|
Name |
Accession |
Description |
Interval |
E-value |
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-267 |
3.43e-102 |
|
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: 307.99 E-value: 3.43e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPIGGffsREKMKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvRS 84
Cdd:COG1123 260 LLEVRNLSKRYPVRG---KGGVRAVDDVSLTLR--RGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTK-LS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAFMAKVQPVFQNPFEAFNPLTRIDEyLLATAHRFKGAKSRTEKEALADVALQRVGLSmAEIKGRFSHELSGGQLQ 164
Cdd:COG1123 334 RRSLRELRRRVQMVFQDPYSSLNPRMTVGD-IIAEPLRLHGLLSRAERRERVAELLERVGLP-PDLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 165 RIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARD 244
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
250 260
....*....|....*....|...
gi 502309174 245 VLEHPKHAYSIALKNAVLPPDPR 267
Cdd:COG1123 492 VFANPQHPYTRALLAAVPSLDPA 514
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-267 |
6.73e-93 |
|
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: 277.70 E-value: 6.73e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPIGgffsREKMKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKA---DRGSIHFDGTDVKA 81
Cdd:COG0444 1 LLEVRNLKVYFPTR----RGVVKAVDGVSFDVR--RGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 82 VRSRRDREAFMAKVQPVFQNPFEAFNPLTRIDEYLLATAHRFKGAkSRTEKEALADVALQRVGLSMAE-IKGRFSHELSG 160
Cdd:COG0444 75 LSEKELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGL-SKAEARERAIELLERVGLPDPErRLDRYPHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 161 GQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 240
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250 260
....*....|....*....|....*..
gi 502309174 241 DARDVLEHPKHAYSIALKNAVLPPDPR 267
Cdd:COG0444 234 PVEELFENPRHPYTRALLSSIPRLDPD 260
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-278 |
3.04e-91 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 273.92 E-value: 3.04e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFPI-GGFFSREK--MKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGT 77
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVrGGLFGRTVgvVKAVDGVSFDIR--RGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 78 DVkAVRSRRDREAFMAKVQPVFQNPFEAFNPLTRIDEyLLATAHRFKGAKSRTEKEALADVALQRVGLSmAEIKGRFSHE 157
Cdd:COG4608 81 DI-TGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGD-IIAEPLRIHGLASKAERRERVAELLELVGLR-PEHADRYPHE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 158 LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVV 237
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIV 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 502309174 238 ESGDARDVLEHPKHAYSIALKNAVLPPDPReasailRLRQR 278
Cdd:COG4608 238 EIAPRDELYARPLHPYTQALLSAVPVPDPE------RRRER 272
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-267 |
7.11e-85 |
|
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: 254.73 E-value: 7.11e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPIGgffsREKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavrs 84
Cdd:COG1124 1 MLEVRNLSVSYGQG----GRRVPVLKDVSLEVAPG--ESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAFMAKVQPVFQNPFEAFNPLTRIDEYLL--ATAHRFKGAKSRTEKealadvALQRVGLSmAEIKGRFSHELSGGQ 162
Cdd:COG1124 71 RRRRKAFRRRVQMVFQDPYASLHPRHTVDRILAepLRIHGLPDREERIAE------LLEQVGLP-PSFLDRYPHQLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 163 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA 242
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTV 223
|
250 260
....*....|....*....|....*
gi 502309174 243 RDVLEHPKHAYSIALKNAVLPPDPR 267
Cdd:COG1124 224 ADLLAGPKHPYTRELLAASLAFERA 248
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-265 |
6.19e-82 |
|
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: 256.54 E-value: 6.19e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPI-GGFFSREK--MKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKAdRGSIHFDGTDVKA 81
Cdd:COG4172 275 LLEARDLKVWFPIkRGLFRRTVghVKAVDGVSLTLRRG--ETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 82 vRSRRDREAFMAKVQPVFQNPFEAFNPLTRIDEyLLA---TAHRfkGAKSRTEKEALADVALQRVGLSmAEIKGRFSHEL 158
Cdd:COG4172 352 -LSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQ-IIAeglRVHG--PGLSAAERRARVAEALEEVGLD-PAARHRYPHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 159 SGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVE 238
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
250 260
....*....|....*....|....*..
gi 502309174 239 SGDARDVLEHPKHAYSIALKNAVLPPD 265
Cdd:COG4172 507 QGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-240 |
1.01e-81 |
|
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: 245.88 E-value: 1.01e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPIGGFfsreKMKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrS 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGG----SVKALDDVSFSIK--KGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKL-S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAFMAKVQPVFQNPFEAFNPLTRIDEYLLATAHRFKGAKSRTEKEALADVALQRVGLSmAEIKGRFSHELSGGQLQ 164
Cdd:cd03257 74 RRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLP-EEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502309174 165 RIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 240
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
3-253 |
5.01e-67 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 209.69 E-value: 5.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 3 SNLLELDHVTKLFPIG-GFFSREKMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK- 80
Cdd:COG4167 2 SALLEVRNLSKTFKYRtGLFRRQQFEAVKPVSFTL--EAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 ---AVRSRRDReafMakvqpVFQNPFEAFNPLTRIDEyLLATAHRFKGAKSRTEKEALADVALQRVGLsMAEIKGRFSHE 157
Cdd:COG4167 80 gdyKYRCKHIR---M-----IFQDPNTSLNPRLNIGQ-ILEEPLRLNTDLTAEEREERIFATLRLVGL-LPEHANFYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 158 LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVV 237
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
250
....*....|....*.
gi 502309174 238 ESGDARDVLEHPKHAY 253
Cdd:COG4167 230 EYGKTAEVFANPQHEV 245
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-267 |
1.08e-66 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 210.98 E-value: 1.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFPI-GGFFSREKM-KAVDDVSFALAADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTD 78
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVkRGLFKPERLvKALDGVSFTLERGK--TLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 79 VkAVRSRRDREAFMAKVQPVFQNPFEAFNPLTRIdEYLLATAHRFKGAKSRTEKEALADVALQRVGLSmAEIKGRFSHEL 158
Cdd:PRK11308 79 L-LKADPEAQKLLRQKIQIVFQNPYGSLNPRKKV-GQILEEPLLINTSLSAAERREKALAMMAKVGLR-PEHYDRYPHMF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 159 SGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVE 238
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVE 235
|
250 260 270
....*....|....*....|....*....|.
gi 502309174 239 SGDARDVLEHPKHAYSIALKNAV--LPPDPR 267
Cdd:PRK11308 236 KGTKEQIFNNPRHPYTQALLSATprLNPDDR 266
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-267 |
3.68e-64 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 204.94 E-value: 3.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPIGG----FFSREK-MKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV 79
Cdd:PRK15079 8 LLEVADLKVHFDIKDgkqwFWQPPKtLKAVDGVTLRLYEG--ETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 80 KAVrSRRDREAFMAKVQPVFQNPFEAFNPLTRIDEYLLATAHRFKGAKSRTEKEALADVALQRVGLsMAEIKGRFSHELS 159
Cdd:PRK15079 86 LGM-KDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGL-LPNLINRYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 160 GGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVES 239
Cdd:PRK15079 164 GGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVEL 243
|
250 260
....*....|....*....|....*...
gi 502309174 240 GDARDVLEHPKHAYSIALKNAVLPPDPR 267
Cdd:PRK15079 244 GTYDEVYHNPLHPYTKALMSAVPIPDPD 271
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-253 |
6.04e-59 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 191.85 E-value: 6.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFpiGGFFsrekmkAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 80
Cdd:COG3842 1 MAMPALELENVSKRY--GDVT------ALDDVSLSIEPG--EFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 AVRSRRdREAFMakvqpVFQNP--------FE--AFnPLtrideyllatahRFKGAkSRTEKEALADVALQRVGLS-MAE 149
Cdd:COG3842 71 GLPPEK-RNVGM-----VFQDYalfphltvAEnvAF-GL------------RMRGV-PKAEIRARVAELLELVGLEgLAD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 150 ikgRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVV 229
Cdd:COG3842 131 ---RYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIA 207
|
250 260
....*....|....*....|....
gi 502309174 230 IMRKGVVVESGDARDVLEHPKHAY 253
Cdd:COG3842 208 VMNDGRIEQVGTPEEIYERPATRF 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-277 |
1.48e-58 |
|
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: 195.12 E-value: 1.48e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 3 SNLLELDHVTKLFPIGGFFsrekmkAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILG---SEKADRGSIHFDGTDV 79
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVP------AVDGVSLTIAPG--ETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 80 KAVRSR-RDREAFMakvqpVFQNPFEAFNPLTRIDEylLATAHRFKGAkSRTEKEALADVALQRVGLsmAEIKGRFSHEL 158
Cdd:COG1123 74 LELSEAlRGRRIGM-----VFQDPMTQLNPVTVGDQ--IAEALENLGL-SRAEARARVLELLEAVGL--ERRLDRYPHQL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 159 SGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVE 238
Cdd:COG1123 144 SGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVE 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 502309174 239 SGDARDVLEHPKH---AYSIALKNAVLPPDPREASAILRLRQ 277
Cdd:COG1123 224 DGPPEEILAAPQAlaaVPRLGAARGRAAPAAAAAEPLLEVRN 265
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-270 |
2.47e-56 |
|
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: 182.70 E-value: 2.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPIGGFFSREKMKAV-DDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVR 83
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFGAKQRAPVlTNVSLSIEEG--ETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 84 sRRDREAFMAKVQPVFQNPFEAFNPLTRIdEYLLATAHRFKGAKSRTEKEALADVALQRVGLSmAEIKGRFSHELSGGQL 163
Cdd:TIGR02769 80 -RKQRRAFRRDVQLVFQDSPSAVNPRMTV-RQIIGEPLRHLTSLDESEQKARIAELLDMVGLR-SEDADKLPRQLSGGQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 164 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDAR 243
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVA 236
|
250 260
....*....|....*....|....*..
gi 502309174 244 DVLEHpKHAYSIALKNAVLPPDPREAS 270
Cdd:TIGR02769 237 QLLSF-KHPAGRNLQSAVLPEHPVRRS 262
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-277 |
4.61e-56 |
|
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: 189.13 E-value: 4.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFPIGGFFSRekmkAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILG----SEKADRGSIHFDG 76
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVE----AVKGVSFDIAAG--ETLALVGESGSGKSVTALSILRllpdPAAHPSGSILFDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 77 TDV-----KAVRSRRDREAFMakvqpVFQNPFEAFNPLTRIdEYLLATAHRFKGAKSRTEKEALADVALQRVGLSMAEIK 151
Cdd:COG4172 76 QDLlglseRELRRIRGNRIAM-----IFQEPMTSLNPLHTI-GKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 152 -GRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVI 230
Cdd:COG4172 150 lDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 502309174 231 MRKGVVVESGDARDVLEHPKHAYSIALKNA----VLPPDPREASAILRLRQ 277
Cdd:COG4172 230 MRQGEIVEQGPTAELFAAPQHPYTRKLLAAeprgDPRPVPPDAPPLLEARD 280
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-271 |
3.60e-55 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 179.50 E-value: 3.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 3 SNLLELDHVTKLFPIGGFFSREKMKAV-DDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKA 81
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLSGKHQHQTVlNNVSLSLKSG--ETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 82 VrSRRDREAFMAKVQPVFQNPFEAFNPLTRIDEyLLATAHRFKGAKSRTEKEALADVALQRVGLSmAEIKGRFSHELSGG 161
Cdd:PRK10419 79 L-NRAQRKAFRRDIQMVFQDSISAVNPRKTVRE-IIREPLRHLLSLDKAERLARASEMLRAVDLD-DSVLDKRPPQLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 162 QLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGD 241
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
250 260 270
....*....|....*....|....*....|
gi 502309174 242 ARDVLeHPKHAYSIALKNAVLPPDPREASA 271
Cdd:PRK10419 236 VGDKL-TFSSPAGRVLQNAVLPAFPVRRRT 264
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-249 |
1.19e-53 |
|
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: 174.78 E-value: 1.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFpiGGFfsrekmKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 80
Cdd:COG1127 1 MSEPMIEVRNLTKSF--GDR------VVLDGVSLDVPRG--EILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 AVrSRRDREAFMAKVQPVFQNP--------FE--AFnPLtrideyllatahRFKGAKSRTEKEALADVALQRVGLSmaEI 150
Cdd:COG1127 71 GL-SEKELYELRRRIGMLFQGGalfdsltvFEnvAF-PL------------REHTDLSEAEIRELVLEKLELVGLP--GA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 151 KGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVI 230
Cdd:COG1127 135 ADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAV 214
|
250
....*....|....*....
gi 502309174 231 MRKGVVVESGDARDVLEHP 249
Cdd:COG1127 215 LADGKIIAEGTPEELLASD 233
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-253 |
1.33e-51 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 172.64 E-value: 1.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSsnlLELDHVTKLFpiGGFfsrekmKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 80
Cdd:COG1118 1 MS---IEVRNISKRF--GSF------TLLDDVSLEIASG--ELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 AVRSRRDReafmaKVQPVFQNpfeafnpltrideYLLatahrFK----------GAKSR--TEKEALADVA--LQRVGLS 146
Cdd:COG1118 68 TNLPPRER-----RVGFVFQH-------------YAL-----FPhmtvaeniafGLRVRppSKAEIRARVEelLELVQLE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 147 maEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISD 226
Cdd:COG1118 125 --GLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELAD 202
|
250 260
....*....|....*....|....*..
gi 502309174 227 RVVIMRKGVVVESGDARDVLEHPKHAY 253
Cdd:COG1118 203 RVVVMNQGRIEQVGTPDEVYDRPATPF 229
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-240 |
2.45e-51 |
|
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: 168.08 E-value: 2.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFpiggffsrEKMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 85
Cdd:cd03259 1 LELKGLSKTY--------GSVRALDDLSLTV--EPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFmakvqpVFQNpFEAFNPLTRIDEylLATAHRFKGaKSRTEKEALADVALQRVGLSmaEIKGRFSHELSGGQLQR 165
Cdd:cd03259 71 RRNIGM------VFQD-YALFPHLTVAEN--IAFGLKLRG-VPKAEIRARVRELLELVGLE--GLLNRYPHELSGGQQQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502309174 166 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 240
Cdd:cd03259 139 VALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-250 |
3.79e-50 |
|
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: 165.45 E-value: 3.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPIGGffsrEKMKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrS 84
Cdd:cd03258 1 MIELKNVSKVFGDTG----GKVTALKDVSLSVP--KGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLL-S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAFMAKVQPVFQNpFEAFNPLTRID--EYLLATAHrfkgaKSRTEKEALADVALQRVGLSmaEIKGRFSHELSGGQ 162
Cdd:cd03258 74 GKELRKARRRIGMIFQH-FNLLSSRTVFEnvALPLEIAG-----VPKAEIEERVLELLELVGLE--DKADAYPAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 163 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA 242
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTV 225
|
....*...
gi 502309174 243 RDVLEHPK 250
Cdd:cd03258 226 EEVFANPQ 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-238 |
4.99e-50 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 164.83 E-value: 4.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 3 SNLLELDHVTKLFPIGGffsrEKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAV 82
Cdd:COG1136 2 SPLLELRNLTKSYGTGE----GEVTALRGVSLSIEAG--EFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 83 RS------RRDREAFmakvqpVFQNpfeaFNpltrideyLLAT---------AHRFKGaKSRTEKEALADVALQRVGLsm 147
Cdd:COG1136 76 SErelarlRRRHIGF------VFQF----FN--------LLPEltalenvalPLLLAG-VSRKERRERARELLERVGL-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 148 AEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYiSDR 227
Cdd:COG1136 135 GDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADR 213
|
250
....*....|.
gi 502309174 228 VVIMRKGVVVE 238
Cdd:COG1136 214 VIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-236 |
1.93e-49 |
|
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: 163.04 E-value: 1.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPIGGffsrEKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrSR 85
Cdd:cd03255 1 IELKNLSKTYGGGG----EKVQALKGVSLSIEKG--EFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKL-SE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAK-VQPVFQNpfeaFN--P-LTRIDEYLLATahRFKGaKSRTEKEALADVALQRVGLsmAEIKGRFSHELSGG 161
Cdd:cd03255 74 KELAAFRRRhIGFVFQS----FNllPdLTALENVELPL--LLAG-VPKKERRERAEELLERVGL--GDRLNHYPSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502309174 162 QLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYiSDRVVIMRKGVV 236
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-252 |
4.13e-49 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 166.02 E-value: 4.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPIGGffsrEKMKAVDDVSfaLAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 85
Cdd:COG1135 2 IELENLSKTFPTKG----GPVTALDDVS--LTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAfMAKVQPVFQNpfeaFNpltrideyLLAT-------AHRFKGAK-SRTEKEALADVALQRVGLSmaEIKGRFSHE 157
Cdd:COG1135 76 ELRAA-RRKIGMIFQH----FN--------LLSSrtvaenvALPLEIAGvPKAEIRKRVAELLELVGLS--DKADAYPSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 158 LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVV 237
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
250
....*....|....*
gi 502309174 238 ESGDARDVLEHPKHA 252
Cdd:COG1135 221 EQGPVLDVFANPQSE 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-250 |
3.37e-48 |
|
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: 160.19 E-value: 3.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTklfpiggFFSREKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavrsR 85
Cdd:COG1122 1 IELENLS-------FSYPGGTPALDDVSLSIEKG--EFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT----K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAKVQPVFQNP----FE-------AFNPLTRideyllatahrfkgAKSRTEKEALADVALQRVGLSmaEIKGRF 154
Cdd:COG1122 68 KNLRELRRKVGLVFQNPddqlFAptveedvAFGPENL--------------GLPREEIRERVEEALELVGLE--HLADRP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 155 SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKG 234
Cdd:COG1122 132 PHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDG 210
|
250
....*....|....*.
gi 502309174 235 VVVESGDARDVLEHPK 250
Cdd:COG1122 211 RIVADGTPREVFSDYE 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-278 |
9.04e-48 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 160.26 E-value: 9.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSN--LLELDHVTKLFPIGGffsrEKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTD 78
Cdd:COG1116 1 MSAAapALELRGVSKRFPTGG----GGVTALDDVSLTVAAG--EFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 79 VKAVRSRRdreAFmakvqpVFQNPfeafnpltrideYLL---------ATAHRFKGaKSRTEKEALADVALQRVGLSMAE 149
Cdd:COG1116 75 VTGPGPDR---GV------VFQEP------------ALLpwltvldnvALGLELRG-VPKAERRERARELLELVGLAGFE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 150 ikGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVV 229
Cdd:COG1116 133 --DAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVV 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 502309174 230 IM--RKGVVVESgdaRDV-LEHPKHaysialknavlpPDPREASAILRLRQR 278
Cdd:COG1116 211 VLsaRPGRIVEE---IDVdLPRPRD------------RELRTSPEFAALRAE 247
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-238 |
4.45e-47 |
|
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: 157.25 E-value: 4.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPIGGffsrEKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 85
Cdd:cd03293 1 LEVRNVSKTYGGGG----GAVTALEDISLSVEEG--EFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RdreAFMakvqpvFQNPfeAFNP-LTRIDEYLLATahRFKGAkSRTEKEALADVALQRVGLSMAEikGRFSHELSGGQLQ 164
Cdd:cd03293 75 R---GYV------FQQD--ALLPwLTVLDNVALGL--ELQGV-PKAEARERAEELLELVGLSGFE--NAYPHQLSGGMRQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502309174 165 RIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIM--RKGVVVE 238
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVA 214
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
28-267 |
5.09e-47 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 160.28 E-value: 5.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 28 AVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKAD---RGSIHFDGTDV-----KAVRSRRDREAFMakvqpVF 99
Cdd:PRK09473 31 AVNDLNFSLRAG--ETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIlnlpeKELNKLRAEQISM-----IF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 100 QNPFEAFNPLTRIDEYLLATAHRFKGAksrTEKEALADVALQRVGLSMAEIKGR---FSHELSGGQLQRIAVARALIPEP 176
Cdd:PRK09473 104 QDPMTSLNPYMRVGEQLMEVLMLHKGM---SKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 177 KLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHAYSIA 256
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIG 260
|
250
....*....|.
gi 502309174 257 LKNAVlppdPR 267
Cdd:PRK09473 261 LLNAV----PR 267
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-247 |
5.25e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.53 E-value: 5.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFpiGGFfsrekmKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrsR 85
Cdd:COG1131 1 IEVRGLTKRY--GDK------TALDGVSLTVE--PGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV-----A 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAKVQPVFQNPfeAFNPLTRIDEYLLATAhRFKGaKSRTEKEALADVALQRVGLsmAEIKGRFSHELSGGQLQR 165
Cdd:COG1131 66 RDPAEVRRRIGYVPQEP--ALYPDLTVRENLRFFA-RLYG-LPRKEARERIDELLELFGL--TDAADRKVGTLSGGMKQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 166 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDV 245
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
..
gi 502309174 246 LE 247
Cdd:COG1131 219 KA 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-253 |
5.33e-47 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 161.01 E-value: 5.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSnlLELDHVTKLFpiGGFfsrekmKAVDDVSFALAaDKpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 80
Cdd:COG3839 1 MAS--LELENVSKSY--GGV------EALKDIDLDIE-DG-EFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 AVRSRrDREAFMakvqpVFQNP--------FE--AFnPLtrideyllatahRFKGAkSRTEKEALADVALQRVGLSmaEI 150
Cdd:COG3839 69 DLPPK-DRNIAM-----VFQSYalyphmtvYEniAF-PL------------KLRKV-PKAEIDRRVREAAELLGLE--DL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 151 KGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVI 230
Cdd:COG3839 127 LDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAV 206
|
250 260
....*....|....*....|...
gi 502309174 231 MRKGVVVESGDARDVLEHPKHAY 253
Cdd:COG3839 207 MNDGRIQQVGTPEELYDRPANLF 229
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-251 |
5.81e-47 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 158.41 E-value: 5.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPI-GGFFSREKMKAVDDVSFALAADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK--- 80
Cdd:PRK15112 4 LLEVRNLSKTFRYrTGWFRRQTVEAVKPLSFTLREGQ--TLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 -AVRSRRDREafmakvqpVFQNPFEAFNPLTRIDEyLLATAHRFKGAKSRTEKEALADVALQRVGLsMAEIKGRFSHELS 159
Cdd:PRK15112 82 ySYRSQRIRM--------IFQDPSTSLNPRQRISQ-ILDFPLRLNTDLEPEQREKQIIETLRQVGL-LPDHASYYPHMLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 160 GGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVES 239
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVER 231
|
250
....*....|..
gi 502309174 240 GDARDVLEHPKH 251
Cdd:PRK15112 232 GSTADVLASPLH 243
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-250 |
4.32e-46 |
|
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: 155.09 E-value: 4.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFpiGGFfsrekmKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsr 85
Cdd:cd03300 1 IELENVSKFY--GGF------VALDGVSLDI--KEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 rdrEAFMAKVQPVFQNpFEAFNPLTRIDEylLATAHRFKGaKSRTEKEALADVALQRVGLSmaEIKGRFSHELSGGQLQR 165
Cdd:cd03300 68 ---PPHKRPVNTVFQN-YALFPHLTVFEN--IAFGLRLKK-LPKAEIKERVAEALDLVQLE--GYANRKPSQLSGGQQQR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 166 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDV 245
Cdd:cd03300 139 VAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
....*
gi 502309174 246 LEHPK 250
Cdd:cd03300 219 YEEPA 223
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
28-262 |
4.31e-44 |
|
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: 149.83 E-value: 4.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 28 AVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILG----SEKADRGSIHFDGTDVKAVrSRRDREAFMakvqpVFQNPF 103
Cdd:TIGR02770 1 LVQDLNLSL--KRGEVLALVGESGSGKSLTCLAILGllppGLTQTSGEILLDGRPLLPL-SIRGRHIAT-----IMQNPR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 104 EAFNPLTRIDEYLLATAHrfkgAKSRTEKEALADV--ALQRVGL-SMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIV 180
Cdd:TIGR02770 73 TAFNPLFTMGNHAIETLR----SLGKLSKQARALIleALEAVGLpDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 181 ADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHAYSIALKNA 260
Cdd:TIGR02770 149 ADEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
..
gi 502309174 261 VL 262
Cdd:TIGR02770 229 HL 230
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-252 |
9.91e-44 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 148.99 E-value: 9.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFpiGGFfsrekmKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvrS 84
Cdd:COG1126 1 MIEIENLHKSF--GDL------EVLKGISLDVE--KGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD--S 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAFMAKVQPVFQNpFEAFNPLTRIDEYLLA--TAHRfkgaKSRTEKEALADVALQRVGLsmAEIKGRFSHELSGGQ 162
Cdd:COG1126 69 KKDINKLRRKVGMVFQQ-FNLFPHLTVLENVTLApiKVKK----MSKAEAEERAMELLERVGL--ADKADAYPAQLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 163 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA 242
Cdd:COG1126 142 QQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPP 220
|
250
....*....|
gi 502309174 243 RDVLEHPKHA 252
Cdd:COG1126 221 EEFFENPQHE 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-253 |
1.33e-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: 149.03 E-value: 1.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFpiGGFfsrekmKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrSR 85
Cdd:cd03296 3 IEVRNVSKRF--GDF------VALDDVSLDIPSG--ELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV-PV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREafmakVQPVFQNpFEAFNPLTRIDEylLATAHRFKGAKSR---TEKEALADVALQRVGLSMAEikGRFSHELSGGQ 162
Cdd:cd03296 72 QERN-----VGFVFQH-YALFRHMTVFDN--VAFGLRVKPRSERppeAEIRAKVHELLKLVQLDWLA--DRYPAQLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 163 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA 242
Cdd:cd03296 142 RQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
250
....*....|.
gi 502309174 243 RDVLEHPKHAY 253
Cdd:cd03296 222 DEVYDHPASPF 232
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-234 |
2.86e-43 |
|
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: 146.18 E-value: 2.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPiggffsreKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavRSR 85
Cdd:cd03229 1 LELKNVSKRYG--------QKTVLNDVSLNIEAG--EIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT--DLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAKVQPVFQNpFEAFNPLTRIDEYLLAtahrfkgaksrtekealadvalqrvglsmaeikgrfsheLSGGQLQR 165
Cdd:cd03229 69 DELPPLRRRIGMVFQD-FALFPHLTVLENIALG---------------------------------------LSGGQQQR 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502309174 166 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKG 234
Cdd:cd03229 109 VALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-249 |
5.03e-43 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 147.45 E-value: 5.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPiGGFfsrekmKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKA---V 82
Cdd:cd03295 1 IEFENVTKRYG-GGK------KAVNNLNLEIA--KGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqdpV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 83 RSRRdreafmaKVQPVFQNPfeAFNPLTRIDEYLlATAHRFKGAkSRTEKEALADVALQRVGLSMAEIKGRFSHELSGGQ 162
Cdd:cd03295 72 ELRR-------KIGYVIQQI--GLFPHMTVEENI-ALVPKLLKW-PKEKIRERADELLALVGLDPAEFADRYPHELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 163 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA 242
Cdd:cd03295 141 QQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
....*..
gi 502309174 243 RDVLEHP 249
Cdd:cd03295 221 DEILRSP 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-246 |
6.58e-43 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 147.50 E-value: 6.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTklfpiggfFSREKMKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrS 84
Cdd:COG1120 1 MLEAENLS--------VGYGGRPVLDDVSLSLP--PGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASL-S 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAFMAKVqpvFQNPFEAFnPLTRIDEYLLA-TAHRFKGAKSRTEKEALADVALQRVGLsmAEIKGRFSHELSGGQL 163
Cdd:COG1120 70 RRELARRIAYV---PQEPPAPF-GLTVRELVALGrYPHLGLFGRPSAEDREAVEEALERTGL--EHLADRPVDELSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 164 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDAR 243
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
...
gi 502309174 244 DVL 246
Cdd:COG1120 224 EVL 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
27-234 |
1.07e-42 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 145.69 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 27 KAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREafmaKVQPVFQNP---F 103
Cdd:cd03225 15 PALDDISLTIK--KGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR----KVGLVFQNPddqF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 104 eaFNPLTRiDEylLATAHRFKGaKSRTEKEALADVALQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADE 183
Cdd:cd03225 89 --FGPTVE-EE--VAFGLENLG-LPEEEIEERVEEALELVGLE--GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502309174 184 PVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKG 234
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-257 |
3.73e-42 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 151.78 E-value: 3.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 2 SSNLLELDHVTKLFPI-GGFFSR--EKMKAVDDVSFALAADkpEIFTIVGESGSGKST----LAKMIlgsekADRGSIHF 74
Cdd:PRK15134 272 ASPLLDVEQLQVAFPIrKGILKRtvDHNVVVKNISFTLRPG--ETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 75 DGTDVKAvRSRRDREAFMAKVQPVFQNPFEAFNP---LTRIDEYLLATAHRFKGAKSRtekEALADVALQRVGLSmAEIK 151
Cdd:PRK15134 345 DGQPLHN-LNRRQLLPVRHRIQVVFQDPNSSLNPrlnVLQIIEEGLRVHQPTLSAAQR---EQQVIAVMEEVGLD-PETR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 152 GRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIM 231
Cdd:PRK15134 420 HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVL 499
|
250 260
....*....|....*....|....*.
gi 502309174 232 RKGVVVESGDARDVLEHPKHAYSIAL 257
Cdd:PRK15134 500 RQGEVVEQGDCERVFAAPQQEYTRQL 525
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-253 |
4.82e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 144.85 E-value: 4.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTklfpiggfFSREKMKAVDDVSFALAAdkPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 80
Cdd:COG1121 2 MMMPAIELENLT--------VSYGGRPVLEDVSLTIPP--GEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 AVRSRrdreafMAKVqPvfQNpfEAFN---PLTRIDeyLLAT----AHRFKGAKSRTEKEALADvALQRVGlsMAEIKGR 153
Cdd:COG1121 72 RARRR------IGYV-P--QR--AEVDwdfPITVRD--VVLMgrygRRGLFRRPSRADREAVDE-ALERVG--LEDLADR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 154 FSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRK 233
Cdd:COG1121 136 PIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNR 214
|
250 260
....*....|....*....|..
gi 502309174 234 GVVVeSGDARDVL--EHPKHAY 253
Cdd:COG1121 215 GLVA-HGPPEEVLtpENLSRAY 235
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-253 |
5.01e-42 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 146.77 E-value: 5.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 7 ELDHVTKLFPiggffsrEKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK---AVR 83
Cdd:COG1125 3 EFENVTKRYP-------DGTVAVDDLSLTIPAG--EFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRdldPVE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 84 SRRDreafMAKV-Q-----P---VFQNpfeafnpltrideylLATAHRFKGaKSRTEKEALADVALQRVGLSMAEIKGRF 154
Cdd:COG1125 74 LRRR----IGYViQqiglfPhmtVAEN---------------IATVPRLLG-WDKERIRARVDELLELVGLDPEEYRDRY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 155 SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKG 234
Cdd:COG1125 134 PHELSGGQQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREG 213
|
250
....*....|....*....
gi 502309174 235 VVVESGDARDVLEHPKHAY 253
Cdd:COG1125 214 RIVQYDTPEEILANPANDF 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-266 |
6.42e-42 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 152.32 E-value: 6.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPI-GGFFSREK--MKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKA 81
Cdd:PRK10261 313 ILQVRNLVTRFPLrSGLLNRVTreVHAVEKVSFDLWPG--ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 82 VrSRRDREAFMAKVQPVFQNPFEAFNPLTRIDeYLLATAHRFKGAKSRTEKEALADVALQRVGLsMAEIKGRFSHELSGG 161
Cdd:PRK10261 391 L-SPGKLQALRRDIQFIFQDPYASLDPRQTVG-DSIMEPLRVHGLLPGKAAAARVAWLLERVGL-LPEHAWRYPHEFSGG 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 162 QLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGD 241
Cdd:PRK10261 468 QRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGP 547
|
250 260
....*....|....*....|....*
gi 502309174 242 ARDVLEHPKHAYSIALKNAVLPPDP 266
Cdd:PRK10261 548 RRAVFENPQHPYTRKLMAAVPVADP 572
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-250 |
5.37e-41 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 141.81 E-value: 5.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFpiGGFfsrekmKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 85
Cdd:cd03219 1 LEVRGLTKRF--GGL------VALDDVSFSVRPG--EIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAKVqpvFQNPfEAFNPLTRIDEYLLA----TAHRFKGAKSRTEKEAL---ADVALQRVGLsmAEIKGRFSHEL 158
Cdd:cd03219 71 EIARLGIGRT---FQIP-RLFPELTVLENVMVAaqarTGSGLLLARARREEREArerAEELLERVGL--ADLADRPAGEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 159 SGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVE 238
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIA 223
|
250
....*....|..
gi 502309174 239 SGDARDVLEHPK 250
Cdd:cd03219 224 EGTPDEVRNNPR 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-277 |
8.62e-41 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 148.31 E-value: 8.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFPIGGffsrEKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKAD-----RGSIHFD 75
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQ----TVRTVVNDVSLQIEAG--ETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 76 GTDVKAVRSRRDREAFMAKVQPVFQNPFEAFNPLTRIDE--YLLATAHR-FKGAKSRTEKEAladvALQRVGLSMAeiKG 152
Cdd:PRK15134 75 GESLLHASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKqlYEVLSLHRgMRREAARGEILN----CLDRVGIRQA--AK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 153 R---FSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVV 229
Cdd:PRK15134 149 RltdYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVA 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 502309174 230 IMRKGVVVESGDARDVLEHPKHAYSIALKNA----VLPPDPREASAILRLRQ 277
Cdd:PRK15134 229 VMQNGRCVEQNRAATLFSAPTHPYTQKLLNSepsgDPVPLPEPASPLLDVEQ 280
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
6-253 |
1.12e-40 |
|
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: 142.01 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLF----------PIGGFFSREKMK------AVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADR 69
Cdd:cd03294 1 IKIKGLYKIFgknpqkafklLAKGKSKEEILKktgqtvGVNDVSLDV--REGEIFVIMGLSGSGKSTLLRCINRLIEPTS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 70 GSIHFDGTDVKAVRSRRDREAFMAKVQPVFQNpFEAFNPLTRID--EYLLATAHRfkgakSRTEKEALADVALQRVGLsm 147
Cdd:cd03294 79 GKVLIDGQDIAAMSRKELRELRRKKISMVFQS-FALLPHRTVLEnvAFGLEVQGV-----PRAEREERAAEALELVGL-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 148 AEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDR 227
Cdd:cd03294 151 EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDR 230
|
250 260
....*....|....*....|....*.
gi 502309174 228 VVIMRKGVVVESGDARDVLEHPKHAY 253
Cdd:cd03294 231 IAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-245 |
3.84e-40 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 140.19 E-value: 3.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPiGGFfsrekmKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRS 84
Cdd:COG3638 2 MLELRNLSKRYP-GGT------PALDDVSLEIE--RGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDReAFMAKVQPVFQNpfeaFN---PLTRIDEYLLATAHRFKGAKS------RTEKE-ALAdvALQRVGLS-MAEIKgr 153
Cdd:COG3638 73 RALR-RLRRRIGMIFQQ----FNlvpRLSVLTNVLAGRLGRTSTWRSllglfpPEDRErALE--ALERVGLAdKAYQR-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 154 fSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITH--DLATAYyiSDRVVIM 231
Cdd:COG3638 144 -ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHqvDLARRY--ADRIIGL 220
|
250
....*....|....
gi 502309174 232 RKGVVVESGDARDV 245
Cdd:COG3638 221 RDGRVVFDGPPAEL 234
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-240 |
6.80e-40 |
|
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: 138.54 E-value: 6.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPiggffsreKMKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 85
Cdd:cd03301 1 VELENVTKRFG--------NVTALDDLNLDIA--DGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 rDREAFMakvqpVFQNpFEAFNPLTRIDEylLATAHRFKGAKSRTEKEALADVALQrvgLSMAEIKGRFSHELSGGQLQR 165
Cdd:cd03301 71 -DRDIAM-----VFQN-YALYPHMTVYDN--IAFGLKLRKVPKDEIDERVREVAEL---LQIEHLLDRKPKQLSGGQRQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502309174 166 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 240
Cdd:cd03301 139 VALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-253 |
1.05e-39 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 139.02 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 2 SSNLLELDHVTKLFpiGGFfsrekmKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKA 81
Cdd:COG0411 1 SDPLLEVRGLTKRF--GGL------VAVDDVSLEVERG--EIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 82 VRSRRDREAFMAKVqpvFQNPfEAFNPLT-----------RIDEYLLATAHRFKGAKsRTEKEALADV--ALQRVGLsmA 148
Cdd:COG0411 71 LPPHRIARLGIART---FQNP-RLFPELTvlenvlvaahaRLGRGLLAALLRLPRAR-REEREARERAeeLLERVGL--A 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 149 EIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRV 228
Cdd:COG0411 144 DRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRI 223
|
250 260
....*....|....*....|....*..
gi 502309174 229 VIMRKGVVVESGDARDVLEHPKH--AY 253
Cdd:COG0411 224 VVLDFGRVIAEGTPAEVRADPRVieAY 250
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-248 |
1.06e-39 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 139.49 E-value: 1.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPiggffsREKMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 85
Cdd:TIGR04520 1 IEVENVSFSYP------ESEKPALKNVSLSI--EKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RD-REafmaKVQPVFQNP---F-----E---AFNP----------LTRIDEyllatahrfkgaksrtekealadvALQRV 143
Cdd:TIGR04520 73 WEiRK----KVGMVFQNPdnqFvgatvEddvAFGLenlgvpreemRKRVDE------------------------ALKLV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 144 GlsMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYY 223
Cdd:TIGR04520 125 G--MEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL 202
|
250 260
....*....|....*....|....*
gi 502309174 224 iSDRVVIMRKGVVVESGDARDVLEH 248
Cdd:TIGR04520 203 -ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-250 |
1.90e-39 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 141.01 E-value: 1.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFpiggffsrEKMKAVDDVSfaLAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 80
Cdd:PRK11432 2 TQKNFVVLKNITKRF--------GSNTVIDNLN--LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 AvRSRRDREAFMakvqpVFQNpfEAFNPLTRIDE---YLLATAHRFKGAKSRTEKEALADVALqrvglsmAEIKGRFSHE 157
Cdd:PRK11432 72 H-RSIQQRDICM-----VFQS--YALFPHMSLGEnvgYGLKMLGVPKEERKQRVKEALELVDL-------AGFEDRYVDQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 158 LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVV 237
Cdd:PRK11432 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
250
....*....|...
gi 502309174 238 ESGDARDVLEHPK 250
Cdd:PRK11432 217 QIGSPQELYRQPA 229
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-249 |
3.97e-39 |
|
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: 137.25 E-value: 3.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFpiGGffsrekmKAV-DDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrS 84
Cdd:cd03261 1 IELRGLTKSF--GG-------RTVlKGVDLDVR--RGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGL-S 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAFMAKVQPVFQNPfeA-FNPLTRID--EYLLatahRFKGAKSRTEKEALADVALQRVGLSMAEIKgrFSHELSGG 161
Cdd:cd03261 69 EAELYRLRRRMGMLFQSG--AlFDSLTVFEnvAFPL----REHTRLSEEEIREIVLEKLEAVGLRGAEDL--YPAELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 162 QLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGD 241
Cdd:cd03261 141 MKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
....*...
gi 502309174 242 ARDVLEHP 249
Cdd:cd03261 221 PEELRASD 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-245 |
5.74e-39 |
|
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: 136.93 E-value: 5.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPIGGffsrekmKAVDDVSFAlaADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV-----K 80
Cdd:cd03256 1 IEVENLSKTYPNGK-------KALKDVSLS--INPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 AVRSRRDREAFmakvqpVFQNpFEAFNPLTRIDEYL---LATAHRFKGAKSRTEKE----ALAdvALQRVGLS-MAEIKg 152
Cdd:cd03256 72 ALRQLRRQIGM------IFQQ-FNLIERLSVLENVLsgrLGRRSTWRSLFGLFPKEekqrALA--ALERVGLLdKAYQR- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 153 rfSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITH--DLATAYyiSDRVVI 230
Cdd:cd03256 142 --ADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHqvDLAREY--ADRIVG 217
|
250
....*....|....*
gi 502309174 231 MRKGVVVESGDARDV 245
Cdd:cd03256 218 LKDGRIVFDGPPAEL 232
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
25-268 |
7.82e-39 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 138.89 E-value: 7.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 25 KMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEK------ADRgsIHFDGTDVKAVrSRRDREAFMAK-VQP 97
Cdd:COG4170 19 RVKAVDRVSLTL--NEGEIRGLVGESGSGKSLIAKAICGITKdnwhvtADR--FRWNGIDLLKL-SPRERRKIIGReIAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 98 VFQNPFEAFNPLTRIDEYLLAT--AHRFKG-----AKSRTeKEALAdvALQRVGLSMAE-IKGRFSHELSGGQLQRIAVA 169
Cdd:COG4170 94 IFQEPSSCLDPSAKIGDQLIEAipSWTFKGkwwqrFKWRK-KRAIE--LLHRVGIKDHKdIMNSYPHELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 170 RALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHP 249
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
250
....*....|....*....
gi 502309174 250 KHAYSIALKNAVlpPDPRE 268
Cdd:COG4170 251 HHPYTKALLRSM--PDFRQ 267
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-240 |
1.27e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 135.18 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPIGGffsrekmKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRsR 85
Cdd:COG2884 2 IRFENVSKRYPGGR-------EALSDVSLEI--EKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLK-R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAKVQPVFQ--------NPFE--AFnPLtrideyllatahRFKGAKSRTEKEALADVaLQRVGLSmaEIKGRFS 155
Cdd:COG2884 72 REIPYLRRRIGVVFQdfrllpdrTVYEnvAL-PL------------RVTGKSRKEIRRRVREV-LDLVGLS--DKAKALP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 156 HELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdALNVSIVYITHDLATAYYISDRVVIMRKGV 235
Cdd:COG2884 136 HELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
....*
gi 502309174 236 VVESG 240
Cdd:COG2884 215 LVRDE 219
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
27-263 |
1.32e-38 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 138.34 E-value: 1.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 27 KAVDDVSFALaaDKPEIFTIVGESGSGKS--TLAKMIL----GSEKADrgSIHFDGTDVKAVRSRRDREAFMAKVQPVFQ 100
Cdd:PRK11022 21 RAVDRISYSV--KQGEVVGIVGESGSGKSvsSLAIMGLidypGRVMAE--KLEFNGQDLQRISEKERRNLVGAEVAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 101 NPFEAFNPLTRIDEYLLATAHRFKGAKSRTEKEALADVaLQRVGLSMAEIK-GRFSHELSGGQLQRIAVARALIPEPKLI 179
Cdd:PRK11022 97 DPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDL-LNQVGIPDPASRlDVYPHQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 180 VADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHAYSIALKN 259
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLR 255
|
....
gi 502309174 260 AvLP 263
Cdd:PRK11022 256 A-LP 258
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
29-250 |
2.20e-38 |
|
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: 135.16 E-value: 2.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 29 VDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFmakvqpVFQNpFEAFNP 108
Cdd:cd03299 15 LKNVSLEV--ERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISY------VPQN-YALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 109 LTRIDEylLATAHRFKGAKSRTEKEALADVALQrvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMV 188
Cdd:cd03299 86 MTVYKN--IAYGLKKRKVDKKEIERKVLEIAEM---LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502309174 189 DASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPK 250
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-264 |
1.41e-37 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 133.90 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFpiGGFfsrekmKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 80
Cdd:PRK11701 2 MDQPLLSVRGLTKLY--GPR------KGCRDVSFDLYPG--EVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 ----AVRSRRDREAFM----AKVQpvfQNPFEAFNPLT----RIDEYLLATAHRFKGAKSRTekealADVALQRVGLSMA 148
Cdd:PRK11701 72 lrdlYALSEAERRRLLrtewGFVH---QHPRDGLRMQVsaggNIGERLMAVGARHYGDIRAT-----AGDWLERVEIDAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 149 EIKGRFShELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRV 228
Cdd:PRK11701 144 RIDDLPT-TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRL 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 502309174 229 VIMRKGVVVESGDARDVLEHPKHAYSIALKNAVLPP 264
Cdd:PRK11701 223 LVMKQGRVVESGLTDQVLDDPQHPYTQLLVSSVLQV 258
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
21-245 |
1.47e-37 |
|
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: 132.69 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 21 FSREKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMI-----LGSEKADRGSIHFDGTDVKAVRSrrDREAFMAKV 95
Cdd:cd03260 8 VYYGDKHALKDISLDIPKG--EITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDV--DVLELRRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 96 QPVFQ--NPFeafnPLTRIDEylLATAHRFKGAKSRTEKEALADVALQRVGLSmAEIKGRFS-HELSGGQLQRIAVARAL 172
Cdd:cd03260 84 GMVFQkpNPF----PGSIYDN--VAYGLRLHGIKLKEELDERVEEALRKAALW-DEVKDRLHaLGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502309174 173 IPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDV 245
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
6-253 |
2.48e-37 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 132.62 E-value: 2.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFpiGGFfsrekmKAVDDVSFALAADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 85
Cdd:TIGR00968 1 IEIANISKRF--GSF------QALDDVNLEVPTGS--LVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFmakvqpVFQNpFEAFNPLTRIDEYLLA-TAHRFKGAKSRTEKEALadvaLQRVGLSmaEIKGRFSHELSGGQLQ 164
Cdd:TIGR00968 71 DRKIGF------VFQH-YALFKHLTVRDNIAFGlEIRKHPKAKIKARVEEL----LELVQLE--GLGDRYPNQLSGGQRQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 165 RIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARD 244
Cdd:TIGR00968 138 RVALARALAVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDE 217
|
....*....
gi 502309174 245 VLEHPKHAY 253
Cdd:TIGR00968 218 VYDHPANPF 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-236 |
2.76e-37 |
|
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: 130.21 E-value: 2.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPiggffsreKMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavrsr 85
Cdd:cd03230 1 IEVRNLSKRYG--------KKTALDDISLTV--EKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAKVQPVFQNP--FEAFNPLtridEYLlatahrfkgaksrtekealadvalqrvglsmaeikgrfshELSGGQL 163
Cdd:cd03230 66 KEPEEVKRRIGYLPEEPslYENLTVR----ENL----------------------------------------KLSGGMK 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502309174 164 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVV 236
Cdd:cd03230 102 QRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-240 |
7.31e-37 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 130.49 E-value: 7.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 27 KAVDDVSFALAADKPEIFT-IVGESGSGKSTLAKMILGSEKADRGSIHFDGT-----DVKAVRSRRDReafmaKVQPVFQ 100
Cdd:cd03297 8 KRLPDFTLKIDFDLNEEVTgIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLPPQQR-----KIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 101 NpfEAFNPLTRIDEYLLATAHRfkgaKSRTEKEALADVALQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIPEPKLIV 180
Cdd:cd03297 83 Q--YALFPHLNVRENLAFGLKR----KRNREDRISVDELLDLLGLD--HLLNRYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 181 ADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 240
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-253 |
1.28e-36 |
|
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: 133.62 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFpigGFFSrekmkAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRS- 84
Cdd:TIGR03265 5 LSIDNIRKRF---GAFT-----ALKDISLSVK--KGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAfmakvqpVFQNpFEAFNPLTRID--EYLLATahrfKGAKsRTEKEALADVALQRVGLSMAEIKgrFSHELSGGQ 162
Cdd:TIGR03265 75 KRDYGI-------VFQS-YALFPNLTVADniAYGLKN----RGMG-RAEVAERVAELLDLVGLPGSERK--YPGQLSGGQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 163 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA 242
Cdd:TIGR03265 140 QQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTP 219
|
250
....*....|.
gi 502309174 243 RDVLEHPKHAY 253
Cdd:TIGR03265 220 QEIYRHPATPF 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
21-240 |
1.42e-36 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 128.71 E-value: 1.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 21 FSREKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvRSRRDREAFMAKV-Qpvf 99
Cdd:cd03214 7 VGYGGRTVLDDLSLSIEAG--EIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS-LSPKELARKIAYVpQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 100 qnpfeafnpltrideyllatahrfkgaksrtekealadvALQRVGLsmAEIKGRFSHELSGGQLQRIAVARALIPEPKLI 179
Cdd:cd03214 81 ---------------------------------------ALELLGL--AHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502309174 180 VADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 240
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-249 |
1.70e-36 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 130.60 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFpiggffsrEKMKAVDDVSfaLAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKA--- 81
Cdd:PRK09493 1 MIEFKNVSKHF--------GPTQVLHNID--LNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkv 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 82 -VRSRRdREAFMakvqpVFQNpFEAFNPLTRIDEYLLATAHrFKGAkSRTEKEALADVALQRVGLsmAEIKGRFSHELSG 160
Cdd:PRK09493 71 dERLIR-QEAGM-----VFQQ-FYLFPHLTALENVMFGPLR-VRGA-SKEEAEKQARELLAKVGL--AERAHHYPSELSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 161 GQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 240
Cdd:PRK09493 140 GQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
|
....*....
gi 502309174 241 DARDVLEHP 249
Cdd:PRK09493 219 DPQVLIKNP 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
28-236 |
1.75e-36 |
|
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: 129.58 E-value: 1.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 28 AVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvKAVRSRRDREAFMAKvqpvfqnpFEAFN 107
Cdd:cd03235 14 VLEDVSFEV--KPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG---KPLEKERKRIGYVPQ--------RRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 108 ---PLTRIDEYLLA-TAHRFKGAKSRTEKEALADVALQRVGlsMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADE 183
Cdd:cd03235 81 rdfPISVRDVVLMGlYGHKGLFRRLSKADKAKVDEALERVG--LSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502309174 184 PVSMVDASLRMSIVNLFRDLRDaLNVSIVYITHDLATAYYISDRVVIMRKGVV 236
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-253 |
2.81e-36 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 133.15 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFpiggffsrEKMKAVDDVSfaLAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 80
Cdd:PRK09452 10 SLSPLVELRGISKSF--------DGKEVISNLD--LTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 AVRS-RRDreafmakVQPVFQNpFEAFNPLTRIDEylLATAHRFKGA-----KSRTEkEALADVALQrvglSMAEikgRF 154
Cdd:PRK09452 80 HVPAeNRH-------VNTVFQS-YALFPHMTVFEN--VAFGLRMQKTpaaeiTPRVM-EALRMVQLE----EFAQ---RK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 155 SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKG 234
Cdd:PRK09452 142 PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
250
....*....|....*....
gi 502309174 235 VVVESGDARDVLEHPKHAY 253
Cdd:PRK09452 222 RIEQDGTPREIYEEPKNLF 240
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-252 |
4.61e-36 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 131.85 E-value: 4.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 7 ELDHVTKLFPIGGffsrEKMKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrSRR 86
Cdd:PRK11153 3 ELKNISKVFPQGG----RTIHALNNVSLHIP--AGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAL-SEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 87 DREAFMAKVQPVFQNpfeaFNPL---TRIDEylLATAHRFKGaKSRTEKEALADVALQRVGLSmaEIKGRFSHELSGGQL 163
Cdd:PRK11153 76 ELRKARRQIGMIFQH----FNLLssrTVFDN--VALPLELAG-TPKAEIKARVTELLELVGLS--DKADRYPAQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 164 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDAR 243
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVS 226
|
....*....
gi 502309174 244 DVLEHPKHA 252
Cdd:PRK11153 227 EVFSHPKHP 235
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-250 |
6.83e-36 |
|
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: 129.88 E-value: 6.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPIGGFFSRekmKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvRSR 85
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEK---KALDDVSLTI--EDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITA-KKK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAKVQPVFQNP----FE-------AFNPltrideyllataHRFKgaKSRTEKEALADVALQRVGLSmAEIKGRF 154
Cdd:TIGR04521 75 KKLKDLRKKVGLVFQFPehqlFEetvykdiAFGP------------KNLG--LSEEEAEERVKEALELVGLD-EEYLERS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 155 SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKG 234
Cdd:TIGR04521 140 PFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKG 219
|
250
....*....|....*.
gi 502309174 235 VVVESGDARDVLEHPK 250
Cdd:TIGR04521 220 KIVLDGTPREVFSDVD 235
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-236 |
8.57e-36 |
|
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: 127.65 E-value: 8.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFpiGGFfsrekmKAVDDVSfaLAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvrSR 85
Cdd:cd03262 1 IEIKNLHKSF--GDF------HVLKGID--LTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD--DK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAKVQPVFQNpFEAFNPLTRIDEYLLATAHRFKgaKSRTEKEALADVALQRVGLsmAEIKGRFSHELSGGQLQR 165
Cdd:cd03262 69 KNINELRQKVGMVFQQ-FNLFPHLTVLENITLAPIKVKG--MSKAEAEERALELLEKVGL--ADKADAYPAQLSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502309174 166 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDL-RDALNVSIVyiTHDLATAYYISDRVVIMRKGVV 236
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVV--THEMGFAREVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-248 |
1.13e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 129.36 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFPiggffsREKMKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDG---- 76
Cdd:PRK13635 1 MKEEIIRVEHISFRYP------DAATYALKDVSFSVY--EGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvls 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 77 -TDVKAVRsrrdreafmAKVQPVFQNPFEAFNPLTRIDEYLLATAHRfkgAKSRTEKEALADVALQRVGlsMAEIKGRFS 155
Cdd:PRK13635 73 eETVWDVR---------RQVGMVFQNPDNQFVGATVQDDVAFGLENI---GVPREEMVERVDQALRQVG--MEDFLNREP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 156 HELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYiSDRVVIMRKGV 235
Cdd:PRK13635 139 HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGE 217
|
250
....*....|...
gi 502309174 236 VVESGDARDVLEH 248
Cdd:PRK13635 218 ILEEGTPEEIFKS 230
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
46-254 |
2.32e-35 |
|
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: 129.54 E-value: 2.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 46 IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsrrdrEAFMAKVQPVFQNpFEAFNPLTRIDEYLLATAHRFKG 125
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNV------PPHLRHINMVFQS-YALFPHMTVEENVAFGLKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 126 AKSRTE--KEALADVALQRVGlsmaeikGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDL 203
Cdd:TIGR01187 74 RAEIKPrvLEALRLVQLEEFA-------DRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502309174 204 RDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHAYS 254
Cdd:TIGR01187 147 QEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFV 197
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-247 |
2.54e-35 |
|
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: 127.28 E-value: 2.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFpiggffsrEKMKAVDDVSFAlaADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrs 84
Cdd:COG4555 1 MIEVENLSKKY--------GKVPALKDVSFT--AKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAFMAKVQPVFQNpFEAFNPLTrIDEYL--LATAHRFKGAksrtEKEALADVALQRVGLSmaEIKGRFSHELSGGQ 162
Cdd:COG4555 66 RKEPREARRQIGVLPDE-RGLYDRLT-VRENIryFAELYGLFDE----ELKKRIEELIELLGLE--EFLDRRVGELSTGM 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 163 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDaLNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA 242
Cdd:COG4555 138 KKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSL 216
|
....*
gi 502309174 243 RDVLE 247
Cdd:COG4555 217 DELRE 221
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-248 |
6.26e-35 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 126.26 E-value: 6.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPIGgffsrekMKAVDDVSFAlaADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRS 84
Cdd:TIGR02315 1 MLEVENLSKVYPNG-------KQALKNINLN--INPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAfMAKVQPVFQNpFEAFNPLTRIDEYLlataHRFKGAK----------SRTEKEaLADVALQRVGLS-MAEIKgr 153
Cdd:TIGR02315 72 KKLRKL-RRRIGMIFQH-YNLIERLTVLENVL----HGRLGYKptwrsllgrfSEEDKE-RALSALERVGLAdKAYQR-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 154 fSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITH--DLATAYyiSDRVVIM 231
Cdd:TIGR02315 143 -ADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHqvDLAKKY--ADRIVGL 219
|
250
....*....|....*..
gi 502309174 232 RKGVVVESGDARDVLEH 248
Cdd:TIGR02315 220 KAGEIVFDGAPSELDDE 236
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-237 |
1.38e-34 |
|
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: 122.92 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFpiGGFfsrekmKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavrsr 85
Cdd:cd03216 1 LELRGITKRF--GGV------KALDGVSLSVRRG--EVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 rdreafmakvqpvFQNPFEAfnpltrideyllatahrfkgaksrtekealadvalQRVGLSMAeikgrfsHELSGGQLQR 165
Cdd:cd03216 66 -------------FASPRDA-----------------------------------RRAGIAMV-------YQLSVGERQM 90
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502309174 166 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVV 237
Cdd:cd03216 91 VEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-249 |
1.77e-34 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 127.89 E-value: 1.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSsnlLELDHVTKlfpiggFFSREKMkaVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 80
Cdd:PRK10851 1 MS---IEIANIKK------SFGRTQV--LNDISLDIPSG--QMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 AVRSRrDReafmaKVQPVFQNpFEAFNPLTRIDEylLATAHRFKGAKSRTEKEALADVALQRvgLSM---AEIKGRFSHE 157
Cdd:PRK10851 68 RLHAR-DR-----KVGFVFQH-YALFRHMTVFDN--IAFGLTVLPRRERPNAAAIKAKVTQL--LEMvqlAHLADRYPAQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 158 LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVV 237
Cdd:PRK10851 137 LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIE 216
|
250
....*....|..
gi 502309174 238 ESGDARDVLEHP 249
Cdd:PRK10851 217 QAGTPDQVWREP 228
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
27-262 |
5.16e-34 |
|
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: 124.17 E-value: 5.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 27 KAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREA---FMAKVQ--PVFQN 101
Cdd:TIGR02323 17 KGCRDVSFDLYPG--EVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAerrRLMRTEwgFVHQN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 102 PFEAF----NPLTRIDEYLLATAHRFKGaksrtEKEALADVALQRVGLSMAEIKGRFShELSGGQLQRIAVARALIPEPK 177
Cdd:TIGR02323 95 PRDGLrmrvSAGANIGERLMAIGARHYG-----NIRATAQDWLEEVEIDPTRIDDLPR-AFSGGMQQRLQIARNLVTRPR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 178 LIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHAYSIAL 257
Cdd:TIGR02323 169 LVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLL 248
|
....*
gi 502309174 258 KNAVL 262
Cdd:TIGR02323 249 VSSIL 253
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-254 |
6.00e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 127.26 E-value: 6.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFpiggffsrEKMKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrs 84
Cdd:PRK11607 19 LLEIRNLTKSF--------DGQHAVDDVSLTIY--KGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 rrdreafmakvqPVFQNPFE------AFNPLTRIDEYLlatahRFKGAKSRTEKEALADVALQRVGL-SMAEIKGRFSHE 157
Cdd:PRK11607 87 ------------PPYQRPINmmfqsyALFPHMTVEQNI-----AFGLKQDKLPKAEIASRVNEMLGLvHMQEFAKRKPHQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 158 LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVV 237
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
250
....*....|....*..
gi 502309174 238 ESGDARDVLEHPKHAYS 254
Cdd:PRK11607 230 QIGEPEEIYEHPTTRYS 246
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-257 |
7.58e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 124.53 E-value: 7.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFPiggffsREKMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILG---SEKADRGSIHFDGT 77
Cdd:PRK13640 1 MKDNIVEFKHVSFTYP------DSKKPALNDISFSI--PRGSWTALIGHNGSGKSTISKLINGlllPDDNPNSKITVDGI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 78 DVKAVRSRRDREafmaKVQPVFQNPFEAFNPLTRIDEYLLATAHRfkgAKSRTEKEALADVALQRVGlsMAEIKGRFSHE 157
Cdd:PRK13640 73 TLTAKTVWDIRE----KVGIVFQNPDNQFVGATVGDDVAFGLENR---AVPRPEMIKIVRDVLADVG--MLDYIDSEPAN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 158 LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAyYISDRVVIMRKGVVV 237
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLL 222
|
250 260
....*....|....*....|
gi 502309174 238 ESGDARDVLEHPKHAYSIAL 257
Cdd:PRK13640 223 AQGSPVEIFSKVEMLKEIGL 242
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
29-184 |
1.23e-33 |
|
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: 120.06 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 29 VDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrSRRDREAFMAKVQPVFQNPFeaFNP 108
Cdd:pfam00005 1 LKNVSLTLNPG--EILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL----TDDERKSLRKEIGYVFQDPQ--LFP 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502309174 109 LTRIDEYLLATAHRFkgAKSRTEKEALADVALQRVGLS--MAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEP 184
Cdd:pfam00005 73 RLTVRENLRLGLLLK--GLSKREKDARAEEALEKLGLGdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
31-276 |
1.72e-33 |
|
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: 125.21 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 31 DVSFALAAdkPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDreafmakVQP-------VFQnpf 103
Cdd:COG4148 17 DVDFTLPG--RGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIF-------LPPhrrrigyVFQ--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 104 EA--FNPLTrIDEYLLATAHRFKGAKSRTEKEALADValqrvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVA 181
Cdd:COG4148 85 EArlFPHLS-VRGNLLYGRKRAPRAERRISFDEVVEL------LGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 182 DEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPkhaysialknAV 261
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP----------DL 227
|
250
....*....|....*.
gi 502309174 262 LPPDP-REASAILRLR 276
Cdd:COG4148 228 LPLAGgEEAGSVLEAT 243
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-240 |
2.09e-33 |
|
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: 121.84 E-value: 2.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPIGGFfsrekmKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrsR 85
Cdd:cd03263 1 LQIRNLTKTYKKGTK------PAVDDLSLNVYKG--EIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-----R 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAKVQPVFQnpfeaFNPLtriDEYLLATAH-----RFKGaKSRTEKEALADVALQRVGLSmaEIKGRFSHELSG 160
Cdd:cd03263 68 TDRKAARQSLGYCPQ-----FDAL---FDELTVREHlrfyaRLKG-LPKSEIKEEVELLLRVLGLT--DKANKRARTLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 161 GQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 240
Cdd:cd03263 137 GMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-257 |
2.59e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 122.94 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFPIGGFFsrekmkAVDDVSFALAADKPEifTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 80
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASF------TLKDVSFNIPKGQWT--SIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 AVRSRRDREafmaKVQPVFQNPFEAFnpLTRIDEYLLA-----TAHRFKGAKSRTeKEALADValqrvglSMAEIKGRFS 155
Cdd:PRK13648 75 DDNFEKLRK----HIGIVFQNPDNQF--VGSIVKYDVAfglenHAVPYDEMHRRV-SEALKQV-------DMLERADYEP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 156 HELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYiSDRVVIMRKGV 235
Cdd:PRK13648 141 NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGT 219
|
250 260
....*....|....*....|..
gi 502309174 236 VVESGDARDVLEHPKHAYSIAL 257
Cdd:PRK13648 220 VYKEGTPTEIFDHAEELTRIGL 241
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
26-265 |
4.50e-33 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 123.76 E-value: 4.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 26 MKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEK------ADRgsIHFDGTDVKAVRSRRDREAFMAKVQPVF 99
Cdd:PRK15093 20 VKAVDRVSMTLT--EGEIRGLVGESGSGKSLIAKAICGVTKdnwrvtADR--MRFDDIDLLRLSPRERRKLVGHNVSMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 100 QNPFEAFNPLTRIDEYLLATA----------HRFKGAKSRtekealADVALQRVGL-SMAEIKGRFSHELSGGQLQRIAV 168
Cdd:PRK15093 96 QEPQSCLDPSERVGRQLMQNIpgwtykgrwwQRFGWRKRR------AIELLHRVGIkDHKDAMRSFPYELTEGECQKVMI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 169 ARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEH 248
Cdd:PRK15093 170 AIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTT 249
|
250
....*....|....*..
gi 502309174 249 PKHAYSIALKNAVlpPD 265
Cdd:PRK15093 250 PHHPYTQALIRAI--PD 264
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
21-234 |
7.20e-33 |
|
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: 118.50 E-value: 7.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 21 FSREKMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDReafmakvqpvfq 100
Cdd:cd00267 7 FRYGGRTALDNVSLTL--KAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 101 npfeafnpltrideyllatahrfkgaksrtekealadvalQRVGlsmaeikgrFSHELSGGQLQRIAVARALIPEPKLIV 180
Cdd:cd00267 73 ----------------------------------------RRIG---------YVPQLSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502309174 181 ADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKG 234
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-245 |
1.35e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 125.13 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPigGFfsrekmKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvKAVRS 84
Cdd:COG1129 4 LLEMRGISKSFG--GV------KALDGVSLELRPG--EVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAFMAKVQPVFQ--NPFEAfnpLTRIDEYLLATAHRFKGAKSRTEKEALADVALQRVGLSM---AEIKgrfshELS 159
Cdd:COG1129 71 RSPRDAQAAGIAIIHQelNLVPN---LSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIdpdTPVG-----DLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 160 GGQLQRIAVARALIPEPKLIVADEPVSMVDASlrmSIVNLF---RDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVV 236
Cdd:COG1129 143 VAQQQLVEIARALSRDARVLILDEPTASLTER---EVERLFriiRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
....*....
gi 502309174 237 VESGDARDV 245
Cdd:COG1129 219 VGTGPVAEL 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-261 |
2.08e-32 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 125.74 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 23 REKMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDG-------------TDVKAVRSRRDRE 89
Cdd:PRK10261 26 QQKIAAVRNLSFSL--QRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvielSEQSAAQMRHVRG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 90 AFMAKVqpvFQNPFEAFNPLTRIDEYLlATAHRFKGAKSRTEKEALADVALQRVGLSMAE-IKGRFSHELSGGQLQRIAV 168
Cdd:PRK10261 104 ADMAMI---FQEPMTSLNPVFTVGEQI-AESIRLHQGASREEAMVEAKRMLDQVRIPEAQtILSRYPHQLSGGMRQRVMI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 169 ARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEH 248
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHA 259
|
250
....*....|...
gi 502309174 249 PKHAYSIALKNAV 261
Cdd:PRK10261 260 PQHPYTRALLAAV 272
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
21-247 |
3.08e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.40 E-value: 3.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 21 FSREKMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREafmaKVQPVFQ 100
Cdd:PRK13632 17 YPNSENNALKNVSFEI--NEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK----KIGIIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 101 NPFEAFNPLTRIDEylLATAHRFKGAKSRTEKEALADVAlQRVGlsMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIV 180
Cdd:PRK13632 91 NPDNQFIGATVEDD--IAFGLENKKVPPKKMKDIIDDLA-KKVG--MEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502309174 181 ADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAyYISDRVVIMRKGVVVESGDARDVLE 247
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-242 |
3.25e-31 |
|
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: 116.38 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFPIGGffsrEKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGA----GELTILKGISLEVEAG--ESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 AV------RSRRDREAFmakvqpVFQNpFEAFNPLTRIdEYLLATAHRfkgaKSRTEKEALADVALQRVGLSmaeikGRF 154
Cdd:COG4181 78 ALdedaraRLRARHVGF------VFQS-FQLLPTLTAL-ENVMLPLEL----AGRRDARARARALLERVGLG-----HRL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 155 SH---ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYiSDRVVIM 231
Cdd:COG4181 141 DHypaQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRL 219
|
250
....*....|.
gi 502309174 232 RKGVVVESGDA 242
Cdd:COG4181 220 RAGRLVEDTAA 230
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-238 |
1.25e-30 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 114.37 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPIGGFfsreKMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrS 84
Cdd:TIGR02211 1 LLKCENLGKRYQEGKL----DTRVLKGVSLSI--GKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKL-S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAFMAK-----VQpvFQNPFEAFNPLTRIDEYLLAtahrfkGAKSRTEKEALADVALQRVGLsmaeiKGRFSH--- 156
Cdd:TIGR02211 74 SNERAKLRNKklgfiYQ--FHHLLPDFTALENVAMPLLI------GKKSVKEAKERAYEMLEKVGL-----EHRINHrps 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 157 ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYIsDRVVIMRKGVV 236
Cdd:TIGR02211 141 ELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
..
gi 502309174 237 VE 238
Cdd:TIGR02211 220 FN 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-248 |
1.88e-30 |
|
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: 119.86 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPIGGFfsrekmkAVDDVSFALAAdkPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsr 85
Cdd:COG4988 337 IELEDVSFSYPGGRP-------ALDGLSLTIPP--GERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL--- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 rDREAFMAKVQPVFQNPfeafnpltrideYLlatahrFKG--------AKSRTEKEALADvALQRVGLS---------MA 148
Cdd:COG4988 405 -DPASWRRQIAWVPQNP------------YL------FAGtirenlrlGRPDASDEELEA-ALEAAGLDefvaalpdgLD 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 149 EIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLrdALNVSIVYITHDLATAyYISDRV 228
Cdd:COG4988 465 TPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITHRLALL-AQADRI 541
|
250 260
....*....|....*....|
gi 502309174 229 VIMRKGVVVESGDARDVLEH 248
Cdd:COG4988 542 LVLDDGRIVEQGTHEELLAK 561
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-236 |
1.98e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 113.76 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTklfpiggfFSREKMKAVDDVSFALAAdkPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDvkavRSR 85
Cdd:COG4619 1 LELEGLS--------FRVGGKPILSPVSLTLEA--GECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKP----LSA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAKVQPVFQNP--FEAfnpltRIDEYLLATAHrfkgAKSRTEKEALADVALQRVGLSmAEIKGRFSHELSGGQL 163
Cdd:COG4619 67 MPPPEWRRQVAYVPQEPalWGG-----TVRDNLPFPFQ----LRERKFDRERALELLERLGLP-PDILDKPVERLSGGER 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502309174 164 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVV 236
Cdd:COG4619 137 QRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-252 |
2.64e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.08 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFpiGGFfsrekmkavdDVSFALAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVR-S 84
Cdd:COG3840 2 LRLDDLTYRY--GDF----------PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRdreafmaKVQPVFQ--NPFE----------AFNPLTRIdeyllatahrfkgakSRTEKEALADvALQRVGLsmAEIKG 152
Cdd:COG3840 70 ER-------PVSMLFQenNLFPhltvaqniglGLRPGLKL---------------TAEQRAQVEQ-ALERVGL--AGLLD 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 153 RFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMR 232
Cdd:COG3840 125 RLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVA 204
|
250 260
....*....|....*....|
gi 502309174 233 KGVVVESGDARDVLEHPKHA 252
Cdd:COG3840 205 DGRIAADGPTAALLDGEPPP 224
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
5-250 |
2.80e-30 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 116.52 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPIGGffsrEKMKAVDDVSfaLAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrS 84
Cdd:TIGR02314 1 MIKLSNITKVFHQGT----KTIQALNNVS--LHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTL-S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAFMAKVQPVFQNpfeaFNPLT-RIDEYLLATAHRFKGaKSRTEKEALADVALQRVGLSmaEIKGRFSHELSGGQL 163
Cdd:TIGR02314 74 NSELTKARRQIGMIFQH----FNLLSsRTVFGNVALPLELDN-TPKDEIKRKVTELLALVGLG--DKHDSYPSNLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 164 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDAR 243
Cdd:TIGR02314 147 QRVAIARALASNPKVLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVS 226
|
....*..
gi 502309174 244 DVLEHPK 250
Cdd:TIGR02314 227 EIFSHPK 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-245 |
5.05e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.21 E-value: 5.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFpiGGFfsrekmKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvK 80
Cdd:COG3845 1 MMPPALELRGITKRF--GGV------VANDDVSLTVR--PGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 AVRSRRDREAFMAKVQPVFQNpFEAFNPLTRIDEYLLATAHRFKGAKSRteKEALADVA--LQRVGLSM---AEIkgrfs 155
Cdd:COG3845 68 PVRIRSPRDAIALGIGMVHQH-FMLVPNLTVAENIVLGLEPTKGGRLDR--KAARARIRelSERYGLDVdpdAKV----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 156 HELSGGQLQRIAVARALIPEPKLIVADEPVSM-----VDAslrmsivnLFRDLRD--ALNVSIVYITHDLATAYYISDRV 228
Cdd:COG3845 140 EDLSVGEQQRVEILKALYRGARILILDEPTAVltpqeADE--------LFEILRRlaAEGKSIIFITHKLREVMAIADRV 211
|
250
....*....|....*..
gi 502309174 229 VIMRKGVVVESGDARDV 245
Cdd:COG3845 212 TVLRRGKVVGTVDTAET 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
36-251 |
5.51e-30 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 113.69 E-value: 5.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 36 LAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFM----AKVQPVFQNpFEAFnPLTR 111
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIrqlrQHVGFVFQN-FNLF-PHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 112 IDEYLLATAHRFKGaKSRTEKEALADVALQRVGLSMAEikGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDAS 191
Cdd:PRK11264 102 VLENIIEGPVIVKG-EPKEEATARARELLAKVGLAGKE--TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 192 LRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKH 251
Cdd:PRK11264 179 LVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
29-260 |
6.18e-30 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 113.64 E-value: 6.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 29 VDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKAD----RGSIHFDGTDV--KAVRSRrdreafmaKVQPVFQNP 102
Cdd:PRK10418 19 VHGVSLTL--QRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVapCALRGR--------KIATIMQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 103 FEAFNPLTRIDEYLLATAHrfkgAKSRTEKEALADVALQRVGLSMAE-IKGRFSHELSGGQLQRIAVARALIPEPKLIVA 181
Cdd:PRK10418 89 RSAFNPLHTMHTHARETCL----ALGKPADDATLTAALEAVGLENAArVLKLYPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502309174 182 DEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHAYSIALKNA 260
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
20-250 |
6.62e-30 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 113.74 E-value: 6.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 20 FFSREKMKAVDdvsfaLAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRR------DR---EA 90
Cdd:COG4598 18 FGDLEVLKGVS-----LTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDgelvpaDRrqlQR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 91 FMAKVQPVFQNpfeaFN---PLTRIDEYLLATAHRFKgaKSRTEKEALADVALQRVGLsmAEIKGRFSHELSGGQLQRIA 167
Cdd:COG4598 93 IRTRLGMVFQS----FNlwsHMTVLENVIEAPVHVLG--RPKAEAIERAEALLAKVGL--ADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 168 VARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVyITHDLATAYYISDRVVIMRKGVVVESGDARDVLE 247
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLV-VTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFG 243
|
...
gi 502309174 248 HPK 250
Cdd:COG4598 244 NPK 246
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
29-245 |
1.49e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 113.29 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 29 VDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV--KAVRSRRDreafmaKVQPVFQNPFEAF 106
Cdd:PRK13650 23 LNDVSFHV--KQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteENVWDIRH------KIGMVFQNPDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 107 NPLTRIDEylLATAHRFKGAKSRTEKEALaDVALQRVGlsMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVS 186
Cdd:PRK13650 95 VGATVEDD--VAFGLENKGIPHEEMKERV-NEALELVG--MQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502309174 187 MVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAyYISDRVVIMRKGVVVESGDARDV 245
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-253 |
1.68e-29 |
|
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: 117.63 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTklfpiggF-FSREKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAV-- 82
Cdd:COG2274 474 IELENVS-------FrYPGDSPPVLDNISLTIKPG--ERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIdp 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 83 RSRRDREAFmakvqpVFQNPFeafnpltrideylLatahrFKG---------AKSRTEKEALAdvALQRVGLsMAEIK-- 151
Cdd:COG2274 545 ASLRRQIGV------VLQDVF-------------L-----FSGtirenitlgDPDATDEEIIE--AARLAGL-HDFIEal 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 152 --------GRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAyY 223
Cdd:COG2274 598 pmgydtvvGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-R 674
|
250 260 270
....*....|....*....|....*....|
gi 502309174 224 ISDRVVIMRKGVVVESGDARDVLEHPKHAY 253
Cdd:COG2274 675 LADRIIVLDKGRIVEDGTHEELLARKGLYA 704
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-234 |
2.52e-29 |
|
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: 109.39 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPiggffSREKmKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsr 85
Cdd:cd03228 1 IEFKNVSFSYP-----GRPK-PVLKDVSLTIKPG--EKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 rDREAFMAKVQPVFQNPFeafnpltrideyllatahRFKGaksrTEKEALadvalqrvglsmaeikgrfsheLSGGQLQR 165
Cdd:cd03228 70 -DLESLRKNIAYVPQDPF------------------LFSG----TIRENI----------------------LSGGQRQR 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502309174 166 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAyYISDRVVIMRKG 234
Cdd:cd03228 105 IAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTI-RDADRIIVLDDG 170
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
23-237 |
3.29e-29 |
|
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: 110.42 E-value: 3.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 23 REKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavRSRRDREAFMakvqpVFQNP 102
Cdd:cd03226 10 KKGTEILDDLSLDLYAG--EIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK--AKERRKSIGY-----VMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 103 FEAFNPLTRIDEYLLatahrfkGAKSRTEKEALADVALQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIPEPKLIVAD 182
Cdd:cd03226 81 DYQLFTDSVREELLL-------GLKELDAGNEQAETVLKDLDLY--ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502309174 183 EPVSMVDASLRMSIVNLFRDLRDALNVSIVyITHDLATAYYISDRVVIMRKGVVV 237
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIV-ITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
27-251 |
3.99e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 111.28 E-value: 3.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 27 KAVDDVSFALAADKpeIFTIVGESGSGKSTLAK-------MILGSeKADrGSIHFDGTDVKAvrSRRDREAFMAKVQPVF 99
Cdd:COG1117 25 QALKDINLDIPENK--VTALIGPSGCGKSTLLRclnrmndLIPGA-RVE-GEILLDGEDIYD--PDVDVVELRRRVGMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 100 Q--NPFeafnPLTrIDE---YLLatahRFKGAKSRTEKEALADVALQRVGLsMAEIKGRFSH---ELSGGQLQRIAVARA 171
Cdd:COG1117 99 QkpNPF----PKS-IYDnvaYGL----RLHGIKSKSELDEIVEESLRKAAL-WDEVKDRLKKsalGLSGGQQQRLCIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 172 LIPEPKLIVADEPVSMVD--ASLRmsIVNLFRDLRDalNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHP 249
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDpiSTAK--IEELILELKK--DYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNP 244
|
..
gi 502309174 250 KH 251
Cdd:COG1117 245 KD 246
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
28-257 |
1.27e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 110.56 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 28 AVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK------AVRSRrdreAFMakvqpVFQN 101
Cdd:PRK13633 25 ALDDVNLEV--KKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeenlwDIRNK----AGM-----VFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 102 PFE-----------AFNPltridEYLlatahrfkGAKSRtEKEALADVALQRVGlsMAEIKGRFSHELSGGQLQRIAVAR 170
Cdd:PRK13633 94 PDNqivativeedvAFGP-----ENL--------GIPPE-EIRERVDESLKKVG--MYEYRRHAPHLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 171 ALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYiSDRVVIMRKGVVVESGDARDVLEHPK 250
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVE 236
|
....*..
gi 502309174 251 HAYSIAL 257
Cdd:PRK13633 237 MMKKIGL 243
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
36-250 |
4.13e-28 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 108.56 E-value: 4.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 36 LAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSI-----HFD---GTDVKAVRSRRDreafmaKVQPVFQNpfeaFN 107
Cdd:PRK11124 23 LDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnHFDfskTPSDKAIRELRR------NVGMVFQQ----YN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 108 --PLTRIDEYLLATAHRFKGAkSRTEKEALADVALQRvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPV 185
Cdd:PRK11124 93 lwPHLTVQQNLIEAPCRVLGL-SKDQALARAEKLLER--LRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502309174 186 SMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDArDVLEHPK 250
Cdd:PRK11124 170 AALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQ 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-261 |
5.11e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 109.43 E-value: 5.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFpiGGFfsrekmKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavRSR 85
Cdd:COG4152 2 LELKGLTKRF--GDK------TAVDDVSFTVP--KGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD--PED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMakvqpvfqnPFE-AFNPLTRIDEYLLATAhRFKGAKSRTEKEALADVaLQRVGLsmAEIKGRFSHELSGGQLQ 164
Cdd:COG4152 70 RRRIGYL---------PEErGLYPKMKVGEQLVYLA-RLKGLSKAEAKRRADEW-LERLGL--GDRANKKVEELSKGNQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 165 RIAVARALIPEPKLIVADEPVSMVD---ASLrmsIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGD 241
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGS 212
|
250 260
....*....|....*....|.
gi 502309174 242 ARDVLE-HPKHAYSIALKNAV 261
Cdd:COG4152 213 VDEIRRqFGRNTLRLEADGDA 233
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-238 |
8.85e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 108.03 E-value: 8.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPIGGffsrEKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 85
Cdd:COG4525 4 LTVRHVSVRYPGGG----QPQPALQDVSLTIESG--EFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RdreafmaKVqpVFQNpfEAFNP-LTRIDEylLATAHRFKGAkSRTEKEALADVALQRVGLSMAEikGRFSHELSGGQLQ 164
Cdd:COG4525 78 R-------GV--VFQK--DALLPwLNVLDN--VAFGLRLRGV-PKAERRARAEELLALVGLADFA--RRRIWQLSGGMRQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502309174 165 RIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIM--RKGVVVE 238
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
25-247 |
1.13e-27 |
|
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: 106.75 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 25 KMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKV---QPVFQN 101
Cdd:cd03224 12 KSQILFGVSLTVPEG--EIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVpegRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 102 pfeafnpLTrIDEYLLATAHRFKGAKsrtEKEALADValqrvgLSM----AEIKGRFSHELSGGQLQRIAVARALIPEPK 177
Cdd:cd03224 90 -------LT-VEENLLLGAYARRRAK---RKARLERV------YELfprlKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 178 LIVADEPVSMVDASLRMSIVNLFRDLRDaLNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLE 247
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-236 |
2.66e-27 |
|
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: 105.57 E-value: 2.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPIGgffsrekMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRsR 85
Cdd:cd03292 1 IEFINVTKTYPNG-------TAALDGINISI--SAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLR-G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAKVQPVFQNpFEAFNPLTRIDEylLATAHRFKGAKSRTEKEALADvALQRVGLSMAEikGRFSHELSGGQLQR 165
Cdd:cd03292 71 RAIPYLRRKIGVVFQD-FRLLPDRNVYEN--VAFALEVTGVPPREIRKRVPA-ALELVGLSHKH--RALPAELSGGEQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502309174 166 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVV 236
Cdd:cd03292 145 VAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-275 |
3.22e-27 |
|
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: 108.66 E-value: 3.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 31 DVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVFQnpfEA--FNP 108
Cdd:TIGR02142 15 DADFTLPGQ--GVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQ---EArlFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 109 LTrIDEYLLATAHRFKGAKSRTEKEALADValqrvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMV 188
Cdd:TIGR02142 90 LS-VRGNLRYGMKRARPSERRISFERVIEL------LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 189 DASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHAY------SIALKNAVL 262
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWlaredqGSLIEGVVA 242
|
250
....*....|...
gi 502309174 263 PPDPREASAILRL 275
Cdd:TIGR02142 243 EHDQHYGLTALRL 255
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-240 |
3.25e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 105.06 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFpiggffsREKmKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvrSR 85
Cdd:cd03269 1 LEVENVTKRF-------GRV-TALDDISFSVE--KGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI--AA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAKVQPVFQNpfeafnplTRIDEYLLATAhRFKGAKsRTEKEALADVALQRVGLSmaEIKGRFSHELSGGQLQR 165
Cdd:cd03269 69 RNRIGYLPEERGLYPK--------MKVIDQLVYLA-QLKGLK-KEEARRRIDEWLERLELS--EYANKRVEELSKGNQQK 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502309174 166 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 240
Cdd:cd03269 137 VQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
27-284 |
3.35e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.06 E-value: 3.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 27 KAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV--KAVRSRRDREafmaKVQPVFQNPfe 104
Cdd:PRK13637 21 KALDNVNIEI--EDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRK----KVGLVFQYP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 105 afnpltridEYLLATAHRFK----GAKSR--TEKEALADV--ALQRVGLSMAEIKGRFSHELSGGQLQRIAVARALIPEP 176
Cdd:PRK13637 93 ---------EYQLFEETIEKdiafGPINLglSEEEIENRVkrAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 177 KLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHAYSIA 256
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLESIG 243
|
250 260
....*....|....*....|....*...
gi 502309174 257 LknAVlppdPREASAILRLRQRNAETNE 284
Cdd:PRK13637 244 L--AV----PQVTYLVRKLRKKGFNIPD 265
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
46-249 |
4.68e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 106.64 E-value: 4.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 46 IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVFQNP----FE-------AFNPLTride 114
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQFPehqlFEetvekdiCFGPMN---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 115 yllatahrFkGAkSRTEKEALADVALQRVGLSmAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRM 194
Cdd:PRK13634 114 --------F-GV-SEEDAKQKAREMIELVGLP-EELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502309174 195 SIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHP 249
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-240 |
5.27e-27 |
|
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: 104.58 E-value: 5.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPiggffsreKMKAVDDVSFALAadkPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrsR 85
Cdd:cd03264 1 LQLENLTKRYG--------KKRALDGVSLTLG---PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-----L 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAKVQPVFQNPfeAFNPLTRIDEYLlATAHRFKGAKSRTEKEAlADVALQRVGLsmAEIKGRFSHELSGGQLQR 165
Cdd:cd03264 65 KQPQKLRRRIGYLPQEF--GVYPNFTVREFL-DYIAWLKGIPSKEVKAR-VDEVLELVNL--GDRAKKKIGSLSGGMRRR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502309174 166 IAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLrdALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 240
Cdd:cd03264 139 VGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
29-246 |
5.57e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 105.62 E-value: 5.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 29 VDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRdreafMAKVQPVF-QNPFEAFn 107
Cdd:PRK13548 18 LDDVSLTLRPG--EVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAE-----LARRRAVLpQHSSLSF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 108 PLTrideyllatAH------RFKGAKSRTEKEALADVALQRVGLsmAEIKGRFSHELSGGQLQRIAVARALI------PE 175
Cdd:PRK13548 90 PFT---------VEevvamgRAPHGLSRAEDDALVAAALAQVDL--AHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502309174 176 PKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLA-TAYYiSDRVVIMRKGVVVESGDARDVL 246
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNlAARY-ADRIVLLHQGRLVADGTPAEVL 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
28-250 |
9.15e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 104.71 E-value: 9.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 28 AVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIH-----FD---GTDVKAVRSRRDreafmaKVQPVF 99
Cdd:COG4161 17 ALFDINLECPSG--ETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqFDfsqKPSEKAIRLLRQ------KVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 100 QNpFEAFNPLTRIDEYLLATAHRFKGAKSRTEKEAlaDVALQRvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLI 179
Cdd:COG4161 89 QQ-YNLWPHLTVMENLIEAPCKVLGLSKEQAREKA--MKLLAR--LRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502309174 180 VADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDArDVLEHPK 250
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQ 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
43-251 |
1.09e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 104.99 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 43 IFTIVGESGSGKSTLAKMI-----LGSEKADRGSIHFDGTDVkavrSRRDREAFMAKVQPVFQNPfeafNPLTR--IDEY 115
Cdd:PRK14247 31 ITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDI----FKMDVIELRRRVQMVFQIP----NPIPNlsIFEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 116 LLATAHRFKGAKSRTEKEALADVALQRVGLsMAEIKGRF---SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASL 192
Cdd:PRK14247 103 VALGLKLNRLVKSKKELQERVRWALEKAQL-WDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPEN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502309174 193 RMSIVNLFRDLRDalNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKH 251
Cdd:PRK14247 182 TAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
35-252 |
1.18e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 105.05 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 35 ALAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRS---------RRDREAFMAKVQPVFQNpFEA 105
Cdd:PRK10619 25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadKNQLRLLRTRLTMVFQH-FNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 106 FNPLTRIDEYLLATAHRFkgAKSRTEKEALADVALQRVGLSMAEiKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPV 185
Cdd:PRK10619 104 WSHMTVLENVMEAPIQVL--GLSKQEARERAVKYLAKVGIDERA-QGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502309174 186 SMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHA 252
Cdd:PRK10619 181 SALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
34-240 |
1.42e-26 |
|
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: 103.73 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 34 FALAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVR-SRRdreafmaKVQPVFQ--NPFEAFNPLT 110
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPpADR-------PVSMLFQenNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 111 RIDeylLAtahRFKGAKSRTEKEALADVALQRVGLsmAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDA 190
Cdd:cd03298 90 NVG---LG---LSPGLKLTAEDRQAIEVALARVGL--AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502309174 191 SLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 240
Cdd:cd03298 162 ALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
35-253 |
7.53e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 105.50 E-value: 7.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 35 ALAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVFQNpFEAFNPLTRIDE 114
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS-FALMPHMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 115 YLLATAHRFKGAKSRTEKealADVALQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRM 194
Cdd:PRK10070 127 TAFGMELAGINAEERREK---ALDALRQVGLE--NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502309174 195 SIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHAY 253
Cdd:PRK10070 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
29-252 |
8.82e-26 |
|
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: 101.77 E-value: 8.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 29 VDDVSfaLAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRdreafMAkvqpVFQNpFEAFNP 108
Cdd:TIGR01184 1 LKGVN--LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR-----MV----VFQN-YSLLPW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 109 LTRIDEYLLATaHRFKGAKSRTEKEALADVALQRVGLSMAEIKgrFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMV 188
Cdd:TIGR01184 69 LTVRENIALAV-DRVLPDLSKSERRAIVEEHIALVGLTEAADK--RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502309174 189 DASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG-----------DARDVLEHPKHA 252
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGqilevpfprprDRLEVVEDPSYY 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-240 |
1.56e-25 |
|
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: 100.91 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFpiGGFfsrekmKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrsR 85
Cdd:cd03265 1 IEVENLVKKY--GDF------EAVRGVSFRVR--RGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-----V 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAKVQPVFQNPfeafnpltRIDEYLLATAH-----RFKGAKSRTEKEALADVaLQRVGLsmAEIKGRFSHELSG 160
Cdd:cd03265 66 REPREVRRRIGIVFQDL--------SVDDELTGWENlyihaRLYGVPGAERRERIDEL-LDFVGL--LEAADRLVKTYSG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 161 GQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 240
Cdd:cd03265 135 GMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
28-253 |
1.92e-25 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 105.62 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 28 AVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVR--SRRDREAFMAkvqpvfQNPFeA 105
Cdd:COG4987 350 VLDGLSLTLPPG--ERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDedDLRRRIAVVP------QRPH-L 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 106 FNplTRIDEYLLAtahrfkGAKSRTEKEALAdvALQRVGLS------------MAEIKGRFsheLSGGQLQRIAVARALI 173
Cdd:COG4987 421 FD--TTLRENLRL------ARPDATDEELWA--ALERVGLGdwlaalpdgldtWLGEGGRR---LSGGERRRLALARALL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 174 PEPKLIVADEPVSMVDASLRMSIvnlFRDLRDAL-NVSIVYITHDLATAYYIsDRVVIMRKGVVVESGDARDVLEHPKHA 252
Cdd:COG4987 488 RDAPILLLDEPTEGLDAATEQAL---LADLLEALaGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQNGRY 563
|
.
gi 502309174 253 Y 253
Cdd:COG4987 564 R 564
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-240 |
3.93e-25 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 99.75 E-value: 3.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPIggffSREKMKAVDDVSFAlaADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavrs 84
Cdd:cd03266 1 MITADALTKRFRD----VKKTVQAVDGVSFT--VKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 rrdreafmakvqpvfQNPFEA------FNPLTRIDEYLLATAH-----RFKGAKSRTEKEALADVALQrvgLSMAEIKGR 153
Cdd:cd03266 71 ---------------KEPAEArrrlgfVSDSTGLYDRLTARENleyfaGLYGLKGDELTARLEELADR---LGMEELLDR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 154 FSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRK 233
Cdd:cd03266 133 RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHR 211
|
....*..
gi 502309174 234 GVVVESG 240
Cdd:cd03266 212 GRVVYEG 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
25-253 |
6.23e-25 |
|
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: 99.67 E-value: 6.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 25 KMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRR-----------DREafma 93
Cdd:COG0410 15 GIHVLHGVSLEVEEG--EIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRiarlgigyvpeGRR---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 94 kvqpVFQNpfeafnpLTrIDEYLLAtahrfkGAKSRTEKEALADvALQRVgLSM----AEIKGRFSHELSGGQLQRIAVA 169
Cdd:COG0410 89 ----IFPS-------LT-VEENLLL------GAYARRDRAEVRA-DLERV-YELfprlKERRRQRAGTLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 170 RALIPEPKLIVADEPV-----SMVDAslrmsIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARD 244
Cdd:COG0410 149 RALMSRPKLLLLDEPSlglapLIVEE-----IFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAE 222
|
250
....*....|.
gi 502309174 245 VLEHP--KHAY 253
Cdd:COG0410 223 LLADPevREAY 233
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
28-245 |
2.32e-24 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 97.98 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 28 AVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVqPVFQnpfEAFN 107
Cdd:TIGR03410 15 ILRGVSLEVPKG--EVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV-PQGR---EIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 108 PLTrIDEYLLATAHRFKGAKSRTEKEALAdvaLQRVGLSMaeiKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSM 187
Cdd:TIGR03410 89 RLT-VEENLLTGLAALPRRSRKIPDEIYE---LFPVLKEM---LGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502309174 188 VDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDV 245
Cdd:TIGR03410 162 IQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-249 |
3.66e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 99.92 E-value: 3.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPiGGFFsrekmkAVDDVSFALAaDKpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 85
Cdd:PRK11650 4 LKLQAVRKSYD-GKTQ------VIKGIDLDVA-DG-EFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 rDREAFMakvqpVFQNpfeafnpltrideYLLaTAHRfkgaksrTEKEALAdVALQRVGLSMAEIKGRFSH--------- 156
Cdd:PRK11650 75 -DRDIAM-----VFQN-------------YAL-YPHM-------SVRENMA-YGLKIRGMPKAEIEERVAEaarilelep 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 157 -------ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVV 229
Cdd:PRK11650 127 lldrkprELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVV 206
|
250 260
....*....|....*....|
gi 502309174 230 IMRKGVVVESGDARDVLEHP 249
Cdd:PRK11650 207 VMNGGVAEQIGTPVEVYEKP 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
27-234 |
4.11e-24 |
|
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: 95.96 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 27 KAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvKAVRSRRDREAFMAKVqpvfqnpfeAF 106
Cdd:cd03215 14 GAVRDVSFEVRAG--EIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG---KPVTRRSPRDAIRAGI---------AY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 107 NPLTRIDEYLLATahrfkgaksrtekealadvalQRVGLSMAeikgrFSHELSGGQLQRIAVARALIPEPKLIVADEPVS 186
Cdd:cd03215 80 VPEDRKREGLVLD---------------------LSVAENIA-----LSSLLSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502309174 187 MVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKG 234
Cdd:cd03215 134 GVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
25-251 |
5.30e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.54 E-value: 5.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 25 KMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMI-----LGSEKADRGSIHFDGTDVKAVRSrrDREAFMAKVQPVF 99
Cdd:PRK14239 17 KKKALNSVSLDF--YPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYSPRT--DTVDLRKEIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 100 Q--NPFeafnPLTRIDEYLLATahRFKGAKsrtEKEALaDVALQR--VGLSM-AEIKGRFsHE----LSGGQLQRIAVAR 170
Cdd:PRK14239 93 QqpNPF----PMSIYENVVYGL--RLKGIK---DKQVL-DEAVEKslKGASIwDEVKDRL-HDsalgLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 171 ALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPK 250
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
.
gi 502309174 251 H 251
Cdd:PRK14239 240 H 240
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-249 |
6.40e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 97.37 E-value: 6.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFpiGGFFsrekmkAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRF--GGLL------AVNNVNLEV--REQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 AVRSRRdrEAFMAKVQpVFQNpFEAFNPLTRIdEYLLATAHR------FKG-----AKSRTEKEAL--ADVALQRVGLSm 147
Cdd:PRK11300 71 GLPGHQ--IARMGVVR-TFQH-VRLFREMTVI-ENLLVAQHQqlktglFSGllktpAFRRAESEALdrAATWLERVGLL- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 148 aEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDR 227
Cdd:PRK11300 145 -EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDR 223
|
250 260
....*....|....*....|..
gi 502309174 228 VVIMRKGVVVESGDARDVLEHP 249
Cdd:PRK11300 224 IYVVNQGTPLANGTPEEIRNNP 245
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
21-257 |
1.33e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.09 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 21 FSREKMKAVDD---VSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREafmaKVQP 97
Cdd:PRK13642 12 FKYEKESDVNQlngVSFSIT--KGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR----KIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 98 VFQNPFEAFNPLTRIDEYLLATAHRfkgAKSRTEKEALADVALqrVGLSMAEIKGRFSHELSGGQLQRIAVARALIPEPK 177
Cdd:PRK13642 86 VFQNPDNQFVGATVEDDVAFGMENQ---GIPREEMIKRVDEAL--LAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 178 LIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYiSDRVVIMRKGVVVESGDARDVLEHPKHAYSIAL 257
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGL 239
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
29-221 |
2.35e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.86 E-value: 2.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 29 VDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKAD---RGSIHFDGTDVKAVRSRRDREAFMakvqpvFQNPFea 105
Cdd:COG4136 17 LAPLSLTVA--PGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGIL------FQDDL-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 106 FNP-LTRIDEYLLATAHRFKGAksrtEKEALADVALQRVGLS-MAEikgRFSHELSGGQLQRIAVARALIPEPKLIVADE 183
Cdd:COG4136 87 LFPhLSVGENLAFALPPTIGRA----QRRARVEQALEEAGLAgFAD---RDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 502309174 184 PVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATA 221
Cdd:COG4136 160 PFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA 197
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-240 |
2.67e-23 |
|
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: 94.59 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFpiggffsrEKMKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 85
Cdd:cd03268 1 LKTNDLTKTY--------GKKRVLDDISLHVK--KGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAKVQPVFQNpfeafnpLT-RIDEYLLATAHRFkgaksrteKEALADVALQRVGLSmaEIKGRFSHELSGGQLQ 164
Cdd:cd03268 71 LRRIGALIEAPGFYPN-------LTaRENLRLLARLLGI--------RKKRIDEVLDVVGLK--DSAKKKVKGFSLGMKQ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502309174 165 RIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 240
Cdd:cd03268 134 RLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
31-234 |
3.47e-23 |
|
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: 94.70 E-value: 3.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 31 DVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrSRRDREAFMAKVQPVFQnpfeAFNPLt 110
Cdd:TIGR02982 23 DINLEI--NPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGA-SKKQLVQLRRRIGYIFQ----AHNLL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 111 ridEYLLATAHRFKGAK-----SRTEKEALADVALQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPV 185
Cdd:TIGR02982 95 ---GFLTARQNVQMALElqpnlSYQEARERARAMLEAVGLG--DHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502309174 186 SMVDASLRMSIVNLFRDLRDALNVSIVYITHDlATAYYISDRVVIMRKG 234
Cdd:TIGR02982 170 AALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDG 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
43-251 |
4.28e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.50 E-value: 4.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 43 IFTIVGESGSGKSTLAKM------ILGSEKADRGSIHFDGTDVKAVRSRRDREafmaKVQPVFQNPfeafNPLTRIDEY- 115
Cdd:PRK14246 38 IFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDIFQIDAIKLRK----EVGMVFQQP----NPFPHLSIYd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 116 LLATAHRFKGAKSRTEKEALADVALQRVGLsMAEIKGRF---SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASL 192
Cdd:PRK14246 110 NIAYPLKSHGIKEKREIKKIVEECLRKVGL-WKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVN 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502309174 193 RMSIVNLFRDLRDalNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKH 251
Cdd:PRK14246 189 SQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
29-246 |
5.54e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.76 E-value: 5.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 29 VDDVSFALAADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRdreafMAKVQPVF-QNPfeAFN 107
Cdd:COG4604 17 LDDVSLTIPKGG--ITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRE-----LAKRLAILrQEN--HIN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 108 PLTRIDEylLATAHRFKGAKSR--TEKEALADVALQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPV 185
Cdd:COG4604 88 SRLTVRE--LVAFGRFPYSKGRltAEDREIIDEAIAYLDLE--DLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502309174 186 SMVDASLRMSIVNLFRDLRDALNVSIVYITHDL--ATAYyiSDRVVIMRKGVVVESGDARDVL 246
Cdd:COG4604 164 NNLDMKHSVQMMKLLRRLADELGKTVVIVLHDInfASCY--ADHIVAMKDGRVVAQGTPEEII 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
28-246 |
1.10e-22 |
|
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: 93.70 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 28 AVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsrrDREAFMAKVQPVFQNPFeAFN 107
Cdd:cd03252 17 ILDNISLRIKPG--EVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA----DPAWLRRQVGVVLQENV-LFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 108 --------------PLTRIDEYL-LATAHRFkgaksrtekealadvaLQRVGLSMAEIKGRFSHELSGGQLQRIAVARAL 172
Cdd:cd03252 90 rsirdnialadpgmSMERVIEAAkLAGAHDF----------------ISELPEGYDTIVGEQGAGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502309174 173 IPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAYYiSDRVVIMRKGVVVESGDARDVL 246
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELL 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
43-251 |
1.27e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.14 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 43 IFTIVGESGSGKSTLAKMI-----LGSEKADRGSIHFDG-----TDVKAVRSRRdreafmaKVQPVFQNPfeafNPLTRI 112
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGrniysPDVDPIEVRR-------EVGMVFQYP----NPFPHL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 113 DEYL-LATAHRFKG-AKSRTEKEALADVALQRVGLsMAEIKGR---FSHELSGGQLQRIAVARALIPEPKLIVADEPVSM 187
Cdd:PRK14267 101 TIYDnVAIGVKLNGlVKSKKELDERVEWALKKAAL-WDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502309174 188 VDASLRMSIVNLFRDLRDALnvSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKH 251
Cdd:PRK14267 180 IDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
31-234 |
1.33e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 93.34 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 31 DVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR-----RDRE-AFMAKvqpvFQNPFE 104
Cdd:PRK11629 27 NVSFSI--GEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaelRNQKlGFIYQ----FHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 105 AFNPLTRIDEYLLAtahrfkGAKSRTEKEALADVALQRVGLSmAEIKGRFShELSGGQLQRIAVARALIPEPKLIVADEP 184
Cdd:PRK11629 101 DFTALENVAMPLLI------GKKKPAEINSRALEMLAAVGLE-HRANHRPS-ELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502309174 185 VSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISdRVVIMRKG 234
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDG 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
23-247 |
1.61e-22 |
|
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: 97.18 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 23 REKMKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTD--VKAVRSRRDREAFMAKVQPVFQ 100
Cdd:TIGR03269 294 RGVVKAVDNVSLEVK--EGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDewVDMTKPGPDGRGRAKRYIGILH 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 101 NPFEAFNPLTRIDEYLLATAHRFKGAKSRTEkealADVALQRVGLS---MAEIKGRFSHELSGGQLQRIAVARALIPEPK 177
Cdd:TIGR03269 372 QEYDLYPHRTVLDNLTEAIGLELPDELARMK----AVITLKMVGFDeekAEEILDKYPDELSEGERHRVALAQVLIKEPR 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 178 LIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLE 247
Cdd:TIGR03269 448 IVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-252 |
1.79e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.01 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 29 VDDVSFALAADKpeIFTIVGESGSGKSTLAKMIlgSEKADRGSIHFDGTDV----KAVRSRRDREAFMAKVQPVFQ--NP 102
Cdd:PRK14271 37 LDQVSMGFPARA--VTSLMGPTGSGKTTFLRTL--NRMNDKVSGYRYSGDVllggRSIFNYRDVLEFRRRVGMLFQrpNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 103 FeafnPLTRIDEYLLAT-AHRFKgakSRTEKEALADVALQRVGLSMAeIKGRFSH---ELSGGQLQRIAVARALIPEPKL 178
Cdd:PRK14271 113 F----PMSIMDNVLAGVrAHKLV---PRKEFRGVAQARLTEVGLWDA-VKDRLSDspfRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502309174 179 IVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVyiTHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHA 252
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIV--THNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
27-246 |
2.10e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 97.12 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 27 KAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsrrDREAFMAKVQPVFQNPFeAF 106
Cdd:TIGR01193 488 NILSDISLTIKMN--SKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI----DRHTLRQFINYLPQEPY-IF 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 107 NPlTRIDEYLLatahrfkGAKSRTEKEALADValqrvgLSMAEIKG-----------RFSHE---LSGGQLQRIAVARAL 172
Cdd:TIGR01193 561 SG-SILENLLL-------GAKENVSQDEIWAA------CEIAEIKDdienmplgyqtELSEEgssISGGQKQRIALARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502309174 173 IPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlnvSIVYITHDLATAYYiSDRVVIMRKGVVVESGDARDVL 246
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
47-248 |
2.15e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.04 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 47 VGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVFQNP----FE-------AFNPltridey 115
Cdd:PRK13649 39 IGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPesqlFEetvlkdvAFGP------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 116 llataHRFkgAKSRTEKEALADVALQRVGLSmAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMS 195
Cdd:PRK13649 112 -----QNF--GVSQEEAEALAREKLALVGIS-ESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502309174 196 IVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEH 248
Cdd:PRK13649 184 LMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
6-248 |
2.39e-22 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 96.65 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPIGgffsreKMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavrsR 85
Cdd:TIGR01842 317 LSVENVTIVPPGG------KKPTLRGISFSL--QAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK----Q 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAKVQPVFQNpFEAFnpltriDEYLLATAHRF-KGAKSRTEKEA--LADVALQRVGLSM---AEIkGRFSHELS 159
Cdd:TIGR01842 385 WDRETFGKHIGYLPQD-VELF------PGTVAENIARFgENADPEKIIEAakLAGVHELILRLPDgydTVI-GPGGATLS 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 160 GGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdALNVSIVYITHDLAtAYYISDRVVIMRKGVVVES 239
Cdd:TIGR01842 457 GGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALK-ARGITVVVITHRPS-LLGCVDKILVLQDGRIARF 534
|
....*....
gi 502309174 240 GDARDVLEH 248
Cdd:TIGR01842 535 GERDEVLAK 543
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
42-242 |
2.55e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.82 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 42 EIFTIVGESGSGKSTLAKMILGSEK--ADRGSIHFDGTDVKAV----RSRRDreAFMAkvqpvFQNPfeafnplTRID-- 113
Cdd:COG0396 27 EVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELspdeRARAG--IFLA-----FQYP-------VEIPgv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 114 --EYLLATA--HRFKGAKSRTEKEALADVALQRVGLSMAEIKgRFSHE-LSGGQLQRIAVARALIPEPKLIVADEPVSMV 188
Cdd:COG0396 93 svSNFLRTAlnARRGEELSAREFLKLLKEKMKELGLDEDFLD-RYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502309174 189 DA-SLRMsIVNLFRDLRDAlNVSIVYITHdlataY-----YIS-DRVVIMRKGVVVESGDA 242
Cdd:COG0396 172 DIdALRI-VAEGVNKLRSP-DRGILIITH-----YqrildYIKpDFVHVLVDGRIVKSGGK 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
28-234 |
7.20e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 92.07 E-value: 7.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 28 AVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDreafmakvqPVFQNpfEAFN 107
Cdd:PRK11248 16 ALEDINLTLESG--ELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERG---------VVFQN--EGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 108 PLTRIDEYLlATAHRFKGAkSRTEKEALADVALQRVGLSMAEikGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSM 187
Cdd:PRK11248 83 PWRNVQDNV-AFGLQLAGV-EKMQRLEIAHQMLKKVGLEGAE--KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502309174 188 VDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKG 234
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
25-250 |
2.02e-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: 90.29 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 25 KMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvrsrrdreafmakvQPVFQN--- 101
Cdd:cd03218 12 KRKVVNGVSLSV--KQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK--------------LPMHKRarl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 102 -----PFEA--FNPLTrIDEYLLATAHRFKgaKSRTEKEALADVALQRvgLSMAEIKGRFSHELSGGQLQRIAVARALIP 174
Cdd:cd03218 76 gigylPQEAsiFRKLT-VEENILAVLEIRG--LSKKEREEKLEELLEE--FHITHLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502309174 175 EPKLIVADEPVSMVDASLRMSIVNLFRDLRDaLNVSIVyIT-HDLATAYYISDRVVIMRKGVVVESGDARDVLEHPK 250
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVL-ITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-217 |
2.41e-21 |
|
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: 89.46 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKlfpiggffSREKMKAVDDVSFALAAdkPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRS 84
Cdd:COG4133 2 MLEAENLSC--------RRGERLLFSGLSFTLAA--GEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAFMakvqpVFQNPfeAFNP-LTrIDEYlLATAHRFKGAKSRtekEALADVALQRVGLsmAEIKGRFSHELSGGQL 163
Cdd:COG4133 72 DYRRRLAY-----LGHAD--GLKPeLT-VREN-LRFWAALYGLRAD---REAIDEALEAVGL--AGLADLPVRQLSAGQK 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502309174 164 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHD 217
Cdd:COG4133 138 RRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-240 |
2.68e-21 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 93.69 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTklfpiggfFS-REKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrs 84
Cdd:COG1132 340 IEFENVS--------FSyPGDRPVLKDISLTIPPG--ETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDL-- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 rrDREAFMAKVQPVFQNPFeafnpltrideyLLA-TAH---RFkGAKSRTEKEALAdvALQRVGL-----SMAE----IK 151
Cdd:COG1132 408 --TLESLRRQIGVVPQDTF------------LFSgTIReniRY-GRPDATDEEVEE--AAKAAQAhefieALPDgydtVV 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 152 GRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVD----ASLRMSIVNLFRDlrdalnVSIVYITHDLATayyI--S 225
Cdd:COG1132 471 GERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDteteALIQEALERLMKG------RTTIVIAHRLST---IrnA 541
|
250
....*....|....*
gi 502309174 226 DRVVIMRKGVVVESG 240
Cdd:COG1132 542 DRILVLDDGRIVEQG 556
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
28-221 |
3.29e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.83 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 28 AVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHfdgtdvkavRSRRDREAFMakVQpvfqnpfeafn 107
Cdd:NF040873 7 VLHGVDLTIPAG--SLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR---------RAGGARVAYV--PQ----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 108 pLTRIDEYLLAT----------AHRFKGAKSRTEKEALADVALQRVGLsmAEIKGRFSHELSGGQLQRIAVARALIPEPK 177
Cdd:NF040873 63 -RSEVPDSLPLTvrdlvamgrwARRGLWRRLTRDDRAAVDDALERVGL--ADLAGRQLGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502309174 178 LIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATA 221
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELV 182
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
34-241 |
5.59e-21 |
|
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: 88.76 E-value: 5.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 34 FALAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV-KAVRSRRdreafmaKVQPVFQNPfEAFNPLTRI 112
Cdd:TIGR01277 17 FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHtGLAPYQR-------PVSMLFQEN-NLFAHLTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 113 DEYLLATAHRFKgaKSRTEKEALADVAlQRVGLsmAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASL 192
Cdd:TIGR01277 89 QNIGLGLHPGLK--LNAEQQEKVVDAA-QQVGI--ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502309174 193 RMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGD 241
Cdd:TIGR01277 164 REEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-286 |
5.59e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.05 E-value: 5.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFpiggffsREKMkAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSY-------GDKA-VVNGLSFTVASG--ECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 AvRSRRDReafmAKVQPVFQnpFEAFNPLTRIDEYLLATAhRFKGAKSRtEKEALADVALQRVGLSmAEIKGRFShELSG 160
Cdd:PRK13536 107 A-RARLAR----ARIGVVPQ--FDNLDLEFTVRENLLVFG-RYFGMSTR-EIEAVIPSLLEFARLE-SKADARVS-DLSG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 161 GQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 240
Cdd:PRK13536 176 GMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 502309174 241 DARDVLEHPKHAYSIALKNAvlppDPREASAILRLRQRNAETNEAT 286
Cdd:PRK13536 255 RPHALIDEHIGCQVIEIYGG----DPHELSSLVKPYARRIEVSGET 296
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
36-253 |
5.68e-21 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 88.35 E-value: 5.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 36 LAADKPEIFTIVGESGSGKSTLAKMILGSE--KADRGSIHFDGTDVKAV----RSRRDreAFMAkvqpvFQNPFEAfnPL 109
Cdd:cd03217 21 LTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLppeeRARLG--IFLA-----FQYPPEI--PG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 110 TRIDEYLlatahrfkgaksrtekealadvalqrvglsmaeikgRFSHE-LSGGQLQRIAVARALIPEPKLIVADEPVSMV 188
Cdd:cd03217 92 VKNADFL------------------------------------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502309174 189 DA-SLRMsIVNLFRDLRDAlNVSIVYITH--DLAtAYYISDRVVIMRKGVVVESGDARDVLEHPKHAY 253
Cdd:cd03217 136 DIdALRL-VAEVINKLREE-GKSVLIITHyqRLL-DYIKPDRVHVLYDGRIVKSGDKELALEIEKKGY 200
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
34-241 |
8.55e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.49 E-value: 8.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 34 FALAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTD-VKAVRSRRdreafmakvqPV---FQ-NPFeaFNP 108
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhTTTPPSRR----------PVsmlFQeNNL--FSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 109 LTrIDEYLLATAHrfKGAK-SRTEKEALADVAlQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSM 187
Cdd:PRK10771 86 LT-VAQNIGLGLN--PGLKlNAAQREKLHAIA-RQMGIE--DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502309174 188 VDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGD 241
Cdd:PRK10771 160 LDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-240 |
9.12e-21 |
|
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: 88.03 E-value: 9.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPiggffsREKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsr 85
Cdd:cd03245 3 IEFRNVSFSYP------NQEIPALDNVSLTIRAG--EKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 rDREAFMAKVQPVFQNPF----------EAFNPLTRiDEYLLATAhRFKGAKSRTEKEALadvalqrvGLSMaEI--KGR 153
Cdd:cd03245 72 -DPADLRRNIGYVPQDVTlfygtlrdniTLGAPLAD-DERILRAA-ELAGVTDFVNKHPN--------GLDL-QIgeRGR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 154 FsheLSGGQLQRIAVARALIPEPKLIVADEPVSMVD-ASLRMSIVNLFRDLRDAlnvSIVYITHDLAtAYYISDRVVIMR 232
Cdd:cd03245 140 G---LSGGQRQAVALARALLNDPPILLLDEPTSAMDmNSEERLKERLRQLLGDK---TLIIITHRPS-LLDLVDRIIVMD 212
|
....*...
gi 502309174 233 KGVVVESG 240
Cdd:cd03245 213 SGRIVADG 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
28-250 |
1.04e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 89.37 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 28 AVDDVSFAlaADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavRSRRDREAFMAKVQPVFQNPFE--- 104
Cdd:PRK13639 17 ALKGINFK--AEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK--YDKKSLLEVRKTVGIVFQNPDDqlf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 105 --------AFNPLTRideyllatahrfkgAKSRTEKEALADVALQRVGLSMAEIKGrfSHELSGGQLQRIAVARALIPEP 176
Cdd:PRK13639 93 aptveedvAFGPLNL--------------GLSKEEVEKRVKEALKAVGMEGFENKP--PHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502309174 177 KLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPK 250
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
18-249 |
1.06e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 89.05 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 18 GGFFSREKMKAVDDVSfaLAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAfMAKVQP 97
Cdd:PRK11831 12 GVSFTRGNRCIFDNIS--LTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTV-RKRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 98 VFQ--------NPFE--AFnPL---TRIDEYLLATAHRFKgaksrtekealadvaLQRVGL-SMAEIKgrfSHELSGGQL 163
Cdd:PRK11831 89 LFQsgalftdmNVFDnvAY-PLrehTQLPAPLLHSTVMMK---------------LEAVGLrGAAKLM---PSELSGGMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 164 QRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDAR 243
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQ 229
|
....*.
gi 502309174 244 DVLEHP 249
Cdd:PRK11831 230 ALQANP 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
29-248 |
1.33e-20 |
|
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: 91.35 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 29 VDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrSRRDREAFMAKV----QPVfqnpfE 104
Cdd:COG4618 348 LRGVSFSLEPG--EVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL----SQWDREELGRHIgylpQDV-----E 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 105 AFNpltrideyllAT-----AhRFKGAKSrtekealADV--ALQRVG-----LSMAE----IKGRFSHELSGGQLQRIAV 168
Cdd:COG4618 417 LFD----------GTiaeniA-RFGDADP-------EKVvaAAKLAGvhemiLRLPDgydtRIGEGGARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 169 ARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLAtAYYISDRVVIMRKGVVVESGDARDVLEH 248
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
29-236 |
2.38e-20 |
|
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: 85.73 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 29 VDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsrrDREAFMAKVQPVFQnpfeafnp 108
Cdd:cd03246 18 LRNVSFSIEPG--ESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW----DPNELGDHVGYLPQ-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 109 ltriDEYLlatahrFKGaksrtekealadvalqrvglSMAEIKgrfsheLSGGQLQRIAVARALIPEPKLIVADEPVSMV 188
Cdd:cd03246 84 ----DDEL------FSG--------------------SIAENI------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502309174 189 DASLRMSIVNLFRDLRdALNVSIVYITHDLATAyYISDRVVIMRKGVV 236
Cdd:cd03246 128 DVEGERALNQAIAALK-AAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
20-243 |
3.05e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 87.76 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 20 FFSREKMKAVDdvsfaLAADKPEIFTIVGESGSGKSTLAKMILG---SEKADRGSIHFDGTDV-KAVRSRRDREAFMAKV 95
Cdd:PRK09984 14 FNQHQALHAVD-----LNIHHGEMVALLGPSGSGKSTLLRHLSGlitGDKSAGSHIELLGRTVqREGRLARDIRKSRANT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 96 QPVFQNpFEAFNPLTRIDEYLLATAHR-------FKGAKSRTEKEALAdvALQRVGLSmaeikgRFSHE----LSGGQLQ 164
Cdd:PRK09984 89 GYIFQQ-FNLVNRLSVLENVLIGALGStpfwrtcFSWFTREQKQRALQ--ALTRVGMV------HFAHQrvstLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502309174 165 RIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDAR 243
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-231 |
3.25e-20 |
|
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: 90.42 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPiggffsrEKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKA--VR 83
Cdd:TIGR02857 322 LEFSGVSVAYP-------GRRPALRPVSFTVPPG--ERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADadAD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 84 SRRDREAFmakvqpVFQNPFeaFNPLTRIDEYLLATahrfKGAKSRTEKEALADVALQRV----GLSMAEIKGRFSHELS 159
Cdd:TIGR02857 393 SWRDQIAW------VPQHPF--LFAGTIAENIRLAR----PDASDAEIREALERAGLDEFvaalPQGLDTPIGEGGAGLS 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502309174 160 GGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAyYISDRVVIM 231
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA-ALADRIVVL 529
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
27-261 |
3.55e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 87.91 E-value: 3.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 27 KAVDDVSFALAADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVFQNP---- 102
Cdd:PRK13646 21 QAIHDVNTEFEQGK--YYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFPesql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 103 FEafnplTRIDEYLLATAHRFK----GAKSRTEKeALADVALQRVGLSMAEIkgrfshELSGGQLQRIAVARALIPEPKL 178
Cdd:PRK13646 99 FE-----DTVEREIIFGPKNFKmnldEVKNYAHR-LLMDLGFSRDVMSQSPF------QMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 179 IVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPKHA--YSIA 256
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLadWHIG 246
|
....*
gi 502309174 257 LKNAV 261
Cdd:PRK13646 247 LPEIV 251
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-247 |
4.27e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.99 E-value: 4.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFPiggffsreKMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKmIL------GSEKadrGSIHF 74
Cdd:PRK13549 1 MMEYLLEMKNITKTFG--------GVKALDNVSLKV--RAGEIVSLCGENGAGKSTLMK-VLsgvyphGTYE---GEIIF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 75 DGTDVKAvRSRRDREA----------FMAKVQPVFQNPFEAfNPLTRideyllatAHRFKGAKSRTEKEALadvaLQRVG 144
Cdd:PRK13549 67 EGEELQA-SNIRDTERagiaiihqelALVKELSVLENIFLG-NEITP--------GGIMDYDAMYLRAQKL----LAQLK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 145 LSMaEIKGRFSHeLSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdALNVSIVYITHDLATAYYI 224
Cdd:PRK13549 133 LDI-NPATPVGN-LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACIYISHKLNEVKAI 209
|
250 260
....*....|....*....|...
gi 502309174 225 SDRVVIMRKGVVVESGDARDVLE 247
Cdd:PRK13549 210 SDTICVIRDGRHIGTRPAAGMTE 232
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
36-247 |
4.97e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.87 E-value: 4.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 36 LAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVFQNPFEAFNPLTRIDEY 115
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEETVLKDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 116 LLATAHRfkgAKSRTEKEALADVALQRVGLSmAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMS 195
Cdd:PRK13643 107 AFGPQNF---GIPKEKAEKIAAEKLEMVGLA-DEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502309174 196 IVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLE 247
Cdd:PRK13643 183 MMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-246 |
5.35e-20 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 86.68 E-value: 5.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 3 SNLLELDHVTklfpiggfFSREKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSE-KADRGSIH-----FDG 76
Cdd:COG1119 1 DPLLELRNVT--------VRRGGKTILDDISWTVKPG--EHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRlfgerRGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 77 TDVKAVRSRrdreafMAKVQPVFQnpfEAFNPLTRIDEYLL----ATAHRFKgaKSRTEKEALADVALQRVGlsMAEIKG 152
Cdd:COG1119 71 EDVWELRKR------IGLVSPALQ---LRFPRDETVLDVVLsgffDSIGLYR--EPTDEQRERARELLELLG--LAHLAD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 153 RFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHdlatayYISD------ 226
Cdd:COG1119 138 RPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH------HVEEippgit 211
|
250 260
....*....|....*....|
gi 502309174 227 RVVIMRKGVVVESGDARDVL 246
Cdd:COG1119 212 HVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-249 |
5.47e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 87.01 E-value: 5.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 11 VTKLFP---IGGF-FSREKMKAVDDVSFALAADKpeIFTIVGESGSGKSTLAKMI-----LGSEKADRGSIHFDGTDVKA 81
Cdd:PRK14258 1 MSKLIPaikVNNLsFYYDTQKILEGVSMEIYQSK--VTAIIGPSGCGKSTFLKCLnrmneLESEVRVEGRVEFFNQNIYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 82 VRSRRDReaFMAKVQPVFQNPfeAFNPLTRIDEylLATAHRFKGAKSRTEKEALADVALQRVGLsMAEIKGRFSH---EL 158
Cdd:PRK14258 79 RRVNLNR--LRRQVSMVHPKP--NLFPMSVYDN--VAYGVKIVGWRPKLEIDDIVESALKDADL-WDEIKHKIHKsalDL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 159 SGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIM-----RK 233
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRI 231
|
250
....*....|....*.
gi 502309174 234 GVVVESGDARDVLEHP 249
Cdd:PRK14258 232 GQLVEFGLTKKIFNSP 247
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
24-264 |
6.42e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.98 E-value: 6.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 24 EKMKAVDDVSFALAADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSI---------HFDGTDVKAVRSRRDREAFMA- 93
Cdd:PRK13631 37 NELVALNNISYTFEKNK--IYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdKKNNHELITNPYSKKIKNFKEl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 94 --KVQPVFQNP-FEAFNplTRIDEYLLATAHRFKGAKSRTEKeaLADVALQRVGLSMAEIKgRFSHELSGGQLQRIAVAR 170
Cdd:PRK13631 115 rrRVSMVFQFPeYQLFK--DTIEKDIMFGPVALGVKKSEAKK--LAKFYLNKMGLDDSYLE-RSPFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 171 ALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPK 250
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
250
....*....|....
gi 502309174 251 HaysIALKNAVLPP 264
Cdd:PRK13631 269 I---INSTSIQVPR 279
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-246 |
1.07e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.83 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFPIGgffsrekMKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 80
Cdd:PRK13636 1 MEDYILKVEELNYNYSDG-------THALKGININIK--KGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 avRSRRDREAFMAKVQPVFQNPFeafNPLTRIDEYLLATAHRFKGAKSRTEKEALADVALQRVGLSmaEIKGRFSHELSG 160
Cdd:PRK13636 72 --YSRKGLMKLRESVGMVFQDPD---NQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIE--HLKDKPTHCLSF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 161 GQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 240
Cdd:PRK13636 145 GQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQG 224
|
....*.
gi 502309174 241 DARDVL 246
Cdd:PRK13636 225 NPKEVF 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-247 |
1.53e-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: 84.97 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 20 FFSREKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREafmaKVQPVF 99
Cdd:cd03254 10 FSYDEKKPVLKDINFSIKPG--ETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS----MIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 100 QNPFeAFNPlTRIDEYLLATahrfKGAKSRTEKEALADVALQRVGLSMAE----IKGRFSHELSGGQLQRIAVARALIPE 175
Cdd:cd03254 84 QDTF-LFSG-TIMENIRLGR----PNATDEEVIEAAKEAGAHDFIMKLPNgydtVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502309174 176 PKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVyITHDLATAYYiSDRVVIMRKGVVVESGDARDVLE 247
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKG-RTSII-IAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
27-250 |
1.66e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 86.04 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 27 KAVDDVSFALAADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVFQNP---- 102
Cdd:PRK13641 21 KGLDNISFELEEGS--FVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPeaql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 103 FE-------AFNPLTrideyllatahrFKGAKSRTEKEALAdvALQRVGLSmAEIKGRFSHELSGGQLQRIAVARALIPE 175
Cdd:PRK13641 99 FEntvlkdvEFGPKN------------FGFSEDEAKEKALK--WLKKVGLS-EDLISKSPFELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502309174 176 PKLIVADEPVSMVDASLRMSIVNLFRDLRDALNvSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPK 250
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-249 |
1.85e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.81 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPIGgffsrekMKAVDDVSfaLAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTD------ 78
Cdd:PRK13644 1 MIRLENVSYSYPDG-------TPALENIN--LVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDtgdfsk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 79 VKAVRSRrdreafmakVQPVFQNPFEAFnpLTRIDEYLLATAhrfkgaksrTEKEALADVAL-QRVGLSMAEIK-GRFSH 156
Cdd:PRK13644 72 LQGIRKL---------VGIVFQNPETQF--VGRTVEEDLAFG---------PENLCLPPIEIrKRVDRALAEIGlEKYRH 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 157 E----LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLaTAYYISDRVVIMR 232
Cdd:PRK13644 132 RspktLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNL-EELHDADRIIVMD 209
|
250
....*....|....*..
gi 502309174 233 KGVVVESGDARDVLEHP 249
Cdd:PRK13644 210 RGKIVLEGEPENVLSDV 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-247 |
4.67e-19 |
|
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: 86.80 E-value: 4.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFpiGGffsrekMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILG--SEKADRGSIHFDGTDVKAv 82
Cdd:TIGR02633 1 LLEMKGIVKTF--GG------VKALDGIDLEVRPG--ECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKA- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 83 RSRRDREAfmaKVQPVFQNPFEAFNPLTRIDEYLLATAHRFKGAksRTEKEAL---ADVALQRVGLSMAEIKgRFSHELS 159
Cdd:TIGR02633 70 SNIRDTER---AGIVIIHQELTLVPELSVAENIFLGNEITLPGG--RMAYNAMylrAKNLLRELQLDADNVT-RPVGDYG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 160 GGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdALNVSIVYITHDLATAYYISDRVVIMRKGVVVES 239
Cdd:TIGR02633 144 GGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQHVAT 222
|
....*...
gi 502309174 240 GDARDVLE 247
Cdd:TIGR02633 223 KDMSTMSE 230
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-242 |
8.48e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.12 E-value: 8.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 2 SSNLLELDHVTKLFPiggffsreKMKAVDDVSFAlaADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvKA 81
Cdd:PRK11288 1 SSPYLSFDGIGKTFP--------GVKALDDISFD--CRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG---QE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 82 VRSRRDREAFMAKVQPVFQNpfeafnpLTRIDE-------YLLATAHRFkGAKSRTEKEALADVALQRVGLSM---AEIK 151
Cdd:PRK11288 68 MRFASTTAALAAGVAIIYQE-------LHLVPEmtvaenlYLGQLPHKG-GIVNRRLLNYEAREQLEHLGVDIdpdTPLK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 152 grfshELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASlrmSIVNLFR---DLRDALNVsIVYITHDLATAYYISDRV 228
Cdd:PRK11288 140 -----YLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR---EIEQLFRvirELRAEGRV-ILYVSHRMEEIFALCDAI 210
|
250
....*....|....
gi 502309174 229 VIMRKGVVVESGDA 242
Cdd:PRK11288 211 TVFKDGRYVATFDD 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
23-263 |
1.52e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.31 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 23 REKMKAVDDVSFaLAADKPEIfTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAfmakVQPVFQNP 102
Cdd:PRK13652 14 SGSKEALNNINF-IAPRNSRI-AVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF----VGLVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 103 FE-----------AFNPLTR-IDEYllATAHRfkgaksrtekealADVALQRVGLSmaEIKGRFSHELSGGQLQRIAVAR 170
Cdd:PRK13652 88 DDqifsptveqdiAFGPINLgLDEE--TVAHR-------------VSSALHMLGLE--ELRDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 171 ALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPK 250
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
250
....*....|...
gi 502309174 251 HAYSIALKNAVLP 263
Cdd:PRK13652 231 LLARVHLDLPSLP 243
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
42-250 |
1.82e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 84.31 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 42 EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRrDREAFMakvqpVFQNpfEAFNPLTRIDEYL----- 116
Cdd:PRK11000 30 EFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA-ERGVGM-----VFQS--YALYPHLSVAENMsfglk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 117 LATAhrfkgAKSRTEK--EALADValqrvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRM 194
Cdd:PRK11000 102 LAGA-----KKEEINQrvNQVAEV------LQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502309174 195 SIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPK 250
Cdd:PRK11000 171 QMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-237 |
2.25e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.16 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPIGgffsREKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKmILGS-EKADRGSIHFDGTDVKAVr 83
Cdd:PRK10535 4 LLELKDIRRSYPSG----EEQVEVLKGISLDIYAG--EMVAIVGASGSGKSTLMN-ILGClDKPTSGTYRVAGQDVATL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 84 srrDREAFMAKVQPVFQNPFEAFNPLTRideylLATAHRFK-----GAKSRTEKEALADVALQRVGLsmAEIKGRFSHEL 158
Cdd:PRK10535 76 ---DADALAQLRREHFGFIFQRYHLLSH-----LTAAQNVEvpavyAGLERKQRLLRAQELLQRLGL--EDRVEYQPSQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502309174 159 SGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVyITHDLATAYYiSDRVVIMRKGVVV 237
Cdd:PRK10535 146 SGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVII-VTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
27-237 |
2.69e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.68 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 27 KAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK------AVRSR-------RDREAFMA 93
Cdd:COG1129 266 GVVRDVSFSVRAG--EILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdAIRAGiayvpedRKGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 94 KvQPVFQNpfeafnpLTrideylLATAHRFKGAK--SRTEKEALADVALQRVGLSMAEIKGRFShELSGGQLQRIAVARA 171
Cdd:COG1129 344 D-LSIREN-------IT------LASLDRLSRGGllDRRRERALAEEYIKRLRIKTPSPEQPVG-NLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502309174 172 LIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVV 237
Cdd:COG1129 409 LATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
27-240 |
2.83e-18 |
|
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: 81.89 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 27 KAVDDVSFALAADKPeiFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVR--SRRDREAFMAKVQPVFQNPFE 104
Cdd:cd03253 15 PVLKDVSFTIPAGKK--VAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTldSLRRAIGVVPQDTVLFNDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 105 ---AFNPLTRIDEYLLATAhrfKGAKSRTEKEALADVALQRVGlsmaeikgrfshE----LSGGQLQRIAVARALIPEPK 177
Cdd:cd03253 93 yniRYGRPDATDEEVIEAA---KAAQIHDKIMRFPDGYDTIVG------------ErglkLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502309174 178 LIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAYYiSDRVVIMRKGVVVESG 240
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-245 |
3.01e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.31 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTklfpiggFFSREKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRS 84
Cdd:COG3845 257 VLEVENLS-------VRDDRGVPALKDVSLEVRAG--EILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAFMAKV------------QPVFQNPFeafnpLTRIDEYLLATAHRFKGAKSRTEKEALA---DVALQRVGLSMAE 149
Cdd:COG3845 328 RERRRLGVAYIpedrlgrglvpdMSVAENLI-----LGRYRRPPFSRGGFLDRKAIRAFAEELIeefDVRTPGPDTPARS 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 150 ikgrfsheLSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVV 229
Cdd:COG3845 403 --------LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIA 473
|
250
....*....|....*.
gi 502309174 230 IMRKGVVVESGDARDV 245
Cdd:COG3845 474 VMYEGRIVGEVPAAEA 489
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
27-240 |
3.03e-18 |
|
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: 80.43 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 27 KAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRsrrdrEAFMAKVQPVFQNPfeaf 106
Cdd:cd03247 16 QVLKNLSLELKQG--EKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-----KALSSLISVLNQRP---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 107 npltrideYLLATAHRfkgaksrtekealadvalQRVGLsmaeikgRFShelsGGQLQRIAVARALIPEPKLIVADEPVS 186
Cdd:cd03247 85 --------YLFDTTLR------------------NNLGR-------RFS----GGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502309174 187 MVDASLRMSIVNL-FRDLRDAlnvSIVYITHDLATAYYIsDRVVIMRKGVVVESG 240
Cdd:cd03247 128 GLDPITERQLLSLiFEVLKDK---TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-217 |
3.30e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.30 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 2 SSNLLELDHVTklfpiggfFSREKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKA 81
Cdd:PRK10247 4 NSPLLQLQNVG--------YLAGDAKILNNISFSLRAG--EFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 82 VRSrrdrEAFMAKVQPVFQNPfeAFNPLTRIDEYLLATAHRfkgaKSRTEKEALADvALQRVGLSMAEIKGRFShELSGG 161
Cdd:PRK10247 74 LKP----EIYRQQVSYCAQTP--TLFGDTVYDNLIFPWQIR----NQQPDPAIFLD-DLERFALPDTILTKNIA-ELSGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502309174 162 QLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHD 217
Cdd:PRK10247 142 EKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
46-236 |
3.91e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.65 E-value: 3.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 46 IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRsrrDREAFMakvqpvFQN----PFEafnplTRIDEYLLatah 121
Cdd:PRK11247 43 VVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR---EDTRLM------FQDarllPWK-----KVIDNVGL---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 122 rfkGAKSRTEKEALAdvALQRVGLsmAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFR 201
Cdd:PRK11247 105 ---GLKGQWRDAALQ--ALAAVGL--ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIE 177
|
170 180 190
....*....|....*....|....*....|....*
gi 502309174 202 DLRDALNVSIVYITHDLATAYYISDRVVIMRKGVV 236
Cdd:PRK11247 178 SLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
27-250 |
4.50e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 81.23 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 27 KAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKA----VRSRRD-----REAfmakvqP 97
Cdd:COG1137 17 TVVKDVSLEVNQG--EIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmhKRARLGigylpQEA------S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 98 VFQNpfeafnpLTrIDEYLLATAHRFKgaKSRTEKEALADVALQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIPEPK 177
Cdd:COG1137 89 IFRK-------LT-VEDNILAVLELRK--LSKKEREERLEELLEEFGIT--HLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502309174 178 LIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVyIT-HD----LAtayyISDRVVIMRKGVVVESGDARDVLEHPK 250
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKER-GIGVL-ITdHNvretLG----ICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-234 |
7.62e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.13 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPiggffsreKMKAVDDVSFALAADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRS 84
Cdd:PRK10762 4 LLQLKGIDKAFP--------GVKALSGAALNVYPGR--VMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAFMAKVQ---------PVFQNPF---EAFNPLTRIDeyllatahrfkgaksRTEKEALADVALQRVGLSMAeikg 152
Cdd:PRK10762 74 KSSQEAGIGIIHqelnlipqlTIAENIFlgrEFVNRFGRID---------------WKKMYAEADKLLARLNLRFS---- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 153 rfSH----ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRV 228
Cdd:PRK10762 135 --SDklvgELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDV 211
|
....*.
gi 502309174 229 VIMRKG 234
Cdd:PRK10762 212 TVFRDG 217
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
29-246 |
9.31e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.58 E-value: 9.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 29 VDDVSfaLAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRrdreAFMAKVQPVFQNPFEAFNP 108
Cdd:PRK09536 19 LDGVD--LSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR----AASRRVASVPQDTSLSFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 109 LTRIDEYLLATAHRFKGAKSRTEKEALADVALQRVGlsMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMV 188
Cdd:PRK09536 93 DVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTG--VAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502309174 189 DASLRMSIVNLFRDLRDALNVSIVYItHDLATAYYISDRVVIMRKGVVVESGDARDVL 246
Cdd:PRK09536 171 DINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-234 |
9.79e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.92 E-value: 9.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFpIGGffsREKMKAVDdvsFALaadKP-EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVR 83
Cdd:PRK10908 1 MIRFEHVSKAY-LGG---RQALQGVT---FHM---RPgEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 84 SRrDREAFMAKVQPVFQnpfeafnpltriDEYLL---------ATAHRFKGAKSRTEKEALAdVALQRVGLsmAEIKGRF 154
Cdd:PRK10908 71 NR-EVPFLRRQIGMIFQ------------DHHLLmdrtvydnvAIPLIIAGASGDDIRRRVS-AALDKVGL--LDKAKNF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 155 SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLrDALNVSIVYITHDLATAYYISDRVVIMRKG 234
Cdd:PRK10908 135 PIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
24-247 |
2.49e-17 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 81.84 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 24 EKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrsrrDREAFMAKVQPVFQNPF 103
Cdd:TIGR03375 476 QETPALDNVSLTIRPG--EKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQI----DPADLRRNIGYVPQDPR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 104 ----------EAFNPLTRiDEYLLATAhRFKGAKSRTEKEALadvalqrvGLSM--AEiKGRFsheLSGGQLQRIAVARA 171
Cdd:TIGR03375 550 lfygtlrdniALGAPYAD-DEEILRAA-ELAGVTEFVRRHPD--------GLDMqiGE-RGRS---LSGGQRQAVALARA 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 172 LIPEPKLIVADEPVSMVDASLRMsivNLFRDLRDAL-NVSIVYITH-----DLAtayyisDRVVIMRKGVVVESGDARDV 245
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMDNRSEE---RFKDRLKRWLaGKTLVLVTHrtsllDLV------DRIIVMDNGRIVADGPKDQV 686
|
..
gi 502309174 246 LE 247
Cdd:TIGR03375 687 LE 688
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-247 |
3.42e-17 |
|
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: 78.74 E-value: 3.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 22 SREKMKAVDDVSFALAADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK--AVRSRRDREAFmakvqpVF 99
Cdd:cd03249 12 SRPDVPILKGLSLTIPPGK--TVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRdlNLRWLRSQIGL------VS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 100 QNPfeafnpltrideYLLATAHRFK---GAKSRTEKEAladvalqrvglsMAEIKGRFSHE------------------- 157
Cdd:cd03249 84 QEP------------VLFDGTIAENiryGKPDATDEEV------------EEAAKKANIHDfimslpdgydtlvgergsq 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 158 LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdaLNVSIVYITHDLATAYYiSDRVVIMRKGVVV 237
Cdd:cd03249 140 LSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVV 216
|
250
....*....|
gi 502309174 238 ESGDARDVLE 247
Cdd:cd03249 217 EQGTHDELMA 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-274 |
3.95e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.39 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 20 FFSREKMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDReafmAKVQPVF 99
Cdd:PRK13647 12 FRYKDGTKALKGLSLSI--PEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR----SKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 100 QNPFEAFNPLTRIDEylLATAHRFKGAkSRTEKEALADVALQRVGlsMAEIKGRFSHELSGGQLQRIAVARALIPEPKLI 179
Cdd:PRK13647 86 QDPDDQVFSSTVWDD--VAFGPVNMGL-DKDEVERRVEEALKAVR--MWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 180 VADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDA-----RDVLEHPKHAYS 254
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKslltdEDIVEQAGLRLP 239
|
250 260
....*....|....*....|....*....
gi 502309174 255 IA---------LKNAVLPPDPREASAILR 274
Cdd:PRK13647 240 LVaqifedlpeLGQSKLPLTVKEAVQIIR 268
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-248 |
3.97e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.58 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 3 SNLLELDHVTKLFPIGGFFSR--------------EKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKAD 68
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPSRslkelllrrrrtrrEEFWALKDVSFEVERG--ESVGIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 69 RGSIHFDGtdvkavrsrrdreafmaKVQPvfqnPFE---AFNP-LT-RidE--YLLATAHRFkgakSRTE-KEALADVAl 140
Cdd:COG1134 80 SGRVEVNG-----------------RVSA----LLElgaGFHPeLTgR--EniYLNGRLLGL----SRKEiDEKFDEIV- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 141 qrvglSMAEIkGRFSHE----LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITH 216
Cdd:COG1134 132 -----EFAEL-GDFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSH 204
|
250 260 270
....*....|....*....|....*....|..
gi 502309174 217 DLATAYYISDRVVIMRKGVVVESGDARDVLEH 248
Cdd:COG1134 205 SMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-250 |
9.78e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.85 E-value: 9.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 3 SNLLELDHVTKLFpiggffsrEKMKAVDDVSFALAADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIhfdgtdvkaV 82
Cdd:PRK09544 2 TSLVSLENVSVSF--------GQRRVLSDVSLELKPGK--ILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------K 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 83 RSRRDREAFMAKVqpvfqnpfeafnplTRIDEYLLATAHRFKGAKSRTEKealADV--ALQRVglSMAEIKGRFSHELSG 160
Cdd:PRK09544 63 RNGKLRIGYVPQK--------------LYLDTTLPLTVNRFLRLRPGTKK---EDIlpALKRV--QAGHLIDAPMQKLSG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 161 GQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVeSG 240
Cdd:PRK09544 124 GETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICC-SG 202
|
250
....*....|
gi 502309174 241 DARDVLEHPK 250
Cdd:PRK09544 203 TPEVVSLHPE 212
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-262 |
1.17e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.00 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFpiggffsREKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 80
Cdd:PRK15056 2 MQQAGIVVNDVTVTW-------RNGHTALRDASFTVPGG--SIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 avrsRRDREAFMAKVqPVFQNPFEAFNPLTRIDEYLLATAHRFKGAKSRTEKEALADVALQRVGlsMAEIKGRFSHELSG 160
Cdd:PRK15056 73 ----QALQKNLVAYV-PQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVD--MVEFRHRQIGELSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 161 GQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYiTHDLATAYYISDRVViMRKGVVVESG 240
Cdd:PRK15056 146 GQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVS-THNLGSVTEFCDYTV-MVKGTVLASG 223
|
250 260
....*....|....*....|....
gi 502309174 241 DARDVL--EHPKHAYSIALKNAVL 262
Cdd:PRK15056 224 PTETTFtaENLELAFSGVLRHVAL 247
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-254 |
2.11e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.29 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPiggffSREKMkAVDDVSFALAADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 85
Cdd:PRK11176 342 IEFRNVTFTYP-----GKEVP-ALRNINFKIPAGK--TVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREafmaKVQPVFQNpFEAFNpltriDEYLLATAHRFKGAKSRTEKEALADVA-----LQRVGLSMAEIKGRFSHELSG 160
Cdd:PRK11176 414 SLRN----QVALVSQN-VHLFN-----DTIANNIAYARTEQYSREQIEEAARMAyamdfINKMDNGLDTVIGENGVLLSG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 161 GQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATayyI--SDRVVIMRKGVVVE 238
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLST---IekADEILVVEDGEIVE 558
|
250
....*....|....*.
gi 502309174 239 SGDARDVLEHpKHAYS 254
Cdd:PRK11176 559 RGTHAELLAQ-NGVYA 573
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
26-287 |
2.27e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.82 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 26 MKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAK--VQPVFQNPF 103
Cdd:PRK13651 20 LKALDNVSVEI--NQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKlvIQKTRFKKI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 104 EAFNPLTR-------IDEYLLATAHRFK----GAKS----RTEKEALADVALQRVGLSMAEIKgRFSHELSGGQLQRIAV 168
Cdd:PRK13651 98 KKIKEIRRrvgvvfqFAEYQLFEQTIEKdiifGPVSmgvsKEEAKKRAAKYIELVGLDESYLQ-RSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 169 ARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEH 248
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
250 260 270
....*....|....*....|....*....|....*....
gi 502309174 249 PKhaysIALKNAVLPpdPREASAILRLRQRNAETNEATS 287
Cdd:PRK13651 256 NK----FLIENNMEP--PKLLNFVNKLEKKGIDVPKVTS 288
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-248 |
2.72e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.54 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFPiggffsrEKMkAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYG-------DKL-VVDGLSFHVQRG--ECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 AvRSRRDReafmAKVQPVFQnpFEAFNPLTRIDEYLLATAHRFkgAKSRTEKEALADVALQRVGL-SMAEIKGRfshELS 159
Cdd:PRK13537 73 S-RARHAR----QRVGVVPQ--FDNLDPDFTVRENLLVFGRYF--GLSAAAARALVPPLLEFAKLeNKADAKVG---ELS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 160 GGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdALNVSIVYITHDLATAYYISDRVVIMRKGVVVES 239
Cdd:PRK13537 141 GGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
....*....
gi 502309174 240 GDARDVLEH 248
Cdd:PRK13537 220 GAPHALIES 228
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
36-254 |
3.87e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 76.22 E-value: 3.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 36 LAADKPEIFTIVGESGSGKSTLAKMILG--SEKADRGSIHFDGTDV--KAVRSRRDREAFMAkvqpvFQNPFEaFNPLTR 111
Cdd:CHL00131 28 LSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESIldLEPEERAHLGIFLA-----FQYPIE-IPGVSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 112 IDEYLLATAHRFKgAKSRTEKEALADVALQRVGLSMAEIKGRFSHE-----LSGGQLQRIAVARALIPEPKLIVADEPVS 186
Cdd:CHL00131 102 ADFLRLAYNSKRK-FQGLPELDPLEFLEIINEKLKLVGMDPSFLSRnvnegFSGGEKKRNEILQMALLDSELAILDETDS 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502309174 187 MVDASLRMSIVNLFRDLRDALNvSIVYITH-----DlataYYISDRVVIMRKGVVVESGDARDVLEHPKHAYS 254
Cdd:CHL00131 181 GLDIDALKIIAEGINKLMTSEN-SIILITHyqrllD----YIKPDYVHVMQNGKIIKTGDAELAKELEKKGYD 248
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-247 |
4.97e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.92 E-value: 4.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFpiggffsrEKMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSE--KADRGSI----------- 72
Cdd:TIGR03269 1 IEVKNLTKKF--------DGKEVLKNISFTI--EEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcg 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 73 -----HFDGTDVKAV-------------RSRRDREAFMAKVQPVFQNPFEAFNPLTRIDEYLlatahrfkgaKSRTEKEA 134
Cdd:TIGR03269 71 yverpSKVGEPCPVCggtlepeevdfwnLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVL----------EALEEIGY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 135 LADVALQRVG--LSMAEIKGRFSH---ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNV 209
Cdd:TIGR03269 141 EGKEAVGRAVdlIEMVQLSHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGI 220
|
250 260 270
....*....|....*....|....*....|....*...
gi 502309174 210 SIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLE 247
Cdd:TIGR03269 221 SMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
42-240 |
5.91e-16 |
|
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: 75.00 E-value: 5.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 42 EIFTIVGESGSGKSTLAKMILG---SEKADRGSIHFDGtdvkavrSRRDREAFMAKVQPVFQnpFEAFNPLTRIDEYLLA 118
Cdd:cd03234 34 QVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNG-------QPRKPDQFQKCVAYVRQ--DDILLPGLTVRETLTY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 119 TAH---RFKGAKSRTEKEAlADVALQRVGLSMaeIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMS 195
Cdd:cd03234 105 TAIlrlPRKSSDAIRKKRV-EDVLLRDLALTR--IGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502309174 196 IVNLFRDLrdALNVSIVYIT-H----DLataYYISDRVVIMRKGVVVESG 240
Cdd:cd03234 182 LVSTLSQL--ARRNRIVILTiHqprsDL---FRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-240 |
1.28e-15 |
|
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: 73.35 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPIGGFFSREKMkaVDDVSFALaadKPEIFT-IVGESGSGKSTLAKMILG--SEKADRGSIHFDGTDvkav 82
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKQL--LKNVSGKA---KPGELTaIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 83 rsrRDREAFMAKVQPVFQnpfeafnpltriDEYLLATAhrfkgaksrTEKEALaDVAlqrvglsmAEIKGrfsheLSGGQ 162
Cdd:cd03213 75 ---LDKRSFRKIIGYVPQ------------DDILHPTL---------TVRETL-MFA--------AKLRG-----LSGGE 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502309174 163 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDaLNVSIVYITHDL-ATAYYISDRVVIMRKGVVVESG 240
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
29-246 |
1.46e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.67 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 29 VDDVSFALAADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRR--DREAFMAKVQPVfqnpfeaf 106
Cdd:PRK11231 18 LNDLSLSLPTGK--ITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLPQHHLT-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 107 nP----LTRIDEYLLATAHRFKGAKSRtEKEALADVALQRVGLS-MAEikgRFSHELSGGQLQRIAVARALIPEPKLIVA 181
Cdd:PRK11231 88 -PegitVRELVAYGRSPWLSLWGRLSA-EDNARVNQAMEQTRINhLAD---RRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502309174 182 DEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVL 246
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
5-234 |
2.42e-15 |
|
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: 73.62 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPI---GGffsrEKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTD--- 78
Cdd:COG4778 4 LLEVENLSKTFTLhlqGG----KRLPVLDGVSFSVAAG--ECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 79 --VKA-----VRSRRDREAFmakvqpVFQnpfeaF-NPLTRIDEYLLAtahrfkgAKSRTEKEALADVALQRVG--LSMA 148
Cdd:COG4778 78 dlAQAspreiLALRRRTIGY------VSQ-----FlRVIPRVSALDVV-------AEPLLERGVDREEARARARelLARL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 149 EIKGR--------FshelSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLAT 220
Cdd:COG4778 140 NLPERlwdlppatF----SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEV 214
|
250
....*....|....
gi 502309174 221 AYYISDRVVIMRKG 234
Cdd:COG4778 215 REAVADRVVDVTPF 228
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
6-240 |
2.73e-15 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 75.89 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPiggffSREKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 85
Cdd:TIGR02204 338 IEFEQVNFAYP-----ARPDQPALDGLNLTVRPG--ETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 --RDREAFMAKVQPVFQNPFE---AFNPLTRIDEYLLATAhrfkgaksrteKEALADVALQRVGLSMAEIKGRFSHELSG 160
Cdd:TIGR02204 411 elRARMALVPQDPVLFAASVMeniRYGRPDATDEEVEAAA-----------RAAHAHEFISALPEGYDTYLGERGVTLSG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 161 GQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIvyITHDLATAYYiSDRVVIMRKGVVVESG 240
Cdd:TIGR02204 480 GQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLI--IAHRLATVLK-ADRIVVMDQGRIVAQG 556
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-245 |
2.83e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.59 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 1 MSSNLLELDHVTKLFPIggffsrekMKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVk 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGP--------VHALKSVNLTVY--PGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINY- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 81 avrSRRD-REAFMAKVQPVFQNpfeafnpLTRIDEyLLATAHRFKGaKSRTEK------------EALADVALQRVGL-- 145
Cdd:PRK09700 70 ---NKLDhKLAAQLGIGIIYQE-------LSVIDE-LTVLENLYIG-RHLTKKvcgvniidwremRVRAAMMLLRVGLkv 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 146 SMAEIKGrfshELSGGQLQRIAVARALIPEPKLIVADEPVSmvdaSLRMSIVN-LF---RDLRDAlNVSIVYITHDLATA 221
Cdd:PRK09700 138 DLDEKVA----NLSISHKQMLEIAKTLMLDAKVIIMDEPTS----SLTNKEVDyLFlimNQLRKE-GTAIVYISHKLAEI 208
|
250 260
....*....|....*....|....
gi 502309174 222 YYISDRVVIMRKGVVVESGDARDV 245
Cdd:PRK09700 209 RRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
28-247 |
2.92e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.91 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 28 AVDDVSFALAADKPEIFTI------------VGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAfMAKV 95
Cdd:PRK10790 342 DIDNVSFAYRDDNLVLQNInlsvpsrgfvalVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG-VAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 96 QpvfQNP------FEAFNPLTR-IDEyllatahrfkgaksrtEK--EALADVALQRVGLSMAE----IKGRFSHELSGGQ 162
Cdd:PRK10790 421 Q---QDPvvladtFLANVTLGRdISE----------------EQvwQALETVQLAELARSLPDglytPLGEQGNNLSVGQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 163 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAYYiSDRVVIMRKGVVVESGDA 242
Cdd:PRK10790 482 KQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTH 558
|
....*
gi 502309174 243 RDVLE 247
Cdd:PRK10790 559 QQLLA 563
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
46-246 |
3.26e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.89 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 46 IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavRSRRDREAFMAKVQPVFQNPFEAFNpLTRIDEYLLATAHRFKG 125
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD--YSKRGLLALRQQVATVFQDPEQQIF-YTDIDSDIAFSLRNLGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 126 AK---SRTEKEALADVALQRvglsmaeikgrFSHE----LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVN 198
Cdd:PRK13638 109 PEaeiTRRVDEALTLVDAQH-----------FRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502309174 199 LFRDLRDALNvSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVL 246
Cdd:PRK13638 178 IIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
28-218 |
3.36e-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: 75.47 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 28 AVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR--RDREAFMAKVQPVFQnpfea 105
Cdd:TIGR02868 350 VLDGVSLDLPPG--ERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevRRRVSVCAQDAHLFD----- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 106 fnplTRIDEYLLAtahrfkGAKSRTEKEALAdvALQRVGLS--MAEIKGRFSHE-------LSGGQLQRIAVARALIPEP 176
Cdd:TIGR02868 423 ----TTVRENLRL------ARPDATDEELWA--ALERVGLAdwLRALPDGLDTVlgeggarLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502309174 177 KLIVADEPVSMVDASLRMSIVnlfRDLRDALN-VSIVYITHDL 218
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELL---EDLLAALSgRTVVLITHHL 530
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-246 |
4.91e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.04 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 32 VSFALAADkpEIFTIVGESGSGKSTL----AKMILGSekadrGSIHFDGTDVKAVRSR---RDReAFMAKVQ------PV 98
Cdd:PRK03695 15 LSAEVRAG--EILHLVGPNGAGKSTLlarmAGLLPGS-----GSIQFAGQPLEAWSAAelaRHR-AYLSQQQtppfamPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 99 FQnpfeafnpltrideYLlaTAHRFKGAKSRTEKEALADVAlQRVGLSMaeiK-GRFSHELSGGQLQRIAVA-------R 170
Cdd:PRK03695 87 FQ--------------YL--TLHQPDKTRTEAVASALNEVA-EALGLDD---KlGRSVNQLSGGEWQRVRLAavvlqvwP 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502309174 171 ALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVL 246
Cdd:PRK03695 147 DINPAGQLLLLDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-221 |
5.56e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.50 E-value: 5.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 4 NLLELDHVTKLFPIGgffsREKMKAVDDVSfaLAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVr 83
Cdd:PRK10584 5 NIVEVHHLKKSVGQG----EHELSILTGVE--LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQM- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 84 SRRDREAFMAK-VQPVFQNpFEAFNPLTRIDEYLLATAHRfkGAKSRTEKEALADVaLQRVGLSMaeikgRFSH---ELS 159
Cdd:PRK10584 78 DEEARAKLRAKhVGFVFQS-FMLIPTLNALENVELPALLR--GESSRQSRNGAKAL-LEQLGLGK-----RLDHlpaQLS 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502309174 160 GGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATA 221
Cdd:PRK10584 149 GGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-247 |
5.69e-15 |
|
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: 72.65 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTklFPIGGffsrEKMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR 85
Cdd:cd03251 1 VEFKNVT--FRYPG----DGPPVLRDISLDI--PAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREafmaKVQPVFQNPFeAFNplTRIDEYLLATAHRfkgaKSRTEKEALADVA-LQRVGLSMAE----IKGRFSHELSG 160
Cdd:cd03251 73 SLRR----QIGLVSQDVF-LFN--DTVAENIAYGRPG----ATREEVEEAARAAnAHEFIMELPEgydtVIGERGVKLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 161 GQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLrdALNVSIVYITHDLATayyI--SDRVVIMRKGVVVE 238
Cdd:cd03251 142 GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERL--MKNRTTFVIAHRLST---IenADRIVVLEDGKIVE 216
|
....*....
gi 502309174 239 SGDARDVLE 247
Cdd:cd03251 217 RGTHEELLA 225
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-270 |
6.56e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 74.61 E-value: 6.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPiggffsrEKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVrs 84
Cdd:PRK13657 334 AVEFDDVSFSYD-------NSRQGVEDVSFEAKPG--QTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV-- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 rrDREAFMAKVQPVFQNPFeAFNplTRIDEYLL-----ATAHRFKGAKSRTEkeALADVALQRVGL-SMAEIKGRfshEL 158
Cdd:PRK13657 403 --TRASLRRNIAVVFQDAG-LFN--RSIEDNIRvgrpdATDEEMRAAAERAQ--AHDFIERKPDGYdTVVGERGR---QL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 159 SGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRmsivnlfRDLRDAL-----NVSIVYITHDLATAYYiSDRVVIMRK 233
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETE-------AKVKAALdelmkGRTTFIIAHRLSTVRN-ADRILVFDN 544
|
250 260 270
....*....|....*....|....*....|....*..
gi 502309174 234 GVVVESGDARDVLEHPKHAYSIALKNAVLPPDPREAS 270
Cdd:PRK13657 545 GRVVESGSFDELVARGGRFAALLRAQGMLQEDERRKQ 581
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
32-240 |
7.95e-15 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 74.39 E-value: 7.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 32 VSFALAADKPEIFT-------------IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAV---------------- 82
Cdd:TIGR01846 461 IRFRYAPDSPEVLSnlnldikpgefigIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIAdpawlrrqmgvvlqen 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 83 ----RSRRDReafMAKVQPvfQNPFEAFNPLTRideylLATAHRFkgaksrtekealadVALQRVGLSmaEIKGRFSHEL 158
Cdd:TIGR01846 541 vlfsRSIRDN---IALCNP--GAPFEHVIHAAK-----LAGAHDF--------------ISELPQGYN--TEVGEKGANL 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 159 SGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLrdALNVSIVYITHDLATAYYiSDRVVIMRKGVVVE 238
Cdd:TIGR01846 595 SGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREI--CRGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAE 671
|
..
gi 502309174 239 SG 240
Cdd:TIGR01846 672 SG 673
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-249 |
8.29e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.37 E-value: 8.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPiggffSREKMKAVDDVSFALaadKP-EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavr 83
Cdd:TIGR00958 478 LIEFQDVSFSYP-----NRPDVPVLKGLTFTL---HPgEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL---- 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 84 SRRDREAFMAKVQPVFQNPFeAFNPLTR----------IDEYLLATAhrfkgaksrteKEALADVALQRVGLSMAEIKGR 153
Cdd:TIGR00958 546 VQYDHHYLHRQVALVGQEPV-LFSGSVReniaygltdtPDEEIMAAA-----------KAANAHDFIMEFPNGYDTEVGE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 154 FSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDAslrmSIVNLFRDLRDALNVSIVYITHDLATAYYiSDRVVIMRK 233
Cdd:TIGR00958 614 KGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKK 688
|
250
....*....|....*.
gi 502309174 234 GVVVESGDARDVLEHP 249
Cdd:TIGR00958 689 GSVVEMGTHKQLMEDQ 704
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-230 |
8.81e-15 |
|
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: 72.44 E-value: 8.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 30 DDVSFALAAD-----KPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV-------KAVRSRRDREAFMAKVQP 97
Cdd:cd03237 9 TLGEFTLEVEggsisESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpqyiKADYEGTVRDLLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 98 VFQNPF---EAFNPLtrideyllatahrfkgaksrtEKEALADvalQRVglsmaeikgrfsHELSGGQLQRIAVARALIP 174
Cdd:cd03237 89 FYTHPYfktEIAKPL---------------------QIEQILD---REV------------PELSGGELQRVAIAACLSK 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502309174 175 EPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVI 230
Cdd:cd03237 133 DADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-248 |
1.02e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.20 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 7 ELDHVTKLFPI-----------GGFFSREK--MKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIH 73
Cdd:COG4586 3 EVENLSKTYRVyekepglkgalKGLFRREYreVEAVDDISFTIE--PGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 74 FDGTDvkavrSRRDREAFMAKVQPVFQN---------PFEAFNpltrideyLLATAHRFKGAKSRTEKEALADValqrvg 144
Cdd:COG4586 81 VLGYV-----PFKRRKEFARRIGVVFGQrsqlwwdlpAIDSFR--------LLKAIYRIPDAEYKKRLDELVEL------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 145 LSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYI 224
Cdd:COG4586 142 LDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAL 221
|
250 260
....*....|....*....|....
gi 502309174 225 SDRVVIMRKGVVVESGDARDVLEH 248
Cdd:COG4586 222 CDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-240 |
1.18e-14 |
|
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: 71.59 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLF-----------PIGGFFSREK--MKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSI 72
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligSLKSLFKRKYreVEALKGISFTI--EKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 73 HfdgtdVKAVRSRRDREAFMAKVQPVFQNPFEAFNPLTRIDEY-LLATAHRFKGAKSRTEKEALADValqrvgLSMAEIK 151
Cdd:cd03267 79 R-----VAGLVPWKRRKKFLRRIGVVFGQKTQLWWDLPVIDSFyLLAAIYDLPPARFKKRLDELSEL------LDLEELL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 152 GRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIM 231
Cdd:cd03267 148 DTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVI 227
|
....*....
gi 502309174 232 RKGVVVESG 240
Cdd:cd03267 228 DKGRLLYDG 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-234 |
1.27e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 73.71 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPIGgffsrEKMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGS-EKADRGSIHFDGtdvKAVR 83
Cdd:TIGR02633 257 ILEARNLTCWDVIN-----PHRKRVDDVSFSL--RRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFING---KPVD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 84 SRRDREAFMAKVQPVFQN-PFEAFNPLTRIDEYL-LATAHRFKGaKSRTEKEAladvALQRVGLSMAEIKGRFSH----- 156
Cdd:TIGR02633 327 IRNPAQAIRAGIAMVPEDrKRHGIVPILGVGKNItLSVLKSFCF-KMRIDAAA----ELQIIGSAIQRLKVKTASpflpi 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502309174 157 -ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdALNVSIVYITHDLATAYYISDRVVIMRKG 234
Cdd:TIGR02633 402 gRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLA-QEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
27-240 |
1.55e-14 |
|
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: 70.90 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 27 KAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREafmaKVQPVFQNP--FE 104
Cdd:cd03369 22 PVLKNVSFKVKAG--EKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS----SLTIIPQDPtlFS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 105 AF--NPLTRIDEYllatahrfkgaksrTEKEALADVALQRVGLSmaeikgrfsheLSGGQLQRIAVARALIPEPKLIVAD 182
Cdd:cd03369 96 GTirSNLDPFDEY--------------SDEEIYGALRVSEGGLN-----------LSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502309174 183 EPVSMV----DASLRMSIVNLFRdlrdalNVSIVYITHDLAT-AYYisDRVVIMRKGVVVESG 240
Cdd:cd03369 151 EATASIdyatDALIQKTIREEFT------NSTILTIAHRLRTiIDY--DKILVMDAGEVKEYD 205
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-244 |
2.13e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.90 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPiggffsreKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKAD--RGSIHFDGtDVKAV 82
Cdd:NF040905 1 ILEMRGITKTFP--------GVKALDDVNLSVREG--EIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDG-EVCRF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 83 RSRRDREAF--------MAKVqpvfqnpfeafnPLTRIDEYL-LATAHRFKGAKSRTEKEALADVALQRVGLSmaEIKGR 153
Cdd:NF040905 70 KDIRDSEALgiviihqeLALI------------PYLSIAENIfLGNERAKRGVIDWNETNRRARELLAKVGLD--ESPDT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 154 FSHELSGGQLQRIAVARALIPEPKLIVADEPVsmvdASLRMS----IVNLFRDLRDALNVSIVyITHDLATAYYISDRVV 229
Cdd:NF040905 136 LVTDIGVGKQQLVEIAKALSKDVKLLILDEPT----AALNEEdsaaLLDLLLELKAQGITSII-ISHKLNEIRRVADSIT 210
|
250
....*....|....*
gi 502309174 230 IMRKGVVVESGDARD 244
Cdd:NF040905 211 VLRDGRTIETLDCRA 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
25-248 |
3.04e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.58 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 25 KMKAVDDVSFALAADKpeIFTIVGESGSGKSTLAKMILGSEKADRG-SIHFDGTDVKAVRSRRDREAFMAKVQPVFQNP- 102
Cdd:PRK13645 23 EFKALNNTSLTFKKNK--VTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLKKIKEVKRLRKEIGLVFQFPe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 103 FEAFNPLTRIDeylLATAHRFKGAKSRTEKEALADVaLQRVGLSMAEIKgRFSHELSGGQLQRIAVARALIPEPKLIVAD 182
Cdd:PRK13645 101 YQLFQETIEKD---IAFGPVNLGENKQEAYKKVPEL-LKLVQLPEDYVK-RSPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502309174 183 EPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEH 248
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
28-226 |
5.23e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.20 E-value: 5.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 28 AVDDVSfaLAADKPEIFTIVGESGSGKSTLAKM------ILGSEKADrGSIHFDG-----TDVKAVRSRRdreafmaKVQ 96
Cdd:PRK14243 25 AVKNVW--LDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFRVE-GKVTFHGknlyaPDVDPVEVRR-------RIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 97 PVFQNPfeafNPLTRIDEYLLATAHRFKGAKSRTEKeaLADVALQRVGLsMAEIKGRFSHE---LSGGQLQRIAVARALI 173
Cdd:PRK14243 95 MVFQKP----NPFPKSIYDNIAYGARINGYKGDMDE--LVERSLRQAAL-WDEVKDKLKQSglsLSGGQQQRLCIARAIA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502309174 174 PEPKLIVADEPVSMVDASLRMSIVNLFRDLRDalNVSIVYITHDLATAYYISD 226
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAARVSD 218
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-246 |
5.41e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.78 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 26 MKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVfqnpfEA 105
Cdd:PRK11160 353 QPVLKGLSLQIKAG--EKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRV-----HL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 106 FNPLTRiDEYLLAtahrfkgAKSRTEkEALADVaLQRVGLS------------MAEiKGRfshELSGGQLQRIAVARALI 173
Cdd:PRK11160 426 FSATLR-DNLLLA-------APNASD-EALIEV-LQQVGLEklleddkglnawLGE-GGR---QLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502309174 174 PEPKLIVADEPVSMVDASLRMSIVNLFRDLrdALNVSIVYITHDLaTAYYISDRVVIMRKGVVVESGDARDVL 246
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEH--AQNKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
27-253 |
8.30e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.54 E-value: 8.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 27 KAVDDVSfaLAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAV----RSRRD-----REAFMAKVQP 97
Cdd:PRK10895 17 RVVEDVS--LTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhaRARRGigylpQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 98 VFQNpfeafnpltrideylLATAHRFKGAKSRTEKEALADVALQRvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPK 177
Cdd:PRK10895 95 VYDN---------------LMAVLQIRDDLSAEQREDRANELMEE--FHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502309174 178 LIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVL--EHPKHAY 253
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILqdEHVKRVY 234
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
31-236 |
2.06e-13 |
|
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: 67.88 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 31 DVSFALaadKP-EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrSRRDREAFMAKVQPVFQNPFEAFNPL 109
Cdd:cd03248 32 DVSFTL---HPgEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI----SQYEHKYLHSKVSLVGQEPVLFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 110 TRIDEYLLATA--HRFKGAKSRtekeALADVALQRVGLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSM 187
Cdd:cd03248 105 QDNIAYGLQSCsfECVKEAAQK----AHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502309174 188 VDASLRMSIVNLFRDlrDALNVSIVYITHDLATAYYiSDRVVIMRKGVV 236
Cdd:cd03248 181 LDAESEQQVQQALYD--WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
42-230 |
2.16e-13 |
|
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: 70.20 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 42 EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDgtdvkavrsrrdreafmAKVqpvfqnpfeAFNPltridEYLlatah 121
Cdd:COG1245 367 EVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-----------------LKI---------SYKP-----QYI----- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 122 rfKGAKSRTEKEALADVALQRVGLSM--AEIKGRFS---------HELSGGQLQRIAVARALIPEPKLIVADEPVSMVDA 190
Cdd:COG1245 411 --SPDYDGTVEEFLRSANTDDFGSSYykTEIIKPLGleklldknvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502309174 191 SLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVI 230
Cdd:COG1245 489 EQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-234 |
2.42e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPIggffsREKMKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGS-EKADRGSIHFDGtdvKAVRS 84
Cdd:PRK13549 260 LEVRNLTAWDPV-----NPHIKRVDDVSFSLR--RGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDG---KPVKI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAFMAKVqpvfqnpfeAFNPLTR-----------IDEYLLATAHRFKGAkSRTEKEALADVALQrvglSMAEIKGR 153
Cdd:PRK13549 330 RNPQQAIAQGI---------AMVPEDRkrdgivpvmgvGKNITLAALDRFTGG-SRIDDAAELKTILE----SIQRLKVK 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 154 FSH------ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDR 227
Cdd:PRK13549 396 TASpelaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDR 474
|
....*..
gi 502309174 228 VVIMRKG 234
Cdd:PRK13549 475 VLVMHEG 481
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
28-240 |
2.58e-13 |
|
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: 67.52 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 28 AVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFmaKVQPvfQNP--FEA 105
Cdd:cd03244 19 VLKNISFSIKPG--EKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI--SIIP--QDPvlFSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 106 ---FN--PLTRI-DEYLLatahrfkgaksrtekEALADVALQRVGLSM-----AEIKGRFSHeLSGGQLQRIAVARALIP 174
Cdd:cd03244 93 tirSNldPFGEYsDEELW---------------QALERVGLKEFVESLpggldTVVEEGGEN-LSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502309174 175 EPKLIVADEPVSMVDASLRMSIVNLfrdLRDAL-NVSIVYITHDLATayyI--SDRVVIMRKGVVVESG 240
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKT---IREAFkDCTVLTIAHRLDT---IidSDRILVLDKGRVVEFD 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
42-230 |
2.69e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.84 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 42 EIFTIVGESGSGKSTLAKMILGSEKADRGSIhfdGTDVKA------VRSRRDR--EAFMAKVQPVFQNPF---EAFNPLt 110
Cdd:PRK13409 366 EVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELKIsykpqyIKPDYDGtvEDLLRSITDDLGSSYyksEIIKPL- 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 111 rideyllatahrfkgaksrtekeALADVALQRVGlsmaeikgrfshELSGGQLQRIAVARALIPEPKLIVADEPVSMVDA 190
Cdd:PRK13409 442 -----------------------QLERLLDKNVK------------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502309174 191 SLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVI 230
Cdd:PRK13409 487 EQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-258 |
2.80e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.31 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 22 SREKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKAD--------RGSIHFDGTDVKAV---RSRRDREA 90
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPG--RVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIdapRLARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 91 FMAKVQPVFqnPFEAfnpltriDEYLLATAH---RFKGAKSRTEKEaLADVALQRVGlsMAEIKGRFSHELSGGQLQRIA 167
Cdd:PRK13547 88 LPQAAQPAF--AFSA-------REIVLLGRYphaRRAGALTHRDGE-IAWQALALAG--ATALVGRDVTTLSGGELARVQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 168 VARAL---------IPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVE 238
Cdd:PRK13547 156 FARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVA 235
|
250 260
....*....|....*....|..
gi 502309174 239 SGDARDVL--EHPKHAYSIALK 258
Cdd:PRK13547 236 HGAPADVLtpAHIARCYGFAVR 257
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
43-276 |
3.24e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.13 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 43 IFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTdvkaVRSRRDREAFMA----KVQPVFQnpfeafnpltridEYLLA 118
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR----VLFDAEKGICLPpekrRIGYVFQ-------------DARLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 119 TAHRFKG----AKSRTEKEALAD-VALqrvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLR 193
Cdd:PRK11144 89 PHYKVRGnlryGMAKSMVAQFDKiVAL----LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 194 MSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHPkhaysialknAVLPPDPR-EASAI 272
Cdd:PRK11144 165 RELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS----------AMRPWLPKeEQSSI 234
|
....
gi 502309174 273 LRLR 276
Cdd:PRK11144 235 LKVT 238
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
25-253 |
3.28e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.60 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 25 KMKAVDDVSfaLAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDV---KAVRSRRDREAFMAKVQPVFqn 101
Cdd:PRK11614 17 KIQALHEVS--LHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwQTAKIMREAVAIVPEGRRVF-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 102 pfeafnplTRID-EYLLATAHRFKGAKSRTEKEALADVALQRvglsMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIV 180
Cdd:PRK11614 93 --------SRMTvEENLAMGGFFAERDQFQERIKWVYELFPR----LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502309174 181 ADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVV--ESGDARDVLEHPKHAY 253
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVleDTGDALLANEAVRSAY 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-234 |
6.27e-13 |
|
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: 69.27 E-value: 6.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 3 SNLLELDHVTKLFPigGFFSrekmKAVDDVSFALaadKP-EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvka 81
Cdd:TIGR01257 1935 TDILRLNELTKVYS--GTSS----PAVDRLCVGV---RPgECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG----- 2000
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 82 vrsrrdrEAFMAKVQPVFQN-----PFEAFNPLTRIDEYLLATAhRFKGAKSRtEKEALADVALQRVGLSMaeIKGRFSH 156
Cdd:TIGR01257 2001 -------KSILTNISDVHQNmgycpQFDAIDDLLTGREHLYLYA-RLRGVPAE-EIEKVANWSIQSLGLSL--YADRLAG 2069
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 157 ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRM----SIVNLFRDLRdalnvSIVYITHDLATAYYISDRVVIMR 232
Cdd:TIGR01257 2070 TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRmlwnTIVSIIREGR-----AVVLTSHSMEECEALCTRLAIMV 2144
|
..
gi 502309174 233 KG 234
Cdd:TIGR01257 2145 KG 2146
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
42-240 |
6.41e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.92 E-value: 6.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 42 EIFTIVGESGSGKSTLAKMIL-----GSEKAdrGSIHFDGTDVKAVRSRRdREAFmakvqpVFQnpFEAFNPLTRIDEYL 116
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMNALAfrspkGVKGS--GSVLLNGMPIDAKEMRA-ISAY------VQQ--DDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 117 LATAH-RFKGAKSRTEKEALADVALQRVGLSMA---------EIKGrfsheLSGGQLQRIAVARALIPEPKLIVADEPVS 186
Cdd:TIGR00955 121 MFQAHlRMPRRVTKKEKRERVDEVLQALGLRKCantrigvpgRVKG-----LSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502309174 187 MVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESG 240
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLG 249
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-240 |
6.66e-13 |
|
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: 66.40 E-value: 6.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPIGGFFSREKMK--------------AVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGS 71
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKlgilgrkgevgefwALKDVSFEVPRG--ERIGLIGRNGAGKSTLLRLLAGIYPPDSGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 72 IHFDGTdvkaVRSrrdreafmakvqpvfqnPFEA---FNP-LTRIDE-YLLATAHRFKGAKSRTEKEALADvalqrvgls 146
Cdd:cd03220 79 VTVRGR----VSS-----------------LLGLgggFNPeLTGRENiYLNGRLLGLSRKEIDEKIDEIIE--------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 147 MAEIkGRFSHE----LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAY 222
Cdd:cd03220 129 FSEL-GDFIDLpvktYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIK 206
|
250
....*....|....*...
gi 502309174 223 YISDRVVIMRKGVVVESG 240
Cdd:cd03220 207 RLCDRALVLEKGKIRFDG 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-216 |
1.34e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.52 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 3 SNLLELDHVTKLFPIGGFFsrekmkaVDDVSFALAAdkPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHF-DGTDVka 81
Cdd:COG4178 360 DGALALEDLTLRTPDGRPL-------LEDLSLSLKP--GERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 82 vrsrrdreAFMAkvqpvfQNPFEafnPLTRIDEYLL--ATAHRFkgaksrTEKEALAdvALQRVGL----SMAEIKGRFS 155
Cdd:COG4178 429 --------LFLP------QRPYL---PLGTLREALLypATAEAF------SDAELRE--ALEAVGLghlaERLDEEADWD 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502309174 156 HELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSivnLFRDLRDAL-NVSIVYITH 216
Cdd:COG4178 484 QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAA---LYQLLREELpGTTVISVGH 542
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
32-241 |
1.36e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.56 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 32 VSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKAdRGSIHFDGTDVKAVrsrrDREAFMAKVQPVFQNP--FEAfnpl 109
Cdd:PRK11174 369 LNFTLPAG--QRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELREL----DPESWRKHLSWVGQNPqlPHG---- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 110 TRIDEYLLATAHrfkgAKSRTEKEALAD------VALQRVGLSmAEIKGRfSHELSGGQLQRIAVARALIPEPKLIVADE 183
Cdd:PRK11174 438 TLRDNVLLGNPD----ASDEQLQQALENawvsefLPLLPQGLD-TPIGDQ-AAGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502309174 184 PVSMVDAS---LRMSIVNlfrdlRDALNVSIVYITH---DLATAyyisDRVVIMRKGVVVESGD 241
Cdd:PRK11174 512 PTASLDAHseqLVMQALN-----AASRRQTTLMVTHqleDLAQW----DQIWVMQDGQIVQQGD 566
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
30-184 |
3.39e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.24 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 30 DDVSFALAA-DKpeiFTIVGESGSGKSTLAKMILGSEKADRGSIHFDgtdvKAVR-SRRDREAFMAKVQPVFQNPFEAFN 107
Cdd:COG0488 15 DDVSLSINPgDR---IGLVGRNGAGKSTLLKILAGELEPDSGEVSIP----KGLRiGYLPQEPPLDDDLTVLDTVLDGDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 108 PLTRIDEYLLATAHRFKGAKSRTEK----------------EALADVALQRVGLSMAEIKGRFShELSGGQLQRIAVARA 171
Cdd:COG0488 88 ELRALEAELEELEAKLAEPDEDLERlaelqeefealggweaEARAEEILSGLGFPEEDLDRPVS-ELSGGWRRRVALARA 166
|
170
....*....|...
gi 502309174 172 LIPEPKLIVADEP 184
Cdd:COG0488 167 LLSEPDLLLLDEP 179
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
31-245 |
3.51e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.23 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 31 DVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvRSRRDREA----FMAKVQPVFQNPFEAf 106
Cdd:PRK15439 281 NISLEVRAG--EILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINA-LSTAQRLArglvYLPEDRQSSGLYLDA- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 107 nPLTRideYLLATAHRFKGAKSRTEKEAladVALQRVGLSMAeIKgrFSHE------LSGGQLQRIAVARALIPEPKLIV 180
Cdd:PRK15439 357 -PLAW---NVCALTHNRRGFWIKPAREN---AVLERYRRALN-IK--FNHAeqaartLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502309174 181 ADEPVSMVDASLRMSIVNLFRDLRdALNVSIVYITHDLATAYYISDRVVIMRKGVVVES--GDARDV 245
Cdd:PRK15439 427 VDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEISGAltGAAINV 492
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
44-246 |
5.84e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.62 E-value: 5.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 44 FT-IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRdreaFMAKVQPVFQNpfeAFNPLTRIDEYLLATA-- 120
Cdd:PRK10253 35 FTaIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE----VARRIGLLAQN---ATTPGDITVQELVARGry 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 121 -HRFKGAKSRTEKEALADVALQRVGLSmaEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNL 199
Cdd:PRK10253 108 pHQPLFTRWRKEDEEAVTKAMQATGIT--HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502309174 200 FRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVL 246
Cdd:PRK10253 186 LSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-244 |
6.04e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 22 SREKMKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvrsRRDREAFMAKVQPVFQN 101
Cdd:PRK09700 272 TSRDRKKVRDISFSVC--RGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP---RSPLDAVKKGMAYITES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 102 PFE-AFNPLTRIDEYL-----LATAhRFKGA----KSRTEKEaLADVALQRVGLSMAEIKGRFShELSGGQLQRIAVARA 171
Cdd:PRK09700 347 RRDnGFFPNFSIAQNMaisrsLKDG-GYKGAmglfHEVDEQR-TAENQRELLALKCHSVNQNIT-ELSGGNQQKVLISKW 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502309174 172 LIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVsIVYITHDLATAYYISDRVVIMRKGVVVESGDARD 244
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
152-246 |
8.17e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.82 E-value: 8.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 152 GRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLATAYYiSDRVVIM 231
Cdd:PTZ00265 1353 GPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVF 1431
|
90
....*....|....*....
gi 502309174 232 ----RKGVVVESGDARDVL 246
Cdd:PTZ00265 1432 nnpdRTGSFVQAHGTHEEL 1450
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
29-234 |
8.60e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 8.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 29 VDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSR-------------RDREAFMAKV 95
Cdd:PRK10762 268 VNDVSFTL--RKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglangivyisedRKRDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 96 QpVFQNpfeafNPLTRIDeYLLATAHRFKGAKsrtEKEALADValqrVGL------SMAEIKGrfshELSGGQLQRIAVA 169
Cdd:PRK10762 346 S-VKEN-----MSLTALR-YFSRAGGSLKHAD---EQQAVSDF----IRLfniktpSMEQAIG----LLSGGNQQKVAIA 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502309174 170 RALIPEPKLIVADEPVSMVDASLRMSI---VNLFRdlrdALNVSIVYITHDLATAYYISDRVVIMRKG 234
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIyqlINQFK----AEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-244 |
1.75e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.22 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFPIGGFfsrekmkAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAvrsr 85
Cdd:PRK10522 323 LELRNVTFAYQDNGF-------SVGPINLTI--KRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA---- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAKVQPVFQnpfeafnpltriDEYLLataHRFKGAKSRTEKEALADVALQRVGLS--MAEIKGRFSH-ELSGGQ 162
Cdd:PRK10522 390 EQPEDYRKLFSAVFT------------DFHLF---DQLLGPEGKPANPALVEKWLERLKMAhkLELEDGRISNlKLSKGQ 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 163 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDlaTAYYIS-DRVVIMRKGVVVE-SG 240
Cdd:PRK10522 455 KKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD--DHYFIHaDRLLEMRNGQLSElTG 532
|
....
gi 502309174 241 DARD 244
Cdd:PRK10522 533 EERD 536
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
31-234 |
1.95e-11 |
|
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: 62.10 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 31 DVSFAlaADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvkavrsrrdREAFMAKvQP-----------VF 99
Cdd:cd03250 23 DINLE--VPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAYVSQ-EPwiqngtireniLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 100 QNPFEAfnpltriDEYllatahrfkgaksrteKEALADVALQR-----VGLSMAEI--KGRfshELSGGQLQRIAVARAL 172
Cdd:cd03250 89 GKPFDE-------ERY----------------EKVIKACALEPdleilPDGDLTEIgeKGI---NLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502309174 173 IPEPKLIVADEPVSMVDASLRMSIVN--LFRDLRDalNVSIVYITHDLataYYIS--DRVVIMRKG 234
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQL---QLLPhaDQIVVLDNG 203
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
131-231 |
2.56e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.04 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 131 EKEALADVALQrvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVS 210
Cdd:COG1245 189 ERGKLDELAEK---LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKY 264
|
90 100
....*....|....*....|.
gi 502309174 211 IVYITHDLATAYYISDRVVIM 231
Cdd:COG1245 265 VLVVEHDLAILDYLADYVHIL 285
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
42-240 |
2.85e-11 |
|
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: 64.26 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 42 EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVFqnpfeaFNPLTrIDEYLLATAh 121
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNIL------FHHLT-VAEHILFYA- 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 122 RFKGaKSRTEKEALADVALQRVGLSMAeiKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFR 201
Cdd:TIGR01257 1029 QLKG-RSWEEAQLEMEAMLEDTGLHHK--RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190
....*....|....*....|....*....|....*....
gi 502309174 202 DLRDALnvSIVYITHDLATAYYISDRVVIMRKGVVVESG 240
Cdd:TIGR01257 1106 KYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-244 |
2.95e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.53 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFpiGGFfsrEKMKAVDdvsFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvkavrs 84
Cdd:PRK15439 11 LLCARSISKQY--SGV---EVLKGID---FTLHAG--EVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAFMAKVQP-----VFQNPFeAFNPLTrIDEYLLatahrFKGAKSRTEKEALADValqrvglsMAEIKGRFSHELS 159
Cdd:PRK15439 73 NPCARLTPAKAHQlgiylVPQEPL-LFPNLS-VKENIL-----FGLPKRQASMQKMKQL--------LAALGCQLDLDSS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 160 GGQL-----QRIAVARALIPEPKLIVADEPVsmvdASLR-MSIVNLFRDLRD--ALNVSIVYITHDLATAYYISDRVVIM 231
Cdd:PRK15439 138 AGSLevadrQIVEILRGLMRDSRILILDEPT----ASLTpAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVM 213
|
250
....*....|...
gi 502309174 232 RKGVVVESGDARD 244
Cdd:PRK15439 214 RDGTIALSGKTAD 226
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
145-231 |
3.34e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 145 LSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLrdALNVSIVYITHDLATAYYI 224
Cdd:PRK13409 200 LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIREL--AEGKYVLVVEHDLAVLDYL 277
|
....*..
gi 502309174 225 SDRVVIM 231
Cdd:PRK13409 278 ADNVHIA 284
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
11-238 |
4.48e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.13 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 11 VTKLFPIGGffSREKMKAVDDVSFALaadKP-EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDgtdvkavrsrrdre 89
Cdd:COG2401 30 VLEAFGVEL--RVVERYVLRDLNLEI---EPgEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 90 afmakvqpVFQNPFEAFNPLtrIDEYllatahrfkgAKSRTEKEALAdvALQRVGLSMAEIKGRFSHELSGGQLQRIAVA 169
Cdd:COG2401 91 --------VPDNQFGREASL--IDAI----------GRKGDFKDAVE--LLNAVGLSDAVLWLRRFKELSTGQKFRFRLA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502309174 170 RALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITH--DLAtAYYISDRVVIMRKGVVVE 238
Cdd:COG2401 149 LLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHhyDVI-DDLQPDLLIFVGYGGVPE 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
46-263 |
5.35e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.73 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 46 IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRrdreAFMAKVQPVFQNPFEA----FNPLTRIDEYLLATA- 120
Cdd:PRK10575 42 LIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK----AFARKVAYLPQQLPAAegmtVRELVAIGRYPWHGAl 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 121 HRFKGAKSRTEKEALADVALQrvglsmaEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLF 200
Cdd:PRK10575 118 GRFGAADREKVEEAISLVGLK-------PLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALV 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502309174 201 RDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEHP--KHAYSIALknAVLP 263
Cdd:PRK10575 191 HRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGEtlEQIYGIPM--GILP 253
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-238 |
5.42e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.77 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKlfpigGFFSRekmKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFdGTDVKAvrs 84
Cdd:COG0488 315 VLELEGLSK-----SYGDK---TLLDDLSLRI--DRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKI--- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 rrdreAFMAKVQpvfqnpfEAFNPLTRIDEYLLAtahrfkGAKSRTEKEALAdvALQRVGLSMAEIKgRFSHELSGGQLQ 164
Cdd:COG0488 381 -----GYFDQHQ-------EELDPDKTVLDELRD------GAPGGTEQEVRG--YLGRFLFSGDDAF-KPVGVLSGGEKA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 165 RIAVARALIPEPKLIVADEP-----VSMVDAslrmsivnlfrdLRDALNV---SIVYITHD---LATayyISDRVVIMRK 233
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPtnhldIETLEA------------LEEALDDfpgTVLLVSHDryfLDR---VATRILEFED 504
|
....*
gi 502309174 234 GVVVE 238
Cdd:COG0488 505 GGVRE 509
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
30-234 |
5.52e-11 |
|
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: 60.03 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 30 DDVSFALAadkpEIFTIVGESGSGKSTLAKMILGSEKADRgsihfdgtdvkavrsrrdreafMAKVQPVFqnpfeAFNPL 109
Cdd:cd03238 14 LDVSIPLN----VLVVVTGVSGSGKSTLVNEGLYASGKAR----------------------LISFLPKF-----SRNKL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 110 TRIDEYllatahrfkgaksrtekEALADVALQRVGLsmaeikGRFSHELSGGQLQRIAVARALI--PEPKLIVADEPVSM 187
Cdd:cd03238 63 IFIDQL-----------------QFLIDVGLGYLTL------GQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTG 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502309174 188 VDASLRMSIVNLFRDLRDaLNVSIVYITHDLATAYYiSDRVVIMRKG 234
Cdd:cd03238 120 LHQQDINQLLEVIKGLID-LGNTVILIEHNLDVLSS-ADWIIDFGPG 164
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
36-237 |
5.58e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.62 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 36 LAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvKAVRSRRDREAFMAKVqpvfqnpfeAFNPLTRIDEY 115
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSPRDAIRAGI---------MLCPEDRKAEG 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 116 LLATA-------------HRFKGA--KSRTEKEaLADVALQRVglsmaEIKGRfSHE-----LSGGQLQRIAVARALIPE 175
Cdd:PRK11288 342 IIPVHsvadninisarrhHLRAGCliNNRWEAE-NADRFIRSL-----NIKTP-SREqlimnLSGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502309174 176 PKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVV 237
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
30-190 |
6.14e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.59 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 30 DDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrsRRDREAFMAK---------VQPVFq 100
Cdd:PRK13538 18 SGLSFTLNAG--ELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-----RRQRDEYHQDllylghqpgIKTEL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 101 NPFEafNpltrideylLATAHRFKGAKSRtekEALADvALQRVGLSmaeikGR---FSHELSGGQLQRIAVARALIPEPK 177
Cdd:PRK13538 90 TALE--N---------LRFYQRLHGPGDD---EALWE-ALAQVGLA-----GFedvPVRQLSAGQQRRVALARLWLTRAP 149
|
170
....*....|...
gi 502309174 178 LIVADEPVSMVDA 190
Cdd:PRK13538 150 LWILDEPFTAIDK 162
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
42-246 |
3.14e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.66 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 42 EIFTIVGESGSGKSTLAKMILGSEKADrgsiHFDGTDVkaVRSRRDREAFMAKVQPVFQNPFeAFNPLTRIDEYLLATAH 121
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGN----NFTGTIL--ANNRKPTKQILKRTGFVTQDDI-LYPHLTVRETLVFCSLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 122 RFKGAKSRTEKEALADVALQRVGLSMAE---IKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVN 198
Cdd:PLN03211 168 RLPKSLTKQEKILVAESVISELGLTKCEntiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502309174 199 LFRDLRDALNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVL 246
Cdd:PLN03211 248 TLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAM 295
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
42-231 |
7.17e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.15 E-value: 7.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 42 EIFTIVGESGSGKSTLAKMILGSEKADRGSI-----------HFDGT------------DVKAVRsrrdreafmaKVQPV 98
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSelqnyftkllegDVKVIV----------KPQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 99 FQNPfEAFNP-----LTRIDEyllatahrfkgaksRTEKEALADValqrvgLSMAEIKGRFSHELSGGQLQRIAVARALI 173
Cdd:cd03236 97 DLIP-KAVKGkvgelLKKKDE--------------RGKLDELVDQ------LELRHVLDRNIDQLSGGELQRVAIAAALA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502309174 174 PEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNvSIVYITHDLATAYYISDRVVIM 231
Cdd:cd03236 156 RDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCL 212
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
32-191 |
7.19e-10 |
|
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: 57.50 E-value: 7.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 32 VSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQPVFQNPFEAFNPLtr 111
Cdd:cd03231 19 LSFTLAAG--EALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 112 ideyllatahRFKGAKSRTEK--EALADVALQRVGlsmaeikGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVD 189
Cdd:cd03231 95 ----------RFWHADHSDEQveEALARVGLNGFE-------DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
..
gi 502309174 190 AS 191
Cdd:cd03231 158 KA 159
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
30-248 |
1.19e-09 |
|
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: 58.68 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 30 DDVSFALAADKPeI-----FT--------IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAfMAKV- 95
Cdd:COG5265 361 ENVSFGYDPERP-IlkgvsFEvpagktvaIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA-IGIVp 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 96 Q-PVFQNPFEAFNpltrIdEYLLATAhrfkgakSRTEKEALADvalqrvglsMAEIkgrfsHE----------------- 157
Cdd:COG5265 439 QdTVLFNDTIAYN----I-AYGRPDA-------SEEEVEAAAR---------AAQI-----HDfieslpdgydtrvgerg 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 158 --LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIvnlfrdlRDALNV------SIVyITHDLATayyI--SDR 227
Cdd:COG5265 493 lkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAI-------QAALREvargrtTLV-IAHRLST---IvdADE 561
|
250 260
....*....|....*....|.
gi 502309174 228 VVIMRKGVVVESGDARDVLEH 248
Cdd:COG5265 562 ILVLEAGRIVERGTHAELLAQ 582
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
11-234 |
1.91e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.20 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 11 VTKLFPiggffsreKMKAVDDVSfaLAADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvKAVRSRRDREA 90
Cdd:PRK10982 4 ISKSFP--------GVKALDNVN--LKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDFKSSKEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 91 FMAKVQPVFQNpFEAFNPLTRIDEYLLAtahRF--KG-----AKSRTEKEALADV------ALQRVGlsmaeikgrfshE 157
Cdd:PRK10982 71 LENGISMVHQE-LNLVLQRSVMDNMWLG---RYptKGmfvdqDKMYRDTKAIFDEldididPRAKVA------------T 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 158 LSGGQLQRIAVARALIPEPKLIVADEPVSmvdaSLRMSIVN-LF---RDLRDAlNVSIVYITHDLATAYYISDRVVIMRK 233
Cdd:PRK10982 135 LSVSQMQMIEIAKAFSYNAKIVIMDEPTS----SLTEKEVNhLFtiiRKLKER-GCGIVYISHKMEEIFQLCDEITILRD 209
|
.
gi 502309174 234 G 234
Cdd:PRK10982 210 G 210
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
31-203 |
3.00e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.65 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 31 DVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvKAVRSRRDREAfMAKVQPvfQNpfeAFNPLT 110
Cdd:PRK13539 20 GLSFTLAAG--EALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEA-CHYLGH--RN---AMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 111 RIDEYLLATAhRFKGAKSRTEKEALADVALQRVglsmAEIKGRfshELSGGQLQRIAVARalipepkLIVADEPVSMVD- 189
Cdd:PRK13539 89 TVAENLEFWA-AFLGGEELDIAAALEAVGLAPL----AHLPFG---YLSAGQKRRVALAR-------LLVSNRPIWILDe 153
|
170
....*....|....*.
gi 502309174 190 --ASLRMSIVNLFRDL 203
Cdd:PRK13539 154 ptAALDAAAVALFAEL 169
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
40-230 |
3.21e-09 |
|
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: 55.27 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 40 KPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVkavrsrrdreafmakvqpvfqnpfeAFNPltrideyllat 119
Cdd:cd03222 24 EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-------------------------VYKP----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 120 ahrfkgaksrtekealadvalQRVglsmaeikgrfshELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNL 199
Cdd:cd03222 68 ---------------------QYI-------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA 113
|
170 180 190
....*....|....*....|....*....|.
gi 502309174 200 FRDLRDALNVSIVYITHDLATAYYISDRVVI 230
Cdd:cd03222 114 IRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
23-240 |
3.79e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 55.35 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 23 REKMKAVDDVSFALaadKP-EIFTIVGESGSGKSTLAKMI---LGSEKADRGSIHFDGTDVKAVRSRRDREAfmakvqpV 98
Cdd:cd03233 17 RSKIPILKDFSGVV---KPgEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEKYPGEI-------I 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 99 FQNPFEAFNPLTRIDEyLLATAHRFKGaksrtekealadvalqrvglsmaeikGRFSHELSGGQLQRIAVARALIPEPKL 178
Cdd:cd03233 87 YVSEEDVHFPTLTVRE-TLDFALRCKG--------------------------NEFVRGISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502309174 179 IVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVYITHDLA-TAYYISDRVVIMRKGVVVESG 240
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
28-249 |
8.19e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 56.26 E-value: 8.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 28 AVDDVSFALaadKP-EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVR--SRRDREAFmakvqpVFQNPF- 103
Cdd:PRK10789 330 ALENVNFTL---KPgQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQldSWRSRLAV------VSQTPFl 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 104 ----EAFN-PLTRIDeyllATahrfkgaKSRTEKEA-LADVALQRVGLSMA---EIkGRFSHELSGGQLQRIAVARALIP 174
Cdd:PRK10789 401 fsdtVANNiALGRPD----AT-------QQEIEHVArLASVHDDILRLPQGydtEV-GERGVMLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502309174 175 EPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNVSIVyiTHDLaTAYYISDRVVIMRKGVVVESGDARDVLEHP 249
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIIS--AHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-217 |
9.21e-09 |
|
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: 56.10 E-value: 9.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 6 LELDHVTKLFpiggffsREKMkAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFdGTDVKAVRSR 85
Cdd:TIGR03719 323 IEAENLTKAF-------GDKL-LIDDLSFKLP--PGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 86 RDREAFMAKvqpvfQNPFEAF---NPLTRIDEYLLAT-----AHRFKGAKSRtekealadvalQRVGlsmaeikgrfshE 157
Cdd:TIGR03719 392 QSRDALDPN-----KTVWEEIsggLDIIKLGKREIPSrayvgRFNFKGSDQQ-----------KKVG------------Q 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502309174 158 LSGGQLQRIAVARALIPEPKLIVADEPVSMVDaslrmsiVNLFRDLRDALNV---SIVYITHD 217
Cdd:TIGR03719 444 LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD-------VETLRALEEALLNfagCAVVISHD 499
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
46-237 |
9.32e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 9.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 46 IVGESGSGKSTLAKMILGSEKADRGSIHFDgTDVKAVRSRRDR-----------------------EAFMAKVQPVFQNP 102
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVARLQQDPprnvegtvydfvaegieeqaeylKRYHDISHLVETDP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 103 FEA-FNPLTRIDEYL-LATAHRFKgakSRtekeaLADVaLQRVGLSmAEIKgrfSHELSGGQLQRIAVARALIPEPKLIV 180
Cdd:PRK11147 113 SEKnLNELAKLQEQLdHHNLWQLE---NR-----INEV-LAQLGLD-PDAA---LSSLSGGWLRKAALGRALVSNPDVLL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502309174 181 ADEPVSMVDASlrmSIVNLFRDLRDaLNVSIVYITHDLATAYYISDRVVIMRKGVVV 237
Cdd:PRK11147 180 LDEPTNHLDIE---TIEWLEGFLKT-FQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-234 |
1.10e-08 |
|
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: 54.26 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 17 IGGFFS-REKMKAVDDVSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKV 95
Cdd:cd03290 4 TNGYFSwGSGLATLSNINIRIPTG--QLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 96 QPVFQNPFEafnpLTRIDEYLLATAHRFKGAKSRTEKEALA---DVALQRVGlSMAEIkGRFSHELSGGQLQRIAVARAL 172
Cdd:cd03290 82 AYAAQKPWL----LNATVEENITFGSPFNKQRYKAVTDACSlqpDIDLLPFG-DQTEI-GERGINLSGGQRQRICVARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502309174 173 IPEPKLIVADEPVSMVDASL-----RMSIVNLFRDLRDalnvSIVYITHDLATAYYiSDRVVIMRKG 234
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
155-216 |
3.43e-08 |
|
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: 52.16 E-value: 3.43e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502309174 155 SHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRdalnVSIVYITH 216
Cdd:cd03223 89 DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGH 146
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-254 |
3.44e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 32 VSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAF-MAKVQPVFqnpfeaFNPLT 110
Cdd:PTZ00243 1329 VSFRIAPR--EKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFsMIPQDPVL------FDGTV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 111 R--IDEYLLATAhrfkgaksrtekealADV--ALQRVGLS---MAEIKGRFSHELSG------GQLQRIAVARALIPE-P 176
Cdd:PTZ00243 1401 RqnVDPFLEASS---------------AEVwaALELVGLRervASESEGIDSRVLEGgsnysvGQRQLMCMARALLKKgS 1465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502309174 177 KLIVADEPVSMVDASLRMSIVNLFRDLRDALNVsiVYITHDLAT-AYYisDRVVIMRKGVVVESGDARDVLEHPKHAYS 254
Cdd:PTZ00243 1466 GFILMDEATANIDPALDRQIQATVMSAFSAYTV--ITIAHRLHTvAQY--DKIIVMDHGAVAEMGSPRELVMNRQSIFH 1540
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
46-256 |
5.28e-08 |
|
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: 54.18 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 46 IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDReafmAKVQPVFQNPFeAFNPLTRIDeyllatahrFKG 125
Cdd:TIGR00957 1317 IVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLR----FKITIIPQDPV-LFSGSLRMN---------LDP 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 126 AKSRTEKEALADVALQRVGLSMAEIKGRFSHE-------LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVN 198
Cdd:TIGR00957 1383 FSQYSDEEVWWALELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQS 1462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 199 LFRDLRDalNVSIVYITHDLATayyISD--RVVIMRKGVVVESGDARDVLEHPKHAYSIA 256
Cdd:TIGR00957 1463 TIRTQFE--DCTVLTIAHRLNT---IMDytRVIVLDKGEVAEFGAPSNLLQQRGIFYSMA 1517
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
42-244 |
6.68e-08 |
|
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: 53.26 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 42 EIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAkvqpVFQnpfeafnpltriDEYLLataH 121
Cdd:COG4615 359 ELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSA----VFS------------DFHLF---D 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 122 RFKGAKSRTEkEALADVALQRVGLS--MAEIKGRFSH-ELSGGQLQRIAVARALIPEPKLIVADE------PVsmvdasl 192
Cdd:COG4615 420 RLLGLDGEAD-PARARELLERLELDhkVSVEDGRFSTtDLSQGQRKRLALLVALLEDRPILVFDEwaadqdPE------- 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502309174 193 rmsivnlFR---------DLRdALNVSIVYITHDlaTAYY-ISDRVVIMRKGVVVE-SGDARD 244
Cdd:COG4615 492 -------FRrvfytellpELK-ARGKTVIAISHD--DRYFdLADRVLKMDYGKLVElTGPAAL 544
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-245 |
1.06e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 22 SREKMKAVDDVSFALAADKPEIFtiVGESGSGKSTLAKMILGSEKADRGSIHF-DGTDVKAVRSRRDReafmAKVQPVFQ 100
Cdd:PTZ00265 394 TRKDVEIYKDLNFTLTEGKTYAF--VGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWR----SKIGVVSQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 101 NPFEAFNPLTRIDEYLL---------------ATAHRFKGAKSRTEKEA-----LADVALQRVGLSMAEIK--------- 151
Cdd:PTZ00265 468 DPLLFSNSIKNNIKYSLyslkdlealsnyyneDGNDSQENKNKRNSCRAkcagdLNDMSNTTDSNELIEMRknyqtikds 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 152 --------------------------GRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRD 205
Cdd:PTZ00265 548 evvdvskkvlihdfvsalpdkyetlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKG 627
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 502309174 206 ALNVSIVYITHDLATAYYISDRVVIMRKgvvvESGDARDV 245
Cdd:PTZ00265 628 NENRITIIIAHRLSTIRYANTIFVLSNR----ERGSTVDV 663
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-254 |
1.57e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 32 VSFALAADkpEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQ-PVFQNPFEAFNplt 110
Cdd:PLN03232 1255 LSFFVSPS--EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQsPVLFSGTVRFN--- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 111 rIDEYllaTAHRFKGAKSRTEKEALADVALQR-VGLSMAEIKGrfSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVD 189
Cdd:PLN03232 1330 -IDPF---SEHNDADLWEALERAHIKDVIDRNpFGLDAEVSEG--GENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502309174 190 ASLRMSIVNLFRDlrDALNVSIVYITHDLATAYYiSDRVVIMRKGVVVESGDARDVLEHPKHAYS 254
Cdd:PLN03232 1404 VRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFF 1465
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
40-241 |
1.88e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.95 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 40 KP-EIFTIVGESGSGKSTLAKMILGSE--KADRGSIHFDGTDVKAV--RSRRDREAFMAKVQPV----FQNPFEAFNPLT 110
Cdd:PRK09580 25 RPgEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELspEDRAGEGIFMAFQYPVeipgVSNQFFLQTALN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 111 RIDEYL-LATAHRFKGAKSRTEKEALADVALQRVGLSMAEikgrfshELSGGQLQRIAVARALIPEPKLIVADEPVSMVD 189
Cdd:PRK09580 105 AVRSYRgQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNV-------GFSGGEKKRNDILQMAVLEPELCILDESDSGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502309174 190 ASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYIS-DRVVIMRKGVVVESGD 241
Cdd:PRK09580 178 IDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGD 229
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
21-189 |
3.52e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.85 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 21 FSREKMKAVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavrsRRDREAFMAKVQPVfq 100
Cdd:PRK13543 19 FSRNEEPVFGPLDFHV--DAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT----RGDRSRFMAYLGHL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 101 npfeafnPLTRIDEYLLATAHRFKGAKSRTEKEALADvALQRVGLsmAEIKGRFSHELSGGQLQRIAVARALIPEPKLIV 180
Cdd:PRK13543 91 -------PGLKADLSTLENLHFLCGLHGRRAKQMPGS-ALAIVGL--AGYEDTLVRQLSAGQKKRLALARLWLSPAPLWL 160
|
....*....
gi 502309174 181 ADEPVSMVD 189
Cdd:PRK13543 161 LDEPYANLD 169
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-248 |
6.04e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.66 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 20 FFSREKMK---AVDDVSFALaaDKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGT-DVKAVRSRRDreafmakv 95
Cdd:PRK13545 28 FFRSKDGEyhyALNNISFEV--PEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaALIAISSGLN-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 96 qpvfqnpfeafNPLTRIDEYLLatahrfKGAKSRTEKEALADVALQRVglSMAEIkGRFSHE----LSGGQLQRIAVARA 171
Cdd:PRK13545 98 -----------GQLTGIENIEL------KGLMMGLTKEKIKEIIPEII--EFADI-GKFIYQpvktYSSGMKSRLGFAIS 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502309174 172 LIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEH 248
Cdd:PRK13545 158 VHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
128-240 |
6.86e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.12 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 128 SRTEKEALADVALQRvgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDL-RDA 206
Cdd:NF000106 117 SRKDARARADELLER--FSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDG 194
|
90 100 110
....*....|....*....|....*....|....
gi 502309174 207 lnVSIVYITHDLATAYYISDRVVIMRKGVVVESG 240
Cdd:NF000106 195 --ATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
46-217 |
1.46e-06 |
|
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: 47.06 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 46 IVGESGSGKSTLAKMILGSEKADRGSIHFDGTdvkavrsrrdreafmakvqpvfqnpfeafnplTRIdeyllatahrfkg 125
Cdd:cd03221 31 LVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------------------------------VKI------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 126 aksrtekealadvalqrvglsmaeikGRFSHeLSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRD 205
Cdd:cd03221 66 --------------------------GYFEQ-LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG 118
|
170
....*....|..
gi 502309174 206 ALnvsiVYITHD 217
Cdd:cd03221 119 TV----ILVSHD 126
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-252 |
2.88e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 20 FFSREKMKAVDDVSFALAADKpeiFTIV-GESGSGKSTLAKMILGSEKADRGSihfdgtdVKAVRSrrdreafMAKV--Q 96
Cdd:PTZ00243 667 FFELEPKVLLRDVSVSVPRGK---LTVVlGATGSGKSTLLQSLLSQFEISEGR-------VWAERS-------IAYVpqQ 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 97 PVFQNPFEAFNPL--TRIDEYLLATAHRFkgakSRTEkealADVALQRVGLSmAEIkGRFSHELSGGQLQRIAVARALIP 174
Cdd:PTZ00243 730 AWIMNATVRGNILffDEEDAARLADAVRV----SQLE----ADLAQLGGGLE-TEI-GEKGVNLSGGQKARVSLARAVYA 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 175 EPKLIVADEPVSMVDASLRMSIV-NLFRD-LRDALNVSIVYITHDLATAyyisDRVVIMRKGVVVESGDARDVLEHPKHA 252
Cdd:PTZ00243 800 NRDVYLLDDPLSALDAHVGERVVeECFLGaLAGKTRVLATHQVHVVPRA----DYVVALGDGRVEFSGSSADFMRTSLYA 875
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-248 |
3.11e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 19 GFFSREKMKAVDDVSFALAADKP-EIFTIVGESGSGKSTLAKMIL----GSEKADRGSIHFDGTDVKAVRSR-RDREAFM 92
Cdd:TIGR00956 64 KLKKFRDTKTFDILKPMDGLIKPgELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHyRGDVVYN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 93 AKVQPVFQNpfeafnpLTRIDEylLATAHRFKGAKSRTE-------KEALADVALQRVGLSM---AEIKGRFSHELSGGQ 162
Cdd:TIGR00956 144 AETDVHFPH-------LTVGET--LDFAARCKTPQNRPDgvsreeyAKHIADVYMATYGLSHtrnTKVGNDFVRGVSGGE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 163 LQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALN-VSIVYITHDLATAYYISDRVVIMRKGVVVESGD 241
Cdd:TIGR00956 215 RKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDtTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGP 294
|
....*..
gi 502309174 242 ARDVLEH 248
Cdd:TIGR00956 295 ADKAKQY 301
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
28-189 |
7.00e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.43 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 28 AVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKA--VRSRRdREAFMAkvQP-------- 97
Cdd:NF033858 281 AVDHVSFRIR--RGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAgdIATRR-RVGYMS--QAfslygelt 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 98 VFQNpfeafnpltrideyLLATAHRFKGAKSRTekEALADVALQRVGLsmAEIKGRFSHELSGGQLQRIAVARALIPEPK 177
Cdd:NF033858 356 VRQN--------------LELHARLFHLPAAEI--AARVAEMLERFDL--ADVADALPDSLPLGIRQRLSLAVAVIHKPE 417
|
170
....*....|..
gi 502309174 178 LIVADEPVSMVD 189
Cdd:NF033858 418 LLILDEPTSGVD 429
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
40-234 |
7.42e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.06 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 40 KPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREafmakvqpvfqnpfeafnpltrideyllat 119
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 120 ahrfkgaksrtekealadvalqrvglsmAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNL 199
Cdd:smart00382 51 ----------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLL 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502309174 200 FRDLRDAL-----NVSIVYITHDL-----ATAYYISDRVVIMRKG 234
Cdd:smart00382 103 EELRLLLLlksekNLTVILTTNDEkdlgpALLRRRFDRRIVLLLI 147
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
29-189 |
8.97e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.71 E-value: 8.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 29 VDDVSFALAADKpeIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKavrsrRDREAFmaKVQPVFQNPFEAFNP 108
Cdd:PRK13540 17 LQQISFHLPAGG--LLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-----KDLCTY--QKQLCFVGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 109 LTRIDEYLLATAHRFKGAKSRTEkealadvaLQRVgLSMAEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMV 188
Cdd:PRK13540 88 YLTLRENCLYDIHFSPGAVGITE--------LCRL-FSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
.
gi 502309174 189 D 189
Cdd:PRK13540 159 D 159
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-236 |
9.14e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLfpiggffsreKMKAVDDVSFALAadKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtdvKAVRS 84
Cdd:PRK10982 250 ILEVRNLTSL----------RQPSIRDVSFDLH--KGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG---KKINN 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 85 RRDREAF---MAKVQP------VFQNPFEAFNPL-TRIDEY-----LLATahrfKGAKSRTekealadvalQRVGLSM-A 148
Cdd:PRK10982 315 HNANEAInhgFALVTEerrstgIYAYLDIGFNSLiSNIRNYknkvgLLDN----SRMKSDT----------QWVIDSMrV 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 149 EIKGRFSH--ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISD 226
Cdd:PRK10982 381 KTPGHRTQigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITD 459
|
250
....*....|
gi 502309174 227 RVVIMRKGVV 236
Cdd:PRK10982 460 RILVMSNGLV 469
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-189 |
1.21e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.83 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 5 LLELDHVTKLFPIGGFFSREKMKA---------VDDVSFALAADKPeiFTIVGESGSGKSTLAKMILGSEKADrGSIHFD 75
Cdd:TIGR01271 1202 VIENPHAQKCWPSGGQMDVQGLTAkyteagravLQDLSFSVEGGQR--VGLLGRTGSGKSTLLSALLRLLSTE-GEIQID 1278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 76 GTDVKAVRSRRDREAFMAKVQPVF---------QNPFEAFNpltriDEYLLATAHRFkGAKSRTEK-EALADVALQRVGl 145
Cdd:TIGR01271 1279 GVSWNSVTLQTWRKAFGVIPQKVFifsgtfrknLDPYEQWS-----DEEIWKVAEEV-GLKSVIEQfPDKLDFVLVDGG- 1351
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502309174 146 smaeikgrfsHELSGGQLQRIAVARALIPEPKLIVADEPVSMVD 189
Cdd:TIGR01271 1352 ----------YVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-72 |
1.37e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 1.37e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502309174 3 SNLLELDHVTKLFPiggffsrEKMkAVDDVSFALaadkPE--IFTIVGESGSGKSTLAKMILGSEKADRGSI 72
Cdd:PRK11819 322 DKVIEAENLSKSFG-------DRL-LIDDLSFSL----PPggIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
46-247 |
1.92e-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: 46.09 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 46 IVGESGSGKSTLAKMILGSEKADRGSIHFDGTdvkavrsrrdreafMAKVqpvfqnPFEAFNPLTRIDEYLLaTAHRFKG 125
Cdd:TIGR00957 669 VVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYV------PQQAWIQNDSLRENIL-FGKALNE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 126 AKSRTEKEA---LADVALQRVGlSMAEIkGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRD 202
Cdd:TIGR00957 728 KYYQQVLEAcalLPDLEILPSG-DRTEI-GEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIG 805
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502309174 203 LRDAL-NVSIVYITHDLAtayYI--SDRVVIMRKGVVVESGDARDVLE 247
Cdd:TIGR00957 806 PEGVLkNKTRILVTHGIS---YLpqVDVIIVMSGGKISEMGSYQELLQ 850
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
46-240 |
2.38e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.74 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 46 IVGESGSGKSTLAKMILGS-EKADRGSIHFDGTdvkavrsrrdrEAFMAKVQPVFqnpfeafNPLTRiDEYLLatahrfk 124
Cdd:PLN03232 648 IVGGTGEGKTSLISAMLGElSHAETSSVVIRGS-----------VAYVPQVSWIF-------NATVR-ENILF------- 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 125 GAKSRTEK--EALADVALQR-----VGLSMAEIkGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIV 197
Cdd:PLN03232 702 GSDFESERywRAIDVTALQHdldllPGRDLTEI-GERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502309174 198 N--LFRDLRDALNVSIVYITHDLAtayyISDRVVIMRKGVVVESG 240
Cdd:PLN03232 781 DscMKDELKGKTRVLVTNQLHFLP----LMDRIILVSEGMIKEEG 821
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
135-189 |
6.24e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 6.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 502309174 135 LADVALQRVGLSMAEIKGRFsHELSGGQlQRIA-VARALIPEPKLIVADEPVSMVD 189
Cdd:PRK10938 380 LAQQWLDILGIDKRTADAPF-HSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD 433
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
46-240 |
6.92e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.26 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 46 IVGESGSGKSTLAKMILGsEKADRGsihfDGTDVKavrsrRDREAFMAKVQPVFqnpfeafNPLTRiDEYLLATAHRfkg 125
Cdd:PLN03130 648 IVGSTGEGKTSLISAMLG-ELPPRS----DASVVI-----RGTVAYVPQVSWIF-------NATVR-DNILFGSPFD--- 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 126 aKSRTEKeALADVALQR-----VGLSMAEIkGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNlf 200
Cdd:PLN03130 707 -PERYER-AIDVTALQHdldllPGGDLTEI-GERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD-- 781
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502309174 201 RDLRDAL-NVSIVYITHDLataYYIS--DRVVIMRKGVVVESG 240
Cdd:PLN03130 782 KCIKDELrGKTRVLVTNQL---HFLSqvDRIILVHEGMIKEEG 821
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
158-217 |
7.05e-04 |
|
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: 41.07 E-value: 7.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 158 LSGGQLQRIAVARALIPEPKLIVADEPVSMVDASlrmSIVNLFRDLRDaLNVSIVYITHD 217
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQE-YPGTVVAVTHD 217
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
144-189 |
7.23e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 7.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 502309174 144 GLSM-AEIKGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVD 189
Cdd:PLN03073 330 GLSFtPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
30-226 |
1.20e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.52 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 30 DDVSFALAAdkpeiFTIV-GESGSGKSTLAKMILG---SEKADRGSIHFDGTDvkavrsRRDREAFMAKVQPVFQNPF-- 103
Cdd:cd03271 14 IDVDIPLGV-----LTCVtGVSGSGKSSLINDTLYpalARRLHLKKEQPGNHD------RIEGLEHIDKVIVIDQSPIgr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 104 -EAFNPLT-------------------RIDEYLLATahRFKGaKS------RTEKEAL---ADV--------ALQRVGLS 146
Cdd:cd03271 83 tPRSNPATytgvfdeirelfcevckgkRYNRETLEV--RYKG-KSiadvldMTVEEALeffENIpkiarklqTLCDVGLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 147 MAEIkGRFSHELSGGQLQRIAVARALI---PEPKLIVADEPVSMVDASLRMSIVNLFRDLRDALNvSIVYITHDL---AT 220
Cdd:cd03271 160 YIKL-GQPATTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLdviKC 237
|
....*.
gi 502309174 221 AYYISD 226
Cdd:cd03271 238 ADWIID 243
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
46-254 |
1.24e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.49 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 46 IVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVKAVRSRRDREAFMAKVQ-PVFQNPFEAFNpltrIDEYllaTAHRFK 124
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQaPVLFSGTVRFN----LDPF---NEHNDA 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 125 GAKSRTEKEALADVaLQRVGLSM-AEIkGRFSHELSGGQLQRIAVARALIPEPKLIVADEPVSMVD----ASLRMSIVNL 199
Cdd:PLN03130 1343 DLWESLERAHLKDV-IRRNSLGLdAEV-SEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDvrtdALIQKTIREE 1420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502309174 200 FRdlrdalNVSIVYITHDLATAyyI-SDRVVIMRKGVVVESGDARDVLEHPKHAYS 254
Cdd:PLN03130 1421 FK------SCTMLIIAHRLNTI--IdCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
28-248 |
1.77e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.03 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 28 AVDDVSFAlaADKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGtDVKAVRSRRDREAFMAKVQpvfqnpfeafn 107
Cdd:PRK13546 39 ALDDISLK--AYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISAGLSGQLTGIE----------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 108 pltRIDEYLLATAHRFKGAKSRT----EKEALADVALQRVglsmaeikgrfsHELSGGQLQRIAVARALIPEPKLIVADE 183
Cdd:PRK13546 105 ---NIEFKMLCMGFKRKEIKAMTpkiiEFSELGEFIYQPV------------KKYSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502309174 184 PVSMVDASLRMSIVNLFRDLRDAlNVSIVYITHDLATAYYISDRVVIMRKGVVVESGDARDVLEH 248
Cdd:PRK13546 170 ALSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
40-241 |
3.07e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.39 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 40 KPEIFTIVGESGSGKSTLAKMILGSEK-----------ADRGSIHFDGTDVKAVRSRRdrEAFMAKVQPVFQNPFEAFNP 108
Cdd:cd03270 20 RNKLVVITGVSGSGKSSLAFDTIYAEGqrryveslsayARQFLGQMDKPDVDSIEGLS--PAIAIDQKTTSRNPRSTVGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 109 LTRIDEYLLATAHRFkGAKSRTEkeALADVALQRVGLSmaeikgRFSHELSGGQLQRIAVARALipEPKLI----VADEP 184
Cdd:cd03270 98 VTEIYDYLRLLFARV-GIRERLG--FLVDVGLGYLTLS------RSAPTLSGGEAQRIRLATQI--GSGLTgvlyVLDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502309174 185 VSMVDASLRMSIVNLFRDLRDALNVSIVyITHDLATAyYISDRVVIMRKGVVVESGD 241
Cdd:cd03270 167 SIGLHPRDNDRLIETLKRLRDLGNTVLV-VEHDEDTI-RAADHVIDIGPGAGVHGGE 221
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
157-216 |
4.32e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 38.58 E-value: 4.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 157 ELSGGQLQRIAVARALIPEPKLIVADEPVSMVDASLRMSIVNLFRDlrdaLNVSIVYITH 216
Cdd:TIGR00954 582 VLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE----FGITLFSVSH 637
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
39-80 |
7.45e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 36.96 E-value: 7.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 502309174 39 DKPEIFTIVGESGSGKSTLAKMILGSEKADRGSIHFDGTDVK 80
Cdd:pfam06414 9 ERPKAILLGGQPGAGKTELARALLDELGRQGNVVRIDPDDFR 50
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
103-250 |
9.18e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.69 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309174 103 FEAFNPLTRIDEYLLATAHRFKGAKSRTEkeALADVALQRVGLSmaeikgRFSHELSGGQLQRIAVARALIPEPK--LIV 180
Cdd:TIGR00630 442 HEFFNQLTLTPEEKKIAEEVLKEIRERLG--FLIDVGLDYLSLS------RAAGTLSGGEAQRIRLATQIGSGLTgvLYV 513
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502309174 181 ADEPVSMVDASLRMSIVNLFRDLRDALNVSIVyITHD---LATAyyisDRVVIMRKGV------VVESGDARDVLEHPK 250
Cdd:TIGR00630 514 LDEPSIGLHQRDNRRLINTLKRLRDLGNTLIV-VEHDedtIRAA----DYVIDIGPGAgehggeVVASGTPEEILANPD 587
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