|
Name |
Accession |
Description |
Interval |
E-value |
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-558 |
0e+00 |
|
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: 666.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 2 IDKQIMKL-PGMKQLLGLLAGLSFLQALFIIGQAYGLARAITGLWEGR-PLEEQWGWILLFFCSFIARQAVIYFRSKRLD 79
Cdd:COG4988 4 LDKRLKRLaRGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGaPLSALLPLLGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 80 DYSYQQAADLRDQLLEKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIMNMSIIPWVILALVFYLDWESGLV 159
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 160 LLLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKYGKSIFASSERFRKATMASLKVGIL 239
Cdd:COG4988 164 LLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 240 STFALDFFTTLSIAVVAVLLGLRLINEGILLFPALTILILAPEYFLPIRDFSSDYHATLDGKNAMTAVTEILHQPEAQVP 319
Cdd:COG4988 244 SSAVLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLDAPEPAAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 320 AVTVP-RWQEDAQLTIDQLAFSYEE-KAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTA 397
Cdd:COG4988 324 AGTAPlPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 398 FRQASWQEQLIYIPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIA 477
Cdd:COG4988 404 LDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLA 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 478 LARAFLdQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQ 557
Cdd:COG4988 484 LARALL-RDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
.
gi 491368637 558 G 558
Cdd:COG4988 563 G 563
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-539 |
0e+00 |
|
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: 555.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 16 LGLLAGLSFLQALFIIGQAYGLARAITGLW-EGRPLEEQWGWILLFFCSFIARQAVIYFRSKRLDDYSYQQAADLRDQLL 94
Cdd:TIGR02857 5 LALLALLGVLGALLIIAQAWLLARVVDGLIsAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 95 EKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIMNMSIIPWVILALVFYLDWESGLVLLLVFPLIIIFMIIL 174
Cdd:TIGR02857 85 EAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMILI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 175 GYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKYGKSIFASSERFRKATMASLKVGILSTFALDFFTTLSIAV 254
Cdd:TIGR02857 165 GWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLSVAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 255 VAVLLGLRLINEGILLFPALTILILAPEYFLPIRDFSSDYHATLDGKNAMTAVTEILHQPEAQVPAVTVPRWQEDAQLTI 334
Cdd:TIGR02857 245 VAVYIGFRLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEF 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 335 DQLAFSYE-EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQN 413
Cdd:TIGR02857 325 SGVSVAYPgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQH 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 414 PYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLDqQRKILLFD 493
Cdd:TIGR02857 405 PFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLR-DAPLLLLD 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 491368637 494 EPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVM 539
Cdd:TIGR02857 484 EPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-563 |
1.90e-126 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 383.43 E-value: 1.90e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 4 KQIMKLpgMKQLLGLLAGLSFLQALFIIGQAYGLARAITGLW-EGRPLEEQWGWILLFFCSFIARQAVIYFRSKrlddYS 82
Cdd:PRK11174 14 KQQSKP--AKRWLNLSILLGFLSGLLLIAQAWLLATILQALIiENIPREALLPPFILLILLFVLRALLAWLRER----VG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 83 YQQAADLRDQL----LEKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIMNMSIIPWVILALVFYLDWESGL 158
Cdd:PRK11174 88 FKAGQHIRQQIrqqvLDKLQQLGPAWIQGKPAGSWATLVLEQVEDMHDFYARYLPQMALAVLVPLLILIAVFPINWAAGL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 159 VLLLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKYGKSIFASSERFRKATMASLKVGI 238
Cdd:PRK11174 168 ILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRTMEVLRMAF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 239 LSTFALDFFTTLSIAVVAVLLGLRLINE--------GILLFPALTILILAPEYFLPIRDFSSDYHATLDGKNAMTAVTEI 310
Cdd:PRK11174 248 LSSAVLEFFASISIALVAVYFGFSYLGElnfghygtGVTLFAGFFVLILAPEFYQPLRDLGTFYHAKAQAVGAAESLVTF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 311 LHQPEAQVPAVTVPrWQEDAQLTI---DQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLvPDSGE 387
Cdd:PRK11174 328 LETPLAHPQQGEKE-LASNDPVTIeaeDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGS 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 388 ITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERH 467
Cdd:PRK11174 406 LKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAG 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 468 LSGGQAQRIALARAFLdQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQ 547
Cdd:PRK11174 486 LSVGQAQRLALARALL-QPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQ 564
|
570
....*....|....*.
gi 491368637 548 GTLAQLQQKQGAFTEL 563
Cdd:PRK11174 565 GDYAELSQAGGLFATL 580
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-565 |
2.84e-119 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 364.49 E-value: 2.84e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 13 KQLLGLLAGLSFLQALFIIGQAYGLARAITGLWEGRPLEEQWGWILLFFCSFIARQAVIYFRSKRLDDYSYQQAADLRDQ 92
Cdd:COG1132 20 RGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 93 LLEKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIMNMSIIPWVILALVFYLDWESGLVLLLVFPLIIIFMI 172
Cdd:COG1132 100 LFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 173 ILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKYGKSIFASSERFRKATMASLKVGILSTFALDFFTTLSI 252
Cdd:COG1132 180 LFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 253 AVVaVLLGLRLINEGILLFPALTILILAPEYFL-PIRDFSSDYHATLDGKNAMTAVTEILHQPEAQV-PAVTVPRWQEDA 330
Cdd:COG1132 260 ALV-LLVGGLLVLSGSLTVGDLVAFILYLLRLFgPLRQLANVLNQLQRALASAERIFELLDEPPEIPdPPGAVPLPPVRG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 331 QLTIDQLAFSY-EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIY 409
Cdd:COG1132 339 EIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 IPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLdQQRKI 489
Cdd:COG1132 419 VPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALL-KDPPI 497
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491368637 490 LLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGAFTELVN 565
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYR 573
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
19-307 |
3.09e-115 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 344.01 E-value: 3.09e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 19 LAGLSFLQALFIIGQAYGLARAITGLW-EGRPLEEQWGWILLFFCSFIARQAVIYFRSKRLDDYSYQQAADLRDQLLEKL 97
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFlEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 98 FRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIMNMSIIPWVILALVFYLDWESGLVLLLVFPLIIIFMIILGYA 177
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 178 AQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKYGKSIFASSERFRKATMASLKVGILSTFALDFFTTLSIAVVAV 257
Cdd:cd18584 161 AQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALVAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 491368637 258 LLGLRLINEGILLFPALTILILAPEYFLPIRDFSSDYHATLDGKNAMTAV 307
Cdd:cd18584 241 YIGFRLLGGSLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAERL 290
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
87-563 |
6.22e-103 |
|
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: 322.10 E-value: 6.22e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 87 ADLRDQLLEKLFRVGPQIAQQQGTGNVTTMVLEGINQVEN-YLKLILAKIMNMSIIPWVILALVFyLDWESGLVLLLVFP 165
Cdd:COG4987 88 ADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNlYLRVLLPLLVALLVILAAVAFLAF-FSPALALVLALGLL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 166 LIIIFMIILGYAAQSKAEKQYRT-FQLLSNHFIDSLRGIDTLKLFGVSKKYGKSIFASSERFRKATMASLKVGILSTFAL 244
Cdd:COG4987 167 LAGLLLPLLAARLGRRAGRRLAAaRAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 245 DFFTTLsiAVVAVL-LGLRLINEGILLFPALTILILAP----EYFLPIRDFSSDYHATLDgknAMTAVTEILHQPEAQVP 319
Cdd:COG4987 247 QLAAGL--AVVAVLwLAAPLVAAGALSGPLLALLVLAAlalfEALAPLPAAAQHLGRVRA---AARRLNELLDAPPAVTE 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 320 AVTVPRWQEDAQLTIDQLAFSY--EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTA 397
Cdd:COG4987 322 PAEPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 398 FRQASWQEQLIYIPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIA 477
Cdd:COG4987 402 LDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLA 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 478 LARAFLdQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQ 557
Cdd:COG4987 482 LARALL-RDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
....*.
gi 491368637 558 GAFTEL 563
Cdd:COG4987 561 GRYRQL 566
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
144-566 |
1.22e-86 |
|
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: 283.26 E-value: 1.22e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 144 VILALVFYLDWESGLVLLLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKYGKSIFASS 223
Cdd:COG2274 285 IFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 224 ERFRKATMASLKVGILSTFALDFFTTLSIAVVaVLLGLRLINEG------ILLFPALTILILAPeyFLPIRDFSSDYHAT 297
Cdd:COG2274 365 AKYLNARFKLRRLSNLLSTLSGLLQQLATVAL-LWLGAYLVIDGqltlgqLIAFNILSGRFLAP--VAQLIGLLQRFQDA 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 298 ldgKNAMTAVTEILHQP-EAQVPAVTVPRWQEDAQLTIDQLAFSY--EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLI 374
Cdd:COG2274 442 ---KIALERLDDILDLPpEREEGRSKLSLPRLKGDIELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 375 NTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELP 454
Cdd:COG2274 519 KLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALP 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 455 QGLDTMLGEGERHLSGGQAQRIALARAFLdQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMD 534
Cdd:COG2274 599 MGYDTVVGEGGSNLSGGQRQRLAIARALL-RNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLAD 677
|
410 420 430
....*....|....*....|....*....|..
gi 491368637 535 EIIVMDQGRIVEQGTLAQLQQKQGAFTELVNG 566
Cdd:COG2274 678 RIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
142-557 |
1.53e-61 |
|
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: 215.50 E-value: 1.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 142 PWVILALV--FYLDWESGLVLLLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVS----KKY 215
Cdd:TIGR03375 271 PFALLFLLviAIIGGPLVWVPLVAIPLILLPGLLLQRPLSRLAEESMRESAQRNAVLVESLSGLETIKALNAEgrfqRRW 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 216 GKSIFASSerfrkatMASLKVGILSTFALDFFTTLS-IAVVA-VLLGLRLINEGILLFPAL-TILILAPEYFLPIRDFSS 292
Cdd:TIGR03375 351 EQTVAALA-------RSGLKSRFLSNLATNFAQFIQqLVSVAiVVVGVYLISDGELTMGGLiACVMLSGRALAPLGQLAG 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 293 ---DYHATldgKNAMTAVTEILHQPEAQVPA---VTVPRWQEDAQLtiDQLAFSY--EEKAALTDINLNVTGFKKIGIIG 364
Cdd:TIGR03375 424 lltRYQQA---KTALQSLDELMQLPVERPEGtrfLHRPRLQGEIEF--RNVSFAYpgQETPALDNVSLTIRPGEKVAIIG 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 365 LSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVA 444
Cdd:TIGR03375 499 RIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALGAPYADDEEILRAAELA 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 445 GLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLdQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFAT 524
Cdd:TIGR03375 579 GVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALL-RDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVT 657
|
410 420 430
....*....|....*....|....*....|....*..
gi 491368637 525 HRLHWMEEMDEIIVMDQGRIVEQGT----LAQLQQKQ 557
Cdd:TIGR03375 658 HRTSLLDLVDRIIVMDNGRIVADGPkdqvLEALRKGR 694
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
334-558 |
2.51e-61 |
|
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: 202.07 E-value: 2.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 334 IDQLAFSYEEKA-ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQ 412
Cdd:cd03254 5 FENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 413 NPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLdQQRKILLF 492
Cdd:cd03254 85 DTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAML-RDPKILIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491368637 493 DEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQG 558
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
332-563 |
8.42e-60 |
|
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: 198.22 E-value: 8.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYE--EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIY 409
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 IPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLDQQRkI 489
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP-I 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491368637 490 LLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGAFTEL 563
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
86-527 |
6.07e-58 |
|
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: 202.21 E-value: 6.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 86 AADLRDQLLEKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIMNMSIIPWVILALVFYLDWESGLVLLLVFP 165
Cdd:TIGR02868 85 LGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 166 LIIIFMIILGYAAQSKAEkqyRTFQLLSNHF----IDSLRGIDTLKLFGVSKKYGKSIFASSERFRKATMASLKVGILST 241
Cdd:TIGR02868 165 LAGFVAPLVSLRAARAAE---QALARLRGELaaqlTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 242 FALDFFTTLSIaVVAVLLGLRLINEGILLFPALTILILAP----EYFLPIRDFSSDYHATLDGKNAMTAVTEilhqPEAQ 317
Cdd:TIGR02868 242 ALTLLAAGLAV-LGALWAGGPAVADGRLAPVTLAVLVLLPlaafEAFAALPAAAQQLTRVRAAAERIVEVLD----AAGP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 318 VPAVTVPR----WQEDAQLTIDQLAFSYEEKA-ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGG 392
Cdd:TIGR02868 317 VAEGSAPAagavGLGKPTLELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 393 AKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQ 472
Cdd:TIGR02868 397 VPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGE 476
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 491368637 473 AQRIALARAFLdQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRL 527
Cdd:TIGR02868 477 RQRLALARALL-ADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
332-548 |
1.13e-56 |
|
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: 189.72 E-value: 1.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSY--EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIY 409
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 IPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLdQQRKI 489
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALL-NDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 490 LLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQG 548
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
88-565 |
2.64e-56 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 198.79 E-value: 2.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 88 DLRDQLLEKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIMNMSIIPWVILALVFYLDWESGLVLLLVFPLI 167
Cdd:TIGR02203 88 DIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 168 IIFMIILG--YAAQSKaEKQYRTFQLlsNHFID-SLRGIDTLKLFGVSKKYGKSIFASSERFRKATMASLKVGILSTFAL 244
Cdd:TIGR02203 168 SILMRRVSkrLRRISK-EIQNSMGQV--TTVAEeTLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPIT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 245 DFFTTLSIAVVaVLLGLRLINEGILLFPALTILILAP-EYFLPIRDFSSDYHATLDGKNAMTAVTEILHQP-EAQVPAVT 322
Cdd:TIGR02203 245 QLIASLALAVV-LFIALFQAQAGSLTAGDFTAFITAMiALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPpEKDTGTRA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 323 VPRWQEDaqLTIDQLAFSY--EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQ 400
Cdd:TIGR02203 324 IERARGD--VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTL 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 401 ASWQEQLIYIPQNPYIYRLTLQENVAFYQP-TATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALA 479
Cdd:TIGR02203 402 ASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIA 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 480 RAFLdQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGA 559
Cdd:TIGR02203 482 RALL-KDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGL 560
|
....*.
gi 491368637 560 FTELVN 565
Cdd:TIGR02203 561 YAQLHN 566
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
332-543 |
2.65e-56 |
|
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: 186.82 E-value: 2.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSY--EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIY 409
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 IPQNPYIYRLTLQENVafyqptatkeavlkaievagltellaelpqgldtmlgegerhLSGGQAQRIALARAFLdQQRKI 489
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALL-RDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491368637 490 LLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGR 543
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
127-563 |
1.22e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 196.97 E-value: 1.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 127 YLKLI---LAKIMnmsiipwVILALVFYLDWESG----------LVLLLVFPLIIIFmiiLGY---AAQSKAEKQYRTfq 190
Cdd:PRK11160 134 YLRLIsplVAALV-------VILVLTIGLSFFDLtlaltlggilLLLLLLLPLLFYR---LGKkpgQDLTHLRAQYRV-- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 191 llsnHFIDSLRGIDTLKLFGVSKKYGKSIFASSERFRKATMASLKVGILSTFALDFFTTLsiavvAVLLGLRLINEGI-- 268
Cdd:PRK11160 202 ----QLTEWLQGQAELTLFGAEDRYRQQLEQTEQQWLAAQRRQANLTGLSQALMILANGL-----TVVLMLWLAAGGVgg 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 269 ----------LLFPAL-TILILAP--EYFLPIRDFSSdyhatldgknAMTAVTEILHQ-PEAQVPAVTVPRWQEDAqLTI 334
Cdd:PRK11160 273 naqpgalialFVFAALaAFEALMPvaGAFQHLGQVIA----------SARRINEITEQkPEVTFPTTSTAAADQVS-LTL 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 335 DQLAFSY--EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQ 412
Cdd:PRK11160 342 NNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQ 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 413 NPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLaELPQGLDTMLGEGERHLSGGQAQRIALARAFLdQQRKILLF 492
Cdd:PRK11160 422 RVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLL-EDDKGLNAWLGEGGRQLSGGEQRRLGIARALL-HDAPLLLL 499
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491368637 493 DEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGAFTEL 563
Cdd:PRK11160 500 DEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
335-563 |
2.60e-54 |
|
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: 183.97 E-value: 2.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 335 DQLAFSYE-EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQN 413
Cdd:cd03253 4 ENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 414 PYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLDQQRkILLFD 493
Cdd:cd03253 84 TVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP-ILLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 494 EPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGAFTEL 563
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
146-564 |
2.12e-52 |
|
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: 188.37 E-value: 2.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 146 LALVFYLDWESGLVLLLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGvskkygkSIFASSER 225
Cdd:TIGR02204 150 LIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFG-------HEDAERSR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 226 FRKATMASLKVGILSTFALDFFTTLSI-----AVVAVL-LGLRLINEGillfpALTILILAPEYFLPIrdFSSDYHATLD 299
Cdd:TIGR02204 223 FGGAVEKAYEAARQRIRTRALLTAIVIvlvfgAIVGVLwVGAHDVIAG-----KMSAGTLGQFVFYAV--MVAGSIGTLS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 300 --------GKNAMTAVTEILH-QPEAQVPAV-TVPRWQEDAQLTIDQLAFSYEEKA---ALTDINLNVTGFKKIGIIGLS 366
Cdd:TIGR02204 296 evwgelqrAAGAAERLIELLQaEPDIKAPAHpKTLPVPLRGEIEFEQVNFAYPARPdqpALDGLNLTVRPGETVALVGPS 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 367 GSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGL 446
Cdd:TIGR02204 376 GAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHA 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 447 TELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLdQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHR 526
Cdd:TIGR02204 456 HEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAIL-KDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHR 534
|
410 420 430
....*....|....*....|....*....|....*...
gi 491368637 527 LHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGAFTELV 564
Cdd:TIGR02204 535 LATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLA 572
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
333-564 |
2.80e-51 |
|
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: 175.81 E-value: 2.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 333 TIDQLAFSYEEKA---ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIY 409
Cdd:cd03249 2 EFKNVSFRYPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 IPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLdQQRKI 489
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL-RNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491368637 490 LLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGAFTELV 564
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
19-310 |
3.78e-50 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 174.78 E-value: 3.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 19 LAGLSFLQALFIIGQAYGLARAITGLWEGRPLEEQWGWILLFFCSFIARQAVIYFRSKRLDDYSYQQAADLRDQLLEKLF 98
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 99 RVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIMNMSIIPWVILALVFYLDWESGLVLLLVFPLIIIFMIILGYAA 178
Cdd:cd18561 81 KLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 179 QSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKYGKSIFASSERFRKATMASLKVGILSTFALDFFTTLSIAVVAVL 258
Cdd:cd18561 161 KDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 491368637 259 LGLRLINEGILLFPALTILILAPEYFLPIRDFSSDYHAtldGKNAMTAVTEI 310
Cdd:cd18561 241 GALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHA---GYQGISAADSI 289
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
332-564 |
2.41e-47 |
|
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: 165.35 E-value: 2.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSY--EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIY 409
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 IPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLDQQRkI 489
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR-I 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491368637 490 LLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGAFTELV 564
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
331-549 |
2.76e-47 |
|
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: 164.59 E-value: 2.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 331 QLTIDQLAFSY--EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLI 408
Cdd:cd03244 2 DIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 409 YIPQNPYIYRLTLQENVAFYQpTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLdQQRK 488
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDPFG-EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL-RKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491368637 489 ILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGT 549
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
139-563 |
9.77e-47 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 172.51 E-value: 9.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 139 SIIPwvILALVFYLDWESGLVLLLVFPLIIIFMIILgyaaqskaEKQYRTfqlLSNHFIDS-----------LRGIDTLK 207
Cdd:PRK11176 152 SIIG--LFIMMFYYSWQLSLILIVIAPIVSIAIRVV--------SKRFRN---ISKNMQNTmgqvttsaeqmLKGHKEVL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 208 LFGVSKKYGKSIFASSERFRKATMASLKVGILSTFALDFFTTLSIAVVAVLLGLRLINEGIllfPALTILILAPEYFLPI 287
Cdd:PRK11176 219 IFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTL---TAGTITVVFSSMIALM 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 288 RDFSSDYHATLDGKNAMTAVT---EILH-QPEAQVPAVTVPRWQEDaqLTIDQLAFSYE--EKAALTDINLNVTGFKKIG 361
Cdd:PRK11176 296 RPLKSLTNVNAQFQRGMAACQtlfAILDlEQEKDEGKRVIERAKGD--IEFRNVTFTYPgkEVPALRNINFKIPAGKTVA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 362 IIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVAF-YQPTATKEAVLKA 440
Cdd:PRK11176 374 LVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYaRTEQYSREQIEEA 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 441 IEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLdQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLV 520
Cdd:PRK11176 454 ARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALL-RDSPILILDEATSALDTESERAIQAALDELQKNRTS 532
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 491368637 521 FFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGAFTEL 563
Cdd:PRK11176 533 LVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
131-565 |
6.84e-46 |
|
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: 172.23 E-value: 6.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 131 ILAKIMNMSIIPWVILALVfYLDWESGLVLLLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFG 210
Cdd:TIGR01193 273 ILSLFLDMWILVIVGLFLV-RQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLT 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 211 VSKKYGKSIFASSERFRKATMASLKVGILSTfALDFFTTLSIAVVAVLLGLRLINEGILLFPALTILILAPEYFLpirdf 290
Cdd:TIGR01193 352 SEAERYSKIDSEFGDYLNKSFKYQKADQGQQ-AIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFL----- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 291 ssdyhatldgknamTAVTEILH-QPEAQVPAVTVPRWQE--------------------DAQLTIDQLAFSYEEKA-ALT 348
Cdd:TIGR01193 426 --------------TPLENIINlQPKLQAARVANNRLNEvylvdsefinkkkrtelnnlNGDIVINDVSYSYGYGSnILS 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 349 DINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVAF- 427
Cdd:TIGR01193 492 DISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLg 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 428 YQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLDQQrKILLFDEPTAHLDIETEVAL 507
Cdd:TIGR01193 572 AKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDS-KVLILDESTSNLDTITEKKI 650
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 491368637 508 KERMLPLMENRLVFFAtHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGAFTELVN 565
Cdd:TIGR01193 651 VNNLLNLQDKTIIFVA-HRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
332-569 |
5.50e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.07 E-value: 5.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQAsWQEQLIYIP 411
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNPYIY-RLTLQENVAFYQ------PTATKEAVLKAIEVAGLTELLAELPqgldtmlgegeRHLSGGQAQRIALARAFLd 484
Cdd:COG1131 80 QEPALYpDLTVRENLRFFArlyglpRKEARERIDELLELFGLTDAADRKV-----------GTLSGGMKQRLGLALALL- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 485 QQRKILLFDEPTAHLDIETEVALKERMLPLM-ENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQLQQKQ--GAF 560
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKARLleDVF 227
|
....*....
gi 491368637 561 TELVNGMRR 569
Cdd:COG1131 228 LELTGEEAR 236
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
332-558 |
2.42e-44 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 157.71 E-value: 2.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQAsWQEQLIYIP 411
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNPYIY-RLTLQENVAFY------QPTATKEAVLKAIEVAGLTELLaelpqglDTMLGEgerhLSGGQAQRIALARAFLd 484
Cdd:COG4555 81 DERGLYdRLTVRENIRYFaelyglFDEELKKRIEELIELLGLEEFL-------DRRVGE----LSTGMKKKVALARALV- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491368637 485 QQRKILLFDEPTAHLDIETEVALKERMLPLM-ENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQLQQKQG 558
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
106-564 |
3.40e-44 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 165.52 E-value: 3.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 106 QQQGTGNVTTMVLEGINQVE----NYLKLILAKIMnmSIIpwVILALVFYLDWESGLVLL---LVFPLIIIFMIILGYAA 178
Cdd:PRK13657 108 SQRGSGRALHTLLRGTDALFglwlEFMREHLATLV--ALV--VLLPLALFMNWRLSLVLVvlgIVYTLITTLVMRKTKDG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 179 QSKAEKQYRTfqlLSNHFIDSLRGIDTLKLFGVSKKYGKSIFASSERFRKATMASLKVGILSTFALDFFTTLSIAVVaVL 258
Cdd:PRK13657 184 QAAVEEHYHD---LFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPVLSWWALASVLNRAASTITMLAI-LV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 259 LGLRLINEG------ILLFPAL-TILILAPEYflpIRDFSSDYHatldgknaMTAVT-EILHQPEAQVPAVTVPRWQEDA 330
Cdd:PRK13657 260 LGAALVQKGqlrvgeVVAFVGFaTLLIGRLDQ---VVAFINQVF--------MAAPKlEEFFEVEDAVPDVRDPPGAIDL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 331 Q-----LTIDQLAFSYEEKA-ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQ 404
Cdd:PRK13657 329 GrvkgaVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLR 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 405 EQLIYIPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLd 484
Cdd:PRK13657 409 RNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALL- 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 485 QQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGAFTELV 564
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALL 567
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
309-571 |
1.30e-43 |
|
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: 164.22 E-value: 1.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 309 EILHQPEAQVPAVTvprwqeDAQLTIDQLAFSYE-EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGE 387
Cdd:COG5265 341 EVADAPDAPPLVVG------GGEVRFENVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 388 ITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERH 467
Cdd:COG5265 415 ILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLK 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 468 LSGGQAQRIALARAFLDQQRkILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQ 547
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPP-ILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVER 573
|
250 260
....*....|....*....|....
gi 491368637 548 GTLAQLQQKQGAFTELVNGMRREQ 571
Cdd:COG5265 574 GTHAELLAQGGLYAQMWARQQEEE 597
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
65-563 |
1.56e-43 |
|
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: 165.30 E-value: 1.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 65 IARQAVIYFRSKRLDDYSYQQAADLRDQLLEKLFRVGPQIAQQQGTGNVTTMVLEgINQVENYLKLILAKIMNMSIIPWV 144
Cdd:TIGR01846 190 IFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVRE-LEQIRNFLTGSALTVVLDLLFVVV 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 145 ILALVFYldWESGLVLLLVFPLIIIFMIILGYAA--QSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKYGKSIFAS 222
Cdd:TIGR01846 269 FLAVMFF--YSPTLTGVVIGSLVCYALLSVFVGPilRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 223 SERFRKATMASLKVGILSTFALDFFTTLSIAVVaVLLGLRLINEGILLFPAL-TILILAPEYFLPIRDFSS---DYHATL 298
Cdd:TIGR01846 347 LAAYVAASFRVTNLGNIAGQAIELIQKLTFAIL-LWFGAHLVIGGALSPGQLvAFNMLAGRVTQPVLRLAQlwqDFQQTG 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 299 DgknAMTAVTEILHQPEAQVPAVTVPRWQEDAQLTIDQLAFSYEEKAA--LTDINLNVTGFKKIGIIGLSGSGKSTLINT 376
Cdd:TIGR01846 426 I---ALERLGDILNSPTEPRSAGLAALPELRGAITFENIRFRYAPDSPevLSNLNLDIKPGEFIGIVGPSGSGKSTLTKL 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 377 LSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQG 456
Cdd:TIGR01846 503 LQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQG 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 457 LDTMLGEGERHLSGGQAQRIALARAFLDQQRkILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEI 536
Cdd:TIGR01846 583 YNTEVGEKGANLSGGQRQRIAIARALVGNPR-ILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRI 661
|
490 500
....*....|....*....|....*..
gi 491368637 537 IVMDQGRIVEQGTLAQLQQKQGAFTEL 563
Cdd:TIGR01846 662 IVLEKGQIAESGRHEELLALQGLYARL 688
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
307-559 |
1.39e-41 |
|
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: 157.99 E-value: 1.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 307 VTEILHQPEAQVPAVTVPRWQedAQLTIDQLAFSY--EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPD 384
Cdd:COG4618 308 LNELLAAVPAEPERMPLPRPK--GRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPT 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 385 SGEITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVA-FYQPTAtkEAVLKAIEVAGLTELLAELPQGLDTMLGE 463
Cdd:COG4618 386 AGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIArFGDADP--EKVVAAAKLAGVHEMILRLPDGYDTRIGE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 464 GERHLSGGQAQRIALARAFLDQQRkILLFDEPTAHLDIETEVALKERMLPL-MENRLVFFATHRLHWMEEMDEIIVMDQG 542
Cdd:COG4618 464 GGARLSGGQRQRIGLARALYGDPR-LVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDG 542
|
250 260
....*....|....*....|.
gi 491368637 543 RIVEQGT----LAQLQQKQGA 559
Cdd:COG4618 543 RVQAFGPrdevLARLARPAAA 563
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
89-564 |
1.65e-40 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 156.42 E-value: 1.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 89 LRDQLLEKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLilakimNMSIIPW------VILALVFYLDWESGLVLLL 162
Cdd:TIGR00958 236 IREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSL------NVNVLLRnlvmllGLLGFMLWLSPRLTMVTLI 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 163 VFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKygksifaSSERFRKATMASLKVGILSTF 242
Cdd:TIGR00958 310 NLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEG-------EASRFKEALEETLQLNKRKAL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 243 ALDFFTTLS-----IAVVAVL-LGLRLINEGILLFPALTILILAPEYFLP-IRDFSSDYHATLDGKNAMTAVTEIL-HQP 314
Cdd:TIGR00958 383 AYAGYLWTTsvlgmLIQVLVLyYGGQLVLTGKVSSGNLVSFLLYQEQLGEaVRVLSYVYSGMMQAVGASEKVFEYLdRKP 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 315 EAQVPAVTVPRWQEdAQLTIDQLAFSY---EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLG 391
Cdd:TIGR00958 463 NIPLTGTLAPLNLE-GLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 392 GAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGG 471
Cdd:TIGR00958 542 GVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGG 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 472 QAQRIALARAFLDQQRkILLFDEPTAHLDIETEVALKErmLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLA 551
Cdd:TIGR00958 622 QKQRIAIARALVRKPR-VLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHK 698
|
490
....*....|...
gi 491368637 552 QLQQKQGAFTELV 564
Cdd:TIGR00958 699 QLMEDQGCYKHLV 711
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
141-549 |
2.29e-40 |
|
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: 154.04 E-value: 2.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 141 IPWVI--LALVFYLDWESGlVLLLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDS-LRGIDTLKLFGVSKKYGK 217
Cdd:TIGR01842 126 APWMPiyLLVCFLLHPWIG-ILALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLADSaLRNAEVIEAMGMMGNLTK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 218 SIFASSERFRKAT-MASLKVGILSTFALDFFTTLSIAVVAvlLGLRLINEGILLfPALTIL--ILAPEYFLPIRDFSSDY 294
Cdd:TIGR01842 205 RWGRFHSKYLSAQsAASDRAGMLSNLSKYFRIVLQSLVLG--LGAYLAIDGEIT-PGMMIAgsILVGRALAPIDGAIGGW 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 295 HATLDGKNAMTAVTEILHQPEAQVPAVTVPRWQedAQLTIDQLAFSY--EEKAALTDINLNVTGFKKIGIIGLSGSGKST 372
Cdd:TIGR01842 282 KQFSGARQAYKRLNELLANYPSRDPAMPLPEPE--GHLSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKST 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 373 LINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAE 452
Cdd:TIGR01842 360 LARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILR 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 453 LPQGLDTMLGEGERHLSGGQAQRIALARAFLDQQrKILLFDEPTAHLDIETEVALKERMLPL-MENRLVFFATHRLHWME 531
Cdd:TIGR01842 440 LPDGYDTVIGPGGATLSGGQRQRIALARALYGDP-KLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLG 518
|
410
....*....|....*...
gi 491368637 532 EMDEIIVMDQGRIVEQGT 549
Cdd:TIGR01842 519 CVDKILVLQDGRIARFGE 536
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
144-558 |
1.47e-39 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 152.56 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 144 VILALVFYLDWESGLVLLLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKYGKSIFASS 223
Cdd:PRK10790 155 AMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEAS 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 224 ERFRKATMASLKV-GILSTFALDFFTTLsiavvaVLLGLrlinegILLF---PALTILILAPEYFL--------PIRDFS 291
Cdd:PRK10790 235 RSHYMARMQTLRLdGFLLRPLLSLFSAL------ILCGL------LMLFgfsASGTIEVGVLYAFIsylgrlnePLIELT 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 292 SDYHATLDGKNAMTAVTEILHQPEAQVPAVTVPrwQEDAQLTIDQLAFSY-EEKAALTDINLNVTGFKKIGIIGLSGSGK 370
Cdd:PRK10790 303 TQQSMLQQAVVAGERVFELMDGPRQQYGNDDRP--LQSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 371 STLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVAFYQPTaTKEAVLKAIEVAGLTELL 450
Cdd:PRK10790 381 STLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDI-SEEQVWQALETVQLAELA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 451 AELPQGLDTMLGEGERHLSGGQAQRIALARAfLDQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWM 530
Cdd:PRK10790 460 RSLPDGLYTPLGEQGNNLSVGQKQLLALARV-LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTI 538
|
410 420
....*....|....*....|....*...
gi 491368637 531 EEMDEIIVMDQGRIVEQGTLAQLQQKQG 558
Cdd:PRK10790 539 VEADTILVLHRGQAVEQGTHQQLLAAQG 566
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
340-543 |
2.47e-39 |
|
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: 142.61 E-value: 2.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 340 SYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGakTTAfrqaswqeqliYIPQNPYIYRL 419
Cdd:cd03250 14 EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIA-----------YVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 420 TLQENVAFYQPTaTKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLdQQRKILLFDEPTAHL 499
Cdd:cd03250 81 TIRENILFGKPF-DEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVY-SDADIYLLDDPLSAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491368637 500 DIETEVALKERML--PLMENRLVFFATHRLHWMEEMDEIIVMDQGR 543
Cdd:cd03250 159 DAHVGRHIFENCIlgLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
332-553 |
1.87e-38 |
|
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: 140.93 E-value: 1.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSY-EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYI 410
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 411 PQNP--YIYRLTLQENVAF------YQPTATKEAVLKAIEVAGLTELLAELPQgldtmlgegerHLSGGQAQRIALARAf 482
Cdd:COG1122 81 FQNPddQLFAPTVEEDVAFgpenlgLPREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAGV- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491368637 483 LDQQRKILLFDEPTAHLDIETEVALKERMLPL-MENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQL 553
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREV 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
332-548 |
2.92e-38 |
|
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: 138.99 E-value: 2.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKA--ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFrQASWQEQLIY 409
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 IPQNPYIYRLTLQENVafyqptatkeavlkaievagltellaelpqgldtmlgeGERhLSGGQAQRIALARAFLdQQRKI 489
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRR-FSGGERQRLALARILL-QDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 490 LLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQG 548
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
82-573 |
2.78e-37 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 145.63 E-value: 2.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 82 SYQQAADLRDQLLEKLFRVGPQIAQQQGTGNVTTMVLEGINQV-----ENYLKLILAKIMNMSiipwVILALVFYLDWEs 156
Cdd:PRK10789 64 SYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVvfaagEGVLTLVDSLVMGCA----VLIVMSTQISWQ- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 157 gLVLLLVFPLIIIFMIILGYAAQ--SKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKYGKSIFASSERFRKATMASL 234
Cdd:PRK10789 139 -LTLLALLPMPVMAIMIKRYGDQlhERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 235 KVGILstfaldFFTTLSIAV-VAVLL----GLRLINEGILLFPALTILILapeyFL-----PIRDFSSDYHATLDGKNAM 304
Cdd:PRK10789 218 RIDAR------FDPTIYIAIgMANLLaiggGSWMVVNGSLTLGQLTSFVM----YLglmiwPMLALAWMFNIVERGSAAY 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 305 TAVTEILHQPeaqvPAV---TVPRWQEDAQLTIDQLAFSY--EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSG 379
Cdd:PRK10789 288 SRIRAMLAEA----PVVkdgSEPVPEGRGELDVNIRQFTYpqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQR 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 380 FLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQGLDT 459
Cdd:PRK10789 364 HFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDT 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 460 MLGEGERHLSGGQAQRIALARAFLdQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVM 539
Cdd:PRK10789 444 EVGERGVMLSGGQKQRISIARALL-LNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVM 522
|
490 500 510
....*....|....*....|....*....|....
gi 491368637 540 DQGRIVEQGTLAQLQQKQGAFTELvngMRREQLE 573
Cdd:PRK10789 523 QHGHIAQRGNHDQLAQQSGWYRDM---YRYQQLE 553
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
307-553 |
4.32e-37 |
|
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: 144.28 E-value: 4.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 307 VTEILHQPE--AQVPAVTVPRWQEDAQ-------LTIDQLAFSY-----EEKAALTDINLNVTGFKKIGIIGLSGSGKST 372
Cdd:COG1123 227 PEEILAAPQalAAVPRLGAARGRAAPAaaaaeplLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKST 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 373 LINTLSGFLVPDSGEITLGGAKTTAFRQASWQE---QLIYIPQNPY---IYRLTLQENVAF---YQPTATKEAVLKAIEv 443
Cdd:COG1123 307 LARLLLGLLRPTSGSILFDGKDLTKLSRRSLRElrrRVQMVFQDPYsslNPRMTVGDIIAEplrLHGLLSRAERRERVA- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 444 agltELLAELpqGLDTMLgeGERH---LSGGQAQRIALARAfLDQQRKILLFDEPTAHLDieteVALKERMLPLME---- 516
Cdd:COG1123 386 ----ELLERV--GLPPDL--ADRYpheLSGGQRQRVAIARA-LALEPKLLILDEPTSALD----VSVQAQILNLLRdlqr 452
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 491368637 517 --NRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQL 553
Cdd:COG1123 453 elGLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEV 492
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
349-564 |
7.76e-37 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 144.65 E-value: 7.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 349 DINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVAFY 428
Cdd:TIGR01192 353 DVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 429 QPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLdQQRKILLFDEPTAHLDIETEVALK 508
Cdd:TIGR01192 433 REGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAIL-KNAPILVLDEATSALDVETEARVK 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491368637 509 ERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGAFTELV 564
Cdd:TIGR01192 512 NAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
332-549 |
2.17e-36 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 136.33 E-value: 2.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIP 411
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNPYI-YRLTLQENVA---------FYQPTAT-KEAVLKAIEVAGLTElLAElpQGLDTmlgegerhLSGGQAQRIALAR 480
Cdd:COG1120 82 QEPPApFGLTVRELVAlgryphlglFGRPSAEdREAVEEALERTGLEH-LAD--RPVDE--------LSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491368637 481 AfLDQQRKILLFDEPTAHLDIETEVALKERM--LPLMENRLVFFATHRL-HWMEEMDEIIVMDQGRIVEQGT 549
Cdd:COG1120 151 A-LAQEPPLLLLDEPTSHLDLAHQLEVLELLrrLARERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
334-543 |
2.61e-36 |
|
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: 134.52 E-value: 2.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 334 IDQLAFSYE--EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIP 411
Cdd:cd03225 2 LKNLSFSYPdgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNP--YIYRLTLQENVAF------YQPTATKEAVLKAIEVAGLTELLAELPQgldtmlgegerHLSGGQAQRIALARAfL 483
Cdd:cd03225 82 QNPddQFFGPTVEEEVAFglenlgLPEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV-L 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491368637 484 DQQRKILLFDEPTAHLDIETEVALKERMLPLMENRL-VFFATHRLHWMEE-MDEIIVMDQGR 543
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
332-544 |
2.61e-35 |
|
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: 130.60 E-value: 2.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAfRQASWQEQLIYIP 411
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNPYIY-RLTLQENVafyqptatkeavlkaievagltellaelpqgldtmlgegerHLSGGQAQRIALARAFLDQQrKIL 490
Cdd:cd03230 80 EEPSLYeNLTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDP-ELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491368637 491 LFDEPTAHLDIETEVALKERMLPLM-ENRLVFFATHRLHWMEEM-DEIIVMDQGRI 544
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
333-548 |
3.55e-35 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 130.25 E-value: 3.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 333 TIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQ 412
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 413 npyiyrltlqenvafyqptatkeavlkAIEVAGLTELlaeLPQGLDTmlgegerhLSGGQAQRIALARAFLdQQRKILLF 492
Cdd:cd03214 81 ---------------------------ALELLGLAHL---ADRPFNE--------LSGGERQRVLLARALA-QEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 493 DEPTAHLDIETEVALKE--RMLPLMENRLVFFATHRL-HWMEEMDEIIVMDQGRIVEQG 548
Cdd:cd03214 122 DEPTSHLDIAHQIELLEllRRLARERGKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
332-548 |
1.79e-34 |
|
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: 129.56 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTafRQASWQEQLIYIP 411
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNPYIY-RLTLQENVAF-----YQPTATKEA-VLKAIEVAGLTELLAELPqgldtmlgegeRHLSGGQAQRIALARAfLD 484
Cdd:cd03259 79 QDYALFpHLTVAENIAFglklrGVPKAEIRArVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARA-LA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491368637 485 QQRKILLFDEPTAHLDIEtevaLKERMLPLMENRL------VFFATHRLHwmEEM---DEIIVMDQGRIVEQG 548
Cdd:cd03259 147 REPSLLLLDEPLSALDAK----LREELREELKELQrelgitTIYVTHDQE--EALalaDRIAVMNEGRIVQVG 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
332-544 |
6.25e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 129.05 E-value: 6.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRqaswqeQLI-YI 410
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR------RRIgYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 411 PQNPYIYR---LTLQENVA---------FYQPTAT-KEAVLKAIEVAGLTELlaelpqgLDTMLGEgerhLSGGQAQRIA 477
Cdd:COG1121 81 PQRAEVDWdfpITVRDVVLmgrygrrglFRRPSRAdREAVDEALERVGLEDL-------ADRPIGE----LSGGQQQRVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 478 LARAfLDQQRKILLFDEPTAHLDIETEVALKERMLPL-MENRLVFFATHRLHWMEEM-DEIIVMDQGRI 544
Cdd:COG1121 150 LARA-LAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREYfDRVLLLNRGLV 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
332-544 |
1.63e-33 |
|
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: 127.22 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSY----EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGG--------AKTTAFR 399
Cdd:cd03255 1 IELKNLSKTYggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdisklseKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 400 qaswQEQLIYIPQNPY-IYRLTLQENVA---FYQPTATKEAVLKAIEV---AGLTELLAELPQgldtmlgegerHLSGGQ 472
Cdd:cd03255 81 ----RRHIGFVFQSFNlLPDLTALENVElplLLAGVPKKERRERAEELlerVGLGDRLNHYPS-----------ELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491368637 473 AQRIALARAfLDQQRKILLFDEPTAHLDIETevalKERMLPLM------ENRLVFFATHRLHWMEEMDEIIVMDQGRI 544
Cdd:cd03255 146 QQRVAIARA-LANDPKIILADEPTGNLDSET----GKEVMELLrelnkeAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
332-544 |
1.82e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.85 E-value: 1.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIP 411
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNPYIYRLTLQENVAFY----QPTATKEAVLKAIEVAGLTELLAELPqgldtmlgegERHLSGGQAQRIALARAFLdQQR 487
Cdd:COG4619 81 QEPALWGGTVRDNLPFPfqlrERKFDRERALELLERLGLPPDILDKP----------VERLSGGERQRLALIRALL-LQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491368637 488 KILLFDEPTAHLDIETEVALkERML---PLMENRLVFFATHRLHWMEEM-DEIIVMDQGRI 544
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRV-EELLreyLAEEGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
332-555 |
6.90e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 125.64 E-value: 6.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAAltDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQAS------WQE 405
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAErpvsmlFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 406 QliyipqN--PYiyrLTLQENVAF-----YQPTAT-KEAVLKAIEVAGLTELLAELPqgldtmlgegeRHLSGGQAQRIA 477
Cdd:COG3840 80 N------NlfPH---LTVAQNIGLglrpgLKLTAEqRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 478 LARAFLdQQRKILLFDEPTAHLDIetevALKERMLPLME------NRLVFFATHRLhwmEEM----DEIIVMDQGRIVEQ 547
Cdd:COG3840 140 LARCLV-RKRPILLLDEPFSALDP----ALRQEMLDLVDelcrerGLTVLMVTHDP---EDAariaDRVLLVADGRIAAD 211
|
....*...
gi 491368637 548 GTLAQLQQ 555
Cdd:COG3840 212 GPTAALLD 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
333-543 |
9.32e-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: 123.12 E-value: 9.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 333 TIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQ 412
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 413 npyiyrltlqenvafyqptatkeavlkaievagltellaelpqgldtmlgegerhLSGGQAQRIALARAFLdQQRKILLF 492
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALL-LNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491368637 493 DEPTAHLDIETEVALKERMLPLM-ENRLVFFATHRLHWMEE-MDEIIVMDQGR 543
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
337-544 |
1.60e-32 |
|
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: 124.51 E-value: 1.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 337 LAFSYEEKAA---LTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQN 413
Cdd:cd03248 17 VTFAYPTRPDtlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 414 PYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLDQQRkILLFD 493
Cdd:cd03248 97 PVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQ-VLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491368637 494 EPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRI 544
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
347-497 |
2.92e-32 |
|
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: 121.22 E-value: 2.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 347 LTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQNPYI-YRLTLQENV 425
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLfPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491368637 426 AFYqptATKEAVLKAIEVAGLTELLAELPQG--LDTMLGEGERHLSGGQAQRIALARAFLdQQRKILLFDEPTA 497
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLGLGdlADRPVGERPGTLSGGQRQRVAIARALL-TKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
330-536 |
4.22e-32 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 122.59 E-value: 4.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 330 AQLTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRqASWQEQLIY 409
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 IPQNPYIYR-LTLQENVAFYQ----PTATKEAVLKAIEVAGLTELLAELPqgldtmlgegeRHLSGGQAQRIALARAFLd 484
Cdd:COG4133 80 LGHADGLKPeLTVRENLRFWAalygLRADREAIDEALEAVGLAGLADLPV-----------RQLSAGQKRRVALARLLL- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491368637 485 QQRKILLFDEPTAHLDIETEVALKERML-PLMENRLVFFATHRLHWMEEMDEI 536
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAaHLARGGAVLLTTHQPLELAAARVL 200
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
330-549 |
5.71e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 126.37 E-value: 5.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 330 AQLTIDQLAFSYEEKAALTDINLNVtgfKK---IGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTafRQASWQEQ 406
Cdd:COG3842 4 PALELENVSKRYGDVTALDDVSLSI---EPgefVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT--GLPPEKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 407 LIYIPQN----PYiyrLTLQENVAF------YQPTATKEAVLKAIEVAGLTELLAELPqgldtmlgegeRHLSGGQAQRI 476
Cdd:COG3842 79 VGMVFQDyalfPH---LTVAENVAFglrmrgVPKAEIRARVAELLELVGLEGLADRYP-----------HQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 477 ALARAfLDQQRKILLFDEPTAHLDieteVALKERM------LpLMENRLVF-FATHRlhwMEE---M-DEIIVMDQGRIV 545
Cdd:COG3842 145 ALARA-LAPEPRVLLLDEPLSALD----AKLREEMreelrrL-QRELGITFiYVTHD---QEEalaLaDRIAVMNDGRIE 215
|
....
gi 491368637 546 EQGT 549
Cdd:COG3842 216 QVGT 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
332-547 |
8.85e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 122.46 E-value: 8.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSY----EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASW---- 403
Cdd:COG1136 5 LELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 404 QEQLIYIPQNPY-IYRLTLQENVAF---YQPTATKEAVLKAIEVA---GLTELLAELPqgldtmlgegeRHLSGGQAQRI 476
Cdd:COG1136 85 RRHIGFVFQFFNlLPELTALENVALpllLAGVSRKERRERARELLervGLGDRLDHRP-----------SQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491368637 477 ALARAFLdQQRKILLFDEPTAHLDIET--EV--ALKErmLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQ 547
Cdd:COG1136 154 AIARALV-NRPKLILADEPTGNLDSKTgeEVleLLRE--LNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
332-548 |
1.12e-31 |
|
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: 122.23 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKA----ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGG---AKTTAFRQASWQ 404
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 405 EQLIYIPQNPYIY---RLTLQENVA----FYQPTATKEAVLKAIEvagltELLAELPQgLDTMLGEGERHLSGGQAQRIA 477
Cdd:cd03257 82 KEIQMVFQDPMSSlnpRMTIGEQIAeplrIHGKLSKKEARKEAVL-----LLLVGVGL-PEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491368637 478 LARAFLdQQRKILLFDEPTAHLDieteVALKERMLPLM-----ENRL-VFFATHRLHWMEEM-DEIIVMDQGRIVEQG 548
Cdd:cd03257 156 IARALA-LNPKLLIADEPTSALD----VSVQAQILDLLkklqeELGLtLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
334-549 |
1.33e-31 |
|
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: 123.31 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 334 IDQLAFSY--EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTtafrqaSWQEQLIYIP 411
Cdd:TIGR04520 3 VENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT------LDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 -------QNP--YIYRLTLQENVAF------YQPTATKEAVLKAIEVAGLTELLAELPQgldtmlgegerHLSGGQAQRI 476
Cdd:TIGR04520 77 kkvgmvfQNPdnQFVGATVEDDVAFglenlgVPREEMRKRVDEALKLVGMEDFRDREPH-----------LLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 477 ALARAfLDQQRKILLFDEPTAHLD-------IETEVALKERmlplmENRLVFFATHRlhwMEEM---DEIIVMDQGRIVE 546
Cdd:TIGR04520 146 AIAGV-LAMRPDIIILDEATSMLDpkgrkevLETIRKLNKE-----EGITVISITHD---MEEAvlaDRVIVMNKGKIVA 216
|
...
gi 491368637 547 QGT 549
Cdd:TIGR04520 217 EGT 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
332-553 |
3.27e-31 |
|
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: 121.45 E-value: 3.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSY----EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQL 407
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 408 IYIPQNPYIY---RLTLqenvafyqptatKEAVLKAIEVAGLTELLAELPQGLDTM-LGEGERH-----LSGGQAQRIAL 478
Cdd:COG1124 82 QMVFQDPYASlhpRHTV------------DRILAEPLRIHGLPDREERIAELLEQVgLPPSFLDryphqLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 479 ARAFLdQQRKILLFDEPTAHLD--IETEV-----ALKERmlplmENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTL 550
Cdd:COG1124 150 ARALI-LEPELLLLDEPTSALDvsVQAEIlnllkDLREE-----RGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTV 223
|
...
gi 491368637 551 AQL 553
Cdd:COG1124 224 ADL 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
327-546 |
4.24e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 121.74 E-value: 4.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 327 QEDAQLTIDQLAFSYEEKA----ALTDINLNVT-G-FkkIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQ 400
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGggvtALDDVSLTVAaGeF--VALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 401 aswqeQLIYIPQNPyiyRL----TLQENVAF------YQPTATKEAVLKAIEVAGLTELLAELPqgldtmlgegeRHLSG 470
Cdd:COG1116 81 -----DRGVVFQEP---ALlpwlTVLDNVALglelrgVPKAERRERARELLELVGLAGFEDAYP-----------HQLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 471 GQAQRIALARAFLdQQRKILLFDEPTAHLDIETEVALKERMLPL-MENRL-VFFATHRLhwmEE---M-DEIIVMDQ--G 542
Cdd:COG1116 142 GMRQRVAIARALA-NDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKtVLFVTHDV---DEavfLaDRVVVLSArpG 217
|
....
gi 491368637 543 RIVE 546
Cdd:COG1116 218 RIVE 221
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
14-310 |
8.19e-31 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs). The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350054 [Multi-domain] Cd Length: 290 Bit Score: 121.49 E-value: 8.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 14 QLLGLLAGlsflqalfiIGQAYGLARAITGLWEGRPLEEQ-WGWILLFFCSFIARQAVIYFRSKrlddYSYQQAAD---- 88
Cdd:cd18781 5 QWISLLAN---------IAFVFSIANLLQKLLEGKLTTASlLIVLGILAIAIIVRFICTRLASR----ASYRASADvkkt 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 89 LRDQLLEKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIMNMSIIPWVILALVFYLDWESGLVLLLVFPLII 168
Cdd:cd18781 72 LREKIYDKLLRLGPSYQEKVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 169 IFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKYGKSIFASSERFRKATMASLKVGILSTFALDFFT 248
Cdd:cd18781 152 ISIIAVQKIAKKLLSKYWGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491368637 249 TLSIAVVAVLLGLRLINEGILLFPALTILILAPEYFLPIRDFSSDYHATLDGknaMTAVTEI 310
Cdd:cd18781 232 YGGAALGIILALLQFANGSISLAGALFIILLSAEFFLPLRLLGSFFHIAMNG---MAASDKI 290
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
330-549 |
1.02e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 122.87 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 330 AQLTIDQLAFSYEEKAALTDINLNVT--GFkkIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTT----AFRQASw 403
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEdgEF--LVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTdlppKDRNIA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 404 qeqliYIPQNPYIY-RLTLQENVAFY-----QPTAT-KEAVLKAIEVAGLTELLAELPqgldtmlgegeRHLSGGQAQRI 476
Cdd:COG3839 79 -----MVFQSYALYpHMTVYENIAFPlklrkVPKAEiDRRVREAAELLGLEDLLDRKP-----------KQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 477 ALARAfLDQQRKILLFDEPTAHLDieteVALKERM---LPLMENRL---VFFATHRLHwmEEM---DEIIVMDQGRIVEQ 547
Cdd:COG3839 143 ALGRA-LVREPKVFLLDEPLSNLD----AKLRVEMraeIKRLHRRLgttTIYVTHDQV--EAMtlaDRIAVMNDGRIQQV 215
|
..
gi 491368637 548 GT 549
Cdd:COG3839 216 GT 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
332-547 |
2.38e-30 |
|
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: 118.34 E-value: 2.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKA----ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRqaswqEQL 407
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 408 IYIPQNPYIYR-LTLQENVAF------YQPTATKEAVLKAIEVAGLTELLAELPqgldtmlgegeRHLSGGQAQRIALAR 480
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALglelqgVPKAEARERAEELLELVGLSGFENAYP-----------HQLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491368637 481 AFLdQQRKILLFDEPTAHLDIETEVALKERMLPLME--NRLVFFATHRLhwmEEM----DEIIVMDQ--GRIVEQ 547
Cdd:cd03293 145 ALA-VDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDI---DEAvflaDRVVVLSArpGRIVAE 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
332-553 |
4.86e-30 |
|
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: 123.86 E-value: 4.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSY--EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGfLVPD----SGEITLGGAKTTAFRQASWQE 405
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHggriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 406 QLIYIPQNPY--IYRLTLQENVAF------YQPTATKEAVLKAIEVAGLTELLAELPQgldtmlgegerHLSGGQAQRIA 477
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEalenlgLSRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 478 LARAfLDQQRKILLFDEPTAHLDIETEVALKERMLPLMENR--LVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQL 553
Cdd:COG1123 153 IAMA-LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
334-557 |
7.55e-30 |
|
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: 117.22 E-value: 7.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 334 IDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQE---QLIYI 410
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 411 PQNPYIY-RLTLQENVAF--YQPTATKEAVLKAIEVAGLTelLAELPQGLDTMLGEgerhLSGGQAQRIALARAF-LDQQ 486
Cdd:cd03261 83 FQSGALFdSLTVFENVAFplREHTRLSEEEIREIVLEKLE--AVGLRGAEDLYPAE----LSGGMKKRVALARALaLDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 487 rkILLFDEPTAHLD-IETEV------ALKERMlplmeNRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQLQQKQ 557
Cdd:cd03261 157 --LLLYDEPTAGLDpIASGViddlirSLKKEL-----GLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRASD 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
139-560 |
7.91e-30 |
|
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: 125.44 E-value: 7.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 139 SIIPWVILALV--FYLDWESGLVLLLVFPLIIIFMIILG---------YAAQSKAEKQYRTFQL--LSNHFIDSLRGIDT 205
Cdd:TIGR00957 1077 SMIPPVIKMFMgsLFNVIGALIVILLATPIAAVIIPPLGllyffvqrfYVASSRQLKRLESVSRspVYSHFNETLLGVSV 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 206 LKLFGVSKKYGKSIFASSERFRKATMASLkvgilstfaldffttlsIAVVAVLLGLRLINEGILLFPALTILI------- 278
Cdd:TIGR00957 1157 IRAFEEQERFIHQSDLKVDENQKAYYPSI-----------------VANRWLAVRLECVGNCIVLFAALFAVIsrhslsa 1219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 279 ----LAPEYFLPIRDF-------SSDYHATLDGKNAMTAVTEILHQPEAQVPAVTVPR-WQEDAQLTIDQLAFSYEE--K 344
Cdd:TIGR00957 1220 glvgLSVSYSLQVTFYlnwlvrmSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSgWPPRGRVEFRNYCLRYREdlD 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 345 AALTDINLNVTGFKKIGIIGLSGSGKSTLinTLSGFLVPDS--GEITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQ 422
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSL--TLGLFRINESaeGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLR 1377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 423 ENV-AFYQptATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLdQQRKILLFDEPTAHLDI 501
Cdd:TIGR00957 1378 MNLdPFSQ--YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALL-RKTKILVLDEATAAVDL 1454
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 502 ETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGAF 560
Cdd:TIGR00957 1455 ETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
334-548 |
1.30e-29 |
|
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: 116.09 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 334 IDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRqaswqEQLIYIPQN 413
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 414 PYI---YRLTLQENVA----------FYQPTATKEAVLKAIEVAGLTELlaelpqgLDTMLGEgerhLSGGQAQRIALAR 480
Cdd:cd03235 77 RSIdrdFPISVRDVVLmglyghkglfRRLSKADKAKVDEALERVGLSEL-------ADRQIGE----LSGGQQQRVLLAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 481 AfLDQQRKILLFDEPTAHLDIETEVALKERMLPL-MENRLVFFATHRLHW-MEEMDEIIVMDqGRIVEQG 548
Cdd:cd03235 146 A-LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLvLEYFDRVLLLN-RTVVASG 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
332-544 |
3.23e-29 |
|
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: 113.47 E-value: 3.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAA--LTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIY 409
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 IPQNPYIYRLTLQENVafyqptatkeavlkaievagltellaelpqgldtmlgegerhLSGGQAQRIALARAFLdQQRKI 489
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALY-GNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491368637 490 LLFDEPTAHLDIETEVALKE--RMLPLMENRLVFFAtHRLHWMEEMDEIIVMDQGRI 544
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQaiAALKAAGATRIVIA-HRPETLASADRILVLEDGRV 173
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
332-553 |
3.47e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 118.33 E-value: 3.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGakTTAFRQASWQEQLI-YI 410
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG--RDLFTNLPPRERRVgFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 411 PQNPYIYR-LTLQENVAF---YQPTATKEAVLKAievaglTELLAELpqGLDtmlGEGER---HLSGGQAQRIALARAfL 483
Cdd:COG1118 81 FQHYALFPhMTVAENIAFglrVRPPSKAEIRARV------EELLELV--QLE---GLADRypsQLSGGQRQRVALARA-L 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 484 DQQRKILLFDEPTAHLDIETEVALkERMLplmenRLVF--------FATH-RLHWMEEMDEIIVMDQGRIVEQGTLAQL 553
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKEL-RRWL-----RRLHdelggttvFVTHdQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
332-548 |
3.55e-29 |
|
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: 114.60 E-value: 3.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVT-GFkkIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQAsWQEQLIYI 410
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGpGM--YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 411 PQNPYIY-RLTLQENVAFY------QPTATKEAVLKAIEVAGLTELLAELPQGLdtmlgegerhlSGGQAQRIALARAFL 483
Cdd:cd03264 78 PQEFGVYpNFTVREFLDYIawlkgiPSKEVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491368637 484 DQQrKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQG 548
Cdd:cd03264 147 GDP-SILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
326-549 |
4.59e-29 |
|
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: 114.43 E-value: 4.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 326 WQEDAQLTIDQLAFSY--EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASW 403
Cdd:cd03369 1 WPEHGEIEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 404 QEQLIYIPQNPYIYRLTLQENVAFYQpTATKEAVLKAIEVAgltellaelpqgldtmlgEGERHLSGGQAQRIALARAFL 483
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFD-EYSDEEIYGALRVS------------------EGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491368637 484 dQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGT 549
Cdd:cd03369 142 -KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
347-550 |
6.16e-29 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 114.74 E-value: 6.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 347 LTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQAswQEQLIYIPQNPYIY-RLTLQENV 425
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 426 AFYQPTATKEAVLKAIEVAGLTELLaelpqGLDTMLGEGERHLSGGQAQRIALARAfLDQQRKILLFDEPTAHLDIETEV 505
Cdd:cd03299 93 AYGLKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARA-LVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491368637 506 ALKErMLPLMENRLVFFATHRLHWMEEM----DEIIVMDQGRIVEQGTL 550
Cdd:cd03299 167 KLRE-ELKKIRKEFGVTVLHVTHDFEEAwalaDKVAIMLNGKLIQVGKP 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
332-553 |
6.97e-29 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 114.71 E-value: 6.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGakttafrqaswqEQLIYIP 411
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDG------------EDLTDSK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNPYIYR---------------LTLQENVAfYQPT-----ATKEAVLKAIE----VaGLTELLAELPqgldtmlgegeRH 467
Cdd:COG1126 70 KDINKLRrkvgmvfqqfnlfphLTVLENVT-LAPIkvkkmSKAEAEERAMEllerV-GLADKADAYP-----------AQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 468 LSGGQAQRIALARAfLDQQRKILLFDEPTAHLDIET--EV-----ALKER---MLplmenrLVffaTHrlhwmeEM---- 533
Cdd:COG1126 137 LSGGQQQRVAIARA-LAMEPKVMLFDEPTSALDPELvgEVldvmrDLAKEgmtMV------VV---TH------EMgfar 200
|
250 260
....*....|....*....|...
gi 491368637 534 ---DEIIVMDQGRIVEQGTLAQL 553
Cdd:COG1126 201 evaDRVVFMDGGRIVEEGPPEEF 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
334-549 |
3.97e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 113.54 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 334 IDQLAFSYEE-KAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYI-- 410
Cdd:PRK13644 4 LENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIvf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 411 --PQNPYIYRlTLQENVAFyqptATKEAVLKAIEVAGLTEL-LAELpqGLDTMLGEGERHLSGGQAQRIALArAFLDQQR 487
Cdd:PRK13644 84 qnPETQFVGR-TVEEDLAF----GPENLCLPPIEIRKRVDRaLAEI--GLEKYRHRSPKTLSGGQGQCVALA-GILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491368637 488 KILLFDEPTAHLDIETEVALKERMLPLMEN-RLVFFATHRLHWMEEMDEIIVMDQGRIVEQGT 549
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
361-553 |
7.62e-28 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 114.81 E-value: 7.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 361 GIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKttafrqasWQ--EQLIYIP----------QNPyiyRL----TLQEN 424
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV--------LQdsARGIFLPphrrrigyvfQEA---RLfphlSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 425 VAF-YQPTATKEAvlkAIEVAGLTELLaelpqGLDTMLGEGERHLSGGQAQRIALARAFLDQQRkILLFDEPTAHLDiet 503
Cdd:COG4148 98 LLYgRKRAPRAER---RISFDEVVELL-----GIGHLLDRRPATLSGGERQRVAIGRALLSSPR-LLLMDEPLAALD--- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491368637 504 eVALKERMLPLMEnRL-------VFFATHRlhwMEEM----DEIIVMDQGRIVEQGTLAQL 553
Cdd:COG4148 166 -LARKAEILPYLE-RLrdeldipILYVSHS---LDEVarlaDHVVLLEQGRVVASGPLAEV 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
332-543 |
8.19e-28 |
|
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: 109.97 E-value: 8.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASW-QEQLI-Y 409
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPpLRRRIgM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 IPQNPYIY-RLTLQENVAFyqptatkeavlkaievagltellaelpqgldtmlgegerHLSGGQAQRIALARAfLDQQRK 488
Cdd:cd03229 81 VFQDFALFpHLTVLENIAL---------------------------------------GLSGGQQQRVALARA-LAMDPD 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491368637 489 ILLFDEPTAHLDieteVALKERMLPLME------NRLVFFATHRLHWMEEM-DEIIVMDQGR 543
Cdd:cd03229 121 VLLLDEPTSALD----PITRREVRALLKslqaqlGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
337-553 |
8.95e-28 |
|
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: 111.12 E-value: 8.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 337 LAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFL-----VPDSGEITLGGAKTTAfrqasWQEQLIYIP 411
Cdd:cd03260 6 LNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYD-----LDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 -------QNPYIYRLTLQENVAF------YQPT-ATKEAVLKAIEVAGLTELLAELPQGLdtmlgegerHLSGGQAQRIA 477
Cdd:cd03260 81 rrvgmvfQKPNPFPGSIYDNVAYglrlhgIKLKeELDERVEEALRKAALWDEVKDRLHAL---------GLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491368637 478 LARAfLDQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQL 553
Cdd:cd03260 152 LARA-LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
331-564 |
9.15e-28 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 112.31 E-value: 9.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 331 QLTIDQLAFSYEE--KAALTDINLNVTGFKKIGIIGLSGSGKSTLinTLSGFLVPD--SGEITLGGAKTTAFRQASWQEQ 406
Cdd:cd03288 19 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 407 LIYIPQNPYIYRLTLQENVAfYQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLdQQ 486
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFV-RK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 487 RKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQL-QQKQGAFTELV 564
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLlAQEDGVFASLV 253
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
346-553 |
1.53e-27 |
|
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: 110.75 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQE---QLIYIPQNpyiYRL--- 419
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKarrRIGMIFQH---FNLlss 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 420 -TLQENVAFyqptatkeavlkAIEVAGLTEllAELPQGLDTML---GEGERH------LSGGQAQRIALARAfLDQQRKI 489
Cdd:cd03258 97 rTVFENVAL------------PLEIAGVPK--AEIEERVLELLelvGLEDKAdaypaqLSGGQKQRVGIARA-LANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 490 LLFDEPTAHLDIETEVALKERMLPLmeNR----LVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQL 553
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDI--NRelglTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
332-556 |
1.94e-27 |
|
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: 110.74 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEE-KAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGG-----AKTTAFRQasWQE 405
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinkLKGKALRQ--LRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 406 QLIYIPQN-PYIYRLTLQENV--------AFYQPTA---TKEAVLKAIevagltELLAELpqGLDTMLGEGERHLSGGQA 473
Cdd:cd03256 79 QIGMIFQQfNLIERLSVLENVlsgrlgrrSTWRSLFglfPKEEKQRAL------AALERV--GLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 474 QRIALARAfLDQQRKILLFDEPTAHLDieteVALKERMLPLM------ENRLVFFATHRLHW-MEEMDEIIVMDQGRIVE 546
Cdd:cd03256 151 QRVAIARA-LMQQPKLILADEPVASLD----PASSRQVMDLLkrinreEGITVIVSLHQVDLaREYADRIVGLKDGRIVF 225
|
250
....*....|
gi 491368637 547 QGTLAQLQQK 556
Cdd:cd03256 226 DGPPAELTDE 235
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
88-572 |
2.00e-27 |
|
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: 118.09 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 88 DLRDQLLEKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIMNMSIIpwvILALVFYLDWESGLVLLLVFPLI 167
Cdd:TIGR01271 959 RLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLI---VLGAIFVVSVLQPYIFIAAIPVA 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 168 IIFMIILGY-------AAQSKAEKQYRTFqllsNHFIDSLRGIDTLKLFGvSKKYGKSIFASSERFRKA-------TMAS 233
Cdd:TIGR01271 1036 VIFIMLRAYflrtsqqLKQLESEARSPIF----SHLITSLKGLWTIRAFG-RQSYFETLFHKALNLHTAnwflylsTLRW 1110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 234 LKVGILSTFALDFFTTLSIAV---------VAVLLGLRLINEGILLFPALTI-----LILAPEYFLPIRDFSSDYHATLD 299
Cdd:TIGR01271 1111 FQMRIDIIFVFFFIAVTFIAIgtnqdgegeVGIILTLAMNILSTLQWAVNSSidvdgLMRSVSRVFKFIDLPQEEPRPSG 1190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 300 GKNAMTAVTE-ILHQPEAQvpavtvPRWQEDAQLTIDQLAFSYEE--KAALTDINLNVTGFKKIGIIGLSGSGKSTLINT 376
Cdd:TIGR01271 1191 GGGKYQLSTVlVIENPHAQ------KCWPSGGQMDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSA 1264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 377 LSGFLVPDsGEITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVAFYQPTATKEaVLKAIEVAGLTELLAELPQG 456
Cdd:TIGR01271 1265 LLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEE-IWKVAEEVGLKSVIEQFPDK 1342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 457 LDTMLGEGERHLSGGQAQRIALARAFLDQQrKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEI 536
Cdd:TIGR01271 1343 LDFVLVDGGYVLSNGHKQLMCLARSILSKA-KILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQF 1421
|
490 500 510
....*....|....*....|....*....|....*.
gi 491368637 537 IVMDQGRIVEQGTLAQLQQKQGAFTELVNGMRREQL 572
Cdd:TIGR01271 1422 LVIEGSSVKQYDSIQKLLNETSLFKQAMSAADRLKL 1457
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
332-548 |
2.32e-27 |
|
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: 109.50 E-value: 2.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAalTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIP 411
Cdd:cd03298 1 VRLDKIRFSYGEQP--MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNPYIYrLTLQENVAFYQPTATK------EAVLKAIEVAGLTELLAELPqgldtmlgegeRHLSGGQAQRIALARAFLdQ 485
Cdd:cd03298 79 NNLFAH-LTVEQNVGLGLSPGLKltaedrQAIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLV-R 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 486 QRKILLFDEPTAHLDieteVALKERMLPLM-----ENRL-VFFATHRLHWMEEMDE-IIVMDQGRIVEQG 548
Cdd:cd03298 146 DKPVLLLDEPFAALD----PALRAEMLDLVldlhaETKMtVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
332-546 |
1.65e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 107.45 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEE-KAALTDINLNVtgfKKiG----IIGLSGSGKSTLINTLSGFLVPDSGEITLGG---AKTTAFRQASW 403
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEI---EK-GefvfLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 404 QEQLIYIPQNpyiYRL----TLQENVAF------YQPTATKEAVLKAIEVAGLTELLAELPqgldtmlgegeRHLSGGQA 473
Cdd:COG2884 78 RRRIGVVFQD---FRLlpdrTVYENVALplrvtgKSRKEIRRRVREVLDLVGLSDKAKALP-----------HELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 474 QRIALARAFLDQQrKILLFDEPTAHLDIETevalKERMLPLME--NRL---VFFATHRLHWMEEMDE-IIVMDQGRIVE 546
Cdd:COG2884 144 QRVAIARALVNRP-ELLLADEPTGNLDPET----SWEIMELLEeiNRRgttVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
327-555 |
4.45e-26 |
|
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: 106.99 E-value: 4.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 327 QEDAQLTIDQLAFSYEEKAALTDINLNV-TGfKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQaswqE 405
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVpRG-EILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSE----K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 406 QLIYIPQnpyiyR-------------LTLQENVAF-------YQPTATKEAVLKAIEVAGLTELLAELPqgldtmlgeGE 465
Cdd:COG1127 76 ELYELRR-----RigmlfqggalfdsLTVFENVAFplrehtdLSEAEIRELVLEKLELVGLPGAADKMP---------SE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 466 rhLSGGQAQRIALARAF-LDQqrKILLFDEPTAHLDIETEVALKE------RMLPLMenrlVFFATHRLHWMEEM-DEII 537
Cdd:COG1127 142 --LSGGMRKRVALARALaLDP--EILLYDEPTAGLDPITSAVIDElirelrDELGLT----SVVVTHDLDSAFAIaDRVA 213
|
250
....*....|....*...
gi 491368637 538 VMDQGRIVEQGTLAQLQQ 555
Cdd:COG1127 214 VLADGKIIAEGTPEELLA 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
332-544 |
5.22e-26 |
|
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: 105.69 E-value: 5.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQ--EQLIY 409
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 IPQNPYIY-RLTLQENVAFYQPTATKEAVLKAIEVAglTELLAELpqGLDTMLGEGERHLSGGQAQRIALARAfLDQQRK 488
Cdd:cd03262 81 VFQQFNLFpHLTVLENITLAPIKVKGMSKAEAEERA--LELLEKV--GLADKADAYPAQLSGGQQQRVAIARA-LAMNPK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 489 ILLFDEPTAHLDIET--EValkermLPLM-----ENRLVFFATHrlhwmeEM-------DEIIVMDQGRI 544
Cdd:cd03262 156 VMLFDEPTSALDPELvgEV------LDVMkdlaeEGMTMVVVTH------EMgfarevaDRVIFMDDGRI 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
69-565 |
6.14e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 113.53 E-value: 6.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 69 AVIYFRSKRLDDYSYQQAADLRDQLLEKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIMNMSiipWVILAL 148
Cdd:PLN03232 965 AVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQL---WQLLST 1041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 149 VFYLDWESGLVLLLVFPLIIIFmiilgYAA----QSKAEKQYR----TFQLLSNHFIDSLRGIDTLKLFG----VSKKYG 216
Cdd:PLN03232 1042 FALIGTVSTISLWAIMPLLILF-----YAAylyyQSTSREVRRldsvTRSPIYAQFGEALNGLSSIRAYKaydrMAKING 1116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 217 KSIfASSERFRKATMASLKVGILSTFALDFFTTLSIAVVAVLLGLRLINEGIllFPALTILILApeYFLPIRDFSSD-YH 295
Cdd:PLN03232 1117 KSM-DNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAENQAG--FASTMGLLLS--YTLNITTLLSGvLR 1191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 296 ATLDGKNAMTAVTEI---LHQPeAQVPAVT-----VPRWQEDAQLTIDQLAFSY--EEKAALTDINLNVTGFKKIGIIGL 365
Cdd:PLN03232 1192 QASKAENSLNSVERVgnyIDLP-SEATAIIennrpVSGWPSRGSIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGR 1270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 366 SGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVAFYqpTATKEAVL-KAIEVA 444
Cdd:PLN03232 1271 TGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPF--SEHNDADLwEALERA 1348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 445 GLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLdQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFAT 524
Cdd:PLN03232 1349 HIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALL-RRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIA 1427
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 491368637 525 HRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQG-AFTELVN 565
Cdd:PLN03232 1428 HRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVH 1469
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
89-564 |
3.62e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 110.84 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 89 LRDQLLEKLFRVGPQIAQQQ----GTGNVTTMvlegINQVENYLKLILAKIMNMSIIPWVILALVFYLDWESGLVL---- 160
Cdd:PLN03232 372 LRSTLVAAIFHKSLRLTHEArknfASGKVTNM----ITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASlfgs 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 161 LLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFiDSLRGIDTLKLFGVSKKYGKSIFASSER----FRKATMaslkv 236
Cdd:PLN03232 448 LILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIIN-EILASMDTVKCYAWEKSFESRIQGIRNEelswFRKAQL----- 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 237 gilsTFALDFFTTLSIAVVAVLLGL---RLINEGILLFPALTILILAPEYFLPIRDFSSDYHATLDGKNAMTAVTEILhQ 313
Cdd:PLN03232 522 ----LSAFNSFILNSIPVVVTLVSFgvfVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELL-L 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 314 PEAQVPAVTVPRWQEDAQLTIDQLAFSYE---EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVP-DSGEIT 389
Cdd:PLN03232 597 SEERILAQNPPLQPGAPAISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVV 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 390 LGGAkttafrqaswqeqLIYIPQNPYIYRLTLQENVAF---YQPtatkEAVLKAIEVAGLTELLAELPQGLDTMLGEGER 466
Cdd:PLN03232 677 IRGS-------------VAYVPQVSWIFNATVRENILFgsdFES----ERYWRAIDVTALQHDLDLLPGRDLTEIGERGV 739
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 467 HLSGGQAQRIALARAFLDQQrKILLFDEPTAHLD-----------IETEVALKERMLplmenrlvffATHRLHWMEEMDE 535
Cdd:PLN03232 740 NISGGQKQRVSMARAVYSNS-DIYIFDDPLSALDahvahqvfdscMKDELKGKTRVL----------VTNQLHFLPLMDR 808
|
490 500
....*....|....*....|....*....
gi 491368637 536 IIVMDQGRIVEQGTLAQLQQKQGAFTELV 564
Cdd:PLN03232 809 IILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
332-549 |
4.17e-25 |
|
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: 104.30 E-value: 4.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEE-KAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYI 410
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 411 PQN----PYiyrLTLQENVAFYqPTATKEAVLKAIEVAglTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAfLDQQ 486
Cdd:cd03295 81 IQQiglfPH---MTVEENIALV-PKLLKWPKEKIRERA--DELLALVGLDPAEFADRYPHELSGGQQQRVGVARA-LAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 487 RKILLFDEPTAHLDIETEVALKERMLPLME--NRLVFFATHRlhwMEEM----DEIIVMDQGRIVEQGT 549
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHD---IDEAfrlaDRIAIMKNGEIVQVGT 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
332-553 |
5.56e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 104.71 E-value: 5.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEE--KAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTafRQASWQ--EQL 407
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS--EETVWDvrRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 408 IYIPQNP--YIYRLTLQENVAF------YQPTATKEAVLKAIEVAGLTELLAELPQgldtmlgegerHLSGGQAQRIALA 479
Cdd:PRK13635 84 GMVFQNPdnQFVGATVQDDVAFglenigVPREEMVERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491368637 480 rAFLDQQRKILLFDEPTAHLDIE--TEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQL 553
Cdd:PRK13635 153 -GVLALQPDIIILDEATSMLDPRgrREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
305-569 |
8.93e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 109.87 E-value: 8.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 305 TAVTEILHqpeaqvPAVTVPRWQEDAQLTIDQLAFSYEEKAALTdinLNVTGFK-----KIGIIGLSGSGKSTLINTLSG 379
Cdd:PTZ00243 1288 TVVIEPAS------PTSAAPHPVQAGSLVFEGVQMRYREGLPLV---LRGVSFRiapreKVGIVGRTGSGKSTLLLTFMR 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 380 FLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENV-AFYQptATKEAVLKAIEVAGLTELLAELPQGLD 458
Cdd:PTZ00243 1359 MVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVdPFLE--ASSAEVWAALELVGLRERVASESEGID 1436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 459 TMLGEGERHLSGGQAQRIALARAFLDQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIV 538
Cdd:PTZ00243 1437 SRVLEGGSNYSVGQRQLMCMARALLKKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIV 1516
|
250 260 270
....*....|....*....|....*....|..
gi 491368637 539 MDQGRIVEQGTLAQL-QQKQGAFTELVNGMRR 569
Cdd:PTZ00243 1517 MDHGAVAEMGSPRELvMNRQSIFHSMVEALGR 1548
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
332-553 |
1.05e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 103.29 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLI--- 408
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIrql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 409 -----YIPQNPYIY-RLTLQENVAFYQPTATKEAVLKAIEVAglTELLAELpqGLDTMLGEGERHLSGGQAQRIALARAf 482
Cdd:PRK11264 84 rqhvgFVFQNFNLFpHRTVLENIIEGPVIVKGEPKEEATARA--RELLAKV--GLAGKETSYPRRLSGGQQQRVAIARA- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491368637 483 LDQQRKILLFDEPTAHLDIET--EVALKERMLPlMENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQL 553
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELvgEVLNTIRQLA-QEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKAL 231
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
346-553 |
1.10e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 105.16 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVtgfKK--I-GIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQE--QLI-YIPQNPY-IYR 418
Cdd:COG1135 20 ALDDVSLTI---EKgeIfGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAarRKIgMIFQHFNlLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 419 LTLQENVAFyqptatkeavlkAIEVAGL---------TELLAELpqGLdtmlgEGERH-----LSGGQAQRIALARAfLD 484
Cdd:COG1135 97 RTVAENVAL------------PLEIAGVpkaeirkrvAELLELV--GL-----SDKADaypsqLSGGQKQRVGIARA-LA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 485 QQRKILLFDEPTAHLDIETEVA----LKE--RmlplmenRL---VFFATHrlhwmeEM-------DEIIVMDQGRIVEQG 548
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSildlLKDinR-------ELgltIVLITH------EMdvvrricDRVAVLENGRIVEQG 223
|
....*
gi 491368637 549 TLAQL 553
Cdd:COG1135 224 PVLDV 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
339-573 |
2.63e-24 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 108.33 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 339 FSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEItlggakttafrqasWQEQLI-YIPQNPYIY 417
Cdd:PTZ00243 668 FELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WAERSIaYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 418 RLTLQENVAFYQPTATkEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLdQQRKILLFDEPTA 497
Cdd:PTZ00243 734 NATVRGNILFFDEEDA-ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVY-ANRDVYLLDDPLS 811
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491368637 498 HLDIET-EVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQkqgafTELVNGMRREQLE 573
Cdd:PTZ00243 812 ALDAHVgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR-----TSLYATLAAELKE 883
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
331-549 |
3.61e-24 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 101.81 E-value: 3.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 331 QLTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYI 410
Cdd:TIGR03873 1 GLRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 411 PQ-NPYIYRLTLQENVAF----------YQPTATKEAVLKAIEVAGLTELLAelpQGLDTmlgegerhLSGGQAQRIALA 479
Cdd:TIGR03873 81 EQdSDTAVPLTVRDVVALgriphrslwaGDSPHDAAVVDRALARTELSHLAD---RDMST--------LSGGERQRVHVA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491368637 480 RAfLDQQRKILLFDEPTAHLDIETEVALKERMLPLMENRL-VFFATHRL-HWMEEMDEIIVMDQGRIVEQGT 549
Cdd:TIGR03873 150 RA-LAQEPKLLLLDEPTNHLDVRAQLETLALVRELAATGVtVVAALHDLnLAASYCDHVVVLDGGRVVAAGP 220
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
329-549 |
3.62e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 102.38 E-value: 3.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 329 DAQLTIDQLAFSY--EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTA--FRQAswQ 404
Cdd:PRK13632 5 SVMIKVENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEI--R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 405 EQLIYIPQNP---YIyRLTLQENVAF------YQPTATKEAVLKAIEVAGLTELLAELPQgldtmlgegerHLSGGQAQR 475
Cdd:PRK13632 83 KKIGIIFQNPdnqFI-GATVEDDIAFglenkkVPPKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 476 IALARAF-LDQqrKILLFDEPTAHLDIETEVALKERMLPLMENR--LVFFATHRlhwMEEM---DEIIVMDQGRIVEQGT 549
Cdd:PRK13632 151 VAIASVLaLNP--EIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHD---MDEAilaDKVIVFSEGKLIAQGK 225
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
331-572 |
3.66e-24 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 102.24 E-value: 3.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 331 QLTIDQLAFSYEE--KAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDsGEITLGGAKTTAFRQASWQEQLI 408
Cdd:cd03289 2 QMTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 409 YIPQNPYIYRLTLQENVAFYQPTATKEaVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLDQQrK 488
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYGKWSDEE-IWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA-K 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 489 ILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGAFTELVNGMR 568
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSD 238
|
....
gi 491368637 569 REQL 572
Cdd:cd03289 239 RLKL 242
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
132-564 |
7.38e-24 |
|
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: 106.95 E-value: 7.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 132 LAKIMNM--SIIPWVILALvfYLDWESGLVLLLVFPLIIIFMIILGYAAQSKAekqyRTFQLLSNHFIDS--------LR 201
Cdd:TIGR00957 431 LATYINMiwSAPLQVILAL--YFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKT----KTYQVAHMKSKDNriklmneiLN 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 202 GIDTLKLFGVSKKYGKSIFASSERFRKATMASLKVGILSTFA---LDFFTTLSIAVVAVLLGLRLINEGILLFPALTI-- 276
Cdd:TIGR00957 505 GIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTwvcTPFLVALITFAVYVTVDENNILDAEKAFVSLALfn 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 277 LILAPEYFLPIRdFSSDYHATLDGKNAMTAVTEILHQPEAqVPAVTVPRWQEDAqLTIDQLAFSY--EEKAALTDINLNV 354
Cdd:TIGR00957 585 ILRFPLNILPMV-ISSIVQASVSLKRLRIFLSHEELEPDS-IERRTIKPGEGNS-ITVHNATFTWarDLPPTLNGITFSI 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 355 TGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAkttafrqaswqeqLIYIPQNPYIYRLTLQENVAFYQPTATK 434
Cdd:TIGR00957 662 PEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGKALNEK 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 435 EaVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLDQQrKILLFDEPTAHLDIETEVALKERMLP- 513
Cdd:TIGR00957 729 Y-YQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNA-DIYLFDDPLSAVDAHVGKHIFEHVIGp 806
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 491368637 514 --LMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGAFTELV 564
Cdd:TIGR00957 807 egVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
16-304 |
1.30e-23 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 101.09 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 16 LGLLAGLSFLQALFIIGQAYGLARAITGLWEGRPLEEQWGWILLFFCSFIARQAVIYFRSKRLDDYSYQQAADLRDQLLE 95
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 96 KLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIMNMSIIPWVILALVFYLDWESGLVLLLVFPLIIIFMIILG 175
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 176 YAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKYGKSIFASSERFRKATMASLKVGILSTFALDFFTTLSIAVV 255
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 491368637 256 AVLLGLRLINEGILLFPALTILILAPEYFLPIRDFSSDYHATLDGKNAM 304
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASL 289
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
346-549 |
1.72e-23 |
|
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: 99.34 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTafRQASWQEQLIYIPQNPYIYR-LTLQEN 424
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQERNVGFVFQHYALFRhMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 425 VAFYQPTATKEAVLKAIEVAGLTELLAELPQgLDTMLGEGERHLSGGQAQRIALARAfLDQQRKILLFDEPTAHLDIETE 504
Cdd:cd03296 95 VAFGLRVKPRSERPPEAEIRAKVHELLKLVQ-LDWLADRYPAQLSGGQRQRVALARA-LAVEPKVLLLDEPFGALDAKVR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491368637 505 VALKeRMLPLMENRL---VFFATH-RLHWMEEMDEIIVMDQGRIVEQGT 549
Cdd:cd03296 173 KELR-RWLRRLHDELhvtTVFVTHdQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
347-566 |
1.81e-23 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 100.32 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 347 LTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGakttafrqaswqeQLIYIPQNPYIYRLTLQENVA 426
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 427 F---YQPTATKeAVLKAIEvagLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLdQQRKILLFDEPTAHLDIET 503
Cdd:cd03291 120 FgvsYDEYRYK-SVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVY-KDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491368637 504 EVALKERML-PLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGAFTELVNG 566
Cdd:cd03291 195 EKEIFESCVcKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMG 258
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
332-549 |
4.48e-23 |
|
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: 98.08 E-value: 4.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYip 411
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNPYIY-RLTLQENVAF------YQPTATKEAVLKAIEVAGLTELLAELPQgldtmlgegerHLSGGQAQRIALARAfLD 484
Cdd:cd03300 79 QNYALFpHLTVFENIAFglrlkkLPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARA-LV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491368637 485 QQRKILLFDEPTAHLDieteVALKERM---LPLMENRL---VFFATHRlhwMEEM----DEIIVMDQGRIVEQGT 549
Cdd:cd03300 147 NEPKVLLLDEPLGALD----LKLRKDMqleLKRLQKELgitFVFVTHD---QEEAltmsDRIAVMNKGKIQQIGT 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
347-553 |
9.07e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.47 E-value: 9.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 347 LTDINLNVTGFKKIGIIGLSGSGKSTL---INTL----SGFLVPDSGEITLGGAKTTAFRQASWQ--EQLIYIPQnpyiy 417
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLlrcINKLeeitSGDLIVDGLKVNDPKVDERLIRQEAGMvfQQFYLFPH----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 418 rLTLQENVAFyQPT----ATKEAvlkAIEVAglTELLAELpqGLDTMLGEGERHLSGGQAQRIALARAfLDQQRKILLFD 493
Cdd:PRK09493 92 -LTALENVMF-GPLrvrgASKEE---AEKQA--RELLAKV--GLAERAHHYPSELSGGQQQRVAIARA-LAVKPKLMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491368637 494 EPTAHLDIEtevaLKERMLPLM-----ENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQL 553
Cdd:PRK09493 162 EPTSALDPE----LRHEVLKVMqdlaeEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVL 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
332-548 |
1.03e-22 |
|
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: 96.67 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKA----ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASwQEQL 407
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA-RRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 408 IYIPQNPYIY-RLTLQENVAFY------QPTATKEAVLKAIEVAGLTELlaelpqgLDTMLGEgerhLSGGQAQRIALAR 480
Cdd:cd03266 81 GFVSDSTGLYdRLTARENLEYFaglyglKGDELTARLEELADRLGMEEL-------LDRRVGG----FSTGMRQKVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 481 AFLdQQRKILLFDEPTAHLDIETEVALKERMLPLME-NRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQG 548
Cdd:cd03266 150 ALV-HDPPVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
339-566 |
1.30e-22 |
|
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: 103.07 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 339 FSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGakttafrqaswqeQLIYIPQNPYIYR 418
Cdd:TIGR01271 434 FSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 419 LTLQENVAF------YQPTAtkeaVLKAIEvagLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAfLDQQRKILLF 492
Cdd:TIGR01271 501 GTIKDNIIFglsydeYRYTS----VIKACQ---LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARA-VYKDADLYLL 572
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491368637 493 DEPTAHLDIETEVALKERML-PLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGAFTELVNG 566
Cdd:TIGR01271 573 DSPFTHLDVVTEKEIFESCLcKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLG 647
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
332-548 |
1.71e-22 |
|
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: 95.78 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYip 411
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNPYIY-RLTLQENVAF------YQPTATKEAVLKAIEVAGLTELLAELPqgldtmlgegeRHLSGGQAQRIALARAfLD 484
Cdd:cd03301 79 QNYALYpHMTVYDNIAFglklrkVPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRA-IV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491368637 485 QQRKILLFDEPTAHLDIETEVALKERmLPLMENRL---VFFATH-RLHWMEEMDEIIVMDQGRIVEQG 548
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAE-LKRLQQRLgttTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
330-547 |
2.03e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 96.85 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 330 AQLTIDQLAFSYE----EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTT---AFRQAS 402
Cdd:COG4525 2 SMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 403 WQEQLIYipqnPYiyrLTLQENVAFyqptATKEA-VLKAIEVAGLTELLAELpqGLDtmlGEGER---HLSGGQAQRIAL 478
Cdd:COG4525 82 FQKDALL----PW---LNVLDNVAF----GLRLRgVPKAERRARAEELLALV--GLA---DFARRriwQLSGGMRQRVGI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 479 ARAfLDQQRKILLFDEPTAHLDIETevalKERMLPLM------ENRLVFFATHRLhwmEEM----DEIIVMD--QGRIVE 546
Cdd:COG4525 146 ARA-LAADPRFLLMDEPFGALDALT----REQMQELLldvwqrTGKGVFLITHSV---EEAlflaTRLVVMSpgPGRIVE 217
|
.
gi 491368637 547 Q 547
Cdd:COG4525 218 R 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
326-546 |
2.13e-22 |
|
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: 95.96 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 326 WQEDAQLTIdqlafsyeekaaLTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTT--------A 397
Cdd:COG4181 19 GTGAGELTI------------LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldedaraR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 398 FRQAS----WQ-EQLiyIPQnpyiyrLTLQENVA-------FYQPTATKEAVLKAIevaGLTELLAELPqgldtmlgege 465
Cdd:COG4181 87 LRARHvgfvFQsFQL--LPT------LTALENVMlplelagRRDARARARALLERV---GLGHRLDHYP----------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 466 RHLSGGQAQRIALARAFLDQQrKILLFDEPTAHLDIETevalKERMLPLME--NR-----LVfFATHRLHWMEEMDEIIV 538
Cdd:COG4181 145 AQLSGGEQQRVALARAFATEP-AILFADEPTGNLDAAT----GEQIIDLLFelNRergttLV-LVTHDPALAARCDRVLR 218
|
....*...
gi 491368637 539 MDQGRIVE 546
Cdd:COG4181 219 LRAGRLVE 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
334-557 |
2.49e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 96.24 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 334 IDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTaFRQASWQEQLIYIPQN 413
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFD-FSQKPSEKAIRLLRQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 414 -----------PYiyrLTLQENVAfyqptatkEAVLKaieVAGLT---------ELLAELpqGLDTMLGEGERHLSGGQA 473
Cdd:COG4161 84 vgmvfqqynlwPH---LTVMENLI--------EAPCK---VLGLSkeqarekamKLLARL--RLTDKADRFPLHLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 474 QRIALARAfLDQQRKILLFDEPTAHLD--IETEVALKERMLPLMENRLVfFATHRLHWMEEM-DEIIVMDQGRIVEQGTL 550
Cdd:COG4161 148 QRVAIARA-LMMEPQVLLFDEPTAALDpeITAQVVEIIRELSQTGITQV-IVTHEVEFARKVaSQVVYMEKGRIIEQGDA 225
|
....*..
gi 491368637 551 AQLQQKQ 557
Cdd:COG4161 226 SHFTQPQ 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
346-554 |
2.49e-22 |
|
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: 95.97 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFR-QASWQEQLIYIPQNPYIY-RLTLQE 423
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpHEIARLGIGRTFQIPRLFpELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 424 NV----------------AFYQPTATKEAVLKAIEVAGLTELLAELPQGldtmlgegerhLSGGQAQRIALARAfLDQQR 487
Cdd:cd03219 95 NVmvaaqartgsglllarARREEREARERAEELLERVGLADLADRPAGE-----------LSYGQQRRLEIARA-LATDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 488 KILLFDEPTAHLDIETEVALKERMLPLMENRL-VFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQLQ 554
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIRELRERGItVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVR 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
337-553 |
2.57e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.18 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 337 LAFSYE-EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQNP- 414
Cdd:PRK13652 9 LCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 415 -YIYRLTLQENVAF------YQPTATKEAVLKAIEVAGLTELLAELPQgldtmlgegerHLSGGQAQRIALArAFLDQQR 487
Cdd:PRK13652 89 dQIFSPTVEQDIAFgpinlgLDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIA-GVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 488 KILLFDEPTAHLDIE--TEVALKERMLPLMENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQL 553
Cdd:PRK13652 157 QVLVLDEPTAGLDPQgvKELIDFLNDLPETYGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEI 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
347-564 |
3.83e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 101.35 E-value: 3.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 347 LTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVA 426
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 427 FYqpTATKEAVL-KAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLdQQRKILLFDEPTAHLDIETEV 505
Cdd:PLN03130 1335 PF--NEHNDADLwESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL-RRSKILVLDEATAAVDVRTDA 1411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 506 ALKERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQG-AFTELV 564
Cdd:PLN03130 1412 LIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGsAFSKMV 1471
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
339-553 |
5.35e-22 |
|
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: 94.49 E-value: 5.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 339 FSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEqLIYIPQNPYIYR 418
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQS-LGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 419 -LTLQENVAFYqptatkeAVLKAI-------EVAGLTELLaELPQGLDTMLGEgerhLSGGQAQRIALARAFLDqQRKIL 490
Cdd:cd03263 89 eLTVREHLRFY-------ARLKGLpkseikeEVELLLRVL-GLTDKANKRART----LSGGMKRKLSLAIALIG-GPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491368637 491 LFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRlhwMEEM----DEIIVMDQGRIVEQGTLAQL 553
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHS---MDEAealcDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
332-543 |
6.35e-22 |
|
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: 92.13 E-value: 6.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAfrqaswqeqliYIP 411
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIG-----------YFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QnpyiyrltlqenvafyqptatkeavlkaievagltellaelpqgldtmlgegerhLSGGQAQRIALARAFLdQQRKILL 491
Cdd:cd03221 70 Q-------------------------------------------------------LSGGEKMRLALAKLLL-ENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491368637 492 FDEPTAHLDIETEVALkERMLpLMENRLVFFATHRLHWMEEM-DEIIVMDQGR 543
Cdd:cd03221 94 LDEPTNHLDLESIEAL-EEAL-KEYPGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
330-552 |
6.72e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 95.22 E-value: 6.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 330 AQLTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIY 409
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 IPQNPYI-YRLTLQENVAF------YQPTATKEAVLKAIEVAGLTELlaelpqgldtmlgeGERH---LSGGQAQRIALA 479
Cdd:PRK13548 81 LPQHSSLsFPFTVEEVVAMgraphgLSRAEDDALVAAALAQVDLAHL--------------AGRDypqLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 480 RAFL-----DQQRKILLFDEPTAHLDIetevALKERMLPLMENrlvfFATHR-------LH-------WmeeMDEIIVMD 540
Cdd:PRK13548 147 RVLAqlwepDGPPRWLLLDEPTSALDL----AHQHHVLRLARQ----LAHERglavivvLHdlnlaarY---ADRIVLLH 215
|
250
....*....|..
gi 491368637 541 QGRIVEQGTLAQ 552
Cdd:PRK13548 216 QGRLVADGTPAE 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
329-549 |
7.01e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.84 E-value: 7.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 329 DAQLTIDQLAFSYEEKA-----ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLG----GAKTTAFR 399
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 400 QASWQEQ------------LIYIPQNP--YIYRLTLQENVAFyQPTATKeavLKAIEVAGLTELLAELpQGLD-TMLGEG 464
Cdd:PRK13631 99 LITNPYSkkiknfkelrrrVSMVFQFPeyQLFKDTIEKDIMF-GPVALG---VKKSEAKKLAKFYLNK-MGLDdSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 465 ERHLSGGQAQRIALArAFLDQQRKILLFDEPTAHLDIETEvalkERMLPLM-----ENRLVFFATHRL-HWMEEMDEIIV 538
Cdd:PRK13631 174 PFGLSGGQKRRVAIA-GILAIQPEILIFDEPTAGLDPKGE----HEMMQLIldakaNNKTVFVITHTMeHVLEVADEVIV 248
|
250
....*....|.
gi 491368637 539 MDQGRIVEQGT 549
Cdd:PRK13631 249 MDKGKILKTGT 259
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
331-549 |
9.31e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.70 E-value: 9.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 331 QLTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYI 410
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 411 PQNPYIYR-LTLQENVAF----YQP------TATKEAVLKAIEVAGLTELlaelpqgLDTMLGEgerhLSGGQAQRIALA 479
Cdd:PRK11231 82 PQHHLTPEgITVRELVAYgrspWLSlwgrlsAEDNARVNQAMEQTRINHL-------ADRRLTD----LSGGQRQRAFLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491368637 480 RAfLDQQRKILLFDEPTAHLDIETEVALKERMLPL-MENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGT 549
Cdd:PRK11231 151 MV-LAQDTPVVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRYcDHLVVLANGHVMAQGT 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
332-555 |
1.02e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 94.26 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDinLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTT----AFRQAS--WQE 405
Cdd:PRK10771 2 LKLTDITWLYHHLPMRFD--LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTttppSRRPVSmlFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 406 qliyipqNPYIYRLTLQENVAF-YQP----TATKEAVLKAI-EVAGLTELLAELPQgldtmlgegerHLSGGQAQRIALA 479
Cdd:PRK10771 80 -------NNLFSHLTVAQNIGLgLNPglklNAAQREKLHAIaRQMGIEDLLARLPG-----------QLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 480 RAFLDQQrKILLFDEPTAHLDieteVALKERMLPLME------NRLVFFATHRLhwmEEMDEI----IVMDQGRIVEQGT 549
Cdd:PRK10771 142 RCLVREQ-PILLLDEPFSALD----PALRQEMLTLVSqvcqerQLTLLMVSHSL---EDAARIaprsLVVADGRIAWDGP 213
|
....*.
gi 491368637 550 LAQLQQ 555
Cdd:PRK10771 214 TDELLS 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
332-549 |
1.60e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 96.31 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTafRQASWQEQLIYIP 411
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS--RLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNPYIYR-LTLQENVAF--------YQPT--ATKEAVLKAIEVAGLTELLAELPQgldtmlgegerHLSGGQAQRIALAR 480
Cdd:PRK10851 81 QHYALFRhMTVFDNIAFgltvlprrERPNaaAIKAKVTQLLEMVQLAHLADRYPA-----------QLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491368637 481 AfLDQQRKILLFDEPTAHLDIETEVALKeRMLPLMENRLVF---FATH-RLHWMEEMDEIIVMDQGRIVEQGT 549
Cdd:PRK10851 150 A-LAVEPQILLLDEPFGALDAQVRKELR-RWLRQLHEELKFtsvFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
347-548 |
1.64e-21 |
|
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: 93.13 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 347 LTDINLNV---TGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQA---SWQEQLI-YIPQNPYIY-R 418
Cdd:cd03297 10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinlPPQQRKIgLVFQQYALFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 419 LTLQENVAFyqPTATKEAVLKAIEVAGLTELLaelpqGLDTMLGEGERHLSGGQAQRIALARAFLDQQRkILLFDEPTAH 498
Cdd:cd03297 90 LNVRENLAF--GLKRKRNREDRISVDELLDLL-----GLDHLLNRYPAQLSGGEKQRVALARALAAQPE-LLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491368637 499 LDieteVALKERMLPLMENRL------VFFATHRLHWMEEM-DEIIVMDQGRIVEQG 548
Cdd:cd03297 162 LD----RALRLQLLPELKQIKknlnipVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-545 |
1.79e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 94.38 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 342 EEKAALTDINLNV-TG-FkkIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGG---AKTTAFRQASWqeqLIYIPQNPYI 416
Cdd:COG1101 17 NEKRALDGLNLTIeEGdF--VTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvTKLPEYKRAKY---IGRVFQDPMM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 417 ---YRLTLQENVAFyqptATKE--------AVLKAiEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLdQ 485
Cdd:COG1101 92 gtaPSMTIEENLAL----AYRRgkrrglrrGLTKK-RRELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLLMATL-T 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491368637 486 QRKILLFDEPTAHLDIETevALKermlpLME--NRLVffATHRL------HWMEEM----DEIIVMDQGRIV 545
Cdd:COG1101 166 KPKLLLLDEHTAALDPKT--AAL-----VLEltEKIV--EENNLttlmvtHNMEQAldygNRLIMMHEGRII 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
334-503 |
1.86e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 334 IDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAfrqaswqeqliYIPQN 413
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIG-----------YLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 414 PYIY-RLTLQENVAF-YQPTATKEAVLKAIEVAGLT-----ELLAELPQGLDTM---------------LG----EGER- 466
Cdd:COG0488 70 PPLDdDLTVLDTVLDgDAELRALEAELEELEAKLAEpdedlERLAELQEEFEALggweaearaeeilsgLGfpeeDLDRp 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 491368637 467 --HLSGGQAQRIALARAFLdQQRKILLFDEPTAHLDIET 503
Cdd:COG0488 150 vsELSGGWRRRVALARALL-SEPDLLLLDEPTNHLDLES 187
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
343-552 |
2.10e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 94.73 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 343 EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAfRQASWQE---QLIYIPQNPYiYRL 419
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDirkKVGLVFQYPE-YQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 420 ---TLQENVAF------YQPTATKEAVLKAIEVAGLTellaelpqgLDTMLGEGERHLSGGQAQRIALArAFLDQQRKIL 490
Cdd:PRK13637 97 feeTIEKDIAFgpinlgLSEEEIENRVKRAMNIVGLD---------YEDYKDKSPFELSGGQKRRVAIA-GVVAMEPKIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491368637 491 LFDEPTAHLDIET--EVALKERMLPLMENRLVFFATHRlhwMEEM----DEIIVMDQGRIVEQGTLAQ 552
Cdd:PRK13637 167 ILDEPTAGLDPKGrdEILNKIKELHKEYNMTIILVSHS---MEDVaklaDRIIVMNKGKCELQGTPRE 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
339-563 |
2.23e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 99.04 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 339 FSYE---EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDS-GEITLGGakTTAfrqaswqeqliYIPQNP 414
Cdd:PLN03130 622 FSWDskaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRG--TVA-----------YVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 415 YIYRLTLQENVAFYQPTaTKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAFLDQQrKILLFDE 494
Cdd:PLN03130 689 WIFNATVRDNILFGSPF-DPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNS-DVYIFDD 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 495 PTAHLD-----------IETEVALKERMLplmenrlvffATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGAFTEL 563
Cdd:PLN03130 767 PLSALDahvgrqvfdkcIKDELRGKTRVL----------VTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
332-546 |
2.69e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLG-GAKTTAFRQAswQEQLiyi 410
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGeTVKIGYFDQH--QEEL--- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 411 pqNPyiyRLTLQENVAFYQPTATKeavlkaIEVAGLtellaelpqgLDTMLGEGERH------LSGGQAQRIALARAFLd 484
Cdd:COG0488 391 --DP---DKTVLDELRDGAPGGTE------QEVRGY----------LGRFLFSGDDAfkpvgvLSGGEKARLALAKLLL- 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 485 QQRKILLFDEPTAHLDIETevalkermLPLMENRL------VFFATHRLHWMEEM-DEIIVMDQGRIVE 546
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIET--------LEALEEALddfpgtVLLVSHDRYFLDRVaTRILEFEDGGVRE 509
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
332-549 |
3.39e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 93.93 E-value: 3.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYE-----EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQaswQEQ 406
Cdd:PRK13634 3 ITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKK---NKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 407 LIYIPQNPYI---------YRLTLQENVAFyQPT----ATKEAVLKA---IEVAGLTE-LLAELPqgldtmlgegeRHLS 469
Cdd:PRK13634 80 LKPLRKKVGIvfqfpehqlFEETVEKDICF-GPMnfgvSEEDAKQKAremIELVGLPEeLLARSP-----------FELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 470 GGQAQRIALArAFLDQQRKILLFDEPTAHLDietEVALKErmlpLMEnrlVFFATHR---------LHWMEEM----DEI 536
Cdd:PRK13634 148 GGQMRRVAIA-GVLAMEPEVLVLDEPTAGLD---PKGRKE----MME---MFYKLHKekglttvlvTHSMEDAaryaDQI 216
|
250
....*....|...
gi 491368637 537 IVMDQGRIVEQGT 549
Cdd:PRK13634 217 VVMHKGTVFLQGT 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
334-557 |
4.57e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 92.38 E-value: 4.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 334 IDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTaFRQASWQEQLIYIPQN 413
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFD-FSKTPSDKAIRELRRN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 414 -----------PYiyrLTLQENVAfyqptatkEAVLKaieVAGLT--ELLAELPQGLDTM-LGE-GER---HLSGGQAQR 475
Cdd:PRK11124 84 vgmvfqqynlwPH---LTVQQNLI--------EAPCR---VLGLSkdQALARAEKLLERLrLKPyADRfplHLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 476 IALARAfLDQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLV-FFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQL 553
Cdd:PRK11124 150 VAIARA-LMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITqVIVTHEVEVARKTaSRVVYMENGHIVEQGDASCF 228
|
....
gi 491368637 554 QQKQ 557
Cdd:PRK11124 229 TQPQ 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
332-564 |
5.19e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 93.63 E-value: 5.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNV-TGfkKI-GIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAfrqasWQEQLI- 408
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVpKG--EIfGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-----EDRRRIg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 409 YIPQNPYIY-RLTLQENVAFYqptatkeAVLKaievaGLTelLAELPQGLDTMLgegERH------------LSGGQAQR 475
Cdd:COG4152 75 YLPEERGLYpKMKVGEQLVYL-------ARLK-----GLS--KAEAKRRADEWL---ERLglgdrankkveeLSKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 476 IALARAFLDQQrKILLFDEPTAHLD-IETEVaLKERMLPLMEN-RLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQ 552
Cdd:COG4152 138 VQLIAALLHDP-ELLILDEPFSGLDpVNVEL-LKDVIRELAAKgTTVIFSSHQMELVEELcDRIVIINKGRKVLSGSVDE 215
|
250
....*....|..
gi 491368637 553 LQQKQGAFTELV 564
Cdd:COG4152 216 IRRQFGRNTLRL 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
328-549 |
7.00e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 92.84 E-value: 7.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 328 EDAQLTIDQLAFSYE------EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTT----- 396
Cdd:PRK13633 1 MNEMIKCKNVSYKYEsneestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeenl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 397 -AFRQASwqeQLIYipQNP--YIYRLTLQENVAF------YQPTATKEAVLKAIEVAGLTELLAELPqgldtmlgegerH 467
Cdd:PRK13633 81 wDIRNKA---GMVF--QNPdnQIVATIVEEDVAFgpenlgIPPEEIRERVDESLKKVGMYEYRRHAP------------H 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 468 -LSGGQAQRIALArAFLDQQRKILLFDEPTAHLDietEVALKERMLPLMENRLVFFATHRL--HWMEEM---DEIIVMDQ 541
Cdd:PRK13633 144 lLSGGQKQRVAIA-GILAMRPECIIFDEPTAMLD---PSGRREVVNTIKELNKKYGITIILitHYMEEAveaDRIIVMDS 219
|
....*...
gi 491368637 542 GRIVEQGT 549
Cdd:PRK13633 220 GKVVMEGT 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
330-568 |
7.38e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 92.36 E-value: 7.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 330 AQLTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIY 409
Cdd:PRK10253 6 ARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 IPQNPYIY-RLTLQENVAF----YQPTATK------EAVLKAIEVAGLTELLAelpQGLDTmlgegerhLSGGQAQRIAL 478
Cdd:PRK10253 86 LAQNATTPgDITVQELVARgrypHQPLFTRwrkedeEAVTKAMQATGITHLAD---QSVDT--------LSGGQRQRAWI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 479 ARAfLDQQRKILLFDEPTAHLDIETEVALKERMLPLME-------------NRLVFFATHrlhwmeemdeIIVMDQGRIV 545
Cdd:PRK10253 155 AMV-LAQETAIMLLDEPTTWLDISHQIDLLELLSELNRekgytlaavlhdlNQACRYASH----------LIALREGKIV 223
|
250 260
....*....|....*....|...
gi 491368637 546 EQGtlAQLQQKQGAFTELVNGMR 568
Cdd:PRK10253 224 AQG--APKEIVTAELIERIYGLR 244
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
345-542 |
2.68e-20 |
|
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: 89.70 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 345 AALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEI----TLGGAKTTAFRQASWQEQLIYIPQNPYIYRLT 420
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 421 LQENVAFYQPTaTKEAVLKAIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAfLDQQRKILLFDEPTAHLD 500
Cdd:cd03290 95 VEENITFGSPF-NKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARA-LYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491368637 501 IE-TEVALKERMLPLMEN--RLVFFATHRLHWMEEMDEIIVMDQG 542
Cdd:cd03290 173 IHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
332-548 |
3.61e-20 |
|
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: 88.81 E-value: 3.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTafRQASWQEQLIYIP 411
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNPYIY-RLTLQENVAFYqptatkeAVLKAIEVAGLTELLAELpqGLDTMLGEGERHLSGGQAQRIALARAFLDQQrKIL 490
Cdd:cd03268 79 EAPGFYpNLTARENLRLL-------ARLLGIRKKRIDEVLDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNP-DLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 491 LFDEPTAHLDIETEVALKERMLPLM-ENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQG 548
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
340-545 |
3.77e-20 |
|
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: 87.48 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 340 SYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKttafrqaswqeqliyipqnpyiyrl 419
Cdd:cd03216 9 RFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 420 tlqenVAFYQPtatKEAVLKAIEVAgltellaelPQgldtmlgegerhLSGGQAQRIALARAfLDQQRKILLFDEPTAHL 499
Cdd:cd03216 64 -----VSFASP---RDARRAGIAMV---------YQ------------LSVGERQMVEIARA-LARNARLLILDEPTAAL 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491368637 500 DiETEValkERMLPLMEnRL------VFFATHRLHWMEEM-DEIIVMDQGRIV 545
Cdd:cd03216 114 T-PAEV---ERLFKVIR-RLraqgvaVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
384-557 |
5.17e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 94.71 E-value: 5.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 384 DSGEITLGGAKTTAFRQASWQEQLIYIPQNPYIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELPQGLDTMLGE 463
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGP 1354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 464 GERHLSGGQAQRIALARAFLdQQRKILLFDEPTAHLDIETEVALKERMLPLME--NRLVFFATHRLHWMEEMDEIIVMDQ 541
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALL-REPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNN 1433
|
170 180
....*....|....*....|.
gi 491368637 542 ----GRIVE-QGTLAQLQQKQ 557
Cdd:PTZ00265 1434 pdrtGSFVQaHGTHEELLSVQ 1454
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
332-548 |
5.63e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.21 E-value: 5.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIP 411
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNPYI-YRLTLQENVA---------FYQPTATKE-AVLKAIEVAGLTELLAelpQGLDTmlgegerhLSGGQAQRIALAR 480
Cdd:PRK09536 84 QDTSLsFEFDVRQVVEmgrtphrsrFDTWTETDRaAVERAMERTGVAQFAD---RPVTS--------LSGGERQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 481 AfLDQQRKILLFDEPTAHLDIETEVALKERMLPLMEN-RLVFFATHRLHWMEEM-DEIIVMDQGRIVEQG 548
Cdd:PRK09536 153 A-LAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYcDELVLLADGRVRAAG 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
332-555 |
6.73e-20 |
|
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: 88.65 E-value: 6.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTafRQASWQ---EQLI 408
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT--GLPPHErarAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 409 YIPQNPYIY-RLTLQEN--VAFYqpTATKEAVLKAIEvagltELLAELPQgLDTMLGEGERHLSGGQAQRIALARAFLdQ 485
Cdd:cd03224 79 YVPEGRRIFpELTVEENllLGAY--ARRRAKRKARLE-----RVYELFPR-LKERRKQLAGTLSGGEQQMLAIARALM-S 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 486 QRKILLFDEPTAHL------DIETEV-ALKER---MLpLMENRlVFFAthrlhwMEEMDEIIVMDQGRIVEQGTLAQLQQ 555
Cdd:cd03224 150 RPKLLLLDEPSEGLapkiveEIFEAIrELRDEgvtIL-LVEQN-ARFA------LEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
332-511 |
9.21e-20 |
|
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: 87.55 E-value: 9.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGaKTTAFRQASWQEQLIYIP 411
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG-GPLDFQRDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNPYIY-RLTLQENVAFYQPTATKEAVLKAIEVAGLTElLAELPQGldtmlgegerHLSGGQAQRIALARAFLDqQRKIL 490
Cdd:cd03231 80 HAPGIKtTLSVLENLRFWHADHSDEQVEEALARVGLNG-FEDRPVA----------QLSAGQQRRVALARLLLS-GRPLW 147
|
170 180
....*....|....*....|.
gi 491368637 491 LFDEPTAHLDIETEVALKERM 511
Cdd:cd03231 148 ILDEPTTALDKAGVARFAEAM 168
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
346-567 |
1.36e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.00 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNV-TGfkKI-GIIGLSGSGKSTLINTLSGFLVPDSGEITLGGaKTTAFR--QASWQEQLIYIPQN----PYiy 417
Cdd:COG1129 19 ALDGVSLELrPG--EVhALLGENGAGKSTLMKILSGVYQPDSGEILLDG-EPVRFRspRDAQAAGIAIIHQElnlvPN-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 418 rLTLQENVAF-YQPTA-----TKEAVLKAievaglTELLAELpqGLD----TMLGEgerhLSGGQAQRIALARAfLDQQR 487
Cdd:COG1129 94 -LSVAENIFLgREPRRgglidWRAMRRRA------RELLARL--GLDidpdTPVGD----LSVAQQQLVEIARA-LSRDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 488 KILLFDEPTAHLDiETEValkERMLPLMEnRL------VFFATHRlhwMEEM----DEIIVMDQGRIVEQGTLAQLQQKq 557
Cdd:COG1129 160 RVLILDEPTASLT-EREV---ERLFRIIR-RLkaqgvaIIYISHR---LDEVfeiaDRVTVLRDGRLVGTGPVAELTED- 230
|
250
....*....|
gi 491368637 558 gaftELVNGM 567
Cdd:COG1129 231 ----ELVRLM 236
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
332-552 |
1.62e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 88.25 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIP 411
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QN-----PYiyrlTLQENVA------FYQPTATKEAVLKAIEVAGLTELlaelpqgldtmlgeGERH---LSGGQAQRIA 477
Cdd:COG4559 82 QHsslafPF----TVEEVVAlgraphGSSAAQDRQIVREALALVGLAHL--------------AGRSyqtLSGGEQQRVQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 478 LARAFL------DQQRKILLFDEPTAHLDIetevALKERMLplmenRLV-FFATHRLHWMEEM----------DEIIVMD 540
Cdd:COG4559 144 LARVLAqlwepvDGGPRWLFLDEPTSALDL----AHQHAVL-----RLArQLARRGGGVVAVLhdlnlaaqyaDRILLLH 214
|
250
....*....|..
gi 491368637 541 QGRIVEQGTLAQ 552
Cdd:COG4559 215 QGRLVAQGTPEE 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
340-549 |
1.65e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 90.39 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 340 SYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTafRQASWQEQLIYIPQNpyiYRL 419
Cdd:PRK09452 23 SFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVNTVFQS---YAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 420 ----TLQENVAF---YQPTATKEA---VLKAIEVAGLTELLAELPQgldtmlgegerHLSGGQAQRIALARAFLDQQrKI 489
Cdd:PRK09452 98 fphmTVFENVAFglrMQKTPAAEItprVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKP-KV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 490 LLFDEPTAHLDIEtevaLKERM---LPLMENRL--VF-FATHRlhwMEE---M-DEIIVMDQGRIVEQGT 549
Cdd:PRK09452 166 LLLDESLSALDYK----LRKQMqneLKALQRKLgiTFvFVTHD---QEEaltMsDRIVVMRDGRIEQDGT 228
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
360-553 |
2.47e-19 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 87.93 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 360 IGIIGLSGSGKSTL---INTLSgflVPDSGEITLGG-------AKTTAFRQASWQE------QLIYIPQNPYIY-RLTLQ 422
Cdd:COG4598 37 ISIIGSSGSGKSTFlrcINLLE---TPDSGEIRVGGeeirlkpDRDGELVPADRRQlqrirtRLGMVFQSFNLWsHMTVL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 423 ENVAfyqptatkEA---VLK-----AIEVAglTELLAELpqgldtmlGEGER------HLSGGQAQRIALARAfLDQQRK 488
Cdd:COG4598 114 ENVI--------EApvhVLGrpkaeAIERA--EALLAKV--------GLADKrdaypaHLSGGQQQRAAIARA-LAMEPE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 489 ILLFDEPTAHLDIE--TEValkermLPLM-----ENRLVFFATHrlhwmeEM-------DEIIVMDQGRIVEQGTLAQL 553
Cdd:COG4598 175 VMLFDEPTSALDPElvGEV------LKVMrdlaeEGRTMLVVTH------EMgfardvsSHVVFLHQGRIEEQGPPAEV 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
346-553 |
7.53e-19 |
|
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: 89.74 E-value: 7.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGfLVPDSGEITLGGAKTTAFRQASWQE-----QLIYipQNPYIY--- 417
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSRRALRPlrrrmQVVF--QDPFGSlsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 418 RLT----LQENVAFYQPTATKEAVLKAIEvagltELLAELpqGLDtmlgEGERH-----LSGGQAQRIALARAfLDQQRK 488
Cdd:COG4172 378 RMTvgqiIAEGLRVHGPGLSAAERRARVA-----EALEEV--GLD----PAARHrypheFSGGQRQRIAIARA-LILEPK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491368637 489 ILLFDEPTAHLDieteVALKERMLPLM-----ENRLVF-FATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQL 553
Cdd:COG4172 446 LLVLDEPTSALD----VSVQAQILDLLrdlqrEHGLAYlFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQV 513
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
341-548 |
7.86e-19 |
|
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: 85.85 E-value: 7.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 341 YEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGakttafrqaswqeqliYIP---QNPYIY 417
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----------------LVPwkrRKKFLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 418 RLTL----QENVAFYQPTATKEAVLKAI----------EVAGLTELLaELPQGLDTMLgegeRHLSGGQAQRIALARAFL 483
Cdd:cd03267 95 RIGVvfgqKTQLWWDLPVIDSFYLLAAIydlpparfkkRLDELSELL-DLEELLDTPV----RQLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491368637 484 dQQRKILLFDEPTAHLDIETEVALKERMLPLMENR--LVFFATHRLHWMEEM-DEIIVMDQGRIVEQG 548
Cdd:cd03267 170 -HEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
343-551 |
8.58e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.93 E-value: 8.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 343 EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAF-----RQASWQEQLIYIPQNPYIY 417
Cdd:PRK11153 17 TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekelRKARRQIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 418 RlTLQENVAFyqptatkeavlkAIEVAGL---------TELLAelpqgldtMLGEGERH------LSGGQAQRIALARAf 482
Cdd:PRK11153 97 R-TVFDNVAL------------PLELAGTpkaeikarvTELLE--------LVGLSDKAdrypaqLSGGQKQRVAIARA- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 483 LDQQRKILLFDEPTAHLDIETEVA----LKE--RMLPLMenrlVFFATHrlhwmeEM-------DEIIVMDQGRIVEQGT 549
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSilelLKDinRELGLT----IVLITH------EMdvvkricDRVAVIDAGRLVEQGT 224
|
..
gi 491368637 550 LA 551
Cdd:PRK11153 225 VS 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
329-549 |
9.63e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.78 E-value: 9.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 329 DAQLTIDQLAFSYE--EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGE---ITLGGAKTTAFRQASW 403
Cdd:PRK13640 3 DNIVEFKHVSFTYPdsKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 404 QEQLIYIPQNP--YIYRLTLQENVAF------YQPTATKEAVLKAIEVAGLTELLAELPQgldtmlgegerHLSGGQAQR 475
Cdd:PRK13640 83 REKVGIVFQNPdnQFVGATVGDDVAFglenraVPRPEMIKIVRDVLADVGMLDYIDSEPA-----------NLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 476 IALArAFLDQQRKILLFDEPTAHLDIETevalKERMLPLM-----ENRL-VFFATHRLHWMEEMDEIIVMDQGRIVEQGT 549
Cdd:PRK13640 152 VAIA-GILAVEPKIIILDESTSMLDPAG----KEQILKLIrklkkKNNLtVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
345-549 |
1.08e-18 |
|
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: 86.16 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 345 AALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQE----QLIYIPQN----PYi 416
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSfallPH- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 417 yrLTLQENVAF-----YQPTATKEAV-LKAIEVAGLTELLAELPqgldtmlgegeRHLSGGQAQRIALARAfLDQQRKIL 490
Cdd:cd03294 117 --RTVLENVAFglevqGVPRAEREERaAEALELVGLEGWEHKYP-----------DELSGGMQQRVGLARA-LAVDPDIL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491368637 491 LFDEPTAHLD--IETEvaLKERMLPL--MENRLVFFATHRLHwmEEM---DEIIVMDQGRIVEQGT 549
Cdd:cd03294 183 LMDEAFSALDplIRRE--MQDELLRLqaELQKTIVFITHDLD--EALrlgDRIAIMKDGRLVQVGT 244
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
334-554 |
1.08e-18 |
|
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: 85.11 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 334 IDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAfRQASWQEQLIYIPQN 413
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 414 PYIYR-LTLQENVAFYqptatkeAVLKAIEVAGLTELLAELPQGLDtmLGEGERHL----SGGQAQRIALARAFLDQQRk 488
Cdd:cd03265 82 LSVDDeLTGWENLYIH-------ARLYGVPGAERRERIDELLDFVG--LLEAADRLvktySGGMRRRLEIARSLVHRPE- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491368637 489 ILLFDEPTAHLDIETEVALKERMLPLME--NRLVFFAThrlHWMEEM----DEIIVMDQGRIVEQGTLAQLQ 554
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTT---HYMEEAeqlcDRVAIIDHGRIIAEGTPEELK 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
332-550 |
1.62e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.52 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTT---AFRQASWQEQLI 408
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgAERGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 409 YIPQNpyiyrltLQENVAFYQPTAtkeAVLKAIEVAGLTELLAELpqGLDtmlGEGER---HLSGGQAQRIALARAfLDQ 485
Cdd:PRK11248 82 LPWRN-------VQDNVAFGLQLA---GVEKMQRLEIAHQMLKKV--GLE---GAEKRyiwQLSGGQRQRVGIARA-LAA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491368637 486 QRKILLFDEPTAHLDIETEVALKERMLPLMEN--RLVFFATHRLhwmEE----MDEIIVM--DQGRIVEQGTL 550
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITHDI---EEavfmATELVLLspGPGRVVERLPL 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
346-553 |
2.80e-18 |
|
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: 85.88 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVtgfKK---IGIIGLSGSGKSTLINTLSGFLVP---DSGEITLGG-----AKTTAFRQASWQEqlI-YIPQN 413
Cdd:COG0444 20 AVDGVSFDV---RRgetLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGedllkLSEKELRKIRGRE--IqMIFQD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 414 PYIY---RLT----LQENVAFYQPTATKEAVLKAIEvaglteLLAELpqGLDtmlgEGERH-------LSGGQAQRIALA 479
Cdd:COG0444 95 PMTSlnpVMTvgdqIAEPLRIHGGLSKAEARERAIE------LLERV--GLP----DPERRldrypheLSGGMRQRVMIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 480 RAfLDQQRKILLFDEPTAHLD--IETEV-----ALKERMlplmeNRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLA 551
Cdd:COG0444 163 RA-LALEPKLLIADEPTTALDvtIQAQIlnllkDLQREL-----GLAILFITHDLGVVAEIaDRVAVMYAGRIVEEGPVE 236
|
..
gi 491368637 552 QL 553
Cdd:COG0444 237 EL 238
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
339-553 |
3.29e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 84.50 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 339 FSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTaFRQASWQEQLI-YIPQNPYIY 417
Cdd:COG4167 21 FRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLE-YGDYKYRCKHIrMIFQDPNTS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 418 ---RLTLQEnvafyqptatkeavlkaievagltelLAELPQGLDTMLGEGERH-----------------------LSGG 471
Cdd:COG4167 100 lnpRLNIGQ--------------------------ILEEPLRLNTDLTAEEREerifatlrlvgllpehanfyphmLSSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 472 QAQRIALARAfLDQQRKILLFDEPTAHLDIETEVALKERMLPLMENR-LVF-FATHRLHWMEEM-DEIIVMDQGRIVEQG 548
Cdd:COG4167 154 QKQRVALARA-LILQPKIIIADEALAALDMSVRSQIINLMLELQEKLgISYiYVSQHLGIVKHIsDKVLVMHQGEVVEYG 232
|
....*
gi 491368637 549 TLAQL 553
Cdd:COG4167 233 KTAEV 237
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
361-553 |
7.55e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 84.78 E-value: 7.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 361 GIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQE-----QLIYipQNPYIY---RLTLQENVAF---YQ 429
Cdd:COG4608 48 GLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrrmQMVF--QDPYASlnpRMTVGDIIAEplrIH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 430 PTATKEAVLKAIEvagltELLAELpqGLDtmlgegERHL-------SGGQAQRIALARAfLDQQRKILLFDEPTAHLD-- 500
Cdd:COG4608 126 GLASKAERRERVA-----ELLELV--GLR------PEHAdryphefSGGQRQRIGIARA-LALNPKLIVCDEPVSALDvs 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491368637 501 IETEValkermLPLME---NRL----VFFAtHRLHWMEEM-DEIIVMDQGRIVEQGTLAQL 553
Cdd:COG4608 192 IQAQV------LNLLEdlqDELgltyLFIS-HDLSVVRHIsDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
345-503 |
9.84e-18 |
|
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: 82.07 E-value: 9.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 345 AALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRqaswQEQLIYIPQ--------NPYI 416
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLR----GRAIPYLRRkigvvfqdFRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 417 YRLTLQENVAF------YQPTATKEAVLKAIEVAGLTELLAELPQGldtmlgegerhLSGGQAQRIALARAFLDQQrKIL 490
Cdd:cd03292 91 PDRNVYENVAFalevtgVPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSP-TIL 158
|
170
....*....|...
gi 491368637 491 LFDEPTAHLDIET 503
Cdd:cd03292 159 IADEPTGNLDPDT 171
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
268-519 |
1.11e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.40 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 268 ILLFPaltILILAPEYF------------------------LPIRDFSS--DYHATLDgknAMTAVTEILHQPEAQVPAV 321
Cdd:COG4178 279 AVIFP---ILVAAPRYFageitlgglmqaasafgqvqgalsWFVDNYQSlaEWRATVD---RLAGFEEALEAADALPEAA 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 322 TVPRWQEDAQLTIDQLA-FSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFrq 400
Cdd:COG4178 353 SRIETSEDGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLF-- 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 401 aswqeqliyIPQNPYIYRLTLQENVAFYQPTA--TKEAVLKAIEVAGLTELLAELPQGLDTmlgegERHLSGGQAQRIAL 478
Cdd:COG4178 431 ---------LPQRPYLPLGTLREALLYPATAEafSDAELREALEAVGLGHLAERLDEEADW-----DQVLSLGEQQRLAF 496
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 491368637 479 ARAFLdQQRKILLFDEPTAHLDIETEvalkERMLPLMENRL 519
Cdd:COG4178 497 ARLLL-HKPDWLFLDEATSALDEENE----AALYQLLREEL 532
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
332-544 |
3.00e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.65 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASwqeqliyip 411
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDT--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 qnpyiyRLTLQE-----------NVAFYQPTATKEAVLKAIEVAGLTELLAELPQGldtmlgegerhLSGGQAQRIALAR 480
Cdd:PRK11247 84 ------RLMFQDarllpwkkvidNVGLGLKGQWRDAALQALAAVGLADRANEWPAA-----------LSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491368637 481 AFLDQQRkILLFDEPTAHLDIETEVALKERMLPLMENR--LVFFATHRLHWMEEM-DEIIVMDQGRI 544
Cdd:PRK11247 147 ALIHRPG-LLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
346-555 |
3.83e-17 |
|
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: 81.24 E-value: 3.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRqaswqeqliyiP------------QN 413
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP-----------PhriarlgiartfQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 414 PYIY-RLTLQENVAFYQPTATKEAVLKAI--------EVAGLT----ELLAELpqGLDTMLGEGERHLSGGQAQRIALAR 480
Cdd:COG0411 88 PRLFpELTVLENVLVAAHARLGRGLLAALlrlprarrEEREAReraeELLERV--GLADRADEPAGNLSYGQQRRLEIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 481 AfLDQQRKILLFDEPTAHLDieteVALKERMLPLM------ENRLVFFATHRLHW-MEEMDEIIVMDQGRIVEQGTLAQL 553
Cdd:COG0411 166 A-LATEPKLLLLDEPAAGLN----PEETEELAELIrrlrdeRGITILLIEHDMDLvMGLADRIVVLDFGRVIAEGTPAEV 240
|
..
gi 491368637 554 QQ 555
Cdd:COG0411 241 RA 242
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
344-544 |
4.16e-17 |
|
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: 79.40 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 344 KAALTDINLNVtgfKK---IGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLI-YIPQNPYIYRL 419
Cdd:cd03215 13 KGAVRDVSFEV---RAgeiVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIaYVPEDRKREGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 420 TLQENVAfyqptatkeavlkaiEVAGLTellaelpqgldtmlgegeRHLSGGQAQRIALARAFLdQQRKILLFDEPTAHL 499
Cdd:cd03215 90 VLDLSVA---------------ENIALS------------------SLLSGGNQQKVVLARWLA-RDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491368637 500 DIETEVALKERMLPL-MENRLVFFAThrlhwmEEMDE-------IIVMDQGRI 544
Cdd:cd03215 136 DVGAKAEIYRLIRELaDAGKAVLLIS------SELDEllglcdrILVMYEGRI 182
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
323-548 |
4.38e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 83.35 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 323 VPRWQEDAQ------LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTT 396
Cdd:PRK11607 5 IPRPQAKTRkaltplLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 397 afRQASWQEQLIYIPQNPYIY-RLTLQENVAFyqptATKEAVLKAIEVAGLTELLAELPQgLDTMLGEGERHLSGGQAQR 475
Cdd:PRK11607 85 --HVPPYQRPINMMFQSYALFpHMTVEQNIAF----GLKQDKLPKAEIASRVNEMLGLVH-MQEFAKRKPHQLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 476 IALARAfLDQQRKILLFDEPTAHLDIEtevaLKERM----LPLMENRLV--FFATH-RLHWMEEMDEIIVMDQGRIVEQG 548
Cdd:PRK11607 158 VALARS-LAKRPKLLLLDEPMGALDKK----LRDRMqlevVDILERVGVtcVMVTHdQEEAMTMAGRIAIMNRGKFVQIG 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
332-548 |
5.16e-17 |
|
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: 80.02 E-value: 5.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTtafrQASWQEQLIYIP 411
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNPYIYR-LTLQENVAF------YQPTATKEAVLKAIEVAGLTELLAelpQGLDTmlgegerhLSGGQAQRIALARAFLd 484
Cdd:cd03269 77 EERGLYPkMKVIDQLVYlaqlkgLKKEEARRRIDEWLERLELSEYAN---KRVEE--------LSKGNQQKVQFIAAVI- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491368637 485 QQRKILLFDEPTAHLD-IETEVaLKERMLPLMEN-RLVFFATHRLHWMEEM-DEIIVMDQGRIVEQG 548
Cdd:cd03269 145 HDPELLILDEPFSGLDpVNVEL-LKDVIRELARAgKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
330-548 |
5.33e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.47 E-value: 5.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 330 AQLTIDQLAFSYEE-KAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTtafRQASWQEQLI 408
Cdd:PRK15056 5 AGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT---RQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 409 YIPQNpyiyrltlqENVAFYQPTATKEAVL-------------KAIEVAGLTELLAELpqgldTMLGEGERH---LSGGQ 472
Cdd:PRK15056 82 YVPQS---------EEVDWSFPVLVEDVVMmgryghmgwlrraKKRDRQIVTAALARV-----DMVEFRHRQigeLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 473 AQRIALARAfLDQQRKILLFDEPTAHLDIETEValkeRMLPLM-----ENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQ 547
Cdd:PRK15056 148 KKRVFLARA-IAQQGQVILLDEPFTGVDVKTEA----RIISLLrelrdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLAS 222
|
.
gi 491368637 548 G 548
Cdd:PRK15056 223 G 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
353-548 |
6.43e-17 |
|
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: 79.13 E-value: 6.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 353 NVTGFKK----IGIIGLSGSGKSTLINTLSGFLVP--DSGEITLGGAKTTAFrqaSWQEQLIYIPQNPYIY-RLTLQENV 425
Cdd:cd03213 27 NVSGKAKpgelTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKR---SFRKIIGYVPQDDILHpTLTVRETL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 426 AFyqptatkeavlkaievagltelLAELpqgldtmlgegeRHLSGGQAQRIALARAFLDQQRkILLFDEPTAHLDIETEV 505
Cdd:cd03213 104 MF----------------------AAKL------------RGLSGGERKRVSIALELVSNPS-LLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491368637 506 ALkerMLPLM----ENRLVFFATHRLHW-MEEM-DEIIVMDQGRIVEQG 548
Cdd:cd03213 149 QV---MSLLRrladTGRTIICSIHQPSSeIFELfDKLLLLSQGRVIYFG 194
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
362-525 |
8.07e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 8.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 362 IIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQAswqEQLIYI-PQNPYIYRLTLQENVAFY-----QPTATKE 435
Cdd:PRK13539 33 LTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVA---EACHYLgHRNAMKPALTVAENLEFWaaflgGEELDIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 436 AVLKAIEVAGLTELLAelpqgldtmlgegeRHLSGGQAQRIALARaFLDQQRKILLFDEPTAHLDieteVALKERMLPLM 515
Cdd:PRK13539 110 AALEAVGLAPLAHLPF--------------GYLSAGQKRRVALAR-LLVSNRPIWILDEPTAALD----AAAVALFAELI 170
|
170
....*....|....*
gi 491368637 516 ENRL-----VFFATH 525
Cdd:PRK13539 171 RAHLaqggiVIAATH 185
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
327-555 |
8.46e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.60 E-value: 8.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 327 QEDAQLTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQ 406
Cdd:PRK10575 7 HSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 407 LIYIPQN-PYIYRLTLQENVAFYQ----------PTATKEAVLKAIEVAGLTELLAELpqgLDTmlgegerhLSGGQAQR 475
Cdd:PRK10575 87 VAYLPQQlPAAEGMTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRL---VDS--------LSGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 476 IALArAFLDQQRKILLFDEPTAHLDIETEV---ALKERMlpLMENRLVFFAThrLHWMEEM----DEIIVMDQGRIVEQG 548
Cdd:PRK10575 156 AWIA-MLVAQDSRCLLLDEPTSALDIAHQVdvlALVHRL--SQERGLTVIAV--LHDINMAarycDYLVALRGGEMIAQG 230
|
....*..
gi 491368637 549 TLAQLQQ 555
Cdd:PRK10575 231 TPAELMR 237
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
331-553 |
1.09e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 80.01 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 331 QLTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYI 410
Cdd:PRK10619 5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 411 PQNPYI-YRLTLQ-ENVAFYQPTATKEAVLKA-IEVAGLTELLA-ELPQGLDTMLGEGER-------HLSGGQAQRIALA 479
Cdd:PRK10619 85 NQLRLLrTRLTMVfQHFNLWSHMTVLENVMEApIQVLGLSKQEArERAVKYLAKVGIDERaqgkypvHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 480 RAfLDQQRKILLFDEPTAHLDIEtevaLKERMLPLM-----ENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQL 553
Cdd:PRK10619 165 RA-LAMEPEVLLFDEPTSALDPE----LVGEVLRIMqqlaeEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQL 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
332-570 |
1.11e-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: 82.93 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGF--LVPDSGEI--------------------- 388
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 389 --TLGGAKTTAFRQASWQeqliyiPQNPYIYRLT------LQENVAFYQPTATKEAVLKAIEVAGLT---------ELLA 451
Cdd:TIGR03269 81 pcPVCGGTLEPEEVDFWN------LSDKLRRRIRkriaimLQRTFALYGDDTVLDNVLEALEEIGYEgkeavgravDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 452 ELpqGLDTMLGEGERHLSGGQAQRIALARAfLDQQRKILLFDEPTAHLDIETEVALKERMLPLM-ENRLVFFATHrlHWM 530
Cdd:TIGR03269 155 MV--QLSHRITHIARDLSGGEKQRVVLARQ-LAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTS--HWP 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 491368637 531 EEMDEI----IVMDQGRIVEQGTLAQLQQKqgaFTELVNGMRRE 570
Cdd:TIGR03269 230 EVIEDLsdkaIWLENGEIKEEGTPDEVVAV---FMEGVSEVEKE 270
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
332-500 |
1.27e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.99 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDIN--LNVTGFKKIgiIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIY 409
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISfsLRAGEFKLI--TGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 IPQNPYIYRLTLQENVAF-YQptATKEAVLKAIEVAGLTELlaELPqglDTMLGEGERHLSGGQAQRIALAR--AFLDqq 486
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIFpWQ--IRNQQPDPAIFLDDLERF--ALP---DTILTKNIAELSGGEKQRISLIRnlQFMP-- 156
|
170
....*....|....
gi 491368637 487 rKILLFDEPTAHLD 500
Cdd:PRK10247 157 -KVLLLDEITSALD 169
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
332-500 |
2.20e-16 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 78.74 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTA---FRQAswQEQLI 408
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmHKRA--RLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 409 YIPQNPYIYR-LTLQENVAFYQPTATKeavLKAIEVAGLTELLAELpqGLDTMLGEGERHLSGGQAQRIALARAfLDQQR 487
Cdd:cd03218 79 YLPQEASIFRkLTVEENILAVLEIRGL---SKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARA-LATNP 152
|
170
....*....|...
gi 491368637 488 KILLFDEPTAHLD 500
Cdd:cd03218 153 KFLLLDEPFAGVD 165
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
15-546 |
2.27e-16 |
|
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: 82.15 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 15 LLGLLAGLSFLQALFIIGQAYGLARAITGlwegRPLeeqWGWILLFFCSFIARqaviyFRSKRLDDYSYQQA-ADLRDQL 93
Cdd:COG4615 20 LLGLLSGLANAGLIALINQALNATGAALA----RLL---LLFAGLLVLLLLSR-----LASQLLLTRLGQHAvARLRLRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 94 LEKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIMNMSIipwVILALVfYLDWESGLVLLLVFpLIIIFMII 173
Cdd:COG4615 88 SRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSVAL---VLGCLA-YLAWLSPPLFLLTL-VLLGLGVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 174 LGYAAQSKAEK---QYRTFQL-LSNHFIDSLRGIDTLKLfgvSKKYGKSIF-----ASSERFRKATM-ASLKVGILSTFA 243
Cdd:COG4615 163 GYRLLVRRARRhlrRAREAEDrLFKHFRALLEGFKELKL---NRRRRRAFFdedlqPTAERYRDLRIrADTIFALANNWG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 244 LDFFTTLSIAVVAVLLGLRLINEGILLFPALTILilapeyFL--PIRDFSSDYHATLDGKNAMTAVTEI---LHQPEAQV 318
Cdd:COG4615 240 NLLFFALIGLILFLLPALGWADPAVLSGFVLVLL------FLrgPLSQLVGALPTLSRANVALRKIEELelaLAAAEPAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 319 PAVTVPRWQEDAQ-LTIDQLAFSYEEKA-----ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGG 392
Cdd:COG4615 314 ADAAAPPAPADFQtLELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 393 AKTTAFRQASWQEQLIYIPQNPYIY-RLtlqenvafYQPTAtkeavlkAIEVAGLTELLAELpqGLD--TMLGEGE---R 466
Cdd:COG4615 394 QPVTADNREAYRQLFSAVFSDFHLFdRL--------LGLDG-------EADPARARELLERL--ELDhkVSVEDGRfstT 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 467 HLSGGQAQRIALARAFLDqQRKILLFDEPTAHLDIE------TEV--ALKERmlplmeNRLVFFATHRLHWMEEMDEIIV 538
Cdd:COG4615 457 DLSQGQRKRLALLVALLE-DRPILVFDEWAADQDPEfrrvfyTELlpELKAR------GKTVIAISHDDRYFDLADRVLK 529
|
....*...
gi 491368637 539 MDQGRIVE 546
Cdd:COG4615 530 MDYGKLVE 537
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
16-279 |
2.41e-16 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 79.22 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 16 LGLLAGLSFLQALFIIGQAYGLARAITGLWEGRPLEEQ----WGWILLFFCsfIARQAVIYFRSKRLDDYSYQQAADLRD 91
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQalnvYSLALLLLG--LAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 92 QLLEKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIMNMSIIPWVILALVFYLDWESGLVLLLVFPLIIIFM 171
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 172 IILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKYGKSIFASSERFRKATMASLKVGILSTFALDFFTTLS 251
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260
....*....|....*....|....*...
gi 491368637 252 IAVVAvLLGLRLINEGILLFPALTILIL 279
Cdd:pfam00664 239 YALAL-WFGAYLVISGELSVGDLVAFLS 265
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
332-549 |
2.42e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 79.67 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKA-----ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTA-------FR 399
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkikeVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 400 QASWQEQLIYIPQNPYIYRLTLQENVAF--YQPTATKEAVLKAIevaglTEL--LAELPQgldTMLGEGERHLSGGQAQR 475
Cdd:PRK13645 87 RLRKEIGLVFQFPEYQLFQETIEKDIAFgpVNLGENKQEAYKKV-----PELlkLVQLPE---DYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491368637 476 IALArAFLDQQRKILLFDEPTAHLDIETE---VALKERMLPLMENRLVfFATHRL-HWMEEMDEIIVMDQGRIVEQGT 549
Cdd:PRK13645 159 VALA-GIIAMDGNTLVLDEPTGGLDPKGEedfINLFERLNKEYKKRII-MVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
362-552 |
2.48e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.69 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 362 IIGLSGSGKSTLINTLSGFLVPDSGEITLGGakttafRQASWQEQLIYIPQNP----YIY---RL----TLQENVAFYQP 430
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNG------RVLFDAEKGICLPPEKrrigYVFqdaRLfphyKVRGNLRYGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 431 TATKEAVLKAIEVAGLTELLAELPqgldtmlgegeRHLSGGQAQRIALARAFLDQQrKILLFDEPTAHLDIETevalKER 510
Cdd:PRK11144 103 KSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAP-ELLLMDEPLASLDLPR----KRE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491368637 511 MLPLMEnRL-------VFFATHRLhwmeemDEI-------IVMDQGRIVEQGTLAQ 552
Cdd:PRK11144 167 LLPYLE-RLareinipILYVSHSL------DEIlrladrvVVLEQGKVKAFGPLEE 215
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
343-548 |
2.76e-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: 78.08 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 343 EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGfLVPD----SGEITLGGAKTTAfrqASWQEQLIYIPQNPYIYR 418
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGggttSGQILFNGQPRKP---DQFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 419 -LTLQENVAFYQ----PTATKEAVLKAIEVAGLTELLAELPQGLDTMLGegerhLSGGQAQRIALARAFLdQQRKILLFD 493
Cdd:cd03234 95 gLTVRETLTYTAilrlPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKG-----ISGGERRRVSIAVQLL-WDPKVLILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491368637 494 EPTAHLD-------IETEVALKERmlplmeNRLVFFATH--RLHWMEEMDEIIVMDQGRIVEQG 548
Cdd:cd03234 169 EPTSGLDsftalnlVSTLSQLARR------NRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
344-512 |
3.74e-16 |
|
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: 81.52 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 344 KAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLG-GAKTTafrqaswqeqliYIPQNPYI-YRLTL 421
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVG------------YLPQEPQLdPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 422 QENV-------------------AFYQPTATKEAVLK-------AIEVAGLTELLAELPQGLDTM-LGEGE---RHLSGG 471
Cdd:TIGR03719 86 RENVeegvaeikdaldrfneisaKYAEPDADFDKLAAeqaelqeIIDAADAWDLDSQLEIAMDALrCPPWDadvTKLSGG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491368637 472 QAQRIALARAFLdQQRKILLFDEPTAHLDIETeVALKERML 512
Cdd:TIGR03719 166 ERRRVALCRLLL-SKPDMLLLDEPTNHLDAES-VAWLERHL 204
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
322-553 |
4.20e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 78.15 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 322 TVPRWQEDAQLTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGF--LVPD---SGEITLGGaktt 396
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDG---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 397 afrqaswqeQLIYIPQ-----------------NPY---IYrltlqENVAF-------YQPTATKEAVLKAIEVAGL-TE 448
Cdd:COG1117 78 ---------EDIYDPDvdvvelrrrvgmvfqkpNPFpksIY-----DNVAYglrlhgiKSKSELDEIVEESLRKAALwDE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 449 LLAELPQ-GLDtmlgegerhLSGGQAQRIALARAfLDQQRKILLFDEPTAHLD-IETEvALKERMLPLMENRLVFFATHR 526
Cdd:COG1117 144 VKDRLKKsALG---------LSGGQQQRLCIARA-LAVEPEVLLMDEPTSALDpISTA-KIEELILELKKDYTIVIVTHN 212
|
250 260 270
....*....|....*....|....*....|....
gi 491368637 527 lhwmeeM-------DEIIVMDQGRIVEQGTLAQL 553
Cdd:COG1117 213 ------MqqaarvsDYTAFFYLGELVEFGPTEQI 240
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
331-525 |
4.49e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.15 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 331 QLTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRqASWQEQLIYI 410
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 411 PQNPYIYR-LTLQENVAFYQP---TATKEAVLKAIEVAGLT---ELLAelpqgldtmlgegeRHLSGGQAQRIALARAFL 483
Cdd:PRK13538 80 GHQPGIKTeLTALENLRFYQRlhgPGDDEALWEALAQVGLAgfeDVPV--------------RQLSAGQQRRVALARLWL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491368637 484 DqQRKILLFDEP-TAhLDIETeVALKERmlpLMENRL-----VFFATH 525
Cdd:PRK13538 146 T-RAPLWILDEPfTA-IDKQG-VARLEA---LLAQHAeqggmVILTTH 187
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
332-569 |
4.83e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.13 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSG----------EITLGGAKTTAFRQA 401
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 402 SWQEQLIYiPQNPYIYRLTLQENV---------------AFYQPtATKEAVLKAIEVAGLTELLAelpQGLDTmlgeger 466
Cdd:PRK09984 85 RANTGYIF-QQFNLVNRLSVLENVligalgstpfwrtcfSWFTR-EQKQRALQALTRVGMVHFAH---QRVST------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 467 hLSGGQAQRIALARAFLdQQRKILLFDEPTAHLDIETEVALKERMLPLMENR--LVFFATHRLHW-MEEMDEIIVMDQGR 543
Cdd:PRK09984 153 -LSGGQQQRVAIARALM-QQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYaLRYCERIVALRQGH 230
|
250 260
....*....|....*....|....*.
gi 491368637 544 IVEQGTLAQLQQKQgaFTELVNGMRR 569
Cdd:PRK09984 231 VFYDGSSQQFDNER--FDHLYRSINR 254
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
340-528 |
7.85e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.12 E-value: 7.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 340 SYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAfrqaswqeqliYIPQNPYIYR- 418
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVA-----------YVPQRSEVPDs 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 419 --LTLQENVA---------FYQPTATKEAVL-KAIEVAGLTELlaeLPQGLDTmlgegerhLSGGQAQRIALARAFLdQQ 486
Cdd:NF040873 70 lpLTVRDLVAmgrwarrglWRRLTRDDRAAVdDALERVGLADL---AGRQLGE--------LSGGQRQRALLAQGLA-QE 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491368637 487 RKILLFDEPTAHLDIETEVALKERMLPLM-ENRLVFFATHRLH 528
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLE 180
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
344-553 |
8.51e-16 |
|
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: 77.54 E-value: 8.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 344 KAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEIT--------LGGAKTTAFR---QASWQEQliYIPQ 412
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfrgqdlyqLDRKQRRAFRrdvQLVFQDS--PSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 413 NPyiyRLTLQENVAfyQPTATKEAVLKAIEVAGLTELLAELpqGLDT-MLGEGERHLSGGQAQRIALARAfLDQQRKILL 491
Cdd:TIGR02769 102 NP---RMTVRQIIG--EPLRHLTSLDESEQKARIAELLDMV--GLRSeDADKLPRQLSGGQLQRINIARA-LAVKPKLIV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491368637 492 FDEPTAHLDIETEVALKERMLPL-MENRLVF-FATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQL 553
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRKLqQAFGTAYlFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQL 238
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
341-564 |
9.21e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 78.59 E-value: 9.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 341 YEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGG----AKTTAFR--------QASwqeQLI 408
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfKRRKEFArrigvvfgQRS---QLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 409 Y-IPQ------NPYIYRL---TLQENVAFYqptatkeavlkaIEVAGLTELlaelpqgLDTMLgegeRHLSGGQAQRIAL 478
Cdd:COG4586 109 WdLPAidsfrlLKAIYRIpdaEYKKRLDEL------------VELLDLGEL-------LDTPV----RQLSLGQRMRCEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 479 ARAFLdQQRKILLFDEPTAHLDIETEVA----LKErmlplmENRL----VFFATHRLHWMEEM-DEIIVMDQGRIVEQGT 549
Cdd:COG4586 166 AAALL-HRPKILFLDEPTIGLDVVSKEAirefLKE------YNRErgttILLTSHDMDDIEALcDRVIVIDHGRIIYDGS 238
|
250
....*....|....*
gi 491368637 550 LAQLQQKQGAFTELV 564
Cdd:COG4586 239 LEELKERFGPYKTIV 253
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
344-554 |
1.14e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.42 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 344 KAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQE-----QLIY--------- 409
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrdiQMVFqdsisavnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 ------IPQNPYIYRLTLQENvafyQPTATKEAVLKAIEVAglTELLAELPQgldtmlgegerHLSGGQAQRIALARAfL 483
Cdd:PRK10419 105 rktvreIIREPLRHLLSLDKA----ERLARASEMLRAVDLD--DSVLDKRPP-----------QLSGGQLQRVCLARA-L 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 484 DQQRKILLFDEPTAHLDIetevALKERMLPLMEnRL-------VFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQLQ 554
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDL----VLQAGVIRLLK-KLqqqfgtaCLFITHDLRLVERFcQRVMVMDNGQIVETQPVGDKL 240
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
358-553 |
1.46e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.14 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 358 KKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTaFRQASWQEQLI-YIPQNP-----------YIYRLTLQENV 425
Cdd:PRK15112 40 QTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSQRIrMIFQDPstslnprqrisQILDFPLRLNT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 426 AFyQPTATKEAVLKAIEVAGLtellaeLPQGLDTMlgegERHLSGGQAQRIALARAfLDQQRKILLFDEPTAHLDIETEV 505
Cdd:PRK15112 119 DL-EPEQREKQIIETLRQVGL------LPDHASYY----PHMLAPGQKQRLGLARA-LILRPKVIIADEALASLDMSMRS 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491368637 506 ALKERMLPLMENRLV--FFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQL 553
Cdd:PRK15112 187 QLINLMLELQEKQGIsyIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADV 237
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
343-549 |
1.48e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.18 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 343 EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTA------FRQASWQEQLIYIPQNPYI 416
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnknLKKLRKKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 417 YRLTLQENVAF------YQPTATKEAVLKAIEVAGLTELLAElpqgldtmlgEGERHLSGGQAQRIALARAFLDQQrKIL 490
Cdd:PRK13641 99 FENTVLKDVEFgpknfgFSEDEAKEKALKWLKKVGLSEDLIS----------KSPFELSGGQMRRVAIAGVMAYEP-EIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491368637 491 LFDEPTAHLDIETevalKERMLPLMEN-----RLVFFATHRLHWMEE-MDEIIVMDQGRIVEQGT 549
Cdd:PRK13641 168 CLDEPAAGLDPEG----RKEMMQLFKDyqkagHTVILVTHNMDDVAEyADDVLVLEHGKLIKHAS 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
332-548 |
1.62e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.97 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQA--SWQEQLIY 409
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 IPQNP--YIYRLTLQENVAFyqptatkeaVLKAIEVAGlTELLAELPQGLDTMLGEGERH-----LSGGQAQRIALARAF 482
Cdd:PRK13638 82 VFQDPeqQIFYTDIDSDIAF---------SLRNLGVPE-AEITRRVDEALTLVDAQHFRHqpiqcLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 483 LDQQRKILLfDEPTAHLDIETE---VALKERMlpLMENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQG 548
Cdd:PRK13638 152 VLQARYLLL-DEPTAGLDPAGRtqmIAIIRRI--VAQGNHVIISSHDIDLIYEIsDAVYVLRQGQILTHG 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
332-550 |
1.63e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.01 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVT----GFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAK----TTAFRQASW 403
Cdd:PRK11629 6 LQCDNLCKRYQEGSVQTDVLHNVSfsigEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmsklSSAAKAELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 404 QEQLIYIPQNPYIY-RLTLQENVA---FYQPTATKEAVLKAIevagltELLAELpqGLDTMLGEGERHLSGGQAQRIALA 479
Cdd:PRK11629 86 NQKLGFIYQFHHLLpDFTALENVAmplLIGKKKPAEINSRAL------EMLAAV--GLEHRANHRPSELSGGERQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491368637 480 RAFLDQQRkILLFDEPTAHLDIETEVALKERMLPLMENRLVFF--ATHRLHWMEEMDEIIVMDQGRIVEQGTL 550
Cdd:PRK11629 158 RALVNNPR-LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFlvVTHDLQLAKRMSRQLEMRDGRLTAELSL 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
330-548 |
1.87e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 76.49 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 330 AQLTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGF--LVPD---SGEITLGGAKTTAFRQASWQ 404
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 405 E--QLIYIPQNPyIYRLTLQENVAF--------YQPTATKEAVLKAIEVAGLTEllaELPQGLDTMLGEgerhLSGGQAQ 474
Cdd:PRK14247 82 RrvQMVFQIPNP-IPNLSIFENVALglklnrlvKSKKELQERVRWALEKAQLWD---EVKDRLDAPAGK----LSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491368637 475 RIALARAfLDQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQG 548
Cdd:PRK14247 154 RLCIARA-LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWG 227
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
347-552 |
2.89e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 75.65 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 347 LTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGfLVPDSGEITLGGaktTAFRQASWQE---QLIYIPQN-------PYI 416
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNG---RPLSDWSAAElarHRAYLSQQqsppfamPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 417 YRLTLqenvaFYQPTATKEAVLKAIEVagLTELLaelpqGLDTMLGEGERHLSGGQAQRIALARAFL------DQQRKIL 490
Cdd:COG4138 88 QYLAL-----HQPAGASSEAVEQLLAQ--LAEAL-----GLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptiNPEGQLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 491 LFDEPTAHLDIETEVALkERMLplmeNRL------VFFATHRL-HWMEEMDEIIVMDQGRIVEQGTLAQ 552
Cdd:COG4138 156 LLDEPMNSLDVAQQAAL-DRLL----RELcqqgitVVMSSHDLnHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
334-548 |
2.91e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 76.31 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 334 IDQLAFSYEE-KAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQ 412
Cdd:PRK13647 7 VEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 413 NP--YIYRLTLQENVAF------YQPTATKEAVLKAIEVAGLTELLAELPQgldtmlgegerHLSGGQAQRIALArAFLD 484
Cdd:PRK13647 87 DPddQVFSSTVWDDVAFgpvnmgLDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIA-GVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491368637 485 QQRKILLFDEPTAHLDIETEVALKERMLPLMEN-RLVFFATHRLHWMEE-MDEIIVMDQGRIVEQG 548
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEG 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
332-541 |
3.59e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.54 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEItlggakttafrQASWQEQLIYIP 411
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNPYIyRLTLQENVAFY---QPTATKEAVLKAIEVAGLTELLAELPQgldtmlgegerHLSGGQAQRIALARAFLDQQrK 488
Cdd:PRK09544 74 QKLYL-DTTLPLTVNRFlrlRPGTKKEDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALLNRP-Q 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491368637 489 ILLFDEPTAHLDIETEVALKERMLPLME--NRLVFFATHRLHW-MEEMDEIIVMDQ 541
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLvMAKTDEVLCLNH 196
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
362-549 |
4.95e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.97 E-value: 4.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 362 IIGLSGSGKSTLINTLSGfLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQN-------PYIYRLTLqenvafYQPT-AT 433
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqtppfamPVFQYLTL------HQPDkTR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 434 KEAVLKAIEVagLTELLaelpqGLDTMLGEGERHLSGGQAQRIALARAFLDQQRKI------LLFDEPTAHLDIETEVAL 507
Cdd:PRK03695 100 TEAVASALNE--VAEAL-----GLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpagqlLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491368637 508 kERMLPLM--ENRLVFFATHRL-HWMEEMDEIIVMDQGRIVEQGT 549
Cdd:PRK03695 173 -DRLLSELcqQGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGR 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
332-549 |
7.51e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 75.20 E-value: 7.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYE-----EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTA------FRQ 400
Cdd:PRK13646 3 IRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 401 ASWQEQLIYIPQNPYIYRLTLQENVAFyQPTATKEAVLKAIEVAglTELLAELPQGLDTMlGEGERHLSGGQAQRIALAr 480
Cdd:PRK13646 83 VRKRIGMVFQFPESQLFEDTVEREIIF-GPKNFKMNLDEVKNYA--HRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIV- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491368637 481 AFLDQQRKILLFDEPTAHLDIETEVALKE--RMLPLMENRLVFFATHRlhwMEEM----DEIIVMDQGRIVEQGT 549
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRllKSLQTDENKTIILVSHD---MNEVaryaDEVIVMKEGSIVSQTS 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
349-553 |
8.49e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 75.91 E-value: 8.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 349 DINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTafrQASWQEQLIYIPQNPYIY--RLTLQENVA 426
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT---HRSIQQRDICMVFQSYALfpHMSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 427 F-----YQPTA-TKEAVLKAIEVAGLTellaelpqgldtmlGEGERH---LSGGQAQRIALARAfLDQQRKILLFDEPTA 497
Cdd:PRK11432 101 YglkmlGVPKEeRKQRVKEALELVDLA--------------GFEDRYvdqISGGQQQRVALARA-LILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 498 HLDIETEVALKERMLPLmENRLVFFATHRLHWMEEM----DEIIVMDQGRIVEQGTLAQL 553
Cdd:PRK11432 166 NLDANLRRSMREKIREL-QQQFNITSLYVTHDQSEAfavsDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
331-548 |
8.58e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 75.51 E-value: 8.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 331 QLTIDQLAFSYEEKA-----ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITL----GGAKTTAFRQA 401
Cdd:PRK13651 2 QIKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 402 SWQEQLIYipQNPYI---------------------YRL---TLQENVAF------YQPTATKEAVLKAIEVAGLTElla 451
Cdd:PRK13651 82 KVLEKLVI--QKTRFkkikkikeirrrvgvvfqfaeYQLfeqTIEKDIIFgpvsmgVSKEEAKKRAAKYIELVGLDE--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 452 elpqgldTMLGEGERHLSGGQAQRIALArAFLDQQRKILLFDEPTAHLDietEVALKErMLPLMEN-----RLVFFATHR 526
Cdd:PRK13651 157 -------SYLQRSPFELSGGQKRRVALA-GILAMEPDFLVFDEPTAGLD---PQGVKE-ILEIFDNlnkqgKTIILVTHD 224
|
250 260
....*....|....*....|...
gi 491368637 527 L-HWMEEMDEIIVMDQGRIVEQG 548
Cdd:PRK13651 225 LdNVLEWTKRTIFFKDGKIIKDG 247
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
352-571 |
9.43e-15 |
|
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: 78.13 E-value: 9.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 352 LNVTGFKK--IGIIGLSGSGKSTLINTLSGFLVPDSGEITLGG----AKTTAFRQAswqeqLIYIPQ-NPYIYRLTLQEN 424
Cdd:TIGR01257 949 LNITFYENqiTAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdieTNLDAVRQS-----LGMCPQhNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 425 VAFYQPTATKEAVLKAIEVAGLTEllaelPQGLDTMLGEGERHLSGGQAQRIALARAFLDQQrKILLFDEPTAHLDIETE 504
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAQLEMEAMLE-----DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDA-KVVVLDEPTSGVDPYSR 1097
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 505 VALKERMLPLMENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQLQQ--KQGAFTELVNGMRREQ 571
Cdd:TIGR01257 1098 RSIWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGTPLFLKNcfGTGFYLTLVRKMKNIQ 1167
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
332-553 |
9.70e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.77 E-value: 9.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSY---EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLI 408
Cdd:PRK13650 5 IEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 409 YIPQNP--YIYRLTLQENVAF--------YQptATKEAVLKAIEVAGLTELLAELPQgldtmlgegerHLSGGQAQRIAL 478
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFglenkgipHE--EMKERVNEALELVGMQDFKEREPA-----------RLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491368637 479 ARAfLDQQRKILLFDEPTAHLDIETEVALKERMLPLME--NRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQL 553
Cdd:PRK13650 152 AGA-VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
340-548 |
1.01e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.64 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 340 SYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAfRQASWQEQLIYIPQNPYIYR- 418
Cdd:PRK13536 50 SYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQFDNLDLe 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 419 LTLQENVAFY-----QPTATKEAVLKAievagLTElLAELPQGLDTMLGEgerhLSGGQAQRIALARAFLDQQrKILLFD 493
Cdd:PRK13536 129 FTVRENLLVFgryfgMSTREIEAVIPS-----LLE-FARLESKADARVSD----LSGGMKRRLTLARALINDP-QLLILD 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 494 EPTAHLDIETEVALKERMLPLMENRLVFFAThrLHWMEEM----DEIIVMDQGRIVEQG 548
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLT--THFMEEAerlcDRLCVLEAGRKIAEG 254
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
362-553 |
1.03e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.01 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 362 IIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIY-IPQNPYIY-RLTLQENVAFYQPtatKEAVLK 439
Cdd:PRK15439 42 LLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYlVPQEPLLFpNLSVKENILFGLP---KRQASM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 440 aievAGLTELLAELPQGLDTMLGEGErhLSGGQAQRIALARAFLdQQRKILLFDEPTAHLD-IETEvALKERMLPLMENR 518
Cdd:PRK15439 119 ----QKMKQLLAALGCQLDLDSSAGS--LEVADRQIVEILRGLM-RDSRILILDEPTASLTpAETE-RLFSRIRELLAQG 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 491368637 519 L-VFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQL 553
Cdd:PRK15439 191 VgIVFISHKLPEIRQLaDRISVMRDGTIALSGKTADL 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
338-548 |
1.10e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 73.34 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 338 AFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGG------AKTTAFrqaswqeqliyip 411
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvssllGLGGGF------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 qNPyiyRLTLQENVAFY-----QPTATKEAVLKAIEVagltelLAELPQGLDTMLgegeRHLSGGQAQRIALARAfLDQQ 486
Cdd:cd03220 96 -NP---ELTGRENIYLNgrllgLSRKEIDEKIDEIIE------FSELGDFIDLPV----KTYSSGMKARLAFAIA-TALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491368637 487 RKILLFDEPTAHLDieteVALKERMLPLMENRL-----VFFATHRLHWMEEM-DEIIVMDQGRIVEQG 548
Cdd:cd03220 161 PDILLIDEVLAVGD----AAFQEKCQRRLRELLkqgktVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
16-292 |
1.50e-14 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 74.38 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 16 LGLLAGLSFLQALFIIGQAYGLARAITGLWEGRPLEEQWGWILLFFCSFIARQAVIYFRSKRLDDYSYQQAADLRDQLLE 95
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 96 KLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIMN--MSIIpwVILALVFYLDWESGLVLLLVFPLIIIFMII 173
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRdpLTVI--GLLGVLFYLDWKLTLIALVVLPLAALPIRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 174 LGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKYGKSIFASSERFRKATMASLKVGILSTFALDFFTTLSIA 253
Cdd:cd18552 159 IGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 491368637 254 VVaVLLGLRLINEGIL----LFPALTILILAPEyflPIRDFSS 292
Cdd:cd18552 239 LV-LWYGGYQVISGELtpgeFISFITALLLLYQ---PIKRLSN 277
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
339-553 |
1.87e-14 |
|
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: 73.20 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 339 FSYEEKAALTDINLNVtgfkKIG----IIGLSGSGKSTLINTLSGFLVPDSG-EITLGGAKttaFRQASWQE--QLIYI- 410
Cdd:COG1119 11 VRRGGKTILDDISWTV----KPGehwaILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGER---RGGEDVWElrKRIGLv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 411 -P--QNPYIYRLTLQENV--AFY-----QPTATKEAVLKAievaglTELLAELpqGLDTMLGEGERHLSGGQAQRIALAR 480
Cdd:COG1119 84 sPalQLRFPRDETVLDVVlsGFFdsiglYREPTDEQRERA------RELLELL--GLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491368637 481 AFLDQQRkILLFDEPTAHLDIETEVALKERMLPLMENR---LVfFATHRLH-WMEEMDEIIVMDQGRIVEQGTLAQL 553
Cdd:COG1119 156 ALVKDPE-LLILDEPTAGLDLGARELLLALLDKLAAEGaptLV-LVTHHVEeIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
346-546 |
1.89e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.10 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGaKTTAFRQAS----------WQEqLIYIPQnpy 415
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG-QEMRFASTTaalaagvaiiYQE-LHLVPE--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 416 iyrLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELpqGLDTMLGEGERHLSGGQAQRIALARAfLDQQRKILLFDEP 495
Cdd:PRK11288 94 ---MTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKA-LARNARVIAFDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491368637 496 TAHLDI-ETEV------ALKErmlplmENRLVFFATHRlhwMEEM----DEIIVMDQGRIVE 546
Cdd:PRK11288 168 TSSLSArEIEQlfrvirELRA------EGRVILYVSHR---MEEIfalcDAITVFKDGRYVA 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
332-553 |
2.10e-14 |
|
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: 72.71 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTafRQASWQ---EQLI 408
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT--GLPPHRiarLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 409 YIPQNPYIY-RLTLQEN--VAFYQPTAtKEAVLKAIEvagltELLAELPQgLDTMLGEGERHLSGGQAQRIALARAfLDQ 485
Cdd:COG0410 82 YVPEGRRIFpSLTVEENllLGAYARRD-RAEVRADLE-----RVYELFPR-LKERRRQRAGTLSGGEQQMLAIGRA-LMS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 486 QRKILLFDEPTAHL------DI-ETEVALKER---MLpLMENRLVF---FAthrlhwmeemDEIIVMDQGRIVEQGTLAQ 552
Cdd:COG0410 154 RPKLLLLDEPSLGLapliveEIfEIIRRLNREgvtIL-LVEQNARFaleIA----------DRAYVLERGRIVLEGTAAE 222
|
.
gi 491368637 553 L 553
Cdd:COG0410 223 L 223
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
330-548 |
2.19e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.07 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 330 AQLTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKT-TAFRQAswQEQLI 408
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHA--RQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 409 YIPQ----NPyiyRLTLQENVA-----FYQPTATKEAVlkaieVAGLTElLAELPQGLDTMLGEgerhLSGGQAQRIALA 479
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLLvfgryFGLSAAAARAL-----VPPLLE-FAKLENKADAKVGE----LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491368637 480 RAFLDQQrKILLFDEPTAHLDIETEVALKERMLPLM-ENRLVFFAThrlHWMEEM----DEIIVMDQGRIVEQG 548
Cdd:PRK13537 151 RALVNDP-DVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTT---HFMEEAerlcDRLCVIEEGRKIAEG 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
332-527 |
2.76e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 72.89 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLS--GFLVPD---SGEITLGGAKTTAFRQASWQ-- 404
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIYSPRTDTVDlr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 405 EQLIYIPQNPYIYRLTLQENVAF-------YQPTATKEAVLKAIEVAGLTEllaELPQGL-DTMLGegerhLSGGQAQRI 476
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIYENVVYglrlkgiKDKQVLDEAVEKSLKGASIWD---EVKDRLhDSALG-----LSGGQQQRV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491368637 477 ALARAfLDQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRL 527
Cdd:PRK14239 158 CIARV-LATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
327-553 |
3.00e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 73.85 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 327 QEDAQLTIDQLAFSYEEK----------AALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGG---- 392
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKrglfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 393 -AKTTAFRQASWQEQLIYipQNPYiyrltlqenvAFYQPTATKEAVLkaievagltellaELPQGLDTMLGEGER----- 466
Cdd:PRK11308 81 kADPEAQKLLRQKIQIVF--QNPY----------GSLNPRKKVGQIL-------------EEPLLINTSLSAAERrekal 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 467 -----------------HL-SGGQAQRIALARAfLDQQRKILLFDEPTAHLDieteVALKERMLPLM-----ENRLVF-F 522
Cdd:PRK11308 136 ammakvglrpehydrypHMfSGGQRQRIAIARA-LMLDPDVVVADEPVSALD----VSVQAQVLNLMmdlqqELGLSYvF 210
|
250 260 270
....*....|....*....|....*....|..
gi 491368637 523 ATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQL 553
Cdd:PRK11308 211 ISHDLSVVEHIaDEVMVMYLGRCVEKGTKEQI 242
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
332-556 |
3.24e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.24 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYE-----EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTA------FRQ 400
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 401 ASWQEQLIYIPQNPYIYRLTLQENVAFyQP----TATKEAVLKAIEVAGLTELLAELpqgldtmLGEGERHLSGGQAQRI 476
Cdd:PRK13649 83 IRKKVGLVFQFPESQLFEETVLKDVAF-GPqnfgVSQEEAEALAREKLALVGISESL-------FEKNPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 477 ALArAFLDQQRKILLFDEPTAHLDIETEvalKErmlpLMEnrlVFFATHRL--------HWMEEM----DEIIVMDQGRI 544
Cdd:PRK13649 155 AIA-GILAMEPKILVLDEPTAGLDPKGR---KE----LMT---LFKKLHQSgmtivlvtHLMDDVanyaDFVYVLEKGKL 223
|
250
....*....|..
gi 491368637 545 VEQGTLAQLQQK 556
Cdd:PRK13649 224 VLSGKPKDIFQD 235
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
340-552 |
4.40e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.04 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 340 SYEEKAALTDINLNV-TGfKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGG------AKTTAFrqaswqeqliyipq 412
Cdd:COG1134 35 RREEFWALKDVSFEVeRG-ESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvsallELGAGF-------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 413 NPyiyRLTLQENVAFY-----QPTATKEAVLKAIevagltELLAELPQGLDTMLgegeRHLSGGQAQRIALARA-FLDQQ 486
Cdd:COG1134 100 HP---ELTGRENIYLNgrllgLSRKEIDEKFDEI------VEFAELGDFIDQPV----KTYSSGMRARLAFAVAtAVDPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491368637 487 rkILLFDEPTAHLDIETEVALKERMLPLMEN-RLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQ 552
Cdd:COG1134 167 --ILLVDEVLAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEE 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
353-553 |
4.51e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.08 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 353 NVTGFKKIG----IIGLSGSGKSTLINTLSGFLVPD---SGEITLGGAKTTA--FRQASW--QEQLIYIPQnpyiyrLTL 421
Cdd:TIGR00955 43 NVSGVAKPGellaVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAkeMRAISAyvQQDDLFIPT------LTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 422 QENVAFYQPTATKEAVLKAIEVAGLTELLAELpqGL----DTMLGEGERH--LSGGQAQRIALARAFLDQQrKILLFDEP 495
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTKKEKRERVDEVLQAL--GLrkcaNTRIGVPGRVkgLSGGERKRLAFASELLTDP-PLLFCDEP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491368637 496 TAHLDIETEVALKERMLPL-MENRLVFFATHR--LHWMEEMDEIIVMDQGRIVEQGTLAQL 553
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
158-539 |
5.09e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.45 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 158 LVLLLVFPLIIIFMIIlgyaAQSKAEKQYRTFQLLSNHFI----DSLRGIDT----------LKLFGVSKKygksiFASS 223
Cdd:PTZ00265 201 LCITCVFPLIYICGVI----CNKKVKINKKTSLLYNNNTMsiieEALVGIRTvvsycgektiLKKFNLSEK-----LYSK 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 224 ERFRKATMASLKVG-----ILSTFALDFFTTLSI-----------------AVVAVLLGLrlinegilLFPALTILILAP 281
Cdd:PTZ00265 272 YILKANFMESLHIGmingfILASYAFGFWYGTRIiisdlsnqqpnndfhggSVISILLGV--------LISMFMLTIILP 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 282 EYflpirdfsSDYHATLDGKNAMTAVteILHQP--EAQVPAVTVPRWQedaQLTIDQLAFSYEEKAAL---TDINLNVTG 356
Cdd:PTZ00265 344 NI--------TEYMKSLEATNSLYEI--INRKPlvENNDDGKKLKDIK---KIQFKNVRFHYDTRKDVeiyKDLNFTLTE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 357 FKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTA-FRQASWQEQLIYIPQNPYIYRLTLQENVAF-------- 427
Cdd:PTZ00265 411 GKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKdINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdl 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 428 -----------------------------------YQPTATKEAV--------LKAIEVAGLT------ELLAELPQGLD 458
Cdd:PTZ00265 491 ealsnyynedgndsqenknkrnscrakcagdlndmSNTTDSNELIemrknyqtIKDSEVVDVSkkvlihDFVSALPDKYE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 459 TMLGEGERHLSGGQAQRIALARAFLdQQRKILLFDEPTAHLDIETEVALKERMLPLM--ENRLVFFATHRLHWMEEMDEI 536
Cdd:PTZ00265 571 TLVGSNASKLSGGQKQRISIARAII-RNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTI 649
|
...
gi 491368637 537 IVM 539
Cdd:PTZ00265 650 FVL 652
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
328-553 |
5.95e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.57 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 328 EDAQLTIDQLAFSYEEKA-ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQA--SWQ 404
Cdd:PRK13636 2 EDYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 405 EQLIYIPQNP--YIYRLTLQENVAF------YQPTATKEAVLKAIEVAGLTELlaelpqgldtmlgegeRH-----LSGG 471
Cdd:PRK13636 82 ESVGMVFQDPdnQLFSASVYQDVSFgavnlkLPEDEVRKRVDNALKRTGIEHL----------------KDkpthcLSFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 472 QAQRIALArAFLDQQRKILLFDEPTAHLDietEVALKERMLPLMENR-----LVFFATHRLHWME-EMDEIIVMDQGRIV 545
Cdd:PRK13636 146 QKKRVAIA-GVLVMEPKVLVLDEPTAGLD---PMGVSEIMKLLVEMQkelglTIIIATHDIDIVPlYCDNVFVMKEGRVI 221
|
....*...
gi 491368637 546 EQGTLAQL 553
Cdd:PRK13636 222 LQGNPKEV 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
332-563 |
1.88e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 70.94 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALT--DINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIY 409
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTlkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 IPQNP--YIYRLTLQENVAF-----YQPT-ATKEAVLKAIEVAGLTELLAELPQGldtmlgegerhLSGGQAQRIALArA 481
Cdd:PRK13648 88 VFQNPdnQFVGSIVKYDVAFglenhAVPYdEMHRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIA-G 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 482 FLDQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFF--ATHRLHWMEEMDEIIVMDQGRIVEQGTLAQLQQKQGA 559
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIisITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
....
gi 491368637 560 FTEL 563
Cdd:PRK13648 236 LTRI 239
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
347-503 |
1.90e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.81 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 347 LTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAF----RQASWQEQLIYIPQN-PYIYRLTL 421
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeaRAKLRAKHVGFVFQSfMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 422 QENV---AFYQPTATKEAVLKAIevagltELLAELpqGLDTMLGEGERHLSGGQAQRIALARAFlDQQRKILLFDEPTAH 498
Cdd:PRK10584 106 LENVelpALLRGESSRQSRNGAK------ALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAF-NGRPDVLFADEPTGN 176
|
....*
gi 491368637 499 LDIET 503
Cdd:PRK10584 177 LDRQT 181
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
344-502 |
2.50e-13 |
|
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: 70.13 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 344 KAALTDINLNVTG--FKK---IGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTtafrqaSWQEQLIYIPQNPYIYR 418
Cdd:cd03237 7 KKTLGEFTLEVEGgsISEsevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------SYKPQYIKADYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 419 LTLQENVAFYQPTATKEAVLKaievagltellaelPQGLDTMLGEGERHLSGGQAQRIALArAFLDQQRKILLFDEPTAH 498
Cdd:cd03237 81 LLSSITKDFYTHPYFKTEIAK--------------PLQIEQILDREVPELSGGELQRVAIA-ACLSKDADIYLLDEPSAY 145
|
....
gi 491368637 499 LDIE 502
Cdd:cd03237 146 LDVE 149
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
342-568 |
2.51e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.83 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 342 EEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGE--------ITLGGAKTTAFRqaswQEQLIYIPQN 413
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdvATLDADALAQLR----REHFGFIFQR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 414 PYIY-RLTLQENV---AFYQPTATKEAVLKAIEvagltellaelpqgLDTMLGEGER------HLSGGQAQRIALARAFL 483
Cdd:PRK10535 95 YHLLsHLTAAQNVevpAVYAGLERKQRLLRAQE--------------LLQRLGLEDRveyqpsQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 484 DQQrKILLFDEPTAHLDIETEValkERMLPLMENR----LVFFATHRLHWMEEMDEIIVMDQGRIV----------EQGT 549
Cdd:PRK10535 161 NGG-QVILADEPTGALDSHSGE---EVMAILHQLRdrghTVIIVTHDPQVAAQAERVIEIRDGEIVrnppaqekvnVAGG 236
|
250
....*....|....*....
gi 491368637 550 LAQLQQKQGAFTELVNGMR 568
Cdd:PRK10535 237 TEPVVNTASGWRQFVSGFR 255
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
332-563 |
3.46e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.57 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGG---------AKTTAFRQAS 402
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlrdlyALSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 403 WQEQLIYIPQNPyiyRLTLQENVA----------------FYQPTATKEAVLKAIEVAglTELLAELPqgldtmlgegeR 466
Cdd:PRK11701 87 LRTEWGFVHQHP---RDGLRMQVSaggnigerlmavgarhYGDIRATAGDWLERVEID--AARIDDLP-----------T 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 467 HLSGGQAQRIALARAFLDQQRkiLLF-DEPTAHLDieteVALKERMLPLM-----ENRL-VFFATH-----RLHwmeeMD 534
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPR--LVFmDEPTGGLD----VSVQARLLDLLrglvrELGLaVVIVTHdlavaRLL----AH 220
|
250 260 270
....*....|....*....|....*....|
gi 491368637 535 EIIVMDQGRIVEQGTLAQ-LQQKQGAFTEL 563
Cdd:PRK11701 221 RLLVMKQGRVVESGLTDQvLDDPQHPYTQL 250
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
346-553 |
3.46e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.89 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQE-----QLIYipQNPYIY--- 417
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrsdiQMIF--QDPLASlnp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 418 RLTLQENVA----FYQPTATKEAV---LKAI--EVAGLTELLAELPQgldtmlgegerHLSGGQAQRIALARAfLDQQRK 488
Cdd:PRK15079 114 RMTIGEIIAeplrTYHPKLSRQEVkdrVKAMmlKVGLLPNLINRYPH-----------EFSGGQCQRIGIARA-LILEPK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491368637 489 ILLFDEPTAHLD--IETEVA--LKE--RMLPLmenRLVFFAtHRLHWMEEM-DEIIVMDQGRIVEQGTLAQL 553
Cdd:PRK15079 182 LIICDEPVSALDvsIQAQVVnlLQQlqREMGL---SLIFIA-HDLAVVKHIsDRVLVMYLGHAVELGTYDEV 249
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
328-499 |
3.93e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.14 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 328 EDAQLTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQAS-WQEQ 406
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 407 LIYIPQNPYIY-RLTLQENVAFYQPTATKEAVLKAIE-VAGLTELLAEL-PQGLDTMlgegerhlSGGQAQRIALARAFL 483
Cdd:PRK11614 82 VAIVPEGRRVFsRMTVEENLAMGGFFAERDQFQERIKwVYELFPRLHERrIQRAGTM--------SGGEQQMLAIGRALM 153
|
170
....*....|....*.
gi 491368637 484 DQQRkILLFDEPTAHL 499
Cdd:PRK11614 154 SQPR-LLLLDEPSLGL 168
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
337-553 |
5.72e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.35 E-value: 5.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 337 LAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTL-------SGFLVpdSGEITLGGAKTTAFRQA-SWQEQLI 408
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYRY--SGDVLLGGRSIFNYRDVlEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 409 YIPQNPYIYRLTLQENV----AFYQPTATKEavLKAIEVAGLTELlaELPQGLDTMLGEGERHLSGGQAQRIALARAfLD 484
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVlagvRAHKLVPRKE--FRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLART-LA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 485 QQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQL 553
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
344-512 |
9.45e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.92 E-value: 9.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 344 KAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLG-GAKTTafrqaswqeqliYIPQNPYI-YRLTL 421
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKVG------------YLPQEPQLdPEKTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 422 QENV-------------------AFYQPTATKEAVLK-------AIEVAGLTELLAELPQGLDTM-LGEGE---RHLSGG 471
Cdd:PRK11819 88 RENVeegvaevkaaldrfneiyaAYAEPDADFDALAAeqgelqeIIDAADAWDLDSQLEIAMDALrCPPWDakvTKLSGG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491368637 472 QAQRIALARAFLdQQRKILLFDEPTAHLDIETeVALKERML 512
Cdd:PRK11819 168 ERRRVALCRLLL-EKPDMLLLDEPTNHLDAES-VAWLEQFL 206
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
346-548 |
1.04e-12 |
|
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: 70.60 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEI---------------TLGGAKTTAFRQASWQEQLIYi 410
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpgPDGRGRAKRYIGILHQEYDLY- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 411 PQNPYIYRLTLQENVAFYQPTATKEAVLkAIEVAGLTELLAE--LPQGLDTmLGEGERHlsggqaqRIALARAFLDQQRk 488
Cdd:TIGR03269 378 PHRTVLDNLTEAIGLELPDELARMKAVI-TLKMVGFDEEKAEeiLDKYPDE-LSEGERH-------RVALAQVLIKEPR- 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491368637 489 ILLFDEPTAHLDIETEVALKERMLPLME--NRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQG 548
Cdd:TIGR03269 448 IVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVcDRAALMRDGKIVKIG 510
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
332-570 |
1.21e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.14 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGfLVPDSGEITLGGaKTTAFRQASWQ------- 404
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEG-RVEFFNQNIYErrvnlnr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 405 --EQLIYIPQNPYIYRLTLQENVAF------YQPTatkeavlkaIEVAGLTELL---AELPQGLDTMLGEGERHLSGGQA 473
Cdd:PRK14258 86 lrRQVSMVHPKPNLFPMSVYDNVAYgvkivgWRPK---------LEIDDIVESAlkdADLWDEIKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 474 QRIALARAfLDQQRKILLFDEPTAHLDIETEVALKERM--LPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVEQGTLA 551
Cdd:PRK14258 157 QRLCIARA-LAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLV 235
|
250
....*....|....*....
gi 491368637 552 QLQQKQGAFTELVNGMRRE 570
Cdd:PRK14258 236 EFGLTKKIFNSPHDSRTRE 254
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
327-557 |
1.22e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 68.25 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 327 QEDAQLTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAF-RQASWQ- 404
Cdd:PRK11831 3 SVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMsRSRLYTv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 405 -EQLIYIPQNPYIYR-LTLQENVAF--YQPTATKEAVLKA-----IEVAGLTElLAELpqgldtMLGEgerhLSGGQAQR 475
Cdd:PRK11831 83 rKRMSMLFQSGALFTdMNVFDNVAYplREHTQLPAPLLHStvmmkLEAVGLRG-AAKL------MPSE----LSGGMARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 476 IALARAF-LDQQrkILLFDEPTAHLD-IETEVALKermlplmenrLVFFATHRL--------HWMEEMDEI-----IVMD 540
Cdd:PRK11831 152 AALARAIaLEPD--LIMFDEPFVGQDpITMGVLVK----------LISELNSALgvtcvvvsHDVPEVLSIadhayIVAD 219
|
250
....*....|....*..
gi 491368637 541 QgRIVEQGTLAQLQQKQ 557
Cdd:PRK11831 220 K-KIVAHGSAQALQANP 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
332-556 |
1.44e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.61 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKA-----ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGG------AKTTAFRQ 400
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 401 ASWQEQLIYIPQNPYIYRLTLQENVAF-------YQPTATKEAVLKaIEVAGLTELLAElpqgldtmlgEGERHLSGGQA 473
Cdd:PRK13643 82 VRKKVGVVFQFPESQLFEETVLKDVAFgpqnfgiPKEKAEKIAAEK-LEMVGLADEFWE----------KSPFELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 474 QRIALArAFLDQQRKILLFDEPTAHLDIETEValkeRMLPLMEN-----RLVFFATHRLHWMEE-MDEIIVMDQGRIVEQ 547
Cdd:PRK13643 151 RRVAIA-GILAMEPEVLVLDEPTAGLDPKARI----EMMQLFESihqsgQTVVLVTHLMDDVADyADYVYLLEKGHIISC 225
|
....*....
gi 491368637 548 GTLAQLQQK 556
Cdd:PRK13643 226 GTPSDVFQE 234
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
330-548 |
1.61e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.29 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 330 AQLTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIY 409
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 ipQNPYIY-RLTLQENVAFyqptATKEAVLKAIEVAGLTELLAELPQgLDTMLGEGERHLSGGQAQRIALARAfLDQQRK 488
Cdd:PRK11000 82 --QSYALYpHLSVAENMSF----GLKLAGAKKEEINQRVNQVAEVLQ-LAHLLDRKPKALSGGQRQRVAIGRT-LVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491368637 489 ILLFDEPTAHLDIETEVALKERMLPLME--NRLVFFATH-RLHWMEEMDEIIVMDQGRIVEQG 548
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
332-518 |
1.74e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.51 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRqASWQEQLIYIP 411
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDL-CTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 Q----NPYiyrLTLQENVAF-YQPTATKEAVLKAIEVAGLTELLaELPQGLdtmlgegerhLSGGQAQRIALARAFLDQQ 486
Cdd:PRK13540 81 HrsgiNPY---LTLRENCLYdIHFSPGAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKA 146
|
170 180 190
....*....|....*....|....*....|..
gi 491368637 487 rKILLFDEPTAHLDietEVALKERMLPLMENR 518
Cdd:PRK13540 147 -KLWLLDEPLVALD---ELSLLTIITKIQEHR 174
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
332-545 |
1.76e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 69.67 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQL-AFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLI-Y 409
Cdd:COG3845 258 LEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVaY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 IPQNPY----IYRLTLQENVA---FYQPTATKEAVLKAIEVAGLTELLAE----LPQGLDTMLgegeRHLSGGQAQRIAL 478
Cdd:COG3845 338 IPEDRLgrglVPDMSVAENLIlgrYRRPPFSRGGFLDRKAIRAFAEELIEefdvRTPGPDTPA----RSLSGGNQQKVIL 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491368637 479 ARAfLDQQRKILLFDEPTAHLDIETEVALKERMLPLMENRL-VFFAThrlhwmEEMDE-------IIVMDQGRIV 545
Cdd:COG3845 414 ARE-LSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAaVLLIS------EDLDEilalsdrIAVMYEGRIV 481
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
362-526 |
2.52e-12 |
|
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: 65.25 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 362 IIGLSGSGKSTLINTLSGfLVP-DSGEITLggakttafrqaSWQEQLIYIPQNPYIYRLTLQENVAFyqptatkeavlka 440
Cdd:cd03223 32 ITGPSGTGKSSLFRALAG-LWPwGSGRIGM-----------PEGEDLLFLPQRPYLPLGTLREQLIY------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 441 ievagltellaelPQGldtmlgegeRHLSGGQAQRIALARAFLdQQRKILLFDEPTAHLDIETEvalkERMLPLMENRL- 519
Cdd:cd03223 87 -------------PWD---------DVLSGGEQQRLAFARLLL-HKPKFVFLDEATSALDEESE----DRLYQLLKELGi 139
|
....*...
gi 491368637 520 -VFFATHR 526
Cdd:cd03223 140 tVISVGHR 147
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
332-553 |
2.56e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.43 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDIN---LNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLI 408
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 409 YIPQNP--YIYRLTLQENVAFYQPTA--TKEAVLKAIEVAglteLLAelPQGLDTMLGEGERhLSGGQAQRIALArAFLD 484
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQgiPREEMIKRVDEA----LLA--VNMLDFKTREPAR-LSGGQKQRVAVA-GIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491368637 485 QQRKILLFDEPTAHLDiETEVALKERMLPLMENRL---VFFATHRLHWMEEMDEIIVMDQGRIVEQGTLAQL 553
Cdd:PRK13642 157 LRPEIIILDESTSMLD-PTGRQEIMRVIHEIKEKYqltVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
337-549 |
4.31e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 66.64 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 337 LAFSYEE-KAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGaKTTAFRQASWQE--QLIYIP-Q 412
Cdd:PRK13639 7 LKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG-EPIKYDKKSLLEvrKTVGIVfQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 413 NP--YIYRLTLQENVAF--YQPTATKEAVLKAIEvagltELLAELpqgldTMLGEGER---HLSGGQAQRIALArAFLDQ 485
Cdd:PRK13639 86 NPddQLFAPTVEEDVAFgpLNLGLSKEEVEKRVK-----EALKAV-----GMEGFENKpphHLSGGQKKRVAIA-GILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491368637 486 QRKILLFDEPTAHLDIETEVALKERMLPLMENRL-VFFATHRLHWMEE-MDEIIVMDQGRIVEQGT 549
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGItIIISTHDVDLVPVyADKVYVMSDGKIIKEGT 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
343-548 |
5.10e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.19 E-value: 5.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 343 EKAALTDINLNVTGFKKIGIIGLSGSGKSTlintlSGF----LVPDSGEITLGGAKTTAFRQASW-----QEQLIYipQN 413
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKST-----TGLallrLINSQGEIWFDGQPLHNLNRRQLlpvrhRIQVVF--QD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 414 PYIY---RLTLQENVA----FYQPTATKEAVLKAIeVAGLTELlaelpqGLDTMLgegeRH-----LSGGQAQRIALARA 481
Cdd:PRK15134 371 PNSSlnpRLNVLQIIEeglrVHQPTLSAAQREQQV-IAVMEEV------GLDPET----RHrypaeFSGGQRQRIAIARA 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 482 FLDQQRKILLfDEPTAHLDIETEVALKERMLPLME-NRLVF-FATHRLHWMEEM-DEIIVMDQGRIVEQG 548
Cdd:PRK15134 440 LILKPSLIIL-DEPTSSLDKTVQAQILALLKSLQQkHQLAYlFISHDLHVVRALcHQVIVLRQGEVVEQG 508
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
360-502 |
6.46e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 360 IGIIGLSGSGKSTLINTLSGFLVPDSGEItlggakttafrqaSWQEQLIYIPQnpYIYRltlqenvafyQPTATKEAVLK 439
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEV-------------DPELKISYKPQ--YIKP----------DYDGTVEDLLR 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491368637 440 AIEVAGLTELL-AEL--PQGLDTMLGEGERHLSGGQAQRIALArAFLDQQRKILLFDEPTAHLDIE 502
Cdd:PRK13409 423 SITDDLGSSYYkSEIikPLQLERLLDKNVKDLSGGELQRVAIA-ACLSRDADLYLLDEPSAHLDVE 487
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
324-546 |
7.06e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.07 E-value: 7.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 324 PRWQedaQLTIDQLAFSYEEKA-ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQAS 402
Cdd:PRK10522 318 PDWQ---TLELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 403 WQEQLIYIPQNPYIY-RLTLQENVAfyqptATKEAVLKAIEVAGLTELLaELPQGLDTMLgegerHLSGGQAQRIALARA 481
Cdd:PRK10522 395 YRKLFSAVFTDFHLFdQLLGPEGKP-----ANPALVEKWLERLKMAHKL-ELEDGRISNL-----KLSKGQKKRLALLLA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491368637 482 FLdQQRKILLFDEPTAHLDIETEVALKERMLPLM--ENRLVFFATHRLHWMEEMDEIIVMDQGRIVE 546
Cdd:PRK10522 464 LA-EERDILLLDEWAADQDPHFRREFYQVLLPLLqeMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
332-510 |
9.52e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 65.05 E-value: 9.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTA---FRQAswQEQLI 408
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmHKRA--RLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 409 YIPQNPYIYR-LTLQENVAfyqptatkeAVLkaiEVAGLT---------ELLAELpqGLDTMlgegeRH-----LSGGQA 473
Cdd:COG1137 82 YLPQEASIFRkLTVEDNIL---------AVL---ELRKLSkkereerleELLEEF--GITHL-----RKskaysLSGGER 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491368637 474 QRIALARAfLDQQRKILLFDEPTAHLD------IETEVA-LKER 510
Cdd:COG1137 143 RRVEIARA-LATNPKFILLDEPFAGVDpiavadIQKIIRhLKER 185
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
336-549 |
2.79e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.44 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 336 QLAFSYEEKAALTDINLNVTGF--------------KKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQA 401
Cdd:PRK10070 19 QRAFKYIEQGLSKEQILEKTGLslgvkdaslaieegEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 402 SWQE----QLIYIPQN-PYIYRLTLQENVAFYQPTA------TKEAVLKAIEVAGLTELLAELPQgldtmlgegerHLSG 470
Cdd:PRK10070 99 ELREvrrkKIAMVFQSfALMPHMTVLDNTAFGMELAginaeeRREKALDALRQVGLENYAHSYPD-----------ELSG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 471 GQAQRIALARAfLDQQRKILLFDEPTAHLD--IETEVALKERMLPLMENRLVFFATHRL-HWMEEMDEIIVMDQGRIVEQ 547
Cdd:PRK10070 168 GMRQRVGLARA-LAINPDILLMDEAFSALDplIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQV 246
|
..
gi 491368637 548 GT 549
Cdd:PRK10070 247 GT 248
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
358-511 |
2.91e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.99 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 358 KKIGIIGLSGSGKSTLINTLSGFLVPDSGEITlggakttafRQASWQEQLIYIP----QNpYIYRLTLQENVAFYQPTA- 432
Cdd:PRK13409 100 KVTGILGPNGIGKTTAVKILSGELIPNLGDYE---------EEPSWDEVLKRFRgtelQN-YFKKLYNGEIKVVHKPQYv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 433 ----------TKEAVLKAIEVAGLTELLAELpqGLDTMLGEGERHLSGGQAQRIALARAFLdQQRKILLFDEPTAHLDIe 502
Cdd:PRK13409 170 dlipkvfkgkVRELLKKVDERGKLDEVVERL--GLENILDRDISELSGGELQRVAIAAALL-RDADFYFFDEPTSYLDI- 245
|
....*....
gi 491368637 503 tevalKERM 511
Cdd:PRK13409 246 -----RQRL 249
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
332-549 |
3.38e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.91 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGaKTTAFRQASWQEQ----- 406
Cdd:PRK14246 11 FNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG-KVLYFGKDIFQIDaiklr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 407 ----LIYIPQNPYIYrLTLQENVAF---YQPTATKEAVLKAIEvagltELLAE--LPQGLDTMLGEGERHLSGGQAQRIA 477
Cdd:PRK14246 90 kevgMVFQQPNPFPH-LSIYDNIAYplkSHGIKEKREIKKIVE-----ECLRKvgLWKEVYDRLNSPASQLSGGQQQRLT 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491368637 478 LARAfLDQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGT 549
Cdd:PRK14246 164 IARA-LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGS 235
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
360-518 |
3.79e-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: 65.58 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 360 IGIIGLSGSGKSTLINTLSGFLVPDSGEItlggakttafrqaSWQEQLIYIPQnpYI---YRLTLQENVafyqptatKEA 436
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQ--YIspdYDGTVEEFL--------RSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 437 VLKAIEVAGLTELLAElPQGLDTMLGEGERHLSGGQAQRIALArAFLDQQRKILLFDEPTAHLDIETEVALKERMLPLME 516
Cdd:COG1245 426 NTDDFGSSYYKTEIIK-PLGLEKLLDKNVKDLSGGELQRVAIA-ACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAE 503
|
..
gi 491368637 517 NR 518
Cdd:COG1245 504 NR 505
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
360-511 |
5.32e-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: 65.19 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 360 IGIIGLSGSGKSTLINTLSGFLVPDSGEITlggakttafRQASWQEQL----------------------IYIPQnpYIY 417
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYD---------EEPSWDEVLkrfrgtelqdyfkklangeikvAHKPQ--YVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 418 RLtlqenvafyqPTA----TKEAVLKAIEVAGLTELLAELpqGLDTMLGEGERHLSGGQAQRIALARAFLdqqRK--ILL 491
Cdd:COG1245 171 LI----------PKVfkgtVRELLEKVDERGKLDELAEKL--GLENILDRDISELSGGELQRVAIAAALL---RDadFYF 235
|
170 180
....*....|....*....|
gi 491368637 492 FDEPTAHLDIetevalKERM 511
Cdd:COG1245 236 FDEPSSYLDI------YQRL 249
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
332-512 |
5.52e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 65.19 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLG-GAKTTAFRqaswQEQLIYI 410
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFA----QHQLEFL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 411 --PQNP--YIYRLTLQenvafyqptatkeavlkaievagltellaELPQGLDTMLG----------EGERHLSGGQAQRI 476
Cdd:PRK10636 389 raDESPlqHLARLAPQ-----------------------------ELEQKLRDYLGgfgfqgdkvtEETRRFSGGEKARL 439
|
170 180 190
....*....|....*....|....*....|....*.
gi 491368637 477 ALArAFLDQQRKILLFDEPTAHLDIETEVALKERML 512
Cdd:PRK10636 440 VLA-LIVWQRPNLLLLDEPTNHLDLDMRQALTEALI 474
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
330-550 |
7.91e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.60 E-value: 7.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 330 AQLTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFR-QASWQEQLI 408
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 409 YIPQNPYIY-RLTLQENV-AFYQptaTKEAVLKAIEVAGLTELLAELP-QGLDTMLGEGerhLSGGQAQRIALARAfLDQ 485
Cdd:PRK10895 82 YLPQEASIFrRLSVYDNLmAVLQ---IRDDLSAEQREDRANELMEEFHiEHLRDSMGQS---LSGGERRRVEIARA-LAA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491368637 486 QRKILLFDEPTAHLDIETEVALKERMLPLMENRL-VFFATHRLHwmEEMDeiiVMDQGRIVEQGTL 550
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLgVLITDHNVR--ETLA---VCERAYIVSQGHL 215
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
332-507 |
8.72e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.53 E-value: 8.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITlggakttafrqasWQE--QLIY 409
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK-------------WSEnaNIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 410 IPQNPYIY---RLTLQENVAFYQPTATKEAVLKAIevagltellaelpqgLDTMLGEGE------RHLSGGQAQRIALAR 480
Cdd:PRK15064 387 YAQDHAYDfenDLTLFDWMSQWRQEGDDEQAVRGT---------------LGRLLFSQDdikksvKVLSGGEKGRMLFGK 451
|
170 180
....*....|....*....|....*..
gi 491368637 481 AFLdQQRKILLFDEPTAHLDIETEVAL 507
Cdd:PRK15064 452 LMM-QKPNVLVMDEPTNHMDMESIESL 477
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
346-545 |
9.54e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 64.28 E-value: 9.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVtgfKK--I-GIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTT--AFRQAswqeqlI-----YIPQNP- 414
Cdd:COG3845 20 ANDDVSLTV---RPgeIhALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirSPRDA------IalgigMVHQHFm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 415 YIYRLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELpqGL----DTMLGEgerhLSGGQAQRIALARAfLDQQRKIL 490
Cdd:COG3845 91 LVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERY--GLdvdpDAKVED----LSVGEQQRVEILKA-LYRGARIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491368637 491 LFDEPTAHL-DIETEvALKERMlplmeNRL------VFFATHRLHwmEEM---DEIIVMDQGRIV 545
Cdd:COG3845 164 ILDEPTAVLtPQEAD-ELFEIL-----RRLaaegksIIFITHKLR--EVMaiaDRVTVLRRGKVV 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
332-553 |
1.28e-10 |
|
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: 63.94 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSY----EEKAALTDINLNVTGFKKIGIIGLSGSGKS----TLINTLSGFLVPDSGEITLGGAKTTAFRQASW 403
Cdd:COG4172 7 LSVEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 404 QE----QLIYIPQ------NPyIYRLTLQ--ENVAFYQPTATKEAVLKAIEvaglteLLAELpqGLDtmlgEGER----- 466
Cdd:COG4172 87 RRirgnRIAMIFQepmtslNP-LHTIGKQiaEVLRLHRGLSGAAARARALE------LLERV--GIP----DPERrlday 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 467 -H-LSGGQAQRIALARAfLDQQRKILLFDEPTAHLDieteVALKERMLPLMEN---RL---VFFATHRLHWMEEM-DEII 537
Cdd:COG4172 154 pHqLSGGQRQRVMIAMA-LANEPDLLIADEPTTALD----VTVQAQILDLLKDlqrELgmaLLLITHDLGVVRRFaDRVA 228
|
250
....*....|....*.
gi 491368637 538 VMDQGRIVEQGTLAQL 553
Cdd:COG4172 229 VMRQGEIVEQGPTAEL 244
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
346-555 |
2.21e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.16 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAF-RQASWQEQLIYIPQNPYIYR-LTLQE 423
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIARMGVVRTFQHVRLFReMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 424 N--VA-------------FYQPT---ATKEAVLKA---IEVAGLTElLAELPQGldtmlgegerHLSGGQAQRIALARAF 482
Cdd:PRK11300 100 NllVAqhqqlktglfsglLKTPAfrrAESEALDRAatwLERVGLLE-HANRQAG----------NLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491368637 483 LDQQRkILLFDEPTAHLDIETEVALKERMLPLME--NRLVFFATHRLHW-MEEMDEIIVMDQGRIVEQGTLAQLQQ 555
Cdd:PRK11300 169 VTQPE-ILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLvMGISDRIYVVNQGTPLANGTPEEIRN 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
362-545 |
2.65e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 60.66 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 362 IIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQAS---WQEQLIYIPQNPY-IYRLTLQENVAFYQPTA----- 432
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHlLMDRTVYDNVAIPLIIAgasgd 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 433 -TKEAVLKAIEVAGLTELLAELPQgldtmlgegerHLSGGQAQRIALARAFLDQQrKILLFDEPTAHLDieteVALKERM 511
Cdd:PRK10908 113 dIRRRVSAALDKVGLLDKAKNFPI-----------QLSGGEQQRVGIARAVVNKP-AVLLADEPTGNLD----DALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491368637 512 LPLME--NRL---VFFATHRLHWMEEMD-EIIVMDQGRIV 545
Cdd:PRK10908 177 LRLFEefNRVgvtVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
337-512 |
3.30e-10 |
|
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: 62.65 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 337 LAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGgaKTTafrqaswqeQLIYIPQNpyi 416
Cdd:TIGR03719 328 LTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETV---------KLAYVDQS--- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 417 yRLTLQENVAFYQptatkeavlkaiEVAGLTELL----AELP----------QGLDTMLGEGErhLSGGQAQRIALARAf 482
Cdd:TIGR03719 394 -RDALDPNKTVWE------------EISGGLDIIklgkREIPsrayvgrfnfKGSDQQKKVGQ--LSGGERNRVHLAKT- 457
|
170 180 190
....*....|....*....|....*....|
gi 491368637 483 LDQQRKILLFDEPTAHLDIETEVALKERML 512
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVETLRALEEALL 487
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
16-291 |
3.40e-10 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 61.25 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 16 LGLLAGLSFLQAL--FIIGQAygLARAITGlwEGRPLEEQWGWILLFFCSFIARQAVIYFRSkrlddYSYQQAA-----D 88
Cdd:cd18544 5 LLLLLLATALELLgpLLIKRA--IDDYIVP--GQGDLQGLLLLALLYLGLLLLSFLLQYLQT-----YLLQKLGqriiyD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 89 LRDQLLEKLFRVGPQIAQQQGTGNVTTMV---LEGINQV-ENYLKLILAKIMNMSiipwVILALVFYLDWESGLVLLLVF 164
Cdd:cd18544 76 LRRDLFSHIQRLPLSFFDRTPVGRLVTRVtndTEALNELfTSGLVTLIGDLLLLI----GILIAMFLLNWRLALISLLVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 165 PLIIIFMIILgyaaQSKAEKQYRTF-QLLS--NHFI-DSLRGIDTLKLFGVSKKYGKSIFASSERFRKATMASLKVGILS 240
Cdd:cd18544 152 PLLLLATYLF----RKKSRKAYREVrEKLSrlNAFLqESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALF 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 491368637 241 TFALDFFTTLSIAVVAVLLGLRLINEGIllfpALTILILAPEY----FLPIRDFS 291
Cdd:cd18544 228 RPLVELLSSLALALVLWYGGGQVLSGAV----TLGVLYAFIQYiqrfFRPIRDLA 278
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
346-545 |
3.42e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 62.34 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVtgfKK---IGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGaKTTAFR--QASWQEQLIYIPQNpyiyR-- 418
Cdd:COG1129 267 VVRDVSFSV---RAgeiLGIAGLVGAGRTELARALFGADPADSGEIRLDG-KPVRIRspRDAIRAGIAYVPED----Rkg 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 419 ------LTLQENVAFyqptatkeAVLKAIEVAGL----------TELLAEL---PQGLDTMLGEgerhLSGGQAQRIALA 479
Cdd:COG1129 339 eglvldLSIRENITL--------ASLDRLSRGGLldrrreralaEEYIKRLrikTPSPEQPVGN----LSGGNQQKVVLA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 480 RAfLDQQRKILLFDEPTAHLDIETEVALKERMlplmeNRL-------VFFAThrlhwmeEMDE-------IIVMDQGRIV 545
Cdd:COG1129 407 KW-LATDPKVLILDEPTRGIDVGAKAEIYRLI-----RELaaegkavIVISS-------ELPEllglsdrILVMREGRIV 473
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
337-512 |
3.48e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 337 LAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQnpYI 416
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPG--LK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 417 YRLTLQENVAF------YQPTATKEAVLKAIEVAGLTELLAelpqgldtmlgegeRHLSGGQAQRIALARAFLDQQrKIL 490
Cdd:PRK13543 95 ADLSTLENLHFlcglhgRRAKQMPGSALAIVGLAGYEDTLV--------------RQLSAGQKKRLALARLWLSPA-PLW 159
|
170 180
....*....|....*....|..
gi 491368637 491 LFDEPTAHLDIETeVALKERML 512
Cdd:PRK13543 160 LLDEPYANLDLEG-ITLVNRMI 180
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
346-511 |
5.19e-10 |
|
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: 59.76 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITL---GGAKTTAfrQASwQEQLIYIPQNPYIY----- 417
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWVDLA--QAS-PREILALRRRTIGYvsqfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 418 ----RLTLQENVAfyQP-----TATKEAVLKAievaglTELLA--ELPQGLdtmlgegeRHL-----SGGQAQRIALARA 481
Cdd:COG4778 103 rvipRVSALDVVA--EPllergVDREEARARA------RELLArlNLPERL--------WDLppatfSGGEQQRVNIARG 166
|
170 180 190
....*....|....*....|....*....|
gi 491368637 482 FLDQQRkILLFDEPTAHLDIETEVALKERM 511
Cdd:COG4778 167 FIADPP-LLLLDEPTASLDAANRAVVVELI 195
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
330-549 |
1.38e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 59.86 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 330 AQLTIDQLAFSYEEKA-ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQAswqEQLI 408
Cdd:PRK11650 2 AGLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA---DRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 409 -YIPQNPYIY-RLTLQENVAfY------QPTATKEA-VLKAIEVAGLTELLAELPqgldtmlgegeRHLSGGQAQRIALA 479
Cdd:PRK11650 79 aMVFQNYALYpHMSVRENMA-YglkirgMPKAEIEErVAEAARILELEPLLDRKP-----------RELSGGQRQRVAMG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491368637 480 RAFLdQQRKILLFDEPTAHLDIETEVALKERMLPLmENRL---VFFATHrlHWMEEM---DEIIVMDQGRIvEQ-GT 549
Cdd:PRK11650 147 RAIV-REPAVFLFDEPLSNLDAKLRVQMRLEIQRL-HRRLkttSLYVTH--DQVEAMtlaDRVVVMNGGVA-EQiGT 218
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
15-279 |
2.05e-09 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 59.03 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 15 LLGLLAGLSFLQalfIIGQaygLARAITGLWEGRPLEEQwgwILLFFCSFIARQAVIYFRSKRLDDYSYQQAADLRDQLL 94
Cdd:cd18576 6 LLSSAIGLVFPL---LAGQ---LIDAALGGGDTASLNQI---ALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 95 EKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIMNMSIIPWVILALVFYLDWESGLVLLLVFPLIIIFMIIL 174
Cdd:cd18576 77 RHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 175 GyaaqskaekqyRTFQLLSNHFID-----------SLRGIDTLKLFG----VSKKYGKSIfassERFRKATMASLKV-GI 238
Cdd:cd18576 157 G-----------RRIRKLSKKVQDelaeantiveeTLQGIRVVKAFTredyEIERYRKAL----ERVVKLALKRARIrAL 221
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 491368637 239 LSTFaLDFFTTLSIAVVaVLLGLRLINEGILLFPALTILIL 279
Cdd:cd18576 222 FSSF-IIFLLFGAIVAV-LWYGGRLVLAGELTAGDLVAFLL 260
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
57-269 |
3.05e-09 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 58.64 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 57 ILLFFCSFIARQAVIYFrskrlddySYQQAADLRDQLLEKLFRvgpQ-IA--QQQGTGNVTTMVLEGINQVENYL--KLI 131
Cdd:cd18577 58 IGSFVLSYIQTACWTIT--------GERQARRIRKRYLKALLR---QdIAwfDKNGAGELTSRLTSDTNLIQDGIgeKLG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 132 LAkIMNMSIIpwvILALV--FYLDWESGLVLLLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLF 209
Cdd:cd18577 127 LL-IQSLSTF---IAGFIiaFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAF 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491368637 210 G----VSKKYGKSI-FASSERFRKATMASLKVGILstfaldFFTTLSIAVVAVLLGLRLINEGIL 269
Cdd:cd18577 203 GgeekEIKRYSKALeKARKAGIKKGLVSGLGLGLL------FFIIFAMYALAFWYGSRLVRDGEI 261
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
327-527 |
3.14e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.87 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 327 QEDAQLTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLI---NTLSGfLVPD---SGEITLGGAKTTAFR- 399
Cdd:PRK14243 6 GTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLND-LIPGfrvEGKVTFHGKNLYAPDv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 400 -QASWQEQLIYIPQNPYIYRLTLQENVAF------YQPTaTKEAVLKAIEVAGL-TELLAELPQ-GLDtmlgegerhLSG 470
Cdd:PRK14243 85 dPVEVRRRIGMVFQKPNPFPKSIYDNIAYgaringYKGD-MDELVERSLRQAALwDEVKDKLKQsGLS---------LSG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491368637 471 GQAQRIALARAfLDQQRKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRL 527
Cdd:PRK14243 155 GQQQRLCIARA-IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
332-558 |
3.69e-09 |
|
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: 56.77 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFlvPD----SGEITLGGAKTTAfrqaswqeql 407
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKyevtEGEILFKGEDITD---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 408 iyipqnpyiyrLTLQEN------VAFYQPtatkeavlkaIEVAGLTelLAELPQGLDtmlgEGerhLSGGQAQRIALARA 481
Cdd:cd03217 69 -----------LPPEERarlgifLAFQYP----------PEIPGVK--NADFLRYVN----EG---FSGGEKKRNEILQL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 482 FLdQQRKILLFDEPTAHLDIEtevALK------ERMLPlmENRLVFFATHRLHWMEEM--DEIIVMDQGRIVEQG--TLA 551
Cdd:cd03217 119 LL-LEPDLAILDEPDSGLDID---ALRlvaeviNKLRE--EGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGdkELA 192
|
....*..
gi 491368637 552 QLQQKQG 558
Cdd:cd03217 193 LEIEKKG 199
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
330-553 |
6.54e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.83 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 330 AQLTIDQLAFSY-EEKA---ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGfLVPDSGEITlggAKTTAFRQASWQ- 404
Cdd:PRK11022 2 ALLNVDKLSVHFgDESApfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMG-LIDYPGRVM---AEKLEFNGQDLQr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 405 ------EQLI-----YIPQNP-------YIYRLTLQENVAFYQPTATKEAVLKAIEVagLTELLAELPQG-LDTMlgegE 465
Cdd:PRK11022 78 isekerRNLVgaevaMIFQDPmtslnpcYTVGFQIMEAIKVHQGGNKKTRRQRAIDL--LNQVGIPDPASrLDVY----P 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 466 RHLSGGQAQRIALARAfLDQQRKILLFDEPTAHLDIETEVALKERMLPLM--ENRLVFFATHRLHWMEEM-DEIIVMDQG 542
Cdd:PRK11022 152 HQLSGGMSQRVMIAMA-IACRPKLLIADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVAEAaHKIIVMYAG 230
|
250
....*....|.
gi 491368637 543 RIVEQGTLAQL 553
Cdd:PRK11022 231 QVVETGKAHDI 241
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
360-509 |
7.13e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 7.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 360 IGIIGLSGSGKSTLINTLSGFLVPDSGEITLGgaKTTafrqaswqeQLIYIPQNpyiyRLTLQENVAFYQptatkeavlk 439
Cdd:PRK11819 353 VGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG--ETV---------KLAYVDQS----RDALDPNKTVWE---------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 440 aiEVAGltellaelpqGLDTM-LGEGE---R------------------HLSGGQAQRIALARAfLDQQRKILLFDEPTA 497
Cdd:PRK11819 408 --EISG----------GLDIIkVGNREipsRayvgrfnfkggdqqkkvgVLSGGERNRLHLAKT-LKQGGNVLLLDEPTN 474
|
170
....*....|..
gi 491368637 498 HLDIETEVALKE 509
Cdd:PRK11819 475 DLDVETLRALEE 486
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
341-525 |
1.12e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.39 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 341 YEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGF--LVPDS---GEITLGGAKTTAFR----QASWQEQLIYIP 411
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEArveGEVRLFGRNIYSPDvdpiEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNPYIYrLTLQENVA----FYQPTATKEAVLKAIEVAgLTEllAELPQGLDTMLGEGERHLSGGQAQRIALARAfLDQQR 487
Cdd:PRK14267 94 PNPFPH-LTIYDNVAigvkLNGLVKSKKELDERVEWA-LKK--AALWDEVKDRLNDYPSNLSGGQRQRLVIARA-LAMKP 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 491368637 488 KILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATH 525
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
57-270 |
1.71e-08 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 56.27 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 57 ILLFFCSFIARQAVIYFrskrlddySYQQAADLRDQLLEKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIM 136
Cdd:cd18541 51 LLIGIFRFLWRYLIFGA--------SRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 137 NMSIIPWVILALVFYLDWESGLVLLLVFPLIIIFMIILGyaaqSKAEKQYR----TFQLLSNHFIDSLRGIDTLKLFGVS 212
Cdd:cd18541 123 DALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLG----KKIHKRFRkvqeAFSDLSDRVQESFSGIRVIKAFVQE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491368637 213 KKYGKSIFASSERFRKATMASLKVGILSTFALDFFTTLSIAVVAVLLGLRLINEGILL 270
Cdd:cd18541 199 EAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITL 256
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
349-544 |
2.93e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 349 DINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQ-LIYIPQNPYIYRLTL------ 421
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARgLVYLPEDRQSSGLYLdaplaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 422 ------QENVAFYQPTATKEAVLKAIEVAgLTELLAELPQGLdtmlgegeRHLSGGQAQRIALARAfLDQQRKILLFDEP 495
Cdd:PRK15439 361 nvcaltHNRRGFWIKPARENAVLERYRRA-LNIKFNHAEQAA--------RTLSGGNQQKVLIAKC-LEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491368637 496 TAHLDIETEVALKERMLPLME-NRLVFFATHRLHWMEEM-DEIIVMDQGRI 544
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAqNVAVLFISSDLEEIEQMaDRVLVMHQGEI 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
334-512 |
2.95e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 334 IDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGgaktTAFRQAswqeqliYIPQn 413
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLEVA-------YFDQ- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 414 pyiYRLTLqenvafyQPTATKEavlkaievagltELLAELPQglDTMLGEGERH---------------------LSGGQ 472
Cdd:PRK11147 390 ---HRAEL-------DPEKTVM------------DNLAEGKQ--EVMVNGRPRHvlgylqdflfhpkramtpvkaLSGGE 445
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491368637 473 AQRIALARAFLdQQRKILLFDEPTAHLDIETeVALKERML 512
Cdd:PRK11147 446 RNRLLLARLFL-KPSNLLILDEPTNDLDVET-LELLEELL 483
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
346-507 |
3.94e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGfLVPD---SGEITLGGAKTTAFRQASWQEQLIYIpqnpyIYR---- 418
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQASNIRDTERAGIAI-----IHQelal 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 419 ---LTLQENVaFYQPTATKEAVLKAIEV-AGLTELLAELpqGLDTMLGEGERHLSGGQAQRIALARAfLDQQRKILLFDE 494
Cdd:PRK13549 94 vkeLSVLENI-FLGNEITPGGIMDYDAMyLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKA-LNKQARLLILDE 169
|
170
....*....|....
gi 491368637 495 PTAHL-DIETEVAL 507
Cdd:PRK13549 170 PTASLtESETAVLL 183
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
360-501 |
4.65e-08 |
|
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: 54.29 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 360 IGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTT---AFRQASWQEQL----------IYIPQnpYIYRLtlqenva 426
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEildEFRGSELQNYFtkllegdvkvIVKPQ--YVDLI------- 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491368637 427 fyqPTATKEAVLKAIEVAGLTELLAELPQ--GLDTMLGEGERHLSGGQAQRIALARAFLdQQRKILLFDEPTAHLDI 501
Cdd:cd03236 100 ---PKAVKGKVGELLKKKDERGKLDELVDqlELRHVLDRNIDQLSGGELQRVAIAAALA-RDADFYFFDEPSSYLDI 172
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
346-557 |
6.26e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 6.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGaKTTAFR--QASwQE--------QLIYIPQnpy 415
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG-KEVTFNgpKSS-QEagigiihqELNLIPQ--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 416 iyrLTLQENVaFY--QPTATKEAVLKAIEVAGLTELLAEL--PQGLDTMLGEgerhLSGGQAQRIALARAfLDQQRKILL 491
Cdd:PRK10762 94 ---LTIAENI-FLgrEFVNRFGRIDWKKMYAEADKLLARLnlRFSSDKLVGE----LSIGEQQMVEIAKV-LSFESKVII 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491368637 492 FDEPTAHL-DIETEV------ALKErmlplmENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQLQQKQ 557
Cdd:PRK10762 165 MDEPTDALtDTETESlfrvirELKS------QGRGIVYISHRLKEIFEIcDDVTVFRDGQFIAEREVADLTEDS 232
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
349-553 |
8.38e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.55 E-value: 8.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 349 DINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPD----SGEITLGGaktTAFRQASWQEQLI-YIPQNPyiyrltlqe 423
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDG---KPVAPCALRGRKIaTIMQNP--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 424 NVAFyQPTATKEA-VLKAIEVAGLTELLAELPQGLDTM-LGEGER-------HLSGGQAQRIALARAFLDQQrKILLFDE 494
Cdd:PRK10418 89 RSAF-NPLHTMHThARETCLALGKPADDATLTAALEAVgLENAARvlklypfEMSGGMLQRMMIALALLCEA-PFIIADE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491368637 495 PTAHLDieteVALKERMLPLMENRL------VFFATH------RLhwmeeMDEIIVMDQGRIVEQGTLAQL 553
Cdd:PRK10418 167 PTTDLD----VVAQARILDLLESIVqkralgMLLVTHdmgvvaRL-----ADDVAVMSHGRIVEQGDVETL 228
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
359-544 |
1.26e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 359 KIGIIGLSGSGKSTLINTLSGFLVPDSGeitlggaktTAFRQASWQeqlIYIPQNPYIYRLTLQENVAFYQ----PTATK 434
Cdd:PLN03073 537 RIAMVGPNGIGKSTILKLISGELQPSSG---------TVFRSAKVR---MAVFSQHHVDGLDLSSNPLLYMmrcfPGVPE 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 435 EAVLKAIEVAGLTELLAelpqgLDTMLGegerhLSGGQAQRIALARAFLDQQRkILLFDEPTAHLDIETEVALKERMLPL 514
Cdd:PLN03073 605 QKLRAHLGSFGVTGNLA-----LQPMYT-----LSGGQKSRVAFAKITFKKPH-ILLLDEPSNHLDLDAVEALIQGLVLF 673
|
170 180 190
....*....|....*....|....*....|.
gi 491368637 515 MENrlVFFATHRLHWME-EMDEIIVMDQGRI 544
Cdd:PLN03073 674 QGG--VLMVSHDEHLISgSVDELWVVSEGKV 702
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
346-549 |
1.38e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.57 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPD---SGEITLGGAKTTAFRQASWQ----EQLIYIPQ------ 412
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNklraEQISMIFQdpmtsl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 413 NPYIyRL--TLQENVAFYQPTATKEAVLKAIEVaglteLLA-ELPQGLDTMlGEGERHLSGGQAQRIALARAFLDQQrKI 489
Cdd:PRK09473 111 NPYM-RVgeQLMEVLMLHKGMSKAEAFEESVRM-----LDAvKMPEARKRM-KMYPHEFSGGMRQRVMIAMALLCRP-KL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491368637 490 LLFDEPTAHLDieteVALKERMLPLME------NRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGT 549
Cdd:PRK09473 183 LIADEPTTALD----VTVQAQIMTLLNelkrefNTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYGN 245
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
54-268 |
2.12e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 52.90 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 54 WGWILLFFCSFIARQAVIYFRSKRLDDYSYQQAADLRDQLLEKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILA 133
Cdd:cd18563 43 LLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 134 KIMNMSIIPWVILALVFYLDWESGLVLLLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSK 213
Cdd:cd18563 123 DFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEK 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491368637 214 KygksifaSSERFRKATMASLKVGI-----LSTF--ALDFFTTLSIAVVAVLLGLRLINEGI 268
Cdd:cd18563 203 R-------EIKRFDEANQELLDANIraeklWATFfpLLTFLTSLGTLIVWYFGGRQVLSGTM 257
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
362-507 |
2.70e-07 |
|
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: 53.60 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 362 IIGLSGSGKSTLINTLSGfLVPdsgeiTLGGAKTTAFRQAswqeqLIYIPQNPYIYRLTLQENVAF------YQPTATKE 435
Cdd:TIGR00954 483 ICGPNGCGKSSLFRILGE-LWP-----VYGGRLTKPAKGK-----LFYVPQRPYMTLGTLRDQIIYpdssedMKRRGLSD 551
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491368637 436 AVLKAI-EVAGLTELLAElPQGLDTMLGEGERhLSGGQAQRIALARAFLDQQRKILLfDEPTAHLDIETEVAL 507
Cdd:TIGR00954 552 KDLEQIlDNVQLTHILER-EGGWSAVQDWMDV-LSGGEKQRIAMARLFYHKPQFAIL-DECTSAVSVDVEGYM 621
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
54-276 |
3.13e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 52.57 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 54 WGWILLFFCSFIARQAVIYFRSKRLDDYSYQQAADLRDQLLEKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILA 133
Cdd:cd18565 54 WLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGAN 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 134 KIMNMSIIPWVILALVFYLDWESGLVLLLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSK 213
Cdd:cd18565 134 SIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAED 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491368637 214 KYGKSIFASSERFRKATMASLKVGILSTFALDFFTTLSIAVVAVLLGLRLINEGILLFPALTI 276
Cdd:cd18565 214 FERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGPPLFTGTLTV 276
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
358-526 |
4.99e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 49.29 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 358 KKIGIIGLSGSGKSTLINTLSGFLVPDSGEItlggakttafrqaswqeqliyipqnpyiyrltlqenvafyqptatkeav 437
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGV------------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 438 lkaIEVAGLTELLAELPQGLDTMLGEGERHLSGGQAQRIALARAfLDQQRKILLFDEPTAHLDIETEVAL-------KER 510
Cdd:smart00382 34 ---IYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALA-RKLKPDVLILDEITSLLDAEQEALLllleelrLLL 109
|
170
....*....|....*.
gi 491368637 511 MLPLMENRLVFFATHR 526
Cdd:smart00382 110 LLKSEKNLTVILTTND 125
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
332-553 |
5.05e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEK----AALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGA-------KTTAFR- 399
Cdd:PRK10261 13 LAVENLNIAFMQEqqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrQVIELSe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 400 QASWQEQLIYIPQNPYIYrltlQENVAFYQPTAT-KEAVLKAIEV---AGLTELLAELPQGLD--------TMLGEGERH 467
Cdd:PRK10261 93 QSAAQMRHVRGADMAMIF----QEPMTSLNPVFTvGEQIAESIRLhqgASREEAMVEAKRMLDqvripeaqTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 468 LSGGQAQRIALARAfLDQQRKILLFDEPTAHLDIETEVALKERMLPLMENRL--VFFATHRLHWMEEM-DEIIVMDQGRI 544
Cdd:PRK10261 169 LSGGMRQRVMIAMA-LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIaDRVLVMYQGEA 247
|
....*....
gi 491368637 545 VEQGTLAQL 553
Cdd:PRK10261 248 VETGSVEQI 256
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
332-553 |
7.58e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.01 E-value: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSY----EEKAALTDINLNVTGFKKIGIIGLSGSGKStlINTLSGF-LVPD------SGEITLGGaktTAFRQ 400
Cdd:PRK15134 6 LAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKS--VTALSILrLLPSppvvypSGDIRFHG---ESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 401 ASWQEqLIYIPQNPYiyRLTLQENVAFYQPTATKEAVLkaIEVAGLTELL------AELPQGLDTM--------LGEGER 466
Cdd:PRK15134 81 ASEQT-LRGVRGNKI--AMIFQEPMVSLNPLHTLEKQL--YEVLSLHRGMrreaarGEILNCLDRVgirqaakrLTDYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 467 HLSGGQAQRIALARAFLDQQrKILLFDEPTAHLDieteVALKERMLPLME------NRLVFFATHRLHWMEEM-DEIIVM 539
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRP-ELLIADEPTTALD----VSVQAQILQLLRelqqelNMGLLFITHNLSIVRKLaDRVAVM 230
|
250
....*....|....
gi 491368637 540 DQGRIVEQGTLAQL 553
Cdd:PRK15134 231 QNGRCVEQNRAATL 244
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
336-503 |
7.80e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 336 QLAFSYeekAALTD-INLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTA----------------F 398
Cdd:PRK11147 10 WLSFSD---APLLDnAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVArlqqdpprnvegtvydF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 399 RQASWQEQLIYIPQNPYIYRLTLQEnvafyqPTATK----EAVLKAIEVAGL-------TELLAELPQGLDTMLGEgerh 467
Cdd:PRK11147 87 VAEGIEEQAEYLKRYHDISHLVETD------PSEKNlnelAKLQEQLDHHNLwqlenriNEVLAQLGLDPDAALSS---- 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 491368637 468 LSGGQAQRIALARAfLDQQRKILLFDEPTAHLDIET 503
Cdd:PRK11147 157 LSGGWLRKAALGRA-LVSNPDVLLLDEPTNHLDIET 191
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
146-269 |
8.67e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 51.02 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 146 LALVFYLDWESGLVLLLVFPLIIIFMIILGYAAQsKAEKQYRTFQLLSNHFID-SLRGIDTLKLFGVSKKygksifaSSE 224
Cdd:cd18557 128 LIILFILSWKLTLVLLLVIPLLLIASKIYGRYIR-KLSKEVQDALAKAGQVAEeSLSNIRTVRSFSAEEK-------EIR 199
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 491368637 225 RFRKATMASLKVGILSTFALDFFTTLS-----IAVVAVL-LGLRLINEGIL 269
Cdd:cd18557 200 RYSEALDRSYRLARKKALANALFQGITslliyLSLLLVLwYGGYLVLSGQL 250
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
57-267 |
9.36e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 50.61 E-value: 9.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 57 ILLFFCSFIARQAVIYFRSKrlddYSYQQAADLRDQLLEKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIM 136
Cdd:cd18778 47 LGAYLLRALLNFLRIYLNHV----AEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 137 NMSIIPWVILALVFYLDWESGLVLLLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKYG 216
Cdd:cd18778 123 TNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491368637 217 KSIFASSERFRKATMASLKVGILSTFALDFFTTLSIAVVaVLLGLRLINEG 267
Cdd:cd18778 203 KRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLV-LGFGGRLVLAG 252
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
343-526 |
1.23e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.57 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 343 EKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLV--PDSGEITlggakttafrqaswqeqliyIPQNPYIYRLT 420
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVD--------------------VPDNQFGREAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 421 LQENVAFYQPTATKEAVLKAievAGLTE--LLAELPqgldtmlgegeRHLSGGQAQRIALARAfLDQQRKILLFDEPTAH 498
Cdd:COG2401 102 LIDAIGRKGDFKDAVELLNA---VGLSDavLWLRRF-----------KELSTGQKFRFRLALL-LAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|
gi 491368637 499 LDIETEVALKERMLPLM-ENRLVF-FATHR 526
Cdd:COG2401 167 LDRQTAKRVARNLQKLArRAGITLvVATHH 196
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
333-552 |
1.79e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.03 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 333 TIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDS--GEITLGGAKTTafRQAswQEQLIYI 410
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT--KQI--LKRTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 411 PQNPYIY-RLTLQENVAFYQPTATKEAVLKAIEVAGLTELLAELpqGL----DTMLGEG-ERHLSGGQAQRIALARAFLD 484
Cdd:PLN03211 146 TQDDILYpHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISEL--GLtkceNTIIGNSfIRGISGGERKRVSIAHEMLI 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491368637 485 QQrKILLFDEPTAHLDIETEVALKERMLPLMEN-RLVFFATH----RLHWMeeMDEIIVMDQGRIVEQGTLAQ 552
Cdd:PLN03211 224 NP-SLLILDEPTSGLDATAAYRLVLTLGSLAQKgKTIVTSMHqpssRVYQM--FDSVLVLSEGRCLFFGKGSD 293
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
87-280 |
2.02e-06 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 49.79 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 87 ADLRDQLLEKLFRVGPQIAQQQGTGNVTTMVLEGINQVEN-YLKLILAKIMNMSIIPwVILALVFYLDWESGLVLLLVFP 165
Cdd:cd18585 68 SNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNlYLRVLSPPVVALLVIL-ATILFLAFFSPALALILLAGLL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 166 LIIIFMIILGYAAQSKAEKQYRTFQ-LLSNHFIDSLRGIDTLKLFGVSKKYGKSIFASSERF--RKATMASLKvgILSTF 242
Cdd:cd18585 147 LAGVVIPLLFYRLGKKIGQQLVQLRaELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALikEQRRLARLS--GLSQA 224
|
170 180 190
....*....|....*....|....*....|....*....
gi 491368637 243 ALDFFTtlSIAVVAVL-LGLRLINEGILLFPALTILILA 280
Cdd:cd18585 225 LMILLS--GLTVWLVLwLGAPLVQNGALDGALLAMLVFA 261
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
353-542 |
2.70e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 353 NVTGFKKIGII----GLSGSGKSTLINTLSGFL---VPDSGEITLGGAKttafRQASWQEQLIYIPQNP-YIYRLTLQEN 424
Cdd:TIGR00956 781 NVDGWVKPGTLtalmGASGAGKTTLLNVLAERVttgVITGGDRLVNGRP----LDSSFQRSIGYVQQQDlHLPTSTVRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 425 VAF----YQPTATK--------EAVLKAIEVAGLTELLAELPqgldtmlGEGerhLSGGQAQRIALARAFLDQQRKILLF 492
Cdd:TIGR00956 857 LRFsaylRQPKSVSksekmeyvEEVIKLLEMESYADAVVGVP-------GEG---LNVEQRKRLTIGVELVAKPKLLLFL 926
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491368637 493 DEPTAHLDIETEVALKERMLPLMEN-RLVFFATHR--LHWMEEMDEIIVMDQG 542
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKLADHgQAILCTIHQpsAILFEEFDRLLLLQKG 979
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
358-546 |
2.74e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 358 KKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGG--------AKTTAFRQASwqeqLIYIPQNPYIYR-LTLQENVAFY 428
Cdd:PRK10636 28 QKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPQPA----LEYVIDGDREYRqLEAQLHDANE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 429 Q----PTATKEAVLKAIEVAGLTELLAELPQGL---DTMLGEGERHLSGGQAQRIALARAFLDQQrKILLFDEPTAHLDI 501
Cdd:PRK10636 104 RndghAIATIHGKLDAIDAWTIRSRAASLLHGLgfsNEQLERPVSDFSGGWRMRLNLAQALICRS-DLLLLDEPTNHLDL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491368637 502 ETEVALkERMLPLMENRLVFFATHRLHWMEEMDEIIVMDQGRIVE 546
Cdd:PRK10636 183 DAVIWL-EKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
144-279 |
3.67e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 49.02 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 144 VILALVFYLDWESGLVLLLVFPLIIIFMIILGyAAQSKAEKQYRTFQLLSN-HFIDSLRGIDTLKLFGVSKKYGKSIFAS 222
Cdd:cd18546 129 GIAVVLLVLDPRLALVALAALPPLALATRWFR-RRSSRAYRRARERIAAVNaDLQETLAGIRVVQAFRRERRNAERFAEL 207
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 491368637 223 SERFRKATMASLKVGILSTFALDFFTTLSIAVVaVLLGLRLINEGILLFPALTILIL 279
Cdd:cd18546 208 SDDYRDARLRAQRLVAIYFPGVELLGNLATAAV-LLVGAWRVAAGTLTVGVLVAFLL 263
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
341-559 |
3.72e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.12 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 341 YEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEIT-LGGakttAFRQASWQEQL---I-YIPQ--- 412
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGG----DMADARHRRAVcprIaYMPQglg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 413 -NPYiYRLTLQENVAFY-----QPTATKEAvlkAIEvagltELLAElpQGLDTMLGEGERHLSGGQAQRIALARAfLDQQ 486
Cdd:NF033858 87 kNLY-PTLSVFENLDFFgrlfgQDAAERRR---RID-----ELLRA--TGLAPFADRPAGKLSGGMKQKLGLCCA-LIHD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 487 RKILLFDEPTAHLD----------IETevaLKERMlPLMEnrlVFFAThrlHWMEE---MDEIIVMDQGRIVEQGTLAQL 553
Cdd:NF033858 155 PDLLILDEPTTGVDplsrrqfwelIDR---IRAER-PGMS---VLVAT---AYMEEaerFDWLVAMDAGRVLATGTPAEL 224
|
....*.
gi 491368637 554 QQKQGA 559
Cdd:NF033858 225 LARTGA 230
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
346-573 |
6.75e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.73 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIPQnpyiyrLTLQENV 425
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIEN------IELKGLM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 426 AFYQPTATKEAVLKAIEVAGLTELLAelpQGLDTMlgegerhlSGGQAQRIALARAfLDQQRKILLFDEPTAHLDIETEV 505
Cdd:PRK13545 113 MGLTKEKIKEIIPEIIEFADIGKFIY---QPVKTY--------SSGMKSRLGFAIS-VHINPDILVIDEALSVGDQTFTK 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 506 ALKERMLPLMEN-RLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQLQQKQGAFTELVNGMRREQLE 573
Cdd:PRK13545 181 KCLDKMNEFKEQgKTIFFISHSLSQVKSFcTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQMSVEERK 250
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
346-548 |
7.94e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.55 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTlsgfLVPDSGEITLGGAKTTAFRQaswqeQLIYIPQnpyiyrltlqenv 425
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNE----GLYASGKARLISFLPKFSRN-----KLIFIDQ------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 426 afyqptatkeavLKAIEVAGLTELlaELPQGLDTmlgegerhLSGGQAQRIALARaFLDQQRK--ILLFDEPTAHLDIET 503
Cdd:cd03238 68 ------------LQFLIDVGLGYL--TLGQKLST--------LSGGELQRVKLAS-ELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491368637 504 EVALKERMLPLM-ENRLVFFATHRLHWMEEMDEIIVM------DQGRIVEQG 548
Cdd:cd03238 125 INQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
360-549 |
9.91e-06 |
|
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: 47.22 E-value: 9.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 360 IGIIGLSGSGKSTLINTLsgfLVPdSGEITLGGAKTTAFRQASWQ-----EQLIYIPQ---------NPYIY-------- 417
Cdd:cd03271 24 TCVTGVSGSGKSSLINDT---LYP-ALARRLHLKKEQPGNHDRIEglehiDKVIVIDQspigrtprsNPATYtgvfdeir 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 418 -------------RLTLQ-----ENVAFYQPTATKEAVLKAIEVAGLTELLAELPQ-GLDTM-LGEGERHLSGGQAQRIA 477
Cdd:cd03271 100 elfcevckgkrynRETLEvrykgKSIADVLDMTVEEALEFFENIPKIARKLQTLCDvGLGYIkLGQPATTLSGGEAQRIK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 478 LARAFLDQQ--RKILLFDEPTAHLDIETEVALKERMLPLMEN-RLVFFATHRLHWMEEMDEIIVMDQ------GRIVEQG 548
Cdd:cd03271 180 LAKELSKRStgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKgNTVVVIEHNLDVIKCADWIIDLGPeggdggGQVVASG 259
|
.
gi 491368637 549 T 549
Cdd:cd03271 260 T 260
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
349-546 |
1.10e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.24 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 349 DINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTafrqaswqeqliyiPQNPYI-------YRLTL 421
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--------------PRSPLDavkkgmaYITES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 422 QENVAFYQPTATKE--AVLKAIEVAGLTELLAELPQGLDTMLGEGER---------------HLSGGQAQRIALARaFLD 484
Cdd:PRK09700 347 RRDNGFFPNFSIAQnmAISRSLKDGGYKGAMGLFHEVDEQRTAENQRellalkchsvnqnitELSGGNQQKVLISK-WLC 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491368637 485 QQRKILLFDEPTAHLDIETEVALKERMLPLMEN-RLVFFATHRL-HWMEEMDEIIVMDQGRIVE 546
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELpEIITVCDRIAVFCEGRLTQ 489
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
346-507 |
1.10e-05 |
|
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: 48.28 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGfLVPD---SGEITLGGAKTTAFRQASWQEQLIYIPQNP--YIYRLT 420
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKASNIRDTERAGIVIIHQEltLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 421 LQENVaFYQPTATKEAVLKAIEVAGL--TELLAELPqgLDTM---LGEGErhLSGGQAQRIALARAfLDQQRKILLFDEP 495
Cdd:TIGR02633 95 VAENI-FLGNEITLPGGRMAYNAMYLraKNLLRELQ--LDADnvtRPVGD--YGGGQQQLVEIAKA-LNKQARLLILDEP 168
|
170
....*....|...
gi 491368637 496 TAHL-DIETEVAL 507
Cdd:TIGR02633 169 SSSLtEKETEILL 181
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
360-569 |
1.16e-05 |
|
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: 46.03 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 360 IGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKttafrqaswqeqLIYIPQnpYIyrltlqenvafyqptatkeavlk 439
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT------------PVYKPQ--YI----------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 440 aievagltellaelpqgldtmlgegerHLSGGQAQRIALARAFLdQQRKILLFDEPTAHLDIETEVALKE--RMLPLMEN 517
Cdd:cd03222 71 ---------------------------DLSGGELQRVAIAAALL-RNATFYLFDEPSAYLDIEQRLNAARaiRRLSEEGK 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491368637 518 RLVFFATHRLHWMEEMDEIIVMDQGrivEQGTLAQLQQKQGafteLVNGMRR 569
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHVFEG---EPGVYGIASQPKG----TREGINR 167
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
361-558 |
1.17e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 48.47 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 361 GIIGLSGSGKSTLINTLSGFLVPDSGEITLGGaKTTAFRQASWQEQLIYIPQNPYIYR-LTLQENVAFYQ-----PTATK 434
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG-KSILTNISDVHQNMGYCPQFDAIDDlLTGREHLYLYArlrgvPAEEI 2047
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 435 EAVLK-AIEVAGLTeLLAELPQGLdtmlgegerhLSGGQAQRIALARAFLDQQrKILLFDEPTAHLDIETEVALKERMLP 513
Cdd:TIGR01257 2048 EKVANwSIQSLGLS-LYADRLAGT----------YSGGNKRKLSTAIALIGCP-PLVLLDEPTTGMDPQARRMLWNTIVS 2115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491368637 514 LM-ENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQLQQKQG 558
Cdd:TIGR01257 2116 IIrEGRAVVLTSHSMEECEALcTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
346-556 |
1.54e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.86 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQASWQEQLIYIpqnpyIYR------- 418
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI-----IYQelsvide 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 419 LTLQENVaFYQPTATKEAV-------LKAIEVAGLTELLAELPQGLDTMLGEgerhLSGGQAQRIALARAfLDQQRKILL 491
Cdd:PRK09700 95 LTVLENL-YIGRHLTKKVCgvniidwREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKT-LMLDAKVII 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491368637 492 FDEPTAHLdIETEValkERMLPLM-----ENRLVFFATHRLHWMEEM-DEIIVMDQGRIVEQGTLAQLQQK 556
Cdd:PRK09700 169 MDEPTSSL-TNKEV---DYLFLIMnqlrkEGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
360-548 |
2.15e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.54 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 360 IGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKT---TAFRQASWQEQLIYIPQNPYIY---RLT----LQENVAFYQ 429
Cdd:PRK10261 353 LSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPYASldpRQTvgdsIMEPLRVHG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 430 PTATKEAvlkAIEVAGLTELLAELPQGLDTMLGEgerhLSGGQAQRIALARAfLDQQRKILLFDEPTAHLDIETEVALKE 509
Cdd:PRK10261 433 LLPGKAA---AARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARA-LALNPKVIIADEAVSALDVSIRGQIIN 504
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491368637 510 RMLPLMENRLV--FFATHRLHWMEEMD-EIIVMDQGRIVEQG 548
Cdd:PRK10261 505 LLLDLQRDFGIayLFISHDMAVVERIShRVAVMYLGQIVEIG 546
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
346-567 |
2.39e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGfLVPD---SGEITLGGaKTTAFRQASWQEQL--IYIPQN----PYi 416
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDG-EVCRFKDIRDSEALgiVIIHQElaliPY- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 417 yrLTLQENVAFYQPTATK------EAVLKAievaglTELLA-----ELPQGLDTMLGEgerhlsgGQAQRIALARAfLDQ 485
Cdd:NF040905 93 --LSIAENIFLGNERAKRgvidwnETNRRA------RELLAkvgldESPDTLVTDIGV-------GKQQLVEIAKA-LSK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 486 QRKILLFDEPTAHLDIETEVALKERMLPLMENRLV-FFATHRLHWMEEM-DEIIVMDQGRIVEqgtlaQLQQKQGAFTE- 562
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLLLELKAQGITsIIISHKLNEIRRVaDSITVLRDGRTIE-----TLDCRADEVTEd 231
|
....*.
gi 491368637 563 -LVNGM 567
Cdd:NF040905 232 rIIRGM 237
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
141-261 |
4.29e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 45.65 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 141 IPWVI--LALVFYLDWESGLVLLLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKygks 218
Cdd:cd18566 126 LPFVLifLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQ---- 201
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 491368637 219 ifaSSERFR----KATMASLKVGILSTFALDFFTTLSIAVVAVLLGL 261
Cdd:cd18566 202 ---MLRRYErlqaNAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAF 245
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
15-280 |
5.25e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 45.52 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 15 LLGLLAglSFLQALFIIGQAYGLARAITGLWEGRPLEEQWG---WILLFF----CSFIArqavIYFRSkrlddYSYQQAA 87
Cdd:cd18578 12 LLGLIG--AIIAGAVFPVFAILFSKLISVFSLPDDDELRSEanfWALMFLvlaiVAGIA----YFLQG-----YLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 88 D-----LRDQLLEKLFRvgpqiaQQQG--------TGNVTTMVLEGINQVENYLKLILAKIMNM--SIIPWVILALVFyl 152
Cdd:cd18578 81 ErltrrLRKLAFRAILR------QDIAwfddpensTGALTSRLSTDASDVRGLVGDRLGLILQAivTLVAGLIIAFVY-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 153 DWESGLVLLLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFG----VSKKYGKSIfasSERFRK 228
Cdd:cd18578 153 GWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTledyFLEKYEEAL---EEPLKK 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 491368637 229 ATMASLKVGILstFALDFFTTLSIAVVAVLLGLRLINEGIL----LFPALTILILA 280
Cdd:cd18578 230 GLRRALISGLG--FGLSQSLTFFAYALAFWYGGRLVANGEYtfeqFFIVFMALIFG 283
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
141-281 |
5.90e-05 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 45.12 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 141 IPWVIL--ALVFYLDWESGLVLLLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFG----VSKK 214
Cdd:cd18587 125 LPFVLLflAVIALIGGPLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGaegrMQRR 204
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491368637 215 YGKSIFASSErfrkatmASLKVGILSTFALDFFTTL----SIAVVAVllGLRLINEGILLFPAL---TIL---ILAP 281
Cdd:cd18587 205 WEEAVAALAR-------SSLKSRLLSSSATNFAQFVqqlvTVAIVIV--GVYLISDGELTMGGLiacVILsgrALAP 272
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
144-255 |
7.05e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 44.86 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 144 VILALVFYLDWESGLVLLLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKYgksIFASS 223
Cdd:cd18568 131 IYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPI---RWRWE 207
|
90 100 110
....*....|....*....|....*....|....*
gi 491368637 224 ERFRKATMASLKVGILS---TFALDFFTTLSIAVV 255
Cdd:cd18568 208 NKFAKALNTRFRGQKLSivlQLISSLINHLGTIAV 242
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
362-539 |
8.16e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.12 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 362 IIGLSGSGKSTLIntlsgflvpdsgeitlggakttafrqaswqEQLIYIpqnpyiyrlTLQENVAFYQPTATKEAVLKAI 441
Cdd:cd03227 26 ITGPNGSGKSTIL------------------------------DAIGLA---------LGGAQSATRRRSGVKAGCIVAA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 442 EVAgltELLAELPQgldtmlgegerhLSGGQAQRIALARAF---LDQQRKILLFDEPTAHLDIETEVALKERMLP-LMEN 517
Cdd:cd03227 67 VSA---ELIFTRLQ------------LSGGEKELSALALILalaSLKPRPLYILDEIDRGLDPRDGQALAEAILEhLVKG 131
|
170 180
....*....|....*....|..
gi 491368637 518 RLVFFATHRLHWMEEMDEIIVM 539
Cdd:cd03227 132 AQVIVITHLPELAELADKLIHI 153
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
349-548 |
9.68e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 9.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 349 DINLNVTGFKKIG----IIGLSGSGKSTLINTLS----GFLVPDSGEITLGGAKTTAFRQaSWQEQLIYIPQN----PYi 416
Cdd:TIGR00956 75 DILKPMDGLIKPGeltvVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKK-HYRGDVVYNAETdvhfPH- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 417 yrLTLQENVAFY----QPTATKEAVLKAIEVAGLTELLAE---LPQGLDTMLG-EGERHLSGGQAQRIALARAFLDQQrK 488
Cdd:TIGR00956 153 --LTVGETLDFAarckTPQNRPDGVSREEYAKHIADVYMAtygLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGA-K 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 489 ILLFDEPTAHLDIETEV----ALKE-----RMLPLMEnrlVFFATHRLHwmEEMDEIIVMDQGRIVEQG 548
Cdd:TIGR00956 230 IQCWDNATRGLDSATALefirALKTsanilDTTPLVA---IYQCSQDAY--ELFDKVIVLYEGYQIYFG 293
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
346-392 |
1.15e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.04 E-value: 1.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 491368637 346 ALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGG 392
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG 85
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
361-510 |
1.50e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 361 GIIGLSGSGKSTLINTLSGFLVPDSGEITLG-GAKTTAFRqaswQEQLIY---------IPQNPYIYRLtLQENVAFY-Q 429
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLR----QDQFAFeeftvldtvIMGHTELWEV-KQERDRIYaL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 430 PTATKEAVLKA--IEVA-----GLTellAELPQGlDTMLGEG---ERH------LSGGQAQRIALARA-FLDQQrkILLF 492
Cdd:PRK15064 106 PEMSEEDGMKVadLEVKfaemdGYT---AEARAG-ELLLGVGipeEQHyglmseVAPGWKLRVLLAQAlFSNPD--ILLL 179
|
170 180
....*....|....*....|..
gi 491368637 493 DEPTAHLDIET----EVALKER 510
Cdd:PRK15064 180 DEPTNNLDINTirwlEDVLNER 201
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
56-268 |
1.62e-04 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 43.96 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 56 WILLFFCSFIARQAVIYFRSKRLDDYSYQQAA-DLRDQLLEKLfrvgpqiaQQQ--------GTGNVTTMVLEGINQVEN 126
Cdd:cd18542 40 LLALLILGVALLRGVFRYLQGYLAEKASQKVAyDLRNDLYDHL--------QRLsfsfhdkaRTGDLMSRCTSDVDTIRR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 127 YLKLILAKIMNMSIIpwVILALV--FYLDWESGLVLLLVFPLIIIFMIILGyaaqSKAEKQYRTFQ----LLSNHFIDSL 200
Cdd:cd18542 112 FLAFGLVELVRAVLL--FIGALIimFSINWKLTLISLAIIPFIALFSYVFF----KKVRPAFEEIReqegELNTVLQENL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491368637 201 RGIDTLKLFGvSKKYGKSIFAS-SERFRKATMASLKvgILSTF--ALDFFTTLSIAVVAVLLGLRLINEGI 268
Cdd:cd18542 186 TGVRVVKAFA-REDYEIEKFDKeNEEYRDLNIKLAK--LLAKYwpLMDFLSGLQIVLVLWVGGYLVINGEI 253
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
53-278 |
1.94e-04 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 43.54 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 53 QWGWILLF--FCSFIARQAVIYFRSKrlddYSYQQAADLRDQLLEKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKL 130
Cdd:cd18548 40 RTGLLMLLlaLLGLIAGILAGYFAAK----ASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 131 ILakimnMSIIPWVILA-----LVFYLDWESGLVLLLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDT 205
Cdd:cd18548 116 LL-----RMLVRAPIMLigaiiMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRV 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491368637 206 LKLFgVSKKYGKsifassERFRKA----TMASLKVGILSTFALDFFT-TLSIAVVAVL-LGLRLINEGILLFPALTILI 278
Cdd:cd18548 191 IRAF-NREDYEE------ERFDKAnddlTDTSLKAGRLMALLNPLMMlIMNLAIVAILwFGGHLINAGSLQVGDLVAFI 262
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
462-561 |
2.09e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 462 GEGERHLSGGQAQRIALARAFLDQQrKILLFDEPTAHLDIETEVALKERMLPLMENRLVFFATHRlhWMEEMD----EII 537
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRP-AVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQ--YMEEAEqlahELT 215
|
90 100
....*....|....*....|....
gi 491368637 538 VMDQGRIVEQGTLAQLQQKQGAFT 561
Cdd:NF000106 216 VIDRGRVIADGKVDELKTKVGGRT 239
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
359-379 |
3.34e-04 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 40.30 E-value: 3.34e-04
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
468-520 |
4.21e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.48 E-value: 4.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491368637 468 LSGGQAQRIALARaFL---DQQRKILLFDEPTAHL---DIETevalkermlpLME--NRLV 520
Cdd:COG0178 827 LSGGEAQRVKLAS-ELskrSTGKTLYILDEPTTGLhfhDIRK----------LLEvlHRLV 876
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
22-268 |
4.73e-04 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 42.39 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 22 LSFLQALFIIGQAYGLARAITGLWEGRPLEEQ------WGWILLFFCSFIARQAVIYFRSKRLDDYSYQQAADLRDQLLE 95
Cdd:cd18547 7 LAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGvdfsglLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 96 KLFRVgPqIA----QQQG---------TGNVTTMVLEGINQvenylkLILAKIMnmsIIpwVILALVFYLDWESGLVLLL 162
Cdd:cd18547 87 KLQRL-P-LSyfdtHSHGdimsrvtndVDNISQALSQSLTQ------LISSILT---IV--GTLIMMLYISPLLTLIVLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 163 VFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKygksifaSSERFRKATMASLKVGILSTF 242
Cdd:cd18547 154 TVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEE-------AIEEFDEINEELYKASFKAQF 226
|
250 260 270
....*....|....*....|....*....|...
gi 491368637 243 -------ALDFFTTLSIAVVAVLLGLRLINEGI 268
Cdd:cd18547 227 ysgllmpIMNFINNLGYVLVAVVGGLLVINGAL 259
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
332-558 |
4.76e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.09 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAALTDINLNVTGFKKIGIIGLSGSGKSTLINTLSG---FLVpDSGEITLGGAKTTAFRQASWQEQLI 408
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGredYEV-TGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 409 YIP-QNP-----YIYRLTLQENVAFYQPTATKEAvLKAIEVAGLTE---LLAELPQGLDTM-LGEGerhLSGGQAQR-IA 477
Cdd:PRK09580 81 FMAfQYPveipgVSNQFFLQTALNAVRSYRGQEP-LDRFDFQDLMEekiALLKMPEDLLTRsVNVG---FSGGEKKRnDI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 478 LARAFLDQQRKILlfDEPTAHLDIETEVALKERMLPLM-ENRLVFFATHRLHWMEEM--DEIIVMDQGRIVEQG--TLAQ 552
Cdd:PRK09580 157 LQMAVLEPELCIL--DESDSGLDIDALKIVADGVNSLRdGKRSFIIVTHYQRILDYIkpDYVHVLYQGRIVKSGdfTLVK 234
|
....*.
gi 491368637 553 LQQKQG 558
Cdd:PRK09580 235 QLEEQG 240
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
144-281 |
5.45e-04 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 42.05 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 144 VILALVFYLDWESGLVLLLVFPLIIIFMIILGYAAQSKAEKQYRTFQLLSNHFIDSLRGIDTLKLFGVSKKYGKSIFASS 223
Cdd:cd18570 131 ISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKF 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491368637 224 ERFRKATMASLKVGILSTFALDFFTTLSIAVVAVLLGLRLINEGI-----LLFPALTILILAP 281
Cdd:cd18570 211 SKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLslgqlIAFNALLGYFLGP 273
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
88-294 |
6.33e-04 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 42.07 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 88 DLRDQLLEKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKL-ILAKIMNMSIIpWVILALVFYLDWESGLVLLLVFPL 166
Cdd:cd18545 74 DLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNgLINLIPDLLTL-VGIVIIMFSLNVRLALVTLAVLPL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 167 IIIFMIILgyaaQSKAEKQYRTFQL----LSNHFIDSLRGIDTLKLFgVSKKYGKSIFAS-SERFRKATMASLKVGILST 241
Cdd:cd18545 153 LVLVVFLL----RRRARKAWQRVRKkisnLNAYLHESISGIRVIQSF-AREDENEEIFDElNRENRKANMRAVRLNALFW 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491368637 242 FALDFFTTLSIAVVAVLLGLRLINEGILLFPALTILILAPEYFLPIRDFSSDY 294
Cdd:cd18545 228 PLVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFY 280
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
332-502 |
9.14e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.63 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 332 LTIDQLAFSYEEKAaLTDINLNVTGFKKIGIIGLSGSGKSTLINTLSGFLVPDSGEITLGGAKTTAFRQAswqeQLIYIP 411
Cdd:PRK13541 2 LSLHQLQFNIEQKN-LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP----YCTYIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 412 QNPYI-YRLTLQENVAFYQPT-ATKEAVLKAIEVAGLTELLAelpqgldtmlgEGERHLSGGQAQRIALARaFLDQQRKI 489
Cdd:PRK13541 77 HNLGLkLEMTVFENLKFWSEIyNSAETLYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIAR-LIACQSDL 144
|
170
....*....|...
gi 491368637 490 LLFDEPTAHLDIE 502
Cdd:PRK13541 145 WLLDEVETNLSKE 157
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
466-501 |
2.38e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 2.38e-03
10 20 30
....*....|....*....|....*....|....*.
gi 491368637 466 RHLSGGQAQRIALARAfLDQQRKILLFDEPTAHLDI 501
Cdd:PLN03073 343 KTFSGGWRMRIALARA-LFIEPDLLLLDEPTNHLDL 377
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
15-261 |
2.72e-03 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 40.11 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 15 LLGLL-AGLSFLQALFIigqayglARAITGLWEGRPLeeqWGWILLFFCSFIArQAVI-----YFRSKrlddYSYQQAAD 88
Cdd:cd18551 6 LLSLLgTAASLAQPLLV-------KNLIDALSAGGSS---GGLLALLVALFLL-QAVLsalssYLLGR----TGERVVLD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 89 LRDQLLEKLFRVGPQIAQQQGTGNVTTMVLEGINQVENYLKLILAKIMNMSIIpwVILALV--FYLDWESGLVLLLVFPL 166
Cdd:cd18551 71 LRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLT--VVGAVVlmFLLDWVLTLVTLAVVPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 167 IIIFMIILGyaaqSKAEKQYRTFQ----LLSNHFIDSLRGIDTLKLFGVSKKYGKSIfasSERFRKATMASLKVGILSTF 242
Cdd:cd18551 149 AFLIILPLG----RRIRKASKRAQdalgELSAALERALSAIRTVKASNAEERETKRG---GEAAERLYRAGLKAAKIEAL 221
|
250
....*....|....*....
gi 491368637 243 ALDFFTTLSIAVVAVLLGL 261
Cdd:cd18551 222 IGPLMGLAVQLALLVVLGV 240
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
362-537 |
2.93e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 362 IIGLSGSGKSTLI-------------NTLSGFLVPD-------SGEITLG-----GAKTTAFRQASWQEQLIYIPQNpyi 416
Cdd:cd03240 27 IVGQNGAGKTTIIealkyaltgelppNSKGGAHDPKliregevRAQVKLAfenanGKKYTITRSLAILENVIFCHQG--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 417 yrltlqenvafyqptatkeavlkaievagltELLAELPQGLDTmlgegerhLSGGQ------AQRIALARAF---LDqqr 487
Cdd:cd03240 104 -------------------------------ESNWPLLDMRGR--------CSGGEkvlaslIIRLALAETFgsnCG--- 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491368637 488 kILLFDEPTAHLDIET-EVALKE--RMLPLMENRLVFFATHRLHWMEEMDEII 537
Cdd:cd03240 142 -ILALDEPTTNLDEENiEESLAEiiEERKSQKNFQLIVITHDEELVDAADHIY 193
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
466-545 |
3.36e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 40.28 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368637 466 RHLSGGQAQRIALARaFLDQQRKILLFDEPTAHLDI--ETEV-----ALKERmlplmeNRLVFFATHRLhwMEEM---DE 535
Cdd:PRK11288 395 MNLSGGNQQKAILGR-WLSEDMKVILLDEPTRGIDVgaKHEIynviyELAAQ------GVAVLFVSSDL--PEVLgvaDR 465
|
90
....*....|
gi 491368637 536 IIVMDQGRIV 545
Cdd:PRK11288 466 IVVMREGRIA 475
|
|
| PRK07261 |
PRK07261 |
DNA topology modulation protein; |
359-378 |
5.12e-03 |
|
DNA topology modulation protein;
Pssm-ID: 180911 [Multi-domain] Cd Length: 171 Bit Score: 38.16 E-value: 5.12e-03
|
| YlqF_related_GTPase |
cd01849 |
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ... |
344-378 |
8.37e-03 |
|
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases.
Pssm-ID: 206746 [Multi-domain] Cd Length: 146 Bit Score: 36.98 E-value: 8.37e-03
10 20 30
....*....|....*....|....*....|....*..
gi 491368637 344 KAALTDINLNVTGFKKI--GIIGLSGSGKSTLINTLS 378
Cdd:cd01849 76 KAEITKQKLKLKYKKGIrvGVVGLPNVGKSSFINALL 112
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
362-402 |
8.37e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.88 E-value: 8.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 491368637 362 IIGLSGSGKSTLINTLSGFLVPdsgeitlggAKTTAFRQAS 402
Cdd:pfam13555 27 LTGPSGSGKSTLLDAIQTLLVP---------AKRARFNKAA 58
|
|
| |
