsnypHEMSGGMLQRAMIA 169
Cdd:PRK10253 94 gditVQELVARGRYPHQPLFTRWRKEDE-----EAVTKAMQATGITHLaDQSV-------------DTLSGGQRQRAWIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523689182 170 MALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDII 246
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
8-250 |
3.67e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 87.74 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFrrGGkaVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLH-PKGtlieGGMTVDGHDIMSLSNRA 86
Cdd:PRK11300 5 LLSVSGLMMRF--GG--LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYkPTG----GTILLRGQHIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSdlRGAVVSmVFQEPRLALDpvYTVgrqIEE-TIMRHEKVSRGL----------------AAERALALFQKVRIpspeR 149
Cdd:PRK11300 77 IA--RMGVVR-TFQHVRLFRE--MTV---IENlLVAQHQQLKTGLfsgllktpafrraeseALDRAATWLERVGL----L 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 150 RLSNYPH-EMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRI 228
Cdd:PRK11300 145 EHANRQAgNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRI 224
|
250 260
....*....|....*....|..
gi 523689182 229 AVMYAGRIVEEGLVGDIIRNPR 250
Cdd:PRK11300 225 YVVNQGTPLANGTPEEIRNNPD 246
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
8-245 |
4.10e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 90.61 E-value: 4.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFrrGGkaVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTlieGGMTVDGHDIMSLSNRAL 87
Cdd:PRK09700 5 YISMAGIGKSF--GP--VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTK---GTITINNINYNKLDHKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 SDLRgavVSMVFQEPRL-----ALDPVYtVGRQIEETIMRHEKVSRGLAAERALALFQKVRIpspERRLSNYPHEMSGGM 162
Cdd:PRK09700 78 AQLG---IGIIYQELSVideltVLENLY-IGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGL---KVDLDEKVANLSISH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 163 LQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLV 242
Cdd:PRK09700 151 KQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMV 229
|
...
gi 523689182 243 GDI 245
Cdd:PRK09700 230 SDV 232
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-228 |
5.91e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 86.38 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTfrRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLrLHPKGTL-----IEGGMTVDGHDIMSL 82
Cdd:COG4136 1 MLSLENLTIT--LGGRPL--LAPLSLTVAPGEILTLMGPSGSGKS----TLL-AAIAGTLspafsASGEVLLNGRRLTAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 83 SNRAlsdlRGavVSMVFQEPrlALDPVYTVGRQI----EETIMRHEkvsRGLAAERALAlfqKVRIPSPERRlsnYPHEM 158
Cdd:COG4136 72 PAEQ----RR--IGILFQDD--LLFPHLSVGENLafalPPTIGRAQ---RRARVEQALE---EAGLAGFADR---DPATL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523689182 159 SGGmlQRAMIAM--ALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGvAAEVADRI 228
Cdd:COG4136 135 SGG--QRARVALlrALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE-DAPAAGRV 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
8-247 |
6.94e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.87 E-value: 6.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFRRGGK-AVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRsllrlHPKGTLIEGGMTVDGHDIMSLSNRA 86
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQ-----HLNGLLQPTEGKVTVGDIVVSSTSK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSDLRGA--VVSMVFQEPRLALdpvytvgrqIEETIMRHEKV---SRGLAAERALALF-QKVRIPSPERRL-SNYPHEMS 159
Cdd:PRK13643 76 QKEIKPVrkKVGVVFQFPESQL---------FEETVLKDVAFgpqNFGIPKEKAEKIAaEKLEMVGLADEFwEKSPFELS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 160 GGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQrEYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEE 239
Cdd:PRK13643 147 GGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISC 225
|
....*...
gi 523689182 240 GLVGDIIR 247
Cdd:PRK13643 226 GTPSDVFQ 233
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
23-248 |
1.13e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.10 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 23 KAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTlieGGMTVDGHDI--MSLSNRALsdlRGavVSMVFQ 100
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA---GNIIIDDEDIslLPLHARAR---RG--IGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 101 EP----RLALDPVYTVGRQIEETIMRHEKvsrglaAERALALFQKVRIpspERRLSNYPHEMSGGMLQRAMIAMALACNP 176
Cdd:PRK10895 86 EAsifrRLSVYDNLMAVLQIRDDLSAEQR------EDRANELMEEFHI---EHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523689182 177 KVLLADEPTTALDATVQIQILLLIRELqREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIRN 248
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-237 |
2.81e-19 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 84.24 E-value: 2.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 13 NLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTLIEGGMTVDGHDIMSLSNRALSDlrg 92
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKEFAEKYPGE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 93 avVSMVFQEPRLalDPVYTVGRQIEETI-MRHEKVSRGLaaeralalfqkvripsperrlsnyphemSGGMLQRAMIAMA 171
Cdd:cd03233 85 --IIYVSEEDVH--FPTLTVRETLDFALrCKGNEFVRGI----------------------------SGGERKRVSIAEA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523689182 172 LACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAA-EVADRIAVMYAGRIV 237
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIyDLFDKVLVLYEGRQI 199
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
9-240 |
3.27e-19 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 83.75 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRG-GKAVKAV-NGVSLSVKPGEVVALLGESGSGKSVTMRSLL-RLHPKGtlIEGGMTVDGHDIMSLSNR 85
Cdd:cd03213 4 LSFRNLTVTVKSSpSKSGKQLlKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLG--VSGEVLINGRPLDKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 ALSdlrgavvSMVFQEprLALDPVYTVgrqiEETIMRHEKVsRGLaaeralalfqkvripsperrlsnyphemSGGMLQR 165
Cdd:cd03213 82 KII-------GYVPQD--DILHPTLTV----RETLMFAAKL-RGL----------------------------SGGERKR 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523689182 166 AMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDigVAAEV---ADRIAVMYAGRIVEEG 240
Cdd:cd03213 120 VSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQ--PSSEIfelFDKLLLLSQGRVIYFG 194
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-240 |
4.67e-19 |
|
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: 84.20 E-value: 4.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGKAVKavnGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMSLSNRALS 88
Cdd:cd03254 3 IEFENVNFSYDEKKPVLK---DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ---KGQILIDGIDIRDISRKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 DLrgavVSMVFQEPRLaldpvytvgrqIEETIMRHEKVSRGLA-AERALALFQKVRIPSPERRLSN-YPHEMS--GGML- 163
Cdd:cd03254 77 SM----IGVVLQDTFL-----------FSGTIMENIRLGRPNAtDEEVIEAAKEAGAHDFIMKLPNgYDTVLGenGGNLs 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 164 --QRAMIAMALAC--NPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIGVAAEvADRIAVMYAGRIVEE 239
Cdd:cd03254 142 qgERQLLAIARAMlrDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEE 218
|
.
gi 523689182 240 G 240
Cdd:cd03254 219 G 219
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-249 |
7.52e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 84.43 E-value: 7.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 3 MQNDAMIDISNLSvtFRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRLHPKGTLIEGG-MTVDGHDIMS 81
Cdd:PRK11831 2 QSVANLVDMRGVS--FTRGNRCI--FDNISLTVPRGKITAIMGPSGIGKT----TLLRLIGGQIAPDHGeILFDGENIPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 82 LSNRALSDLRGAVvSMVFQEPRLALDpvYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIPSPERRLsnyPHEMSGG 161
Cdd:PRK11831 74 MSRSRLYTVRKRM-SMLFQSGALFTD--MNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 162 MLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGL 241
Cdd:PRK11831 148 MARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGS 227
|
....*...
gi 523689182 242 VGDIIRNP 249
Cdd:PRK11831 228 AQALQANP 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-240 |
2.80e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 85.24 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFrrggKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSL----------------LRLHPKGTLIE--- 69
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptsgriiyhVALCEKCGYVErps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 70 ----------GGMTVDGHDIMSLSNRALSDLRGAVVSMvFQEPrLALdpvYTVGRQIEETIMRHEKV--SRGLAAERALA 137
Cdd:TIGR03269 77 kvgepcpvcgGTLEPEEVDFWNLSDKLRRRIRKRIAIM-LQRT-FAL---YGDDTVLDNVLEALEEIgyEGKEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 138 LFQKVRIpspERRLSNYPHEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHD 217
Cdd:TIGR03269 152 LIEMVQL---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHW 228
|
250 260
....*....|....*....|...
gi 523689182 218 IGVAAEVADRIAVMYAGRIVEEG 240
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKEEG 251
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
30-240 |
3.32e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.16 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 30 GVSLSVKPGEVVALLGESGSGKSVTMRSLLRLH-PKGtlieGGMTVDGHDIMSLSNRALSdlrgAVVSMVFQEPRLaldp 108
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYqPTG----GQVLLDGVPLVQYDHHYLH----RQVALVGQEPVL---- 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 109 vytVGRQIEETIM----RHEKVSRGLAAERALAlfqkvripspERRLSNYPH-----------EMSGGMLQRAMIAMALA 173
Cdd:TIGR00958 567 ---FSGSVRENIAygltDTPDEEIMAAAKAANA----------HDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523689182 174 CNPKVLLADEPTTALDATVQiqilLLIRELQREYGLSVIFVTHDIGVaAEVADRIAVMYAGRIVEEG 240
Cdd:TIGR00958 634 RKPRVLILDEATSALDAECE----QLLQESRSRASRTVLLIAHRLST-VERADQILVLKKGSVVEMG 695
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
7-239 |
5.30e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.46 E-value: 5.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 7 AMIDISNLSVTFrrgGKaVKAVNGVSLSVKPGEVVALLGESGSGKSvTMRSLLRLHPKGTliEGGMTVDGHDIMSLSNRA 86
Cdd:PRK11614 4 VMLSFDKVSAHY---GK-IQALHEVSLHINQGEIVTLIGANGAGKT-TLLGTLCGDPRAT--SGRIVFDGKDITDWQTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSDLRGAVV-------SMVFQEPRLALDPVYTVGRQIEETImrhekvsrglaaERALALFQKVRipspERRLSNyPHEMS 159
Cdd:PRK11614 77 IMREAVAIVpegrrvfSRMTVEENLAMGGFFAERDQFQERI------------KWVYELFPRLH----ERRIQR-AGTMS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 160 GGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELqREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEE 239
Cdd:PRK11614 140 GGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-236 |
5.45e-18 |
|
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: 79.95 E-value: 5.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 16 VTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDImslsNRALSDLRGAVV 95
Cdd:cd03246 6 VSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT---SGRVRLDGADI----SQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 96 SMVFQEPRLaldpvytvgrqIEETImrhekvsrglaAERALalfqkvripsperrlsnyphemSGGMLQRAMIAMALACN 175
Cdd:cd03246 79 GYLPQDDEL-----------FSGSI-----------AENIL----------------------SGGQRQRLGLARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523689182 176 PKVLLADEPTTALDATVQIQILLLIRELqREYGLSVIFVTHDIGVAAEvADRIAVMYAGRI 236
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
8-247 |
5.76e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.67 E-value: 5.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFRRGGKA------------------VKAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRL-----HP- 63
Cdd:COG1134 4 MIEVENVSKSYRLYHEPsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKS----TLLKLiagilEPt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 64 KGTLIeggmtvdghdimslsnralsdLRGAVVSMVfqEPRLALDP-------VYTVGRqieetIMrhekvsrGLAAERAL 136
Cdd:COG1134 80 SGRVE---------------------VNGRVSALL--ELGAGFHPeltgrenIYLNGR-----LL-------GLSRKEID 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 137 ALFQKVR--------IPSPerrLSNYphemSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyG 208
Cdd:COG1134 125 EKFDEIVefaelgdfIDQP---VKTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-G 196
|
250 260 270
....*....|....*....|....*....|....*....
gi 523689182 209 LSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDIIR 247
Cdd:COG1134 197 RTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-240 |
5.91e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.98 E-value: 5.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 3 MQNdaMIDISNLSVTFRRGgkavKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLlrlhpkGTLIEGGMTVDGH----- 77
Cdd:PRK09984 1 MQT--IIRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHL------SGLITGDKSAGSHiellg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 78 DIMSLSNRALSDLRG--AVVSMVFQE----PRLALDPVYTVG--------RQIEETIMRHEKvsrglaaERALALFQKVR 143
Cdd:PRK09984 69 RTVQREGRLARDIRKsrANTGYIFQQfnlvNRLSVLENVLIGalgstpfwRTCFSWFTREQK-------QRALQALTRVG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 144 IPS-PERRLSNypheMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAA 222
Cdd:PRK09984 142 MVHfAHQRVST----LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAL 217
|
250
....*....|....*...
gi 523689182 223 EVADRIAVMYAGRIVEEG 240
Cdd:PRK09984 218 RYCERIVALRQGHVFYDG 235
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-240 |
6.95e-18 |
|
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: 80.78 E-value: 6.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 18 FRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTLIEGGMTVDGhdimSLSNRALSDLRgavVSM 97
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNG----QPRKPDQFQKC---VAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 98 VFQEPRLAldPVYTVgrqiEETIM--------RH--EKVSRGLAAERALALFQKVRIPSPERRlsnyphEMSGGMLQRAM 167
Cdd:cd03234 86 VRQDDILL--PGLTV----RETLTytailrlpRKssDAIRKKRVEDVLLRDLALTRIGGNLVK------GISGGERRRVS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523689182 168 IAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAA-EVADRIAVMYAGRIVEEG 240
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQPRSDLfRLFDRILLLSSGEIVYSG 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-246 |
9.25e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.16 E-value: 9.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 7 AMIDISNlsVTFRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRL-HPKGtlieGGMTVDGHDIMSLSNR 85
Cdd:PRK13537 6 APIDFRN--VEKRYGDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLtHPDA----GSISLCGEPVPSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 ALSdlRGAVVsmvfqePRL-ALDPVYTVgRQIEETIMRHEKVSRGLAAERALALFQKVRIpspERRLSNYPHEMSGGMLQ 164
Cdd:PRK13537 78 ARQ--RVGVV------PQFdNLDPDFTV-RENLLVFGRYFGLSAAAARALVPPLLEFAKL---ENKADAKVGELSGGMKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 165 RAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGD 244
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHA 224
|
..
gi 523689182 245 II 246
Cdd:PRK13537 225 LI 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
9-240 |
1.00e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.72 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNlsVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRL-----HPKgtliEGGMTVDGHDIMSLS 83
Cdd:PRK11160 339 LTLNN--VSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLltrawDPQ----QGEILLNGQPIADYS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 84 NralSDLRGAVvSMVFQEprlaldpVYTVGRQIEETIMrhekvsrgLAAERA-----LALFQKV---RIPSPERRLSNYP 155
Cdd:PRK11160 409 E---AALRQAI-SVVSQR-------VHLFSATLRDNLL--------LAAPNAsdealIEVLQQVgleKLLEDDKGLNAWL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 156 HE----MSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIgVAAEVADRIAVM 231
Cdd:PRK11160 470 GEggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRL-TGLEQFDRICVM 546
|
....*....
gi 523689182 232 YAGRIVEEG 240
Cdd:PRK11160 547 DNGQIIEQG 555
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-246 |
2.30e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.42 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFrrGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMSLSNRALS 88
Cdd:PRK13536 42 IDLAGVSKSY--GDKAV--VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD---AGKITVLGVPVPARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 dlRGAVVSMvFQEprlaLDPVYTVgrqiEETIMRHEKVSRGLAAERALALFQKVRIPSPERRLSNYPHEMSGGMLQRAMI 168
Cdd:PRK13536 115 --RIGVVPQ-FDN----LDLEFTV----RENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523689182 169 AMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDII 246
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-240 |
2.70e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 82.46 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGKAVKAVNgvsLSVKPGEVVALLGESGSGKSvTMRSLLR-LHPkgtLIEGGMTVDGHDIMSLSNRAL 87
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNIN---LSVPSRGFVALVGHTGSGKS-TLASLLMgYYP---LTEGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 SDlrgaVVSMVFQEPRLALDPVY---TVGRQIEEtimrhEKVSRGLAAERaLALFQKVRIPSPERRLSNYPHEMSGGmlQ 164
Cdd:PRK10790 414 RQ----GVAMVQQDPVVLADTFLanvTLGRDISE-----EQVWQALETVQ-LAELARSLPDGLYTPLGEQGNNLSVG--Q 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523689182 165 RAMIAMA--LACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIfvTHDIGVAAEvADRIAVMYAGRIVEEG 240
Cdd:PRK10790 482 KQLLALArvLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVI--AHRLSTIVE-ADTILVLHRGQAVEQG 556
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-245 |
4.03e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.59 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 25 VKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPK--GTLIEGGMTVdghdimSLSNRALSDLRGavVSMVFQEp 102
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRdaGSILYLGKEV------TFNGPKSSQEAG--IGIIHQE- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 103 rLALDPVYTVGRQIeetIMRHEKVSR-------GLAAErALALFQKVRIP-SPERRLSnyphEMSGGMLQRAMIAMALAC 174
Cdd:PRK10762 88 -LNLIPQLTIAENI---FLGREFVNRfgridwkKMYAE-ADKLLARLNLRfSSDKLVG----ELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523689182 175 NPKVLLADEPTTALDATVQIQILLLIRELqREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDI 245
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
27-231 |
4.29e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.04 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 27 AVNGVSLSVKPGEVVALLGESGSGKSVTMRSLlrlhpKGTLIEGGMTVDGHdimslsnralsdlRGAVVSMVFQepRLAL 106
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVL-----AGVLRPTSGTVRRA-------------GGARVAYVPQ--RSEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 107 DP--------VYTVGRQIEETIMRHEKVSRGLAAERALAlfqKVRIpspeRRLSNYP-HEMSGGMLQRAMIAMALACNPK 177
Cdd:NF040873 67 PDslpltvrdLVAMGRWARRGLWRRLTRDDRAAVDDALE---RVGL----ADLAGRQlGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 523689182 178 VLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEvADRIAVM 231
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
11-240 |
5.02e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.96 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 11 ISNLSVTFrrGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSvTMRSLLRLHPKGTLIEGGMTVDGHDIMSLS--NRALs 88
Cdd:COG0396 3 IKNLHVSV--EGKEI--LKGVNLTIKPGEVHAIMGPNGSGKS-TLAKVLMGHPKYEVTSGSILLDGEDILELSpdERAR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 dlRGavVSMVFQEP------------RLALdpvytvgrqieeTIMRHEKVSRGLAAERALALFQKVRIPspERRLSNYPH 156
Cdd:COG0396 77 --AG--IFLAFQYPveipgvsvsnflRTAL------------NARRGEELSAREFLKLLKEKMKELGLD--EDFLDRYVN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 157 E-MSGGMLQRAMIAMALACNPKVLLADEPTTALDA-TVQIqILLLIRELQREyGLSVIFVTH------DIgvaaeVADRI 228
Cdd:COG0396 139 EgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHyqrildYI-----KPDFV 211
|
250
....*....|..
gi 523689182 229 AVMYAGRIVEEG 240
Cdd:COG0396 212 HVLVDGRIVKSG 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-236 |
8.62e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.88 E-value: 8.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 11 ISNLSVTFrrGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRLhpkgtlIEGGMTVDGHDImSLSnralsdl 90
Cdd:COG0488 1 LENLSKSF--GGRPL--LDDVSLSINPGDRIGLVGRNGAGKS----TLLKI------LAGELEPDSGEV-SIP------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 91 RGAVVSMVFQEPRL------------ALDPVYTVGRQIEE----------TIMRHEKVSRGLAAE-------RALALFQK 141
Cdd:COG0488 59 KGLRIGYLPQEPPLdddltvldtvldGDAELRALEAELEEleaklaepdeDLERLAELQEEFEALggweaeaRAEEILSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 142 VRIPS--PERRLSnyphEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVqiqILLLIRELQReYGLSVIFVTHDIG 219
Cdd:COG0488 139 LGFPEedLDRPVS----ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEWLEEFLKN-YPGTVLVVSHDRY 210
|
250
....*....|....*..
gi 523689182 220 VAAEVADRIAVMYAGRI 236
Cdd:COG0488 211 FLDRVATRILELDRGKL 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-217 |
1.43e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.45 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 16 VTFRRGGKavKAVNGVSLSVKPGEVVALLGESGSGKSVTMR---SLLRlhPKgtliEGGMTVDGHDIMSLSNRALSDLrg 92
Cdd:PRK10247 13 VGYLAGDA--KILNNISFSLRAGEFKLITGPSGCGKSTLLKivaSLIS--PT----SGTLLFEGEDISTLKPEIYRQQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 93 avVSMVFQEPRLALDPVY---TVGRQIEETIMRHEKVSRGLAaeralalfqkvRIPSPERRLSNYPHEMSGGMLQRAMIA 169
Cdd:PRK10247 83 --VSYCAQTPTLFGDTVYdnlIFPWQIRNQQPDPAIFLDDLE-----------RFALPDTILTKNIAELSGGEKQRISLI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 523689182 170 MALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHD 217
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-236 |
1.61e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 79.87 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 25 VKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtlIEGGMTVDGHDImslSNRALSDLRGAVVSMVFQE-PR 103
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGK--FEGNVFINGKPV---DIRNPAQAIRAGIAMVPEDrKR 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 104 LALDPVYTVGRQIEETIM-RHEKVSRGLAAERALALFQ-----KVRIPSPERRLSNypheMSGGMLQRAMIAMALACNPK 177
Cdd:TIGR02633 348 HGIVPILGVGKNITLSVLkSFCFKMRIDAAAELQIIGSaiqrlKVKTASPFLPIGR----LSGGNQQKAVLAKMLLTNPR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 523689182 178 VLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRI 236
Cdd:TIGR02633 424 VLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-240 |
3.12e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.32 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 29 NGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTLIEGGMTVDGHDIMSLSNRALSdlrgAVVsmvfQEPRLALdP 108
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDAKEMRAIS----AYV----QQDDLFI-P 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 109 VYTVGRQIeeTIMRHEKVSRGLAAE----------RALALF--QKVRIPSPERRLSnypheMSGGMLQRAMIAMALACNP 176
Cdd:TIGR00955 113 TLTVREHL--MFQAHLRMPRRVTKKekrervdevlQALGLRkcANTRIGVPGRVKG-----LSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523689182 177 KVLLADEPTTALDATVQIQILLLIREL-QReyGLSVIFVTH----DIgvaAEVADRIAVMYAGRIVEEG 240
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGLaQK--GKTIICTIHqpssEL---FELFDKIILMAEGRVAYLG 249
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
29-240 |
3.62e-16 |
|
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: 79.09 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 29 NGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLH-PKGtlieGGMTVDGHDIMSLSnraLSDLRGAVvSMVFQEPRLALD 107
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYdVTS----GRILIDGQDIRDVT---QASLRAAI-GIVPQDTVLFND 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 108 pvyTVGRQI--------EETIMRhekvsrglAAERA------LALFQKVRIPSPERRLsnyphEMSGGMLQRAMIAMALA 173
Cdd:COG5265 447 ---TIAYNIaygrpdasEEEVEA--------AARAAqihdfiESLPDGYDTRVGERGL-----KLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523689182 174 CNPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIGVAAEvADRIAVMYAGRIVEEG 240
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-236 |
3.68e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.82 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 25 VKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTliEGGMTVDGHDImslSNRALSDLRGAVVSMVFQE-PR 103
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRW--EGEIFIDGKPV---KIRNPQQAIAQGIAMVPEDrKR 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 104 LALDPVYTVGRQIeeTIMRHEKVSRG----LAAERALALFQ----KVRIPSPERRLSNypheMSGGMLQRAMIAMALACN 175
Cdd:PRK13549 350 DGIVPVMGVGKNI--TLAALDRFTGGsridDAAELKTILESiqrlKVKTASPELAIAR----LSGGNQQKAVLAKCLLLN 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523689182 176 PKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRI 236
Cdd:PRK13549 424 PKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-240 |
1.20e-15 |
|
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: 74.37 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 6 DAMIDISNLSVtfRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHpkgTLIEGGMTVDGHDIMSLSnr 85
Cdd:cd03369 4 HGEIEVENLSV--RYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFL---EAEEGKIEIDGIDISTIP-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 aLSDLRGAvVSMVFQEP-------RLALDPvytVGRQIEETIMRHEKVSRGlaaeralalfqkvripsperrLSNypheM 158
Cdd:cd03369 77 -LEDLRSS-LTIIPQDPtlfsgtiRSNLDP---FDEYSDEEIYGALRVSEG---------------------GLN----L 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 159 SGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIGVAAEVaDRIAVMYAGRIVE 238
Cdd:cd03369 127 SQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKE 203
|
..
gi 523689182 239 EG 240
Cdd:cd03369 204 YD 205
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-217 |
1.43e-15 |
|
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: 77.02 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 16 VTFRRGGKAVkAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgtlIEGGMTVDGHDIMSLSNRALSdlrgAVV 95
Cdd:TIGR02868 340 LSAGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP---LQGEVTLDGVPVSSLDQDEVR----RRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 96 SMVFQEPRLaldpvytvgrqIEETIMRHEKVSRGLAA-ERALALFQKVRIPSPERRL----SNYPHEM----SGGMLQRA 166
Cdd:TIGR02868 412 SVCAQDAHL-----------FDTTVRENLRLARPDATdEELWAALERVGLADWLRALpdglDTVLGEGgarlSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 523689182 167 MIAMALACNPKVLLADEPTTALDATVQIQILLLIreLQREYGLSVIFVTHD 217
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
13-238 |
1.83e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.87 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 13 NLSVTFrrggKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTlieGGMTVDGHDIMSLSNRALSDlrg 92
Cdd:PRK11288 9 GIGKTF----PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDA---GSILIDGQEMRFASTTAALA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 93 AVVSMVFQEprLALDPVYTVGrqieETIM------RHEKVSRGLAAERALALFQK--VRIpSPERRLSnyphEMSGGmlQ 164
Cdd:PRK11288 79 AGVAIIYQE--LHLVPEMTVA----ENLYlgqlphKGGIVNRRLLNYEAREQLEHlgVDI-DPDTPLK----YLSIG--Q 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523689182 165 RAM--IAMALACNPKVLLADEPTTALDATvQIQILL-LIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVE 238
Cdd:PRK11288 146 RQMveIAKALARNARVIAFDEPTSSLSAR-EIEQLFrVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-231 |
2.00e-15 |
|
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: 72.10 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFrrGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRLhpkgtlIEGGMTVDghdimslsnrals 88
Cdd:cd03221 1 IELENLSKTY--GGKLL--LKDISLTINPGDRIGLVGRNGAGKS----TLLKL------IAGELEPD------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 dlrgavvsmvfqEPRLALDPVYTVGrqieetimrhekvsrglaaeralalfqkvripsperrlsnYPHEMSGGMLQRAMI 168
Cdd:cd03221 54 ------------EGIVTWGSTVKIG----------------------------------------YFEQLSGGEKMRLAL 81
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523689182 169 AMALACNPKVLLADEPTTALDATvqiQILLLIRELQREYGlSVIFVTHDIGVAAEVADRIAVM 231
Cdd:cd03221 82 AKLLLENPNLLLLDEPTNHLDLE---SIEALEEALKEYPG-TVILVSHDRYFLDQVATKIIEL 140
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-240 |
2.75e-15 |
|
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: 73.72 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGKA------------------VKAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRLhpkgtlIEG 70
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgeFWALKDVSFEVPRGERIGLIGRNGAGKS----TLLRL------LAG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 71 GMTVDGHDImslsnralsDLRGAVVSMVfqEPRLALDPVYTvGRqiEETIMRHekVSRGLAAERALALFQKV-------- 142
Cdd:cd03220 71 IYPPDSGTV---------TVRGRVSSLL--GLGGGFNPELT-GR--ENIYLNG--RLLGLSRKEIDEKIDEIiefselgd 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 143 RIPSPERRLSNyphemsgGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAA 222
Cdd:cd03220 135 FIDLPVKTYSS-------GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIK 206
|
250
....*....|....*...
gi 523689182 223 EVADRIAVMYAGRIVEEG 240
Cdd:cd03220 207 RLCDRALVLEKGKIRFDG 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-239 |
3.12e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.20 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 28 VNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMSLSNRA--------LSDLR---GAVVS 96
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRT---SGYVTLDGHEVVTRSPQDglangivyISEDRkrdGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 97 MVFQE--PRLALDPVYTVGRQIeetimRHEKvsRGLAAERALALFqKVRIPSPERRLSNypheMSGGMLQRAMIAMALAC 174
Cdd:PRK10762 345 MSVKEnmSLTALRYFSRAGGSL-----KHAD--EQQAVSDFIRLF-NIKTPSMEQAIGL----LSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523689182 175 NPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEE 239
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRISGE 476
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-245 |
3.53e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 74.27 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 28 VNGVSLSVKPGEVVALLGESGSGKS---VTMRSLLRLHpKGTLIEGGMTVDghdimsLSNRALSDLRGAVVSmVFQEPRL 104
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKStlfMNLSGLLRPQ-KGAVLWQGKPLD------YSKRGLLALRQQVAT-VFQDPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 105 ALdpVYTvgrQIEETI---MRHEKVSRGLAAER---ALALFQKvripspeRRLSNYPHE-MSGGMLQRAMIAMALACNPK 177
Cdd:PRK13638 89 QI--FYT---DIDSDIafsLRNLGVPEAEITRRvdeALTLVDA-------QHFRHQPIQcLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523689182 178 VLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDI 245
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
3-240 |
1.48e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 3 MQNDAMIDISNLSVTFRRGGKAVKavnGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHpkgTLIEGGMTVDGHDImsl 82
Cdd:PRK15056 1 MMQQAGIVVNDVTVTWRNGHTALR---DASFTVPGGSIAALVGVNGSGKSTLFKALMGFV---RLASGKISILGQPT--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 83 sNRALsdlRGAVVSMVFQE-------PRLALDpVYTVGRQIEETIMRHEKVSRGLAAERALAlfqkvRIPSPERRLSNYp 155
Cdd:PRK15056 72 -RQAL---QKNLVAYVPQSeevdwsfPVLVED-VVMMGRYGHMGWLRRAKKRDRQIVTAALA-----RVDMVEFRHRQI- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 156 HEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELqREYGLSVIFVTHDIGVAAEVADrIAVMYAGR 235
Cdd:PRK15056 141 GELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD-YTVMVKGT 218
|
....*
gi 523689182 236 IVEEG 240
Cdd:PRK15056 219 VLASG 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-239 |
2.20e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 22 GKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgtlIEGGMTVDGHDImslsnralsdlrgavvsmvfqE 101
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKR---AGGEIRLNGKDI---------------------S 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 102 PRLALDPVYTVGRQIEE-----------TIMRHEKVSRGLAAER---ALALFQKV---RIPSPERRLSNYP--------H 156
Cdd:PRK09700 329 PRSPLDAVKKGMAYITEsrrdngffpnfSIAQNMAISRSLKDGGykgAMGLFHEVdeqRTAENQRELLALKchsvnqniT 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 157 EMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRI 236
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
...
gi 523689182 237 VEE 239
Cdd:PRK09700 488 TQI 490
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
8-218 |
1.81e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFrrGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRL-HPKGTLIEggmtvdghdimslsnra 86
Cdd:PRK09544 4 LVSLENVSVSF--GQRRV--LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLvAPDEGVIK----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 lsdlRGAVVSMVFQEPRLALDPVYTVgrqieeTIMRHEKVSRGLAAERALALFQKVRipspERRLSNYP-HEMSGGMLQR 165
Cdd:PRK09544 63 ----RNGKLRIGYVPQKLYLDTTLPL------TVNRFLRLRPGTKKEDILPALKRVQ----AGHLIDAPmQKLSGGETQR 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 523689182 166 AMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDI 218
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-239 |
2.02e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.71 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 31 VSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgtlIEGGMTVDGHDImslsnrALSDLRGAVVS--MVFQEPRLALD- 107
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRR---TAGQVYLDGKPI------DIRSPRDAIRAgiMLCPEDRKAEGi 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 108 -PVYTVGRQIEETIMRH---------EKVSRGLAAERALALfqKVRIPSPERRLSNypheMSGGMLQRAMIAMALACNPK 177
Cdd:PRK11288 343 iPVHSVADNINISARRHhlragclinNRWEAENADRFIRSL--NIKTPSREQLIMN----LSGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523689182 178 VLLADEPTTALDATVQIQILLLIRELQrEYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEE 239
Cdd:PRK11288 417 VILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
31-246 |
2.81e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.08 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 31 VSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTlieGGMTVDGHDIMSLSNRAL--------------------SDL 90
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARG---GRIMLNGKEINALSTAQRlarglvylpedrqssglyldAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 91 RGAVVSMVFQEPRLALDPVYtvgrqiEETIMRHEKVSRGLAAERAlalfqkvriPSPERRLSnyphemsGGMLQRAMIAM 170
Cdd:PRK15439 359 AWNVCALTHNRRGFWIKPAR------ENAVLERYRRALNIKFNHA---------EQAARTLS-------GGNQQKVLIAK 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523689182 171 ALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEgLVGDII 246
Cdd:PRK15439 417 CLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGA-LTGAAI 490
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-216 |
3.79e-13 |
|
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: 66.88 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 12 SNLSVTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTlIEGGMTVDGHDIMSLSNRalsdlr 91
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGV-ITGEILINGRPLDKNFQR------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 92 gaVVSMVFQEPrlALDPVYTVgrqiEETIMRHekvsrglAAERALALFQKvripspeRRLSnyphemsggmlqramIAMA 171
Cdd:cd03232 80 --STGYVEQQD--VHSPNLTV----REALRFS-------ALLRGLSVEQR-------KRLT---------------IGVE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 523689182 172 LACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTH 216
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIH 166
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-216 |
4.41e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.45 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 4 QNDAMIDISNLSVtFRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTlieGGMTV-DGHDIMSL 82
Cdd:COG4178 358 SEDGALALEDLTL-RTPDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGS---GRIARpAGARVLFL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 83 SNRA---LSDLRGAVVSmvfqePRLAldpvytvgrqieetimrhEKVSRglaaERALALFQKVRIPSPERRLS---NYPH 156
Cdd:COG4178 432 PQRPylpLGTLREALLY-----PATA------------------EAFSD----AELREALEAVGLGHLAERLDeeaDWDQ 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 157 EMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRElqREYGLSVIFVTH 216
Cdd:COG4178 485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-240 |
4.86e-13 |
|
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: 69.39 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 16 VTFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtLIEGGMTVDGHDImSLSNRalsDLRGAVV 95
Cdd:COG4618 336 LTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP---PTAGSVRLDGADL-SQWDR---EELGRHI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 96 SMVFQEPRLaLDpvytvGRqIEETIMRH-----EKVSRglAAERALAlfqkvripsperrlsnypHEM------------ 158
Cdd:COG4618 409 GYLPQDVEL-FD-----GT-IAENIARFgdadpEKVVA--AAKLAGV------------------HEMilrlpdgydtri 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 159 -------SGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELqREYGLSVIFVTHDIGVAAeVADRIAVM 231
Cdd:COG4618 462 geggarlSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLA-AVDKLLVL 539
|
....*....
gi 523689182 232 YAGRIVEEG 240
Cdd:COG4618 540 RDGRVQAFG 548
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-246 |
1.13e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.22 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 25 VKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDI-MSLSNRALSDlrgaVVSMVFQE-- 101
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD---SGSILFQGKEIdFKSSKEALEN----GISMVHQEln 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 102 ---PRLALDPVYtVGRQIEETI-MRHEKVSRglaaeRALALFQKVRIP-SPERRLSNypheMSGGMLQRAMIAMALACNP 176
Cdd:PRK10982 84 lvlQRSVMDNMW-LGRYPTKGMfVDQDKMYR-----DTKAIFDELDIDiDPRAKVAT----LSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523689182 177 KVLLADEPTTALDATVQIQILLLIRELqREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVE----EGLVGDII 246
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIAtqplAGLTMDKI 226
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
25-245 |
1.87e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 67.07 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 25 VKAVNGVSLSVKPGEVVALLGESGSGKSvtmRSLLRLHPKGTliEGGMTVDGHDIMSLSNRALSDLRGA--VVSMVFQEP 102
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**---RGALPAHV*GP--DAGRRPWRF*TWCANRRALRRTIG*hrPVR*GRRES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 103 RLALDPVYTVGRQIEetimrhekVSRGLAAERALALFQKVRIPSPERRLSNyphEMSGGMLQRAMIAMALACNPKVLLAD 182
Cdd:NF000106 101 FSGRENLYMIGR*LD--------LSRKDARARADELLERFSLTEAAGRAAA---KYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523689182 183 EPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDI 245
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
31-240 |
2.26e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.56 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 31 VSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtlIEGGMTVDGhdiMSLSNRALSDLRGAVvSMVFQEPRL----AL 106
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP----YQGSLKING---IELRELDPESWRKHL-SWVGQNPQLphgtLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 107 DPVyTVGR------QIEETIMR---HEKVSR---GLA---AERALALfqkvripsperrlsnyphemSGGMLQRAMIAMA 171
Cdd:PRK11174 441 DNV-LLGNpdasdeQLQQALENawvSEFLPLlpqGLDtpiGDQAAGL--------------------SVGQAQRLALARA 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523689182 172 LACNPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIGVAAEVaDRIAVMYAGRIVEEG 240
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQG 565
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
33-228 |
2.94e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.28 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 33 LSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtLIEGGMTVDGhdimslsnralsDLrgaVVSMVFQEP-RLALDPVYT 111
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVL---LDDGRIIYEQ------------DL---IVARLQQDPpRNVEGTVYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 112 -VGRQIEET---IMRHEKVSRGLA---AERALALFQKV--------------RIP--------SPERRLSnyphEMSGGM 162
Cdd:PRK11147 86 fVAEGIEEQaeyLKRYHDISHLVEtdpSEKNLNELAKLqeqldhhnlwqlenRINevlaqlglDPDAALS----SLSGGW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523689182 163 LQRAMIAMALACNPKVLLADEPTTALDatvqIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRI 228
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRI 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
40-242 |
3.76e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.05 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 40 VVALLGESGSGKSvtmrSLLrlhpkgTLIeGGMTVDGHDIMSLSNRALSDLRGAV--------VSMVFQEPRLAldPVYT 111
Cdd:PRK11144 26 ITAIFGRSGAGKT----SLI------NAI-SGLTRPQKGRIVLNGRVLFDAEKGIclppekrrIGYVFQDARLF--PHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 112 VgrqieETIMRHekvsrGLAAERAlALFQK-VRIPSPERRLSNYPHEMSGGMLQRAMIAMALACNPKVLLADEPTTALDA 190
Cdd:PRK11144 93 V-----RGNLRY-----GMAKSMV-AQFDKiVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 523689182 191 TVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLV 242
Cdd:PRK11144 162 PRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-216 |
1.90e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 7 AMIDISNLSVTFRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHpKGTLIEGgmTVDGHDIMSLSNRA 86
Cdd:COG2401 27 VAIVLEAFGVELRVVERYV--LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL-KGTPVAG--CVDVPDNQFGREAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 87 LSDlrgavvsmvfqeprlALDPVYTVgrqieetimrhekvsrgLAAERALALFQKVRIPSPERRlsnyPHEMSGGMLQRA 166
Cdd:COG2401 102 LID---------------AIGRKGDF-----------------KDAVELLNAVGLSDAVLWLRR----FKELSTGQKFRF 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 523689182 167 MIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTH 216
Cdd:COG2401 146 RLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-240 |
3.83e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.58 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 17 TFRRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSvTMRSLLRLHpkgtlieggMTVDGHDI----MSLSNRALSDLRG 92
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKS-TLLSLIQRH---------FDVSEGDIrfhdIPLTKLQLDSWRS 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 93 --AVVSmvfQEPRLALDpvyTVGRQI-----EETIMRHEKVSRgLAA--ERALALFQKVRIPSPERRLSnypheMSGGML 163
Cdd:PRK10789 390 rlAVVS---QTPFLFSD---TVANNIalgrpDATQQEIEHVAR-LASvhDDILRLPQGYDTEVGERGVM-----LSGGQK 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523689182 164 QRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFVTHDIGVAAEvADRIAVMYAGRIVEEG 240
Cdd:PRK10789 458 QRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRG 531
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-238 |
1.18e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.00 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFrrGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRlhpkgtLIEGGMTVDGHDIMslsnral 87
Cdd:COG0488 315 VLELEGLSKSY--GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKS----TLLK------LLAGELEPDSGTVK------- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 sdlRGAVVSMVF--QEpRLALDPVYTVgrqiEETIMRH-----EKVSRGLAA------ERAlalFQKVRipsperrlsny 154
Cdd:COG0488 374 ---LGETVKIGYfdQH-QEELDPDKTV----LDELRDGapggtEQEVRGYLGrflfsgDDA---FKPVG----------- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 155 phEMSGGmlQRA--MIAMALACNPKVLLADEPTTALD-ATVQIQILLLIrelqrEYGLSVIFVTHDIGVAAEVADRIAVM 231
Cdd:COG0488 432 --VLSGG--EKArlALAKLLLSPPNVLLLDEPTNHLDiETLEALEEALD-----DFPGTVLLVSHDRYFLDRVATRILEF 502
|
....*..
gi 523689182 232 YAGRIVE 238
Cdd:COG0488 503 EDGGVRE 509
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-240 |
1.52e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.99 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 24 AVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTlieGGMTVDGHDIMSLSNrALSDLRGavVSMVFQEPR 103
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS---GTLEIGGNPCARLTP-AKAHQLG--IYLVPQEPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 104 LAldPVYTVGRQIEETIMRHEKVSRGLAAerALALFQkvripsperrlSNYPHEMSGGML-----QRAMIAMALACNPKV 178
Cdd:PRK15439 97 LF--PNLSVKENILFGLPKRQASMQKMKQ--LLAALG-----------CQLDLDSSAGSLevadrQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523689182 179 LLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-232 |
3.37e-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: 59.69 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 34 SVKPGEVVALLGESGSGKSVTMRSLL-RLHPkgTLIEGGMTVDGHDImsLSNRALSDLRGAVVSMVFQEPRLALDPVY-- 110
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAgKLKP--NLGKFDDPPDWDEI--LDEFRGSELQNYFTKLLEGDVKVIVKPQYvd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 111 --------TVGRQIEETIMRH--EKVSRGLAAERALalfqkvripspERRLSNypheMSGGMLQRAMIAMALACNPKVLL 180
Cdd:cd03236 98 lipkavkgKVGELLKKKDERGklDELVDQLELRHVL-----------DRNIDQ----LSGGELQRVAIAAALARDADFYF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 523689182 181 ADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMY 232
Cdd:cd03236 163 FDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-234 |
3.40e-10 |
|
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: 61.18 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 22 GKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLrlhPKGTLIEGGMTVDGHDIMSlsnrALSDLRGavvSMVFQE 101
Cdd:TIGR01257 1949 GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLT---GDTTVTSGDATVAGKSILT----NISDVHQ---NMGYCP 2018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 102 PRLALDPVYTvGRqieETIMRHEKVsRGLAAERalalFQKVRIPSPERR-LSNYPHEM----SGGMLQRAMIAMALACNP 176
Cdd:TIGR01257 2019 QFDAIDDLLT-GR---EHLYLYARL-RGVPAEE----IEKVANWSIQSLgLSLYADRLagtySGGNKRKLSTAIALIGCP 2089
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 523689182 177 KVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAG 234
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-240 |
3.68e-10 |
|
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: 61.18 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 11 ISNLSVTFRRGGKAvkAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTlieGGMTVDGHDIMSlsnrALSDL 90
Cdd:TIGR01257 931 VKNLVKIFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTS---GTVLVGGKDIET----NLDAV 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 91 RGAvvsmvfqeprLALDPVYTV---GRQIEETIMRHEKVSRGLAAERALALFQKVRIPSPERRLSNYPHEMSGGMLQRAM 167
Cdd:TIGR01257 1002 RQS----------LGMCPQHNIlfhHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLS 1071
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523689182 168 IAMALACNPKVLLADEPTTALDATVQIQILLLIreLQREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:TIGR01257 1072 VAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-230 |
4.49e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.57 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 25 VKAVNGVSLSVKPG-----EVVALLGESGSGKSVTMRSLL-RLHPKGTLIEGGMTVdghdimSLSNRALS-DLRGAVVSM 97
Cdd:COG1245 348 TKSYGGFSLEVEGGeiregEVLGIVGPNGIGKTTFAKILAgVLKPDEGEVDEDLKI------SYKPQYISpDYDGTVEEF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 98 VFQeprlaldpvyTVGRQIEETIMRHEkVSRGLAAERALalfqkvripspERRLSnyphEMSGGMLQRAMIAMALACNPK 177
Cdd:COG1245 422 LRS----------ANTDDFGSSYYKTE-IIKPLGLEKLL-----------DKNVK----DLSGGELQRVAIAACLSRDAD 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 523689182 178 VLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAV 230
Cdd:COG1245 476 LYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-240 |
5.72e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.88 E-value: 5.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 2 TMQNDAMIDISNLSVTFrrggKAVKAVNGVSLSVKPGEVVALLGESGSGKSvTMRSLLRLHPKGTLIEGGMTVDGHDIMS 81
Cdd:CHL00131 1 MNKNKPILEIKNLHASV----NENEILKGLNLSINKGEIHAIMGPNGSGKS-TLSKVIAGHPAYKILEGDILFKGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 82 LSNRALSDLRgavVSMVFQEP------------RLALDPVytvgrqieetimrheKVSRGLAAERALALFQKVR-----I 144
Cdd:CHL00131 76 LEPEERAHLG---IFLAFQYPieipgvsnadflRLAYNSK---------------RKFQGLPELDPLEFLEIINeklklV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 145 PSPERRLSNYPHE-MSGGMLQRAMI-AMALAcNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTH-----D 217
Cdd:CHL00131 138 GMDPSFLSRNVNEgFSGGEKKRNEIlQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHyqrllD 215
|
250 260
....*....|....*....|....
gi 523689182 218 -IgvaaeVADRIAVMYAGRIVEEG 240
Cdd:CHL00131 216 yI-----KPDYVHVMQNGKIIKTG 234
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-238 |
9.56e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 9.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLhpkGTLIEGGMTVDGHDIMSLsnrAL 87
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPV--LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRI---VELEKGRIMIDDCDVAKF---GL 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 SDLRgAVVSMVFQEP-------RLALDPvytvgrqieetIMRHEKVSRGLAAERalALFQKVRIPSP---ERRLSNYPHE 157
Cdd:PLN03232 1306 TDLR-RVLSIIPQSPvlfsgtvRFNIDP-----------FSEHNDADLWEALER--AHIKDVIDRNPfglDAEVSEGGEN 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 158 MSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREygLSVIFVTHDIGVAAEvADRIAVMYAGRIV 237
Cdd:PLN03232 1372 FSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS--CTMLVIAHRLNTIID-CDKILVLSSGQVL 1448
|
.
gi 523689182 238 E 238
Cdd:PLN03232 1449 E 1449
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-230 |
1.06e-09 |
|
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: 57.80 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 25 VKAVNGVSLSVKPG-----EVVALLGESGSGKSvTMRSLL--RLHPKgtliEGGMTVDGHDIMSLSNRALSDLRGAVVSM 97
Cdd:cd03237 7 KKTLGEFTLEVEGGsisesEVIGILGPNGIGKT-TFIKMLagVLKPD----EGDIEIELDTVSYKPQYIKADYEGTVRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 98 VFQE-PRLALDPVYTVgrqieetimrheKVSRGLAAERALalfqkvripspERRLSnyphEMSGGMLQRAMIAMALACNP 176
Cdd:cd03237 82 LSSItKDFYTHPYFKT------------EIAKPLQIEQIL-----------DREVP----ELSGGELQRVAIAACLSKDA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 523689182 177 KVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAV 230
Cdd:cd03237 135 DIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-218 |
1.41e-09 |
|
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: 59.15 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 5 NDAMIDISNLSVTFRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgtliEGGMTVDGHDIMSLSN 84
Cdd:TIGR01271 1214 SGGQMDVQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST----EGEIQIDGVSWNSVTL 1287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 85 RALSDLRGAVVSMVF---QEPRLALDPvytVGRQIEETIMrheKVSRGLAAERALALFqkvripsPER---RLSNYPHEM 158
Cdd:TIGR01271 1288 QTWRKAFGVIPQKVFifsGTFRKNLDP---YEQWSDEEIW---KVAEEVGLKSVIEQF-------PDKldfVLVDGGYVL 1354
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523689182 159 SGGMLQRAMIAMALACNPKVLLADEPTTALDAtVQIQILLliRELQREYG-LSVIFVTHDI 218
Cdd:TIGR01271 1355 SNGHKQLMCLARSILSKAKILLLDEPSAHLDP-VTLQIIR--KTLKQSFSnCTVILSEHRV 1412
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
30-255 |
1.95e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 30 GVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHpkgTLIEGGMTVDGHDIMSLsnrALSDLRgAVVSMVFQEP------- 102
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIV---ELERGRILIDGCDISKF---GLMDLR-KVLGIIPQAPvlfsgtv 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 103 RLALDPV---------YTVGR-QIEETIMRHekvSRGLAAEralalfqkvripsperrLSNYPHEMSGGMLQRAMIAMAL 172
Cdd:PLN03130 1330 RFNLDPFnehndadlwESLERaHLKDVIRRN---SLGLDAE-----------------VSEAGENFSVGQRQLLSLARAL 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 173 ACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIfvTHDIGVAAEvADRIAVMYAGRIVEEGLVGDIIRNPRHP 252
Cdd:PLN03130 1390 LRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLII--AHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEGSA 1466
|
...
gi 523689182 253 YTK 255
Cdd:PLN03130 1467 FSK 1469
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-240 |
3.40e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.48 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 31 VSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgtliEGGMTVDGHDIMSLSNRALSDLRGAVVSmvfQEPRLALDPVY 110
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG----SGSIQFAGQPLEAWSAAELARHRAYLSQ---QQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 111 tvgrqieETIMRHEKVSRGLAAERALA--LFQKVRIpspERRLSNYPHEMSGGMLQRAMIAMAL-----ACNP--KVLLA 181
Cdd:PRK03695 88 -------QYLTLHQPDKTRTEAVASALneVAEALGL---DDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 523689182 182 DEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEG 240
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASG 215
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-250 |
4.15e-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: 57.49 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 28 VNGVSL----SVKPGEVVALLGESGSGKSVTMRSLlrlhpKGTLI----EGGMTVDGHDImslsnraLSDLRGAVVSMVF 99
Cdd:COG1245 85 ENGFRLyglpVPKKGKVTGILGPNGIGKSTALKIL-----SGELKpnlgDYDEEPSWDEV-------LKRFRGTELQDYF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 100 Q-----EPRLALDP--VYTVGRQIEETIMR-HEKV-SRGLAAEralaLFQKVRI-PSPERRLSnyphEMSGGMLQRAMIA 169
Cdd:COG1245 153 KklangEIKVAHKPqyVDLIPKVFKGTVRElLEKVdERGKLDE----LAEKLGLeNILDRDIS----ELSGGELQRVAIA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 170 MALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAAEVADRIAVMYAgrivEEGLVGdIIRNP 249
Cdd:COG1245 225 AALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILYG----EPGVYG-VVSKP 298
|
.
gi 523689182 250 R 250
Cdd:COG1245 299 K 299
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-240 |
6.64e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.26 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGKAvkAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKgtlIEGGMTVDGHdimslsnrals 88
Cdd:TIGR00957 637 ITVHNATFTWARDLPP--TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK---VEGHVHMKGS----------- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 dlrgavVSMVFQEPRLALDPVYT---VGRQIEETIMRhekvsrglAAERALALFQKVRI-PSPER-RLSNYPHEMSGGML 163
Cdd:TIGR00957 701 ------VAYVPQQAWIQNDSLREnilFGKALNEKYYQ--------QVLEACALLPDLEIlPSGDRtEIGEKGVNLSGGQK 766
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523689182 164 QRAMIAMALACNPKVLLADEPTTALDATVQIQIL-LLIRELQREYGLSVIFVTHDIGVAAEVaDRIAVMYAGRIVEEG 240
Cdd:TIGR00957 767 QRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
9-218 |
8.33e-09 |
|
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: 55.63 E-value: 8.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLhpkgTLIEGGMTVDGHDIMSLSNRALS 88
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL----LNTEGDIQIDGVSWNSVPLQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 DLRGAVVSMVF---QEPRLALDPvytVGRQIEETIMRhekvsrgLAAERALALFQKVRIPSPERRLSNYPHEMSGGMLQR 165
Cdd:cd03289 77 KAFGVIPQKVFifsGTFRKNLDP---YGKWSDEEIWK-------VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 523689182 166 AMIAMALACNPKVLLADEPTTALDAtVQIQILLliRELQREY-GLSVIFVTHDI 218
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDP-ITYQVIR--KTLKQAFaDCTVILSEHRI 197
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
8-240 |
8.41e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.18 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVTFRrgGKAVkaVNGVSLSVKPGEVVALLGESGSGKSvTMRSLLRLHPKGTLIEGGMTVDGHDIMSLSNral 87
Cdd:PRK09580 1 MLSIKDLHVSVE--DKAI--LRGLNLEVRPGEVHAIMGPNGSGKS-TLSATLAGREDYEVTGGTVEFKGKDLLELSP--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 SDLRGAVVSMVFQEprlaldPVYTVGRQIEETIMRHEKVSRGLAAERALALFQKVRIPSPERRLSNYPHEM--------- 158
Cdd:PRK09580 73 EDRAGEGIFMAFQY------PVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLltrsvnvgf 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 159 SGGMLQRAMIAMALACNPKVLLADEPTTALDatvqIQILLLIRE---LQREYGLSVIFVTHDIGVAAEVA-DRIAVMYAG 234
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLD----IDALKIVADgvnSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQG 222
|
....*.
gi 523689182 235 RIVEEG 240
Cdd:PRK09580 223 RIVKSG 228
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
9-232 |
1.11e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNL------SVTFRRGgkavkaVNGVSL----SVKPGEVVALLGESGSGKSVTMRSLlrlhpKGTLI------EGGM 72
Cdd:PRK13409 66 ISIVNLpeeleeEPVHRYG------VNGFKLyglpIPKEGKVTGILGPNGIGKTTAVKIL-----SGELIpnlgdyEEEP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 73 TVDghdimslsnRALSDLRGAVVSMVFQ-----EPRLALDPVY----------TVG---RQIEETIMRHEKVSRgLAAER 134
Cdd:PRK13409 135 SWD---------EVLKRFRGTELQNYFKklyngEIKVVHKPQYvdlipkvfkgKVRellKKVDERGKLDEVVER-LGLEN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 135 ALalfqkvripspERRLSNypheMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQReyGLSVIFV 214
Cdd:PRK13409 205 IL-----------DRDISE----LSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVV 267
|
250
....*....|....*...
gi 523689182 215 THDIGVAAEVADRIAVMY 232
Cdd:PRK13409 268 EHDLAVLDYLADNVHIAY 285
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
8-216 |
1.35e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.11 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVtfRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPkgtLIEGGMTVDGHDImslsnrAL 87
Cdd:PRK13539 2 MLEGEDLAC--VRGGRVL--FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP---PAAGTIKLDGGDI------DD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 SDLRGAvvsMVFQEPRLALDPVYTVGRQIEetIMRHEKVSRGLAAERALALFQkvripsperrLSNYPH----EMSGGML 163
Cdd:PRK13539 69 PDVAEA---CHYLGHRNAMKPALTVAENLE--FWAAFLGGEELDIAAALEAVG----------LAPLAHlpfgYLSAGQK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 523689182 164 QRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRElQREYGLSVIFVTH 216
Cdd:PRK13539 134 RRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA-HLAQGGIVIAATH 185
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
157-232 |
1.66e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 53.34 E-value: 1.66e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523689182 157 EMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAVMY 232
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-241 |
2.78e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.11 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 25 VKAVNGVslsVKPGEVVALLGESGSGKSVTMRSLL-RLHPKGTLIEGGMTVDGHDIMSLSNRalsdLRGAVVSMVFQEPR 103
Cdd:TIGR00956 77 LKPMDGL---IKPGELTVVLGRPGSGCSTLLKTIAsNTDGFHIGVEGVITYDGITPEEIKKH----YRGDVVYNAETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 104 LaldPVYTVGRQIEETIM------RHEKVSRGLAAERALALFQKVRIPSPERRlSNYPHEM----SGGMLQRAMIAMALA 173
Cdd:TIGR00956 150 F---PHLTVGETLDFAARcktpqnRPDGVSREEYAKHIADVYMATYGLSHTRN-TKVGNDFvrgvSGGERKRVSIAEASL 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523689182 174 CNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSViFVThdIGVAAEVA----DRIAVMYAGRIVEEGL 241
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTP-LVA--IYQCSQDAyelfDKVIVLYEGYQIYFGP 294
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-239 |
4.73e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.03 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 26 KAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRlHPKGTLIEGGMTVDGHDImslsnrALSDLRGAV------VSmvf 99
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG-RSYGRNISGTVFKDGKEV------DVSTVSDAIdaglayVT--- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 100 qEPR--LALDPVYTVGRQIeeTIMRHEKVSRG----LAAERALA--LFQKVRI--PSPERRLSNypheMSGGMLQRAMIA 169
Cdd:NF040905 344 -EDRkgYGLNLIDDIKRNI--TLANLGKVSRRgvidENEEIKVAeeYRKKMNIktPSVFQKVGN----LSGGNQQKVVLS 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523689182 170 MALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHD----IGvaaeVADRIAVMYAGRIVEE 239
Cdd:NF040905 417 KWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSElpelLG----MCDRIYVMNEGRITGE 485
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
9-235 |
9.31e-08 |
|
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: 51.70 E-value: 9.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTF-RRGGKAVKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLrlhpkG--TLIEGGMTVDGHdimslsnr 85
Cdd:cd03250 1 ISVEDASFTWdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALL-----GelEKLSGSVSVPGS-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 86 alsdlrgavVSMVFQEPRLALDpvyTV------GRQIEEtiMRHEKVSRGLAAERALALFqkvripsP--------ERRL 151
Cdd:cd03250 68 ---------IAYVSQEPWIQNG---TIrenilfGKPFDE--ERYEKVIKACALEPDLEIL-------PdgdlteigEKGI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 152 SnypheMSGGmlQRAMIAMALAC--NPKVLLADEPTTALDATVQIQIL--LLIRELQReyGLSVIFVTHDIGVAAEvADR 227
Cdd:cd03250 127 N-----LSGG--QKQRISLARAVysDADIYLLDDPLSAVDAHVGRHIFenCILGLLLN--NKTRILVTHQLQLLPH-ADQ 196
|
....*...
gi 523689182 228 IAVMYAGR 235
Cdd:cd03250 197 IVVLDNGR 204
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-230 |
1.19e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 25 VKAVNGVSLSVKPG-----EVVALLGESGSGKSVTMRsllrlhpkgtLIEGGMTVDGHDimslsnralsdlrgavvsmVF 99
Cdd:PRK13409 347 TKKLGDFSLEVEGGeiyegEVIGIVGPNGIGKTTFAK----------LLAGVLKPDEGE-------------------VD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 100 QEPRLALDPVY-------TVG---RQIEETIM----RHEkVSRGLAAERALalfqkvripspERRLSnyphEMSGGMLQR 165
Cdd:PRK13409 398 PELKISYKPQYikpdydgTVEdllRSITDDLGssyyKSE-IIKPLQLERLL-----------DKNVK----DLSGGELQR 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523689182 166 AMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTHDIGVAAEVADRIAV 230
Cdd:PRK13409 462 VAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-230 |
1.39e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 4 QNDAMIDISNLSVTFRRGGKA-VKAVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLH-------------------- 62
Cdd:PTZ00265 1159 KNDIKGKIEIMDVNFRYISRPnVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtndmtn 1238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 63 -----------------------------PKGTLIE--GGMTVDGHDIMSLSnraLSDLRGaVVSMVFQEPRLALDPVYT 111
Cdd:PTZ00265 1239 eqdyqgdeeqnvgmknvnefsltkeggsgEDSTVFKnsGKILLDGVDICDYN---LKDLRN-LFSIVSQEPMLFNMSIYE 1314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 112 VGRQIEETIMRhEKVSRglaAERALALFQKVR-IPSP-ERRLSNYPHEMSGGMLQRAMIAMALACNPKVLLADEPTTALD 189
Cdd:PTZ00265 1315 NIKFGKEDATR-EDVKR---ACKFAAIDEFIEsLPNKyDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 523689182 190 ATVQIQILLLIRELQREYGLSVIFVTHDIGvAAEVADRIAV 230
Cdd:PTZ00265 1391 SNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIKRSDKIVV 1430
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-217 |
1.53e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.63 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 17 TFRRGGKAV----KAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRlhpkgtlIEGGMTVDghdimsLSNRALSDLrG 92
Cdd:TIGR03719 6 TMNRVSKVVppkkEILKDISLSFFPGAKIGVLGLNGAGKS----TLLR-------IMAGVDKD------FNGEARPQP-G 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 93 AVVSMVFQEPRLalDPVYTVGRQIEE-------TIMRHEKVSRGLAAERAL--ALFQK---------------------- 141
Cdd:TIGR03719 68 IKVGYLPQEPQL--DPTKTVRENVEEgvaeikdALDRFNEISAKYAEPDADfdKLAAEqaelqeiidaadawdldsqlei 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 142 ----VRIPSPERRLSNypheMSGGMLQRAMIAMALACNPKVLLADEPTTALDATvqiQILLLIRELQrEYGLSVIFVTHD 217
Cdd:TIGR03719 146 amdaLRCPPWDADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQ-EYPGTVVAVTHD 217
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-240 |
1.64e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.57 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 28 VNGVSLSVKPGEVVALLGESGSGKSVTMRSLL-RLHpkGTLIEGGMTVDGHDIMSLSNRALsdlrGAVVSMVFQEPRLAL 106
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQ--GNNFTGTILANNRKPTKQILKRT----GFVTQDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 107 DP--VYTVGRQIEETIMRHEK--VSRGLAAERALALFQKVRIPSperrlsNYPHEMSGGMLQRAMIAMALACNPKVLLAD 182
Cdd:PLN03211 158 REtlVFCSLLRLPKSLTKQEKilVAESVISELGLTKCENTIIGN------SFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 523689182 183 EPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGVAA-EVADRIAVMYAGRIVEEG 240
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPSSRVyQMFDSVLVLSEGRCLFFG 289
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
9-216 |
1.90e-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: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGKAVKAVngvSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTlieggmtvdGHDIMSLSNRALs 88
Cdd:cd03223 1 IELENLSLATPDGRVLLKDL---SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGS---------GRIGMPEGEDLL- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 dlrgavvsMVFQEPRLaldPVYTVGRQIeetimrhekvsrglaaeralalfqkvripsperrlsNYP--HEMSGGMLQRA 166
Cdd:cd03223 68 --------FLPQRPYL---PLGTLREQL------------------------------------IYPwdDVLSGGEQQRL 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 523689182 167 MIAMALACNPKVLLADEPTTALDATVQIQILLLIRELqreyGLSVIFVTH 216
Cdd:cd03223 101 AFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL----GITVISVGH 146
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-230 |
3.99e-07 |
|
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: 48.91 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 37 PGEVVALLGESGSGKSVTMRSLLRLhpkgtlieggmtvdghdimslsnraLSDLRGAVVsmvfqepRLALDPVYTVGRQI 116
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARE-------------------------LGPPGGGVI-------YIDGEDILEEVLDQ 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 117 EETIMRHEKVSRGlaaeralalfqkvripsperrlsnyphemSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQI 196
Cdd:smart00382 49 LLLIIVGGKKASG-----------------------------SGELRLRLALALARKLKPDVLILDEITSLLDAEQEALL 99
|
170 180 190
....*....|....*....|....*....|....*....
gi 523689182 197 LLLIR-----ELQREYGLSVIFVTHDIGVAAEVADRIAV 230
Cdd:smart00382 100 LLLEElrlllLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-203 |
1.04e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 29 NGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGTLIEGGMTVDGHDIMSLSNRALsdlrGAVvsmvfQEPRLALdP 108
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRPLDSSFQRSI----GYV-----QQQDLHL-P 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 109 VYTVG---------RQ-----IEETIMRHEKVSRGLAAER-ALALfqkVRIP----SPERRlsnyphemsggmlQRAMIA 169
Cdd:TIGR00956 850 TSTVReslrfsaylRQpksvsKSEKMEYVEEVIKLLEMESyADAV---VGVPgeglNVEQR-------------KRLTIG 913
|
170 180 190
....*....|....*....|....*....|....*
gi 523689182 170 MALACNPKVLL-ADEPTTALDATVQIQILLLIREL 203
Cdd:TIGR00956 914 VELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-249 |
4.80e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 28 VNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRlhpkgtLIE---GGMTVDGHDIMSLSNRALSDLrgavVSMVFQEP-- 102
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMR------MVEvcgGEIRVNGREIGAYGLRELRRQ----FSMIPQDPvl 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 103 -----RLALDPVYT-----VGRQIEETIMRhEKVsrglAAERAlalfqkvRIPSpeRRL---SNYphemSGGmlQRAMIA 169
Cdd:PTZ00243 1396 fdgtvRQNVDPFLEassaeVWAALELVGLR-ERV----ASESE-------GIDS--RVLeggSNY----SVG--QRQLMC 1455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 170 MALACNPK---VLLADEPTTALDATVQIQILLLIRELQREYglSVIFVTHDIGVAAEVaDRIAVMYAGRIVEEGLVGDII 246
Cdd:PTZ00243 1456 MARALLKKgsgFILMDEATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELV 1532
|
...
gi 523689182 247 RNP 249
Cdd:PTZ00243 1533 MNR 1535
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
141-238 |
5.12e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 141 KVRIPSPERRLSNypheMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGV 220
Cdd:PRK10982 379 RVKTPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPE 453
|
90 100
....*....|....*....|.
gi 523689182 221 AAEVADRIAVMYAGR---IVE 238
Cdd:PRK10982 454 LLGITDRILVMSNGLvagIVD 474
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
27-236 |
8.56e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.43 E-value: 8.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 27 AVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEG-----GMTVDGHDI--------MSLSNRALSDLrga 93
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGeawlfGQPVDAGDIatrrrvgyMSQAFSLYGEL--- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 94 vvsmvfqeprlaldpvyTVgRQieeTIMRHEKVSRgLAAERAlalfqKVRIPSPERR--LSNYPHEMSG----GMLQRAM 167
Cdd:NF033858 355 -----------------TV-RQ---NLELHARLFH-LPAAEI-----AARVAEMLERfdLADVADALPDslplGIRQRLS 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523689182 168 IAMALACNPKVLLADEPTT-----ALDATVQiqilLLIrELQREYGLSvIFV-THDIGvAAEVADRIAVMYAGRI 236
Cdd:NF033858 408 LAVAVIHKPELLILDEPTSgvdpvARDMFWR----LLI-ELSREDGVT-IFIsTHFMN-EAERCDRISLMHAGRV 475
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
31-248 |
8.56e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 8.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 31 VSLSVKPGEVVALLGESGSGKSvtmrSLLrlhpKGTLIEGGMTVDGHDImslsnralsdLRGAV-----VSMVFQEprla 105
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKT----SLI----SAMLGELPPRSDASVV----------IRGTVayvpqVSWIFNA---- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 106 ldpvyTVGRQI----EETIMRHEKVSRGLAAERALALFQKVRIPSPERRLSNypheMSGGMLQRAMIAMALACNPKVLLA 181
Cdd:PLN03130 694 -----TVRDNIlfgsPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVN----ISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523689182 182 DEPTTALDATVQIQIL--LLIRELQREyglSVIFVTHDIGVAAEVaDRIAVMYAGRIVEEGLVGDIIRN 248
Cdd:PLN03130 765 DDPLSALDAHVGRQVFdkCIKDELRGK---TRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
8-228 |
1.13e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 8 MIDISNLSVtfRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSvTMRSLLRlhpkgtlieGGMTVDGHDIMSLSNRAL 87
Cdd:PRK10636 1 MIVFSSLQI--RRGVRVL--LDNATATINPGQKVGLVGKNGCGKS-TLLALLK---------NEISADGGSYTFPGNWQL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 88 SdlrgavvsMVFQE-PRL---ALDpvYTVG-----RQIEETIMRHEKVSRGLA----------------AERALAL---- 138
Cdd:PRK10636 67 A--------WVNQEtPALpqpALE--YVIDgdreyRQLEAQLHDANERNDGHAiatihgkldaidawtiRSRAASLlhgl 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 139 -FQKVRIPSPERrlsnyphEMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVqiqILLLIRELqREYGLSVIFVTHD 217
Cdd:PRK10636 137 gFSNEQLERPVS-------DFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWL-KSYQGTLILISHD 205
|
250
....*....|.
gi 523689182 218 IGVAAEVADRI 228
Cdd:PRK10636 206 RDFLDPIVDKI 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-246 |
1.32e-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: 46.86 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMSLsnrALS 88
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLV--LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESA---EGEIIIDGLNIAKI---GLH 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 DLRGAvVSMVFQEP-------RLALDPvytVGRQIEETIMrhekvsrgLAAERA-LALFQKVRIPSPERRLSNYPHEMSG 160
Cdd:TIGR00957 1357 DLRFK-ITIIPQDPvlfsgslRMNLDP---FSQYSDEEVW--------WALELAhLKTFVSALPDKLDHECAEGGENLSV 1424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 161 GMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRElQREyGLSVIFVTHDIGVAAEVAdRIAVMYAGRIVEEG 240
Cdd:TIGR00957 1425 GQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
....*.
gi 523689182 241 LVGDII 246
Cdd:TIGR00957 1502 APSNLL 1507
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
158-240 |
2.43e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.24 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 158 MSGGMLQRAMIAMALACNPK--VLLADEPTTALDATVQIQILLLIRELqREYGLSVIFVTHDIGVaAEVADRIAVM---- 231
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDV-LSSADWIIDFgpgs 165
|
90
....*....|.
gi 523689182 232 --YAGRIVEEG 240
Cdd:cd03238 166 gkSGGKVVFSG 176
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
31-248 |
2.69e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 31 VSLSVKPGEVVALLGESGSGKSVTMRSLLrlhpkGTLieggmtvdghdimSLSNRALSDLRGAV-----VSMVFQEprlA 105
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAML-----GEL-------------SHAETSSVVIRGSVayvpqVSWIFNA---T 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 106 LDPVYTVGRQIEETimRHEKVSRGLAAERALALFQKVRIPSPERRLSNypheMSGGMLQRAMIAMALACNPKVLLADEPT 185
Cdd:PLN03232 695 VRENILFGSDFESE--RYWRAIDVTALQHDLDLLPGRDLTEIGERGVN----ISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523689182 186 TALDATVQIQIL--LLIRELQreyGLSVIFVTHDIGVAAEVaDRIAVMYAGRIVEEGLVGDIIRN 248
Cdd:PLN03232 769 SALDAHVAHQVFdsCMKDELK---GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-246 |
2.81e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 22 GKAVKAVNGVSLSVKPGEVVALLGESGSGKSvTMRSLLrlhpKGTL--IEGGMTVDGHDIMSLSNRALSDLRGAVVSMVF 99
Cdd:PRK13546 34 NKTFFALDDISLKAYEGDVIGLVGINGSGKS-TLSNII----GGSLspTVGKVDRNGEVSVIAISAGLSGQLTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 100 QEPRLALDPvytvgRQIEETIMRHEKVSrglaaERALALFQKVRipsperrlsNYphemSGGMLQRAMIAMALACNPKVL 179
Cdd:PRK13546 109 KMLCMGFKR-----KEIKAMTPKIIEFS-----ELGEFIYQPVK---------KY----SSGMRAKLGFSINITVNPDIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523689182 180 LADEPTTALDATVQIQILLLIRELqREYGLSVIFVTHDIGVAAEVADRIAVMYAGRIVEEGLVGDII 246
Cdd:PRK13546 166 VIDEALSVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
9-108 |
6.09e-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: 43.74 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 9 IDISNLSVTFRRGGKAV-KAVNGVslsVKPGEVVALLGESGSGKSVTMRSLLRLHpkgTLIEGGMTVDGHDIMSLsnrAL 87
Cdd:cd03288 20 IKIHDLCVRYENNLKPVlKHVKAY---IKPGQKVGICGRTGSGKSSLSLAFFRMV---DIFDGKIVIDGIDISKL---PL 90
|
90 100
....*....|....*....|....*...
gi 523689182 88 SDLRgAVVSMVFQEP-------RLALDP 108
Cdd:cd03288 91 HTLR-SRLSIILQDPilfsgsiRFNLDP 117
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
156-232 |
9.17e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.35 E-value: 9.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 156 HEMSGGMLQRAMIAMALA---CNPKVLLA-DEPTTALDATVQIQILLLIRElQREYGLSVIFVTHDIGVaAEVADRIAVM 231
Cdd:cd03227 76 LQLSGGEKELSALALILAlasLKPRPLYIlDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHLPEL-AELADKLIHI 153
|
.
gi 523689182 232 Y 232
Cdd:cd03227 154 K 154
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-223 |
9.46e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 32 SLSVKPGEVVALLGESGSGKSvtmrSLLR-LHPKGTLIEGGMTVDGHDIMSLSNRALSDLrgavVSMVFQEPR---LALD 107
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKS----ALARaLAGELPLLSGERQSQFSHITRLSFEQLQKL----VSDEWQRNNtdmLSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 108 PVYTvGRQIEETIMRHEKvsrglAAERALALFQKVRIPSPERRLSNYpheMSGGMLQRAMIAMALACNPKVLLADEPTTA 187
Cdd:PRK10938 95 EDDT-GRTTAEIIQDEVK-----DPARCEQLAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 523689182 188 LDATVQIQILLLIRELQRE-YGLSVI---------FVTHdIGVAAE 223
Cdd:PRK10938 166 LDVASRQQLAELLASLHQSgITLVLVlnrfdeipdFVQF-AGVLAD 210
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-228 |
1.60e-04 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 42.09 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 20 RGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRLhpkgtlIEGGMTVDGHDImSLSNRALSDLRGAVV-SMV 98
Cdd:cd03231 10 RDGRAL--FSGLSFTLAAGEALQVTGPNGSGKT----TLLRI------LAGLSPPLAGRV-LLNGGPLDFQRDSIArGLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 99 FQEPRLALDPVYTVgrqiEETIMRHEKVSRGLAAERALAlfqKVRIPSPERRLSNYpheMSGGMLQRAMIAMALACNPKV 178
Cdd:cd03231 77 YLGHAPGIKTTLSV----LENLRFWHADHSDEQVEEALA---RVGLNGFEDRPVAQ---LSAGQQRRVALARLLLSGRPL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 523689182 179 LLADEPTTALDATVQIQILLLIRElQREYGLSVIFVTH-DIGVAAEVADRI 228
Cdd:cd03231 147 WILDEPTTALDKAGVARFAEAMAG-HCARGGMVVLTTHqDLGLSEAGAREL 196
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
155-220 |
2.70e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.99 E-value: 2.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523689182 155 PHEMSGGMLQ-RAMIAMALACNPK--VLLADEPTTALDATVQIQILLLIRELQREyGLSVIFVTHDIGV 220
Cdd:pfam13304 234 AFELSDGTKRlLALLAALLSALPKggLLLIDEPESGLHPKLLRRLLELLKELSRN-GAQLILTTHSPLL 301
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
17-217 |
3.39e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.03 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 17 TFRRGGKAV----KAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRlhpkgtlIEGGMtvdghDIMSLSNRALSDlrG 92
Cdd:PRK11819 8 TMNRVSKVVppkkQILKDISLSFFPGAKIGVLGLNGAGKS----TLLR-------IMAGV-----DKEFEGEARPAP--G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 93 AVVSMVFQEPRLalDPVYTVGRQIEE-------TIMRHEKVSRGLAA-------------------------------ER 134
Cdd:PRK11819 70 IKVGYLPQEPQL--DPEKTVRENVEEgvaevkaALDRFNEIYAAYAEpdadfdalaaeqgelqeiidaadawdldsqlEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 135 AL-ALfqkvRIPSPERRLSNypheMSGGMLQRAMIAMALACNPKVLLADEPTTALDATvqiQILLLIRELQReYGLSVIF 213
Cdd:PRK11819 148 AMdAL----RCPPWDAKVTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLEQFLHD-YPGTVVA 215
|
....
gi 523689182 214 VTHD 217
Cdd:PRK11819 216 VTHD 219
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
158-232 |
4.81e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 40.67 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 158 MSGGmlQRAMIAMALAC--------NPKVLLADEPTTALDA-TVQIQILLLIRELQREYGLSVIFVTHDigvaAEVADRI 228
Cdd:cd03240 116 CSGG--EKVLASLIIRLalaetfgsNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD----EELVDAA 189
|
....
gi 523689182 229 AVMY 232
Cdd:cd03240 190 DHIY 193
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
158-285 |
9.01e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 158 MSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQIlllIRE--LQREYGLSVIFVTHDIGVAAEvADRIAVMYAGR 235
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV---VEEcfLGALAGKTRVLATHQVHVVPR-ADYVVALGDGR 858
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 523689182 236 IVEEGLVGDIIRNPRHPYTKGLLGARVELAEG-RDRLVTIPGAPPDLAAMP 285
Cdd:PTZ00243 859 VEFSGSSADFMRTSLYATLAAELKENKDSKEGdADAEVAEVDAAPGGAVDH 909
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
157-216 |
9.45e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 9.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 157 EMSGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREYGLSVIFVTH 216
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
16-240 |
1.03e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 16 VTFRRGgkAVKAVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLrlhpkgTLI-------EGGMTVDGHDIMSLSNRAls 88
Cdd:NF033858 7 VSHRYG--KTVALDDVSLDIPAGCMVGLIGPDGVGKS----SLL------SLIagarkiqQGRVEVLGGDMADARHRR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 89 dlrgAVVsmvfqePRLA---------LDPVYTVgrqiEETImrhEKVSR--GL-AAERAlalfqkVRI----------PS 146
Cdd:NF033858 73 ----AVC------PRIAympqglgknLYPTLSV----FENL---DFFGRlfGQdAAERR------RRIdellratglaPF 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 147 PER---RLSnyphemsGGMLQRAMIAMALACNPKVLLADEPTTALDATVQIQILLLIRELQREY-GLSVIfvthdigVA- 221
Cdd:NF033858 130 ADRpagKLS-------GGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVL-------VAt 195
|
250 260
....*....|....*....|....
gi 523689182 222 -----AEVADRIAVMYAGRIVEEG 240
Cdd:NF033858 196 aymeeAERFDWLVAMDAGRVLATG 219
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
158-234 |
1.47e-03 |
|
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: 39.24 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 158 MSGGMLQRAMIAMALACNPKVLLADEPTTALDA-----TVQIQILLLIRELQReyglSVIFVTHDIGVAAEvADRIAVMY 232
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAMK 215
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..
gi 523689182 233 AG 234
Cdd:cd03290 216 DG 217
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| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
8-61 |
2.28e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 38.63 E-value: 2.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 523689182 8 MIDISNLsvTFRRGGKAVkaVNGVSLSVKPGEVVALLGESGSGKSvtmrSLLRL 61
Cdd:PRK13538 1 MLEARNL--ACERDERIL--FSGLSFTLNAGELVQIEGPNGAGKT----SLLRI 46
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| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
31-238 |
6.73e-03 |
|
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: 38.24 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 31 VSLSVKPGEVVALLGESGSGKSVTMRSLLRLHPKGtliEGGMTVDGHDIMSLSNRALSDLRGAVVSMVFQEPRLaldpvy 110
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPE---SGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------ 421
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523689182 111 tvgrqieetIMRHEKVSRGLAAE--RALALFQKVRIpsPERRLSNYphEMSGGmlQRAMIAMALAcnpkvLLADEPttal 188
Cdd:COG4615 422 ---------LGLDGEADPARAREllERLELDHKVSV--EDGRFSTT--DLSQG--QRKRLALLVA-----LLEDRP---- 477
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170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523689182 189 datvqiqILL-------------------LIRELQREyGLSVIFVTHDiGVAAEVADRIAVMYAGRIVE 238
Cdd:COG4615 478 -------ILVfdewaadqdpefrrvfyteLLPELKAR-GKTVIAISHD-DRYFDLADRVLKMDYGKLVE 537
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