|
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: 592.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 2 IDKQIFK-IEGVKNILSWLVLLTFLQAVSILFQAFFLSKSIVILWH-QSAFSSAVPYIFGFAISLLCRHFFSLIKEGSAN 79
Cdd:COG4988 4 LDKRLKRlARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIgGAPLSALLPLLGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 80 SFSVTASEGLRDQLLGKYLSFGDQTIFKTGTGHAVSLLHAGIDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLRWQEALF 159
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 160 LLLIFPVIIFFFVILGLAAQKRADNEYRNFTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMT 239
Cdd:COG4988 164 LLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 240 STFSLDFFTTLSIAVIAVFLGFSLMEGKMSLFPALTLLVLAPEYFLPLRTFSEDYHATLDGKNAFTEVLSVINQKKTSEI 319
Cdd:COG4988 244 SSAVLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLDAPEPAAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 320 SALKVPAIDSETVLSVHNFSFQYPDGQQpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKF 398
Cdd:COG4988 324 AGTAPLPAAGPPSIELEDVSFSYPGGRP--ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGfLPPYSGSILINGVDL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 399 LNFQNTSWQKQIIYIPQKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQR 478
Cdd:COG4988 402 SDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQR 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 479 IALARAFLaSDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLE 558
Cdd:COG4988 482 LALARALL-RDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLA 560
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
12-542 |
1.34e-160 |
|
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: 468.69 E-value: 1.34e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 12 VKNILSWLVLLTFLQAVSILFQAFFLSKSIVILWHQS-AFSSAVPYIFGFAISLLCRHFFSLIKEGSANSFSVTASEGLR 90
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWLLARVVDGLISAGePLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 91 DQLLGKYLSFGDQTIFKTGTGHAVSLLHAGIDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLRWQEALFLLLIFPVIIFF 170
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 171 FVILGLAAQKRADNEYRNFTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTL 250
Cdd:TIGR02857 161 MILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 251 SIAVIAVFLGFSLMEGKMSLFPALTLLVLAPEYFLPLRTFSEDYHATLDGKNAFTEVLSVINQKKTSEISALKVPAIDSE 330
Cdd:TIGR02857 241 SVALVAVYIGFRLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 331 TvLSVHNFSFQYPDGqqPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFLNFQNTSWQKQ 409
Cdd:TIGR02857 321 S-LEFSGVSVAYPGR--RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGfVDPTEGSIAVNGVPLADADADSWRDQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 410 IIYIPQKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLaSD 489
Cdd:TIGR02857 398 IAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFL-RD 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 488907140 490 RHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVM 542
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-558 |
6.63e-106 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 330.20 E-value: 6.63e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 13 KNILSWLVLLTFLQAVSILFQAFFLSKSIVILWHQSAFSSAVPYIFGFAISLLCRHFFSLIKEGSANSFSVTASEGLRDQ 92
Cdd:COG1132 20 RGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 93 LLGKYLSFGDQTIFKTGTGHAVSLLHAGIDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLRWQEALFLLLIFPVIIFFFV 172
Cdd:COG1132 100 LFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 173 ILGLAAQKRADNEYRNFTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSI 252
Cdd:COG1132 180 LFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 253 AVIAVFLGFSLMEGKMSLFPALTLLVLAPEYFLPLRTFSEDYHATLDGKNAFTEVLSVINQKKTSEISALKVPAIDSETV 332
Cdd:COG1132 260 ALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLPPVRGE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQQpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG---INSGR---GDISINrnkflNFQNTSW 406
Cdd:COG1132 340 IEFENVSFSYPGDRP--VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfydPTSGRiliDGVDIR-----DLTLESL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 407 QKQIIYIPQKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFL 486
Cdd:COG1132 413 RRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALL 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488907140 487 AsDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLE 558
Cdd:COG1132 493 K-DPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA 563
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
19-307 |
1.92e-94 |
|
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: 290.46 E-value: 1.92e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 19 LVLLTFLQAVSILFQAFFLSKSIVILW-HQSAFSSAVPYIFGFAISLLCRHFFSLIKEGSANSFSVTASEGLRDQLLGKY 97
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFlEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 98 LSFGDQTIFKTGTGHAVSLLHAGIDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLRWQEALFLLLIFPVIIFFFVILGLA 177
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 178 AQKRADNEYRNFTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAV 257
Cdd:cd18584 161 AQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALVAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488907140 258 FLGFSLMEGKMSLFPALTLLVLAPEYFLPLRTFSEDYHATLDGKNAFTEV 307
Cdd:cd18584 241 YIGFRLLGGSLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAERL 290
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-556 |
4.56e-93 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 296.76 E-value: 4.56e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 18 WL---VLLTFLQAVSILFQAFFLSKsivILWH----QSAFSSAVPYIFGFAISLLCRHFFSLIKEgsanSFSVTASEGLR 90
Cdd:PRK11174 23 WLnlsILLGFLSGLLLIAQAWLLAT---ILQAliieNIPREALLPPFILLILLFVLRALLAWLRE----RVGFKAGQHIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 91 DQL----LGKYLSFGDQTIFKTGTGHAVSLLHAGIDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLRWQEALFLLLIFPV 166
Cdd:PRK11174 96 QQIrqqvLDKLQQLGPAWIQGKPAGSWATLVLEQVEDMHDFYARYLPQMALAVLVPLLILIAVFPINWAAGLILLGTAPL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 167 IIFFFVILGLAAqkrADNEYRNFTVL---NNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFS 243
Cdd:PRK11174 176 IPLFMALVGMGA---ADANRRNFLALarlSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRTMEVLRMAFLSSAV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 244 LDFFTTLSIAVIAVFLGFSLM--------EGKMSLFPALTLLVLAPEYFLPLRTFSEDYHATLDGKNAFTEVLSVINQKK 315
Cdd:PRK11174 253 LEFFASISIALVAVYFGFSYLgelnfghyGTGVTLFAGFFVLILAPEFYQPLRDLGTFYHAKAQAVGAAESLVTFLETPL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 316 TSEISALKVPAIDSETVLSVHNFSFQYPDGQQpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGRGDISINR 395
Cdd:PRK11174 333 AHPQQGEKELASNDPVTIEAEDLEILSPDGKT--LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKING 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 396 NKFLNFQNTSWQKQIIYIPQKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQ 475
Cdd:PRK11174 411 IELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQ 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 476 AQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRE 555
Cdd:PRK11174 491 AQRLALARA-LLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAE 569
|
.
gi 488907140 556 L 556
Cdd:PRK11174 570 L 570
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-570 |
6.10e-81 |
|
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: 268.24 E-value: 6.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 20 VLLTFLQAVSILFQAFFLSKSIVilwhQSAFSSAVPYIFGFAISLLCRHFFSLIK----EGSANSFSVTASEGLRDQLLG 95
Cdd:COG2274 166 LLINLLALATPLFTQVVIDRVLP----NQDLSTLWVLAIGLLLALLFEGLLRLLRsyllLRLGQRIDLRLSSRFFRHLLR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 96 KYLSFGDQTifktGTGHAVSLLHAgIDNVQNYF--QLIFIkIIDLSIIpWLLLIYMFFLRWQEALFLLLIFPVIIFFFVI 173
Cdd:COG2274 242 LPLSFFESR----SVGDLASRFRD-VESIREFLtgSLLTA-LLDLLFV-LIFLIVLFFYSPPLALVVLLLIPLYVLLGLL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 174 LGLAAQKRADNEYRNFTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSIA 253
Cdd:COG2274 315 FQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATV 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 254 VIAVFLGFSLMEGKMSL-----FPALTLLVLAPeyFLPLRTFSEDYHATldgKNAFTEVLSVINQKKTSEISALKVPAID 328
Cdd:COG2274 395 ALLWLGAYLVIDGQLTLgqliaFNILSGRFLAP--VAQLIGLLQRFQDA---KIALERLDDILDLPPEREEGRSKLSLPR 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 329 SETVLSVHNFSFQYPdGQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGR---GDISINrnkflNFQ 402
Cdd:COG2274 470 LKGDIELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLyepTSGRiliDGIDLR-----QID 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 403 NTSWQKQIIYIPQKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALA 482
Cdd:COG2274 544 PASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIA 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 483 RAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLEDfDG 562
Cdd:COG2274 624 RA-LLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR-KG 701
|
....*...
gi 488907140 563 KLNELRKE 570
Cdd:COG2274 702 LYAELVQQ 709
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
107-559 |
2.33e-80 |
|
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: 263.17 E-value: 2.33e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 107 KTGTGHAVSLLHAGIDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLRWQEALFLLLIFPVIIFFFVILGLAAQKRADNEY 186
Cdd:COG4987 108 RLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGLLLAGLLLPLLAARLGRRAGRRL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 187 -RNFTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVFLGFSLME 265
Cdd:COG4987 188 aAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 266 GKMSlFPALTLLVLAP----EYFLPLRTFSEDYHATLDgknAFTEVLSVINQKKTSEISALKVPAiDSETVLSVHNFSFQ 341
Cdd:COG4987 268 GALS-GPLLALLVLAAlalfEALAPLPAAAQHLGRVRA---AARRLNELLDAPPAVTEPAEPAPA-PGGPSLELEDVSFR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 342 YPDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG---INSGR---GDISINRnkflnFQNTSWQKQIIYIPQ 415
Cdd:COG4987 343 YPGAGRPV-LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRfldPQSGSitlGGVDLRD-----LDEDDLRRRIAVVPQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 416 KPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLaSDRHILLF 495
Cdd:COG4987 417 RPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALL-RDAPILLL 495
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488907140 496 DEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLED 559
Cdd:COG4987 496 DEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQ 559
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
135-555 |
3.38e-56 |
|
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: 200.86 E-value: 3.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 135 IIDLsiiPW--LLLIYMFFLRWQEALFLLLIFPVIIfffvILGLAAQKR----ADNEYRNFTVLNNRFADTLRGMQTLKQ 208
Cdd:TIGR03375 267 LIDL---PFalLFLLVIAIIGGPLVWVPLVAIPLIL----LPGLLLQRPlsrlAEESMRESAQRNAVLVESLSGLETIKA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 209 LGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVFLGFSLMEGKMSL--FPALTLL---VLAPey 283
Cdd:TIGR03375 340 LNAEGRFQRRWEQTVAALARSGLKSRFLSNLATNFAQFIQQLVSVAIVVVGVYLISDGELTMggLIACVMLsgrALAP-- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 284 flplrtfsedyhatldgKNAFTEVLSVINQKKTS-----EISALKVPAIDSETVLSV---------HNFSFQYPdGQQPA 349
Cdd:TIGR03375 418 -----------------LGQLAGLLTRYQQAKTAlqsldELMQLPVERPEGTRFLHRprlqgeiefRNVSFAYP-GQETP 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 350 ALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGR---GDISINrnkflnfqntswQ-------KQIIYIPQK 416
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLyqpTEGSvllDGVDIR------------QidpadlrRNIGYVPQD 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 417 PYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAfLASDRHILLFD 496
Cdd:TIGR03375 548 PRLFYGTLRDNIALGAPYADDEEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARA-LLRDPPILLLD 626
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 488907140 497 EPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGrPRE 555
Cdd:TIGR03375 627 EPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADG-PKD 684
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
337-558 |
2.78e-55 |
|
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: 186.67 E-value: 2.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 337 NFSFQYPDGQQpaALKDINFLVRGFAKVAVVGLSGSGKTT---LLSSLAGINSGRgdISINRNKFLNFQNTSWQKQIIYI 413
Cdd:cd03253 5 NVTFAYDPGRP--VLKDVSFTIPAGKKVAIVGPSGSGKSTilrLLFRFYDVSSGS--ILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 414 PQKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLaSDRHIL 493
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAIL-KNPPIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488907140 494 LFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLE 558
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA 224
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
333-568 |
2.88e-55 |
|
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: 186.67 E-value: 2.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPdGQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLA---GINSGRgdISINRNKFLNFQNTSWQKQ 409
Cdd:cd03251 1 VEFKNVTFRYP-GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPrfyDVDSGR--ILIDGHDVRDYTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 410 IIYIPQKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLAsD 489
Cdd:cd03251 78 IGLVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLK-D 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488907140 490 RHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLEDfDGKLNELR 568
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKLH 234
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
333-546 |
3.08e-53 |
|
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: 178.73 E-value: 3.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSG-RGDISINRNKFLNFQNTSWQKQII 411
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV-LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPtSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 412 YIPQKPYIFHTSLRENIafyqpdapkeqvvkaakaagiyelasglfngfdtmigeseqsLSGGQAQRIALARAFLaSDRH 491
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALL-RDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488907140 492 ILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGH 546
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
337-558 |
1.27e-52 |
|
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: 179.34 E-value: 1.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 337 NFSFQYpDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI-NSGRGDISINRNKFLNFQNTSWQKQIIYIPQ 415
Cdd:cd03254 7 NVNFSY-DEKKPV-LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFyDPQKGQILIDGIDIRDISRKSLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 416 KPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLAsDRHILLF 495
Cdd:cd03254 85 DTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR-DPKILIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488907140 496 DEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLE 558
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
88-558 |
5.45e-51 |
|
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: 184.53 E-value: 5.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 88 GLRDQLLGKYLSFGDQTIFKTGTGHAVSLLHAGIDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLRWQEALFLLLIFPVI 167
Cdd:TIGR02203 88 DIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 168 ifffVILGLAAQKRADNEYRNFTVLNNRFADTLRgmQTLKQLGLSRIFTKRIYETsERYRK--STMRSLTIAMTSTFSL- 244
Cdd:TIGR02203 168 ----SILMRRVSKRLRRISKEIQNSMGQVTTVAE--ETLQGYRVVKLFGGQAYET-RRFDAvsNRNRRLAMKMTSAGSIs 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 245 DFFTTLSIAV-IAVFLGFSLMEGKMSLFPALTLLVL---APEYFLPLRTFSEDYHATLDGKNAFTEVLSVINQkkTSEIS 320
Cdd:TIGR02203 241 SPITQLIASLaLAVVLFIALFQAQAGSLTAGDFTAFitaMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDS--PPEKD 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 321 ALKVPAIDSETVLSVHNFSFQYPDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFL 399
Cdd:TIGR02203 319 TGTRAIERARGDVEFRNVTFRYPGRDRPA-LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRfYEPDSGQILLDGHDLA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 400 NFQNTSWQKQIIYIPQKPYIFHTSLRENIAFYQP-DAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQR 478
Cdd:TIGR02203 398 DYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQR 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 479 IALARAFLaSDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLE 558
Cdd:TIGR02203 478 LAIARALL-KDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLA 556
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
336-558 |
7.48e-50 |
|
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: 172.34 E-value: 7.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 336 HNFSFQYPDGQQPAALKDINFLVRGFAKVAVVGLSGSGKTT---LLSSLAGINSGRgdISINR--NKFLNFQntSWQKQI 410
Cdd:cd03249 4 KNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTvvsLLERFYDPTSGE--ILLDGvdIRDLNLR--WLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 411 IYIPQKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLaSDR 490
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL-RNP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488907140 491 HILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLE 558
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
337-551 |
1.15e-49 |
|
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: 171.23 E-value: 1.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 337 NFSFQYPDgQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISINrnkflnfqNT-SWQ------- 407
Cdd:cd03245 7 NVSFSYPN-QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKpTSGSVLLD--------GTdIRQldpadlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 408 KQIIYIPQKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLA 487
Cdd:cd03245 78 RNIGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488907140 488 sDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQG 551
Cdd:cd03245 158 -DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
109-530 |
4.44e-49 |
|
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: 178.32 E-value: 4.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 109 GTGHAVSLLHAGIDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLRWQEALFLLLIfpVIIFFFV---ILGLAAQKRADNE 185
Cdd:TIGR02868 108 RRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAG--LLLAGFVaplVSLRAARAAEQAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 186 YRNFTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERY-----RKSTMRSLTIAMTSTFsldffttLSIAVIAVFL- 259
Cdd:TIGR02868 186 ARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELtraerRAAAATALGAALTLLA-------AGLAVLGALWa 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 260 -GFSLMEGKMSLfPALTLLVLAP----EYFLPLRTFSEDYHATLDGKNAFTEVLSVINQKKTSEISALKVPAIDSETvLS 334
Cdd:TIGR02868 259 gGPAVADGRLAP-VTLAVLVLLPlaafEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPT-LE 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 335 VHNFSFQYPDGqqPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGR-GDISINRNKFLNFQNTSWQKQIIYI 413
Cdd:TIGR02868 337 LRDLSAGYPGA--PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLqGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 414 PQKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAfLASDRHIL 493
Cdd:TIGR02868 415 AQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARA-LLADAPIL 493
|
410 420 430
....*....|....*....|....*....|....*..
gi 488907140 494 LFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRL 530
Cdd:TIGR02868 494 LLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
337-557 |
1.27e-46 |
|
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: 163.43 E-value: 1.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 337 NFSFQY-PDGqqPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGIN-SGRGDISINRNKFLNFQNTSWQKQIIYIP 414
Cdd:cd03252 5 HVRFRYkPDG--PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYvPENGRVLVDGHDLALADPAWLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 415 QKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAfLASDRHILL 494
Cdd:cd03252 83 QENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARA-LIHNPRILI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488907140 495 FDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELL 557
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
146-557 |
7.61e-46 |
|
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: 170.27 E-value: 7.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 146 LIYMFFLRWQEALFLLLIFPVIIFFFVILGLAAQKRADNEYRNFTVLNNRFADTLRGMQTLKQlglsriFTKRIYETSeR 225
Cdd:TIGR02204 150 LIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQA------FGHEDAERS-R 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 226 YRKSTMRSLTIAMTSTFSLDFFTTLSI-----AVIAV--FLGFSLMEGKMS-----LFPALTLLVLAPeyflpLRTFSED 293
Cdd:TIGR02204 223 FGGAVEKAYEAARQRIRTRALLTAIVIvlvfgAIVGVlwVGAHDVIAGKMSagtlgQFVFYAVMVAGS-----IGTLSEV 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 294 YhATLDGKNAFTEVLSVINQKKtSEISALKVP---AIDSETVLSVHNFSFQYPDGQQPAALKDINFLVRGFAKVAVVGLS 370
Cdd:TIGR02204 298 W-GELQRAAGAAERLIELLQAE-PDIKAPAHPktlPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPS 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 371 GSGKTTLLSSLAGI-NSGRGDISINRNKFLNFQNTSWQKQIIYIPQKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGI 449
Cdd:TIGR02204 376 GAGKSTLFQLLLRFyDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHA 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 450 YELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLAsDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHR 529
Cdd:TIGR02204 456 HEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILK-DAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHR 534
|
410 420
....*....|....*....|....*...
gi 488907140 530 LHWLKQMDYVLVMDNGHIIEQGRPRELL 557
Cdd:TIGR02204 535 LATVLKADRIVVMDQGRIVAQGTHAELI 562
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
141-557 |
1.21e-43 |
|
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: 163.29 E-value: 1.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 141 IPW----LLLIYMF--FLRwqealFLLLIFPVIIFFFVILGLAAQKRADNEYRNFTVLNNRFAD-TLRGMQTLKQLGLSR 213
Cdd:TIGR01842 126 APWmpiyLLVCFLLhpWIG-----ILALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLADsALRNAEVIEAMGMMG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 214 IFTKRIYETSERYRKSTMR-SLTIAMTSTFSLDFFTTLSIAVIAvfLGFSL-MEGKMS--LFPALTLLV---LAPeyflp 286
Cdd:TIGR01842 201 NLTKRWGRFHSKYLSAQSAaSDRAGMLSNLSKYFRIVLQSLVLG--LGAYLaIDGEITpgMMIAGSILVgraLAP----- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 287 LRTFSEDYHATLDGKNAFTEVLSVINQKKTSEiSALKVPAidSETVLSVHNFSFQYPDGQQPAaLKDINFLVRGFAKVAV 366
Cdd:TIGR01842 274 IDGAIGGWKQFSGARQAYKRLNELLANYPSRD-PAMPLPE--PEGHLSVENVTIVPPGGKKPT-LRGISFSLQAGEALAI 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 367 VGLSGSGKTTLLSSLAGINS-GRGDISINRNKFLNFQNTSWQKQIIYIPQKPYIFHTSLRENIAFYQPDAPKEQVVKAAK 445
Cdd:TIGR01842 350 IGPSGSGKSTLARLIVGIWPpTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAK 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 446 AAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLAsDRHILLFDEPTAHLDIQTEYDLKQTMLPL-LENHLVF 524
Cdd:TIGR01842 430 LAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYG-DPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVV 508
|
410 420 430
....*....|....*....|....*....|...
gi 488907140 525 FATHRLHWLKQMDYVLVMDNGHIIEQGRPRELL 557
Cdd:TIGR01842 509 VITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
305-557 |
1.26e-42 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 161.15 E-value: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 305 TEVLSVINQKKTSEISALKVPAIDSETvLSVHNFSFQYPDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLA-G 383
Cdd:PRK11160 312 RRINEITEQKPEVTFPTTSTAAADQVS-LTLNNVSFTYPDQPQPV-LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 384 INSGRGDISINRNKFLNFQNTSWQKQIIYIPQKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLfNGFDTM 463
Cdd:PRK11160 390 WDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLEDD-KGLNAW 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 464 IGESEQSLSGGQAQRIALARAFLaSDRHILLFDEPTAHLDIQTEydlkQTMLPLLENHL----VFFATHRLHWLKQMDYV 539
Cdd:PRK11160 469 LGEGGRQLSGGEQRRLGIARALL-HDAPLLLLDEPTEGLDAETE----RQILELLAEHAqnktVLMITHRLTGLEQFDRI 543
|
250
....*....|....*...
gi 488907140 540 LVMDNGHIIEQGRPRELL 557
Cdd:PRK11160 544 CVMDNGQIIEQGTHQELL 561
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
139-558 |
1.77e-42 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 160.57 E-value: 1.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 139 SIIPwlLLIYMFFLRWQEALFLLLIFPVIifFFVIlglaaqkradneyrnfTVLNNRFADTLRGMQT------------L 206
Cdd:PRK11176 152 SIIG--LFIMMFYYSWQLSLILIVIAPIV--SIAI----------------RVVSKRFRNISKNMQNtmgqvttsaeqmL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 207 KQLGLSRIF------TKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVFLGF-SLMEgkmSLFPALTLLVL 279
Cdd:PRK11176 212 KGHKEVLIFggqeveTKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFpSVMD---TLTAGTITVVF 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 280 APEYFL--PLRTFSEDYHATLDGKNAFTEVLSVINQKKTSEISALKVPAIDSEtvLSVHNFSFQYPDGQQPAaLKDINFL 357
Cdd:PRK11176 289 SSMIALmrPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDEGKRVIERAKGD--IEFRNVTFTYPGKEVPA-LRNINFK 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 358 VRGFAKVAVVGLSGSGKTT---LLSSLAGINSGRgdISINRNKFLNFQNTSWQKQIIYIPQKPYIFHTSLRENIAFYQPD 434
Cdd:PRK11176 366 IPAGKTVALVGRSGSGKSTianLLTRFYDIDEGE--ILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTE 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 435 A-PKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLaSDRHILLFDEPTAHLDIQTEYDLKQT 513
Cdd:PRK11176 444 QySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALL-RDSPILILDEATSALDTESERAIQAA 522
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 488907140 514 MLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLE 558
Cdd:PRK11176 523 LDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLA 567
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
144-557 |
4.43e-42 |
|
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: 161.06 E-value: 4.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 144 LLLIYMFF---LRWQEALFLLLIFPVIIFFFVILGLAA--QKRADNEYRNFTVLNNRFADTLRGMQTLKQLGLSRIFTKR 218
Cdd:TIGR01846 263 LLFVVVFLavmFFYSPTLTGVVIGSLVCYALLSVFVGPilRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 219 IYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVFLGFSLMEGKMSL-----FPALTLLVLAPeyFLPLRTFSED 293
Cdd:TIGR01846 343 WDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPgqlvaFNMLAGRVTQP--VLRLAQLWQD 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 294 YHATLDgknAFTEVLSVINQ-KKTSEISALKVPAIDSEtvLSVHNFSFQY-PDgqQPAALKDINFLVRGFAKVAVVGLSG 371
Cdd:TIGR01846 421 FQQTGI---ALERLGDILNSpTEPRSAGLAALPELRGA--ITFENIRFRYaPD--SPEVLSNLNLDIKPGEFIGIVGPSG 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 372 SGKTTLLSSLAGINS-GRGDISINRNKFLNFQNTSWQKQIIYIPQKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIY 450
Cdd:TIGR01846 494 SGKSTLTKLLQRLYTpQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAH 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 451 ELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLASDRhILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRL 530
Cdd:TIGR01846 574 DFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPR-ILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRL 652
|
410 420
....*....|....*....|....*..
gi 488907140 531 HWLKQMDYVLVMDNGHIIEQGRPRELL 557
Cdd:TIGR01846 653 STVRACDRIIVLEKGQIAESGRHEELL 679
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
333-555 |
8.01e-42 |
|
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: 158.37 E-value: 8.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGR---GDISInrnkflnfqnTSW 406
Cdd:COG4618 331 LSVENLTVVPPGSKRPI-LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVwppTAGSvrlDGADL----------SQW 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 407 QKQ-----IIYIPQKPYIFHTSLRENIA-FYQPDApkEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIA 480
Cdd:COG4618 400 DREelgrhIGYLPQDVELFDGTIAENIArFGDADP--EKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIG 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488907140 481 LARAFLASDRhILLFDEPTAHLDIQTEYDLKQTMLPL-LENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGrPRE 555
Cdd:COG4618 478 LARALYGDPR-LVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFG-PRD 551
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
135-557 |
3.28e-41 |
|
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: 158.75 E-value: 3.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 135 IIDLSIIPWLLLIYMFFLRWQEALFLLLIFPVIIFFFVILGL---AAQKRADNEYRNFTVLNNRFADTLRGMQTLKQLGL 211
Cdd:TIGR01193 273 ILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILfkrTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 212 SRIFTKRIYETSERYRKSTMRsLTIAMTSTFSLDFFTTLSIAVIAVFLG-FSLMEGKMSLFPALTLLVLAPEYFLPLRT- 289
Cdd:TIGR01193 353 EAERYSKIDSEFGDYLNKSFK-YQKADQGQQAIKAVTKLILNVVILWTGaYLVMRGKLTLGQLITFNALLSYFLTPLENi 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 290 --FSEDYHATLDGKNAFTEVLSVINQ-KKTSEISALKVPAIDsetvLSVHNFSFQYpdGQQPAALKDINFLVRGFAKVAV 366
Cdd:TIGR01193 432 inLQPKLQAARVANNRLNEVYLVDSEfINKKKRTELNNLNGD----IVINDVSYSY--GYGSNILSDISLTIKMNSKTTI 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 367 VGLSGSGKTTLLSSLAGI-NSGRGDISINRNKFLNFQNTSWQKQIIYIPQKPYIFHTSLRENIAF-YQPDAPKEQVVKAA 444
Cdd:TIGR01193 506 VGMSGSGKSTLAKLLVGFfQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAAC 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 445 KAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLaSDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVF 524
Cdd:TIGR01193 586 EIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALL-TDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTIIF 664
|
410 420 430
....*....|....*....|....*....|...
gi 488907140 525 FAtHRLHWLKQMDYVLVMDNGHIIEQGRPRELL 557
Cdd:TIGR01193 665 VA-HRLSVAKQSDKIIVLDHGKIIEQGSHDELL 696
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
333-553 |
3.63e-41 |
|
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: 148.41 E-value: 3.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSG-RGDISINRnkflnfQNTS------ 405
Cdd:cd03244 3 IEFKNVSLRYRPNLPPV-LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELsSGSILIDG------VDISkiglhd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 406 WQKQIIYIPQKPYIFHTSLRENIAFYQpDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAF 485
Cdd:cd03244 76 LRSRISIIPQDPVLFSGTIRSNLDPFG-EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488907140 486 LaSDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRP 553
Cdd:cd03244 155 L-RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
145-561 |
4.51e-41 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 158.35 E-value: 4.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 145 LLIYMFFLRWQEALFLLLIFPVIIFFFVILGLAAQKRADnEYRNFTVLNNRFA-DTLRGMQTLkqlglsRIFTKRIYETS 223
Cdd:TIGR00958 292 LLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSE-ELQEAVAKANQVAeEALSGMRTV------RSFAAEEGEAS 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 224 eRYRKSTMRSLTIAMTSTFSLDFFTTLS------IAVIAVFLGFSL-MEGKMSLFPALTLLVLAPEYFLPLRTFSEDYHA 296
Cdd:TIGR00958 365 -RFKEALEETLQLNKRKALAYAGYLWTTsvlgmlIQVLVLYYGGQLvLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSG 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 297 TLDGKNAFTEVLSVINQKKTSEISALKVPAIDsETVLSVHNFSFQYPDGQQPAALKDINFLVRGFAKVAVVGLSGSGKTT 376
Cdd:TIGR00958 444 MMQAVGASEKVFEYLDRKPNIPLTGTLAPLNL-EGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKST 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 377 LLSSLAGI-NSGRGDISINRNKFLNFQNTSWQKQIIYIPQKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASG 455
Cdd:TIGR00958 523 VAALLQNLyQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIME 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 456 LFNGFDTMIGESEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQtmLPLLENHLVFFATHRLHWLKQ 535
Cdd:TIGR00958 603 FPNGYDTEVGEKGSQLSGGQKQRIAIARA-LVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVER 679
|
410 420
....*....|....*....|....*.
gi 488907140 536 MDYVLVMDNGHIIEQGRPRELLEDFD 561
Cdd:TIGR00958 680 ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
333-545 |
2.31e-40 |
|
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: 145.30 E-value: 2.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQQPAA--LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGinsgrgDISINRNKFlnfqntSWQKQI 410
Cdd:cd03250 1 ISVEDASFTWDSGEQETSftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG------ELEKLSGSV------SVPGSI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 411 IYIPQKPYIFHTSLRENIAFYQP-DAPK-EQVVKAAkaAGIYELASgLFNGFDTMIGESEQSLSGGQAQRIALARAFLaS 488
Cdd:cd03250 69 AYVSQEPWIQNGTIRENILFGKPfDEERyEKVIKAC--ALEPDLEI-LPDGDLTEIGEKGINLSGGQKQRISLARAVY-S 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488907140 489 DRHILLFDEPTAHLDIQTEYDLKQTML--PLLENHLVFFATHRLHWLKQMDYVLVMDNG 545
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFENCIlgLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
337-558 |
2.60e-38 |
|
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: 149.20 E-value: 2.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 337 NFSFQYpDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTT---LLSSLAGINSGRgdISINRNKFLNFQNTSWQKQIIYI 413
Cdd:COG5265 362 NVSFGY-DPERPI-LKGVSFEVPAGKTVAIVGPSGAGKSTlarLLFRFYDVTSGR--ILIDGQDIRDVTQASLRAAIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 414 PQKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLASDRhIL 493
Cdd:COG5265 438 PQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPP-IL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488907140 494 LFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLE 558
Cdd:COG5265 517 IFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLA 581
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
333-551 |
4.56e-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: 138.21 E-value: 4.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFLNFQNTSwQKQII 411
Cdd:cd03247 1 LSINNVSFSYPEQEQQV-LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEITLDGVPVSDLEKAL-SSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 412 YIPQKPYIFHTSLRENIAfyqpdapkeqvvkaakaagiyelasglfngfdtmigeseQSLSGGQAQRIALARAFLaSDRH 491
Cdd:cd03247 79 VLNQRPYLFDTTLRNNLG---------------------------------------RRFSGGERQRLALARILL-QDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 492 ILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQG 551
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
336-570 |
9.41e-37 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 144.33 E-value: 9.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 336 HNFSFQYPDGQQpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGRgdISINRNKFLNFQNTSWQKQIIY 412
Cdd:PRK13657 338 DDVSFSYDNSRQ--GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVfdpQSGR--ILIDGTDIRTVTRASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 413 IPQKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLaSDRHI 492
Cdd:PRK13657 414 VFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALL-KDPPI 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488907140 493 LLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLeDFDGKLNELRKE 570
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELV-ARGGRFAALLRA 569
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
333-561 |
1.54e-36 |
|
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: 135.92 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQQpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISINRNKFLNFQNTSWQKQII 411
Cdd:COG1122 1 IELENLSFSYPGGTP--ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKpTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 412 YIPQKP--YIFHTSLRENIAF------YQPDAPKEQVVKAAKAAGIYELAsglfngfdtmiGESEQSLSGGQAQRIALAR 483
Cdd:COG1122 79 LVFQNPddQLFAPTVEEDVAFgpenlgLPREEIRERVEEALELVGLEHLA-----------DRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 484 AfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHL-VFFATHRLHWLKQM-DYVLVMDNGHIIEQGRPRELLEDFD 561
Cdd:COG1122 148 V-LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKtVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
152-558 |
3.40e-34 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 136.77 E-value: 3.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 152 LRWQEALFLLLIFPVIIFFFVILGLAAQKRADNEYRNFTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTM 231
Cdd:PRK10789 135 ISWQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNM 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 232 RSLTIamtstfSLDFFTTLSIAV-IAVFL---GFSLM--EGKMSLfPALTLLVLapeyFL-----PLRTFSEDYHATLDG 300
Cdd:PRK10789 215 RVARI------DARFDPTIYIAIgMANLLaigGGSWMvvNGSLTL-GQLTSFVM----YLglmiwPMLALAWMFNIVERG 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 301 KNAFTEVLSVINQKKTSEISALKVPAidSETVLSVHNFSFQYPDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSS 380
Cdd:PRK10789 284 SAAYSRIRAMLAEAPVVKDGSEPVPE--GRGELDVNIRQFTYPQTDHPA-LENVNFTLKPGQMLGICGPTGSGKSTLLSL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 381 LA-GINSGRGDISINRNKFLNFQNTSWQKQIIYIPQKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNG 459
Cdd:PRK10789 361 IQrHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQG 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 460 FDTMIGESEQSLSGGQAQRIALARAFLAsDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYV 539
Cdd:PRK10789 441 YDTEVGERGVMLSGGQKQRISIARALLL-NAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEI 519
|
410
....*....|....*....
gi 488907140 540 LVMDNGHIIEQGRPRELLE 558
Cdd:PRK10789 520 LVMQHGHIAQRGNHDQLAQ 538
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
328-547 |
9.26e-34 |
|
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: 127.97 E-value: 9.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 328 DSETVLSVHNFSFQYPDGQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGRGDISINRNKFLN-FQNTSW 406
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 407 QKQIIYIPQKPYIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAfL 486
Cdd:cd03248 87 HSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA-L 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488907140 487 ASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHI 547
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
334-546 |
2.53e-33 |
|
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: 126.43 E-value: 2.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 334 SVHNFSFQYPDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFLNFQNTSWQKQIIY 412
Cdd:cd03225 1 ELKNLSFSYPDGARPA-LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGlLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 413 IPQKP--YIFHTSLRENIAF------YQPDAPKEQVVKAAKAAGIYELAsglfngfdtmiGESEQSLSGGQAQRIALARA 484
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFglenlgLPEEEIEERVEEALELVGLEGLR-----------DRSPFTLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488907140 485 fLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLL-ENHLVFFATHRLHWLKQ-MDYVLVMDNGH 546
Cdd:cd03225 149 -LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
19-296 |
4.14e-33 |
|
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: 128.17 E-value: 4.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 19 LVLLTFLQAVSILFQAFFLSKSIVILWHQSAFSSAVPYIFGFAISLLCRHFFSLIKEGSANSFSVTASEGLRDQLLGKYL 98
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 99 SFGDQTIFKTGTGHAVSLLHAGIDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLRWQEALFLLLIFPVIIFFFVILGLAA 178
Cdd:cd18561 81 KLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 179 QKRADNEYRNFTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVF 258
Cdd:cd18561 161 KDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGV 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 488907140 259 LGFSLMEGKMSLFPALTLLVLAPEYFLPLRTFSEDYHA 296
Cdd:cd18561 241 GALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHA 278
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
333-575 |
5.13e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 126.33 E-value: 5.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINrNKFLNFQNTSWQKQII 411
Cdd:COG1131 1 IEVRGLTKRYGDKT---ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGlLRPTSGEVRVL-GEDVARDPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 412 YIPQKPYIFHT-SLRENIAFYQ------PDAPKEQVVKAAKAAGIYELAsglfngfDTMIGeseqSLSGGQAQRIALARA 484
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFFArlyglpRKEARERIDELLELFGLTDAA-------DRKVG----TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 485 fLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLL-ENHLVFFATHRLHWLKQM-DYVLVMDNGHIIEQGRPRELLEDFdg 562
Cdd:COG1131 146 -LLHDPELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKARL-- 222
|
250
....*....|...
gi 488907140 563 kLNELRKELTDEK 575
Cdd:COG1131 223 -LEDVFLELTGEE 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
330-559 |
1.63e-32 |
|
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: 131.18 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 330 ETVLSVHNFSFQYPDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI--NSGR--GDISINRNKFLNFQNTS 405
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPA-VDGVSLTIAPGETVALVGESGSGKSTLALALMGLlpHGGRisGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 406 WQKQIIYIPQKPY--IFHTSLRENIAF------YQPDAPKEQVVKAAKAAGIyelasglfngfDTMIGESEQSLSGGQAQ 477
Cdd:COG1123 81 RGRRIGMVFQDPMtqLNPVTVGDQIAEalenlgLSRAEARARVLELLEAVGL-----------ERRLDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 478 RIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENH--LVFFATHRLHWLKQM-DYVLVMDNGHIIEQGRPR 554
Cdd:COG1123 150 RVAIAMA-LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPE 228
|
....*
gi 488907140 555 ELLED 559
Cdd:COG1123 229 EILAA 233
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
332-558 |
3.47e-32 |
|
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: 124.20 E-value: 3.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYpdgQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINrNKFLNFQNTSWQKQI 410
Cdd:COG4555 1 MIEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGlLKPDSGSILID-GEDVRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 411 IYIPQKPYIF-HTSLRENIAFYqpdAPKEQVVKAAKAAGIYELAS--GLFNGFDTMIGEseqsLSGGQAQRIALARAfLA 487
Cdd:COG4555 77 GVLPDERGLYdRLTVRENIRYF---AELYGLFDEELKKRIEELIEllGLEEFLDRRVGE----LSTGMKKKVALARA-LV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488907140 488 SDRHILLFDEPTAHLDIQTEYDLKQTMLPLL-ENHLVFFATHRLHWLKQM-DYVLVMDNGHIIEQGRPRELLE 558
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELRE 221
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
145-558 |
6.69e-32 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 130.22 E-value: 6.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 145 LLIYMFFLRWQEALFLLLIFPVIIFFFVIlglaaqkradneYRNFTV------------LNNRFADTLRGMQTLKQLGLS 212
Cdd:PRK10790 156 MLVAMFSLDWRMALVAIMIFPAVLVVMVI------------YQRYSTpivrrvrayladINDGFNEVINGMSVIQQFRQQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 213 RIFTKRIYETSERYRKSTMRSLtiamtstfSLDffttlsiaviavflGFsLMEGKMSLFPALTLLVLapeyfLPLRTFSE 292
Cdd:PRK10790 224 ARFGERMGEASRSHYMARMQTL--------RLD--------------GF-LLRPLLSLFSALILCGL-----LMLFGFSA 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 293 DYHATLDGKNAFTEVLSVINQ---KKTSEISALKVPAIDSETV----------------------LSVHNFSFQYPDGQQ 347
Cdd:PRK10790 276 SGTIEVGVLYAFISYLGRLNEpliELTTQQSMLQQAVVAGERVfelmdgprqqygnddrplqsgrIDIDNVSFAYRDDNL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 348 paALKDINFLV--RGFakVAVVGLSGSGKTTLLSSLAGINS-GRGDISINRNKFLNFQNTSWQKQIIYIPQKPYIFHTSL 424
Cdd:PRK10790 356 --VLQNINLSVpsRGF--VALVGHTGSGKSTLASLLMGYYPlTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTF 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 425 RENIAFYQpDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLASDRhILLFDEPTAHLDI 504
Cdd:PRK10790 432 LANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQ-ILILDEATANIDS 509
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 488907140 505 QTEYDLKQTmLPLLENH--LVFFAtHRLHWLKQMDYVLVMDNGHIIEQGRPRELLE 558
Cdd:PRK10790 510 GTEQAIQQA-LAAVREHttLVVIA-HRLSTIVEADTILVLHRGQAVEQGTHQQLLA 563
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
332-551 |
2.34e-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: 121.46 E-value: 2.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPDGQQP-AALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG---INSGR-----GDISINRNKFLNFq 402
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGllkPTSGSiifdgKDLLKLSRRLRKI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 403 ntsWQKQIIYIPQKPY--------IFHtSLRENIAFYQPDAPKEqvvkaAKAAGIYELASGlfngfdtmIGESEQ----- 469
Cdd:cd03257 80 ---RRKEIQMVFQDPMsslnprmtIGE-QIAEPLRIHGKLSKKE-----ARKEAVLLLLVG--------VGLPEEvlnry 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 470 --SLSGGQAQRIALARAfLASDRHILLFDEPTAHLD-------------IQTEYDLkqTMLpllenhlvfFATHRLHWLK 534
Cdd:cd03257 143 phELSGGQRQRVAIARA-LALNPKLLIADEPTSALDvsvqaqildllkkLQEELGL--TLL---------FITHDLGVVA 210
|
250
....*....|....*...
gi 488907140 535 QM-DYVLVMDNGHIIEQG 551
Cdd:cd03257 211 KIaDRVAVMYAGKIVEEG 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
333-556 |
9.52e-30 |
|
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: 116.90 E-value: 9.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGR------GDISIN-RNKFLNFQNTS 405
Cdd:cd03260 1 IELRDLNVYYGDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdeGEVLLDgKDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 406 W-QKQIIYIPQKPYIFHTSLRENIAF------YQP-DAPKEQVVKAAKAAGIYELASGLFNGFdtmigeseqSLSGGQAQ 477
Cdd:cd03260 78 ElRRRVGMVFQKPNPFPGSIYDNVAYglrlhgIKLkEELDERVEEALRKAALWDEVKDRLHAL---------GLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 478 RIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQM-DYVLVMDNGHIIEQGRPREL 556
Cdd:cd03260 149 RLCLARA-LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
333-550 |
1.39e-29 |
|
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: 116.03 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQQP-AALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISINrNKFLNFQNtswqKQI 410
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERpTSGEVLVD-GEPVTGPG----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 411 IYIPQKPYIF-HTSLRENIAFyqpdAPKEQVVKAAKAAgiyELASGLFNgfdtMIG--ESEQS----LSGGQAQRIALAR 483
Cdd:cd03293 76 GYVFQQDALLpWLTVLDNVAL----GLELQGVPKAEAR---ERAEELLE----LVGlsGFENAyphqLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488907140 484 AfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHL--VFFATHRLHWLKQM-DYVLVMDN--GHIIEQ 550
Cdd:cd03293 145 A-LAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGktVLLVTHDIDEAVFLaDRVVVLSArpGRIVAE 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
329-574 |
1.68e-29 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 117.11 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 329 SETVLSVHNFSFQYPDGQQP-AALKDINFLVR-G-FakVAVVGLSGSGKTTLLSSLAG-INSGRGDISINrnkflNFQNT 404
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGvTALDDVSLTVAaGeF--VALVGPSGCGKSTLLRLIAGlEKPTSGEVLVD-----GKPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 405 SWQKQIIYIPQKPYIF-HTSLRENIAFyqpdAPKEQVVKAAKAAgiyELASGLFNgfdtMIG--ESEQS----LSGGQAQ 477
Cdd:COG1116 77 GPGPDRGVVFQEPALLpWLTVLDNVAL----GLELRGVPKAERR---ERARELLE----LVGlaGFEDAyphqLSGGMRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 478 RIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENH--LVFFATH------RLhwlkqMDYVLVMDN--GHI 547
Cdd:COG1116 146 RVAIARA-LANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHdvdeavFL-----ADRVVVLSArpGRI 219
|
250 260 270
....*....|....*....|....*....|..
gi 488907140 548 IEQ-----GRPRELLEDFDGKLNELRKELTDE 574
Cdd:COG1116 220 VEEidvdlPRPRDRELRTSPEFAALRAEILDL 251
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
325-559 |
2.51e-29 |
|
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: 121.55 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 325 PAIDSETVLSVHNFSFQYPDGQQPA--ALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGR----G-DISIN 394
Cdd:COG1123 253 AAAAAEPLLEVRNLSKRYPVRGKGGvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLlrpTSGSilfdGkDLTKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 395 RNKFLNfqntSWQKQIIYIPQKPYifhTSL------RENIAF---YQPDAPKEQVV-KAAKAAGIYELASGLFNGFdtmI 464
Cdd:COG1123 333 SRRSLR----ELRRRVQMVFQDPY---SSLnprmtvGDIIAEplrLHGLLSRAERReRVAELLERVGLPPDLADRY---P 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 465 GEseqsLSGGQAQRIALARAfLASDRHILLFDEPTAHLD-------------IQTEYDLkqTMLpllenhlvfFATHRLH 531
Cdd:COG1123 403 HE----LSGGQRQRVAIARA-LALEPKLLILDEPTSALDvsvqaqilnllrdLQRELGL--TYL---------FISHDLA 466
|
250 260
....*....|....*....|....*....
gi 488907140 532 WLKQM-DYVLVMDNGHIIEQGRPRELLED 559
Cdd:COG1123 467 VVRYIaDRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
332-557 |
2.67e-29 |
|
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: 116.30 E-value: 2.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPDGQqpaALKDINF-LVRG-FakVAVVGLSGSGKTTLLSSLAGINS-GRGDISINRNKFLNFQNTSWQK 408
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLsLPPGeV--TALLGPNGSGKSTLLRALAGLLKpSSGEVLLDGRDLASLSRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 409 QIIYIPQKPYI-FHTSLRENIA---------FYQPDAPKEQVVKAA-KAAGIYELAsglfngfDTMIGEseqsLSGGQAQ 477
Cdd:COG1120 76 RIAYVPQEPPApFGLTVRELVAlgryphlglFGRPSAEDREAVEEAlERTGLEHLA-------DRPVDE----LSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 478 RIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTM--LPLLENHLVFFATHRL-HWLKQMDYVLVMDNGHIIEQGRPR 554
Cdd:COG1120 145 RVLIARA-LAQEPPLLLLDEPTSHLDLAHQLEVLELLrrLARERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPE 223
|
...
gi 488907140 555 ELL 557
Cdd:COG1120 224 EVL 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
328-557 |
3.95e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.57 E-value: 3.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 328 DSETVLSVHNFSFQYpdGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFlnfqnTSW 406
Cdd:COG1121 2 MMMPAIELENLTVSY--GGRPV-LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGlLPPTSGTVRLFGKPP-----RRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 407 QKQIIYIPQKPYI---FHTSLRENIA---------FYQPDAP-KEQVVKAAKAAGIYELAsglfngfDTMIGEseqsLSG 473
Cdd:COG1121 74 RRRIGYVPQRAEVdwdFPITVRDVVLmgrygrrglFRRPSRAdREAVDEALERVGLEDLA-------DRPIGE----LSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 474 GQAQRIALARAfLASDRHILLFDEPTAHLDIQTEydlkQTMLPLL-----ENHLVFFATHRLHWLKQM-DYVLVMdNGHI 547
Cdd:COG1121 143 GQQQRVLLARA-LAQDPDLLLLDEPFAGVDAATE----EALYELLrelrrEGKTILVVTHDLGAVREYfDRVLLL-NRGL 216
|
250
....*....|
gi 488907140 548 IEQGRPRELL 557
Cdd:COG1121 217 VAHGPPEEVL 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
333-547 |
9.38e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 113.37 E-value: 9.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYpdgQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSG-RGDISINRNKFLNFQNTSWQKQII 411
Cdd:COG4619 1 LELEGLSFRV---GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPtSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 412 YIPQKPYIFHTSLRENIAFyqPDAPKEQVVKAAKAAGIYELAsglfnGFDTMIGESE-QSLSGGQAQRIALARAfLASDR 490
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPF--PFQLRERKFDRERALELLERL-----GLPPDILDKPvERLSGGERQRLALIRA-LLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488907140 491 HILLFDEPTAHLDIQTeydlKQTMLPLLENHL------VFFATHRLHWLKQM-DYVLVMDNGHI 547
Cdd:COG4619 150 DVLLLDEPTSALDPEN----TRRVEELLREYLaeegraVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
333-558 |
1.94e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 116.40 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGRgdISIN------------RN- 396
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLetpDSGR--IVLNgrdlftnlppreRRv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 397 KFLnFQNtswqkqiiyipqkpY-IF-HTSLRENIAFYQPDAPKEQVVKAAKAAGIYEL--ASGLFNGFDTmigeseQsLS 472
Cdd:COG1118 78 GFV-FQH--------------YaLFpHMTVAENIAFGLRVRPPSKAEIRARVEELLELvqLEGLADRYPS------Q-LS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 473 GGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLE--NHLVFFATH------RLhwlkqMDYVLVMDN 544
Cdd:COG1118 136 GGQRQRVALARA-LAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHdqeealEL-----ADRVVVMNQ 209
|
250
....*....|....
gi 488907140 545 GHIIEQGRPRELLE 558
Cdd:COG1118 210 GRIEQVGTPDEVYD 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
328-559 |
2.14e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 114.32 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 328 DSETVLSVHNFSFQYPDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI-NSGRGDISINrNKFLNFQN-TS 405
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSENNA-LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLlKPQSGEIKID-GITISKENlKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 406 WQKQIIYIPQKP---YIfHTSLRENIAF------YQPDAPKEQVVKAAKAAGIYELasglfngfdtmIGESEQSLSGGQA 476
Cdd:PRK13632 81 IRKKIGIIFQNPdnqFI-GATVEDDIAFglenkkVPPKKMKDIIDDLAKKVGMEDY-----------LDKEPQNLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 477 QRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLE--NHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPR 554
Cdd:PRK13632 149 QRVAIASV-LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPK 227
|
....*
gi 488907140 555 ELLED 559
Cdd:PRK13632 228 EILNN 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
334-546 |
3.28e-28 |
|
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: 110.41 E-value: 3.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 334 SVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI-NSGRGDISINRNKFLNFQNTSWQKQIIY 412
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLlKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 413 IPQkpyifhtslreniafyqpdapkeqvvkaakaagiyelasglfngfdtmigeseqsLSGGQAQRIALARAfLASDRHI 492
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARA-LLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488907140 493 LLFDEPTAHLDIQTEYDLKQTMLPLL-ENHLVFFATHRLHWLKQ-MDYVLVMDNGH 546
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
334-551 |
6.16e-28 |
|
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: 110.22 E-value: 6.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 334 SVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISINRNKFLNFQNTSWQKQIIY 412
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKpSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 413 IPQkpyifhtslreniafyqpdapkeqvvkAAKAAGIYELASGLFNgfdtmigeseqSLSGGQAQRIALARAfLASDRHI 492
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLADRPFN-----------ELSGGERQRVLLARA-LAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488907140 493 LLFDEPTAHLDIQTEYDLKQTM--LPLLENHLVFFATHRL-HWLKQMDYVLVMDNGHIIEQG 551
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLrrLARERGKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
351-500 |
2.04e-27 |
|
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: 107.73 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSG-RGDISINRNKFLNFQNTSWQKQIIYIPQKPYIF-HTSLRENI 428
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPtEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488907140 429 AF------YQPDAPKEQVVKAAKAAGIYELAsglfngfDTMIGESEQSLSGGQAQRIALARAfLASDRHILLFDEPTA 500
Cdd:pfam00005 81 RLglllkgLSKREKDARAEEALEKLGLGDLA-------DRPVGERPGTLSGGQRQRVAIARA-LLTKPKLLLLDEPTA 150
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
333-560 |
2.57e-27 |
|
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: 110.66 E-value: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDG-QQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSG-RGDISINRNKFLNFQNTSWQKQI 410
Cdd:COG1124 2 LEVRNLSVSYGQGgRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPwSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 411 IYIPQKPY-IFH------TSLRENIAFYQPDAPKEQVVKAAKAAGiyeLASGLFNGFdtmigesEQSLSGGQAQRIALAR 483
Cdd:COG1124 82 QMVFQDPYaSLHprhtvdRILAEPLRIHGLPDREERIAELLEQVG---LPPSFLDRY-------PHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 484 AfLASDRHILLFDEPTAHLD--IQTE-----YDLKQ----TMLpllenhlvfFATHRLHWLKQM-DYVLVMDNGHIIEQG 551
Cdd:COG1124 152 A-LILEPELLLLDEPTSALDvsVQAEilnllKDLREerglTYL---------FVSHDLAVVAHLcDRVAVMQNGRIVEEL 221
|
....*....
gi 488907140 552 RPRELLEDF 560
Cdd:COG1124 222 TVADLLAGP 230
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
333-547 |
6.02e-27 |
|
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: 107.30 E-value: 6.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISINRNKFLNFQNTSWQKQII 411
Cdd:cd03246 1 LEVENVSFRYPGAEPPV-LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 412 YIPQKPYIFHTSLRENIafyqpdapkeqvvkaakaagiyelasglfngfdtmigeseqsLSGGQAQRIALARAFLASDRh 491
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPR- 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488907140 492 ILLFDEPTAHLDIQTEYDLKQT--MLPLLENHLVFFAtHRLHWLKQMDYVLVMDNGHI 547
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAiaALKAAGATRIVIA-HRPETLASADRILVLEDGRV 173
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
330-552 |
7.19e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 108.59 E-value: 7.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 330 ETVLSVHNFSFQYPDGQQP-AALKDINFLV-RG-FakVAVVGLSGSGKTTLLSSLAGI---NSGR---GDISIN------ 394
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEvTALRGVSLSIeAGeF--VAIVGPSGSGKSTLLNILGGLdrpTSGEvliDGQDISslsere 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 395 RNKFLNfqntswqKQIIYIPQKPYIF-HTSLRENIAF------YQPDAPKEQVVKAAKAAGIYELAsglfngfDTMIGEs 467
Cdd:COG1136 80 LARLRR-------RHIGFVFQFFNLLpELTALENVALplllagVSRKERRERARELLERVGLGDRL-------DHRPSQ- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 468 eqsLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPL--LENHLVFFATHRLHWLKQMDYVLVMDNG 545
Cdd:COG1136 145 ---LSGGQQQRVAIARA-LVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDG 220
|
....*..
gi 488907140 546 HIIEQGR 552
Cdd:COG1136 221 RIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
333-547 |
3.69e-26 |
|
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: 106.42 E-value: 3.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQQP-AALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISINRNKFLNFQNTSW---- 406
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRpTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 407 QKQIIYIPQKPY-IFHTSLRENIA---FYQPDAPKEQVVKAAKAAGIYELASGLfngfDTMIGEseqsLSGGQAQRIALA 482
Cdd:cd03255 81 RRHIGFVFQSFNlLPDLTALENVElplLLAGVPKKERRERAEELLERVGLGDRL----NHYPSE----LSGGQQQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488907140 483 RAfLASDRHILLFDEPTAHLDIQTeydlKQTMLPLL------ENHLVFFATHRLHWLKQMDYVLVMDNGHI 547
Cdd:cd03255 153 RA-LANDPKIILADEPTGNLDSET----GKEVMELLrelnkeAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
333-547 |
5.22e-26 |
|
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: 104.40 E-value: 5.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISINrNKFLNFQNTSWQKQII 411
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKpDSGEIKVL-GKDIKKEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 412 YIPQKPYIFHT-SLRENIafyqpdapkeqvvkaakaagiyelasglfngfdtmigeseqSLSGGQAQRIALARAfLASDR 490
Cdd:cd03230 77 YLPEEPSLYENlTVRENL-----------------------------------------KLSGGMKQRLALAQA-LLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488907140 491 HILLFDEPTAHLDIQTEYDLKQTMLPLL-ENHLVFFATHRLHWLKQM-DYVLVMDNGHI 547
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
333-575 |
1.05e-25 |
|
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: 112.73 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQqPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISInrnkflnfqntswQKQII 411
Cdd:TIGR00957 637 ITVHNATFTWARDL-PPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAeMDKVEGHVHM-------------KGSVA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 412 YIPQKPYIFHTSLRENIAFYQPDAPK--EQVVKAAKAAGIYELASGlfnGFDTMIGESEQSLSGGQAQRIALARAfLASD 489
Cdd:TIGR00957 703 YVPQQAWIQNDSLRENILFGKALNEKyyQQVLEACALLPDLEILPS---GDRTEIGEKGVNLSGGQKQRVSLARA-VYSN 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 490 RHILLFDEPTAHLDIQT-EYDLKQTMLP--LLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLeDFDGKLNE 566
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVgKHIFEHVIGPegVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL-QRDGAFAE 857
|
250
....*....|
gi 488907140 567 -LRKELTDEK 575
Cdd:TIGR00957 858 fLRTYAPDEQ 867
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
333-573 |
1.62e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 107.88 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYpdGQQPAaLKDINF-LVRG-FakVAVVGLSGSGKTTLLSSLAGINS-GRGDISIN-----------RNkf 398
Cdd:COG3842 6 LELENVSKRY--GDVTA-LDDVSLsIEPGeF--VALLGPSGCGKTTLLRMIAGFETpDSGRILLDgrdvtglppekRN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 399 LN--FQNtswqkqiiyipqkpY-IF-HTSLRENIAFY--QPDAPKEQVVKAAKAA----GIYELAsglfngfDTMIGEse 468
Cdd:COG3842 79 VGmvFQD--------------YaLFpHLTVAENVAFGlrMRGVPKAEIRARVAELlelvGLEGLA-------DRYPHQ-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 469 qsLSGGQAQRIALARAfLASDRHILLFDEPTAHLD----IQTEYDLKQ-------TMLpllenhlvfFATHRlhwlkQM- 536
Cdd:COG3842 136 --LSGGQQQRVALARA-LAPEPRVLLLDEPLSALDaklrEEMREELRRlqrelgiTFI---------YVTHD-----QEe 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488907140 537 -----DYVLVMDNGHIIEQGRPRELLE--------DFDGKLNELRKELTD 573
Cdd:COG3842 199 alalaDRIAVMNDGRIEQVGTPEEIYErpatrfvaDFIGEANLLPGTVLG 248
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
333-551 |
5.07e-25 |
|
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: 102.98 E-value: 5.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINrNKflNFQNTS-WQKQI 410
Cdd:cd03259 1 LELKGLSKTYGSVR---ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGlERPDSGEILID-GR--DVTGVPpERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 411 IYIPQKPYIF-HTSLRENIAFyqpdAPKEQVV-KAAKAAGIYELASGLfnGFDTMIGESEQSLSGGQAQRIALARAfLAS 488
Cdd:cd03259 75 GMVFQDYALFpHLTVAENIAF----GLKLRGVpKAEIRARVRELLELV--GLEGLLNRYPHELSGGQQQRVALARA-LAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488907140 489 DRHILLFDEPTAHLDIQTEYDLKQTMLPLLENH--LVFFATHRL-HWLKQMDYVLVMDNGHIIEQG 551
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQeEALALADRIAVMNEGRIVQVG 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
114-558 |
8.45e-25 |
|
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: 109.65 E-value: 8.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 114 VSLLHAGIDNVQNYFQLI--------FIKIIDL--SIIPWLLLIYM--FF--------LRWQEALFLLLIFPV-IIFFFV 172
Cdd:TIGR00957 1042 QDLLHNKLRSPMSFFERTpsgnlvnrFSKELDTvdSMIPPVIKMFMgsLFnvigalivILLATPIAAVIIPPLgLLYFFV 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 173 ILGLAAQ----KRADNEYRnfTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFF- 247
Cdd:TIGR00957 1122 QRFYVASsrqlKRLESVSR--SPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVg 1199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 248 --TTLSIAVIAVFLGFSLMEGKMSLFPALTLLVLAPEYFLpLRTFSEdyhatldgknAFTEVLSVINQKKTSEISAlKVP 325
Cdd:TIGR00957 1200 ncIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWL-VRMSSE----------METNIVAVERLKEYSETEK-EAP 1267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 326 AIDSETV----------LSVHNFSFQYPDGQQpAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGIN-SGRGDISIN 394
Cdd:TIGR00957 1268 WQIQETAppsgwpprgrVEFRNYCLRYREDLD-LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINeSAEGEIIID 1346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 395 RNKFLNFQNTSWQKQIIYIPQKPYIFHTSLRENI-AFYQpdAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSG 473
Cdd:TIGR00957 1347 GLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQ--YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSV 1424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 474 GQAQRIALARAFLASDRhILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLkqMDY--VLVMDNGHIIEQG 551
Cdd:TIGR00957 1425 GQRQLVCLARALLRKTK-ILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTI--MDYtrVIVLDKGEVAEFG 1501
|
....*..
gi 488907140 552 RPRELLE 558
Cdd:TIGR00957 1502 APSNLLQ 1508
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
333-553 |
1.52e-24 |
|
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: 101.72 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQY-PDgqQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSL-AGINSGRGDISINRNKFLNFQNTSWQKQI 410
Cdd:cd03369 7 IEVENLSVRYaPD--LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALfRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 411 IYIPQKPYIFHTSLRENIAFYQpDAPKEQVVKAAKaagiyelasglfngfdtmIGESEQSLSGGQAQRIALARAFLASDR 490
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLDPFD-EYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488907140 491 hILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRP 553
Cdd:cd03369 146 -VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
333-546 |
1.53e-24 |
|
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: 100.72 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISINRNKF--LNFQNTSWQKQ 409
Cdd:cd03229 1 LELKNVSKRYGQKT---VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEpDSGSILIDGEDLtdLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 410 IIYIPQKPYIF-HTSLRENIAFyqpdapkeqvvkaakaagiyelasglfngfdtmigeseqSLSGGQAQRIALARAfLAS 488
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIAL---------------------------------------GLSGGQQQRVALARA-LAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488907140 489 DRHILLFDEPTAHLDIQTEYDLKQTMLPLLENH--LVFFATHRLHWLKQM-DYVLVMDNGH 546
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
350-559 |
1.89e-24 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 101.99 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 350 ALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG---INSGR---GDISINRNKF-LN---------FQNtswqkqiiyi 413
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLleePDSGTitvDGEDLTDSKKdINklrrkvgmvFQQ---------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 414 pqkpyiF----HTSLRENIAFyqpdAPKeQVVKAAKAAGIyELASGLFngfdTMIGESEQ------SLSGGQAQRIALAR 483
Cdd:COG1126 86 ------FnlfpHLTVLENVTL----API-KVKKMSKAEAE-ERAMELL----ERVGLADKadaypaQLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 484 AfLASDRHILLFDEPTAHLD-------IQTEYDLKQ---TMLpllenhLVffaTHRLHWLKQM-DYVLVMDNGHIIEQGR 552
Cdd:COG1126 150 A-LAMEPKVMLFDEPTSALDpelvgevLDVMRDLAKegmTMV------VV---THEMGFAREVaDRVVFMDGGRIVEEGP 219
|
....*..
gi 488907140 553 PRELLED 559
Cdd:COG1126 220 PEEFFEN 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
341-567 |
3.18e-24 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 107.94 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 341 QYPDGQqPAALKDINFLVRGFAKVAVVGLSGSGKTTLL-SSLAGINSGRGDISINRNKFLNFQNTSWQKQIIYIPQKPYI 419
Cdd:PTZ00243 1317 RYREGL-PLVLRGVSFRIAPREKVGIVGRTGSGKSTLLlTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVL 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 420 FHTSLRENI-AFYQpdAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLASDRHILLFDEP 498
Cdd:PTZ00243 1396 FDGTVRQNVdPFLE--ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILMDEA 1473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488907140 499 TAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLEDFDGKLNEL 567
Cdd:PTZ00243 1474 TANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSM 1542
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
365-561 |
4.06e-24 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 104.03 E-value: 4.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 365 AVVGLSGSGKTTLLSSLAGINSG-RGDISIN--------RNKFLnfqnTSWQKQIIYIPQKPYIF-HTSLRENIAFYQPD 434
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPdSGRIRLGgevlqdsaRGIFL----PPHRRRIGYVFQEARLFpHLSVRGNLLYGRKR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 435 APKEQvvKAAKAAGIYELasgLfnGFDTMIGESEQSLSGGQAQRIALARAFLASDRhILLFDEPTAHLDIQTeydlKQTM 514
Cdd:COG4148 105 APRAE--RRISFDEVVEL---L--GIGHLLDRRPATLSGGERQRVAIGRALLSSPR-LLLMDEPLAALDLAR----KAEI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488907140 515 LPLLEN---HL---VFFATHRLHWLKQM-DYVLVMDNGHIIEQGRPRELLEDFD 561
Cdd:COG4148 173 LPYLERlrdELdipILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
126-575 |
6.27e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 106.98 E-value: 6.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 126 NYFQLIFIKIIDLSIIPWLLLIYMFFLRWQ---EALFLLLIFPVIIFFFVILgLAAQKRADNEYRNFTvlNNRFA---DT 199
Cdd:PLN03232 409 NALQQIAEQLHGLWSAPFRIIVSMVLLYQQlgvASLFGSLILFLLIPLQTLI-VRKMRKLTKEGLQWT--DKRVGiinEI 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 200 LRGMQTLKQLGLSRIFTKRIY----ETSERYRKSTMrsltiamTSTFSLDFFTTLSIAVIAVFLG-FSLMEGKMSLFPAL 274
Cdd:PLN03232 486 LASMDTVKCYAWEKSFESRIQgirnEELSWFRKAQL-------LSAFNSFILNSIPVVVTLVSFGvFVLLGGDLTPARAF 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 275 TLLVLAPEYFLPLRTFSEDYHATLDGKNAFTEVLSVINQKKtsEISALKVPAIDSETVLSVHNFSFQYPDGQQPAALKDI 354
Cdd:PLN03232 559 TSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEE--RILAQNPPLQPGAPAISIKNGYFSWDSKTSKPTLSDI 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 355 NFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGRGDISINrnkflnfqntsWQKQIIYIPQKPYIFHTSLRENIAFyQPD 434
Cdd:PLN03232 637 NLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIFNATVRENILF-GSD 704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 435 APKEQVVKAAKAAGI-YELasGLFNGFD-TMIGESEQSLSGGQAQRIALARAFLaSDRHILLFDEPTAHLDIQTEYDL-K 511
Cdd:PLN03232 705 FESERYWRAIDVTALqHDL--DLLPGRDlTEIGERGVNISGGQKQRVSMARAVY-SNSDIYIFDDPLSALDAHVAHQVfD 781
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488907140 512 QTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPREL---------LEDFDGKLNELRKELTDEK 575
Cdd:PLN03232 782 SCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELsksgslfkkLMENAGKMDATQEVNTNDE 854
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
332-528 |
1.04e-23 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 99.09 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYpdGQQPAaLKDINF-LVRGFAkVAVVGLSGSGKTTLLSSLAG-INSGRGDISINrNKFLNFQNTSWQKQ 409
Cdd:COG4133 2 MLEAENLSCRR--GERLL-FSGLSFtLAAGEA-LALTGPNGSGKTTLLRILAGlLPPSAGEVLWN-GEPIRDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 410 IIYIPQKPYIFHT-SLRENIAFYQ----PDAPKEQVVKAAKAAGIYELAsglfngfDTMIGEseqsLSGGQAQRIALARA 484
Cdd:COG4133 77 LAYLGHADGLKPElTVRENLRFWAalygLRADREAIDEALEAVGLAGLA-------DLPVRQ----LSAGQKRRVALARL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488907140 485 FLaSDRHILLFDEPTAHLDIQTeydlKQTMLPLLENHL-----VFFATH 528
Cdd:COG4133 146 LL-SPAPLWLLDEPFTALDAAG----VALLAELIAAHLarggaVLLTTH 189
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
334-551 |
1.45e-23 |
|
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: 98.76 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 334 SVHNFSFQYpdGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSG-RGDISINRNKFLNFqntswQKQIIY 412
Cdd:cd03235 1 EVEDLTVSY--GGHPV-LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPtSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 413 IPQKPYI---FHTSLRENIA---------FYQPDAPKEQVVKAA-KAAGIYELAsglfngfDTMIGEseqsLSGGQAQRI 479
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLmglyghkglFRRLSKADKAKVDEAlERVGLSELA-------DRQIGE----LSGGQQQRV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488907140 480 ALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPL-LENHLVFFATHRLHW-LKQMDYVLVMdNGHIIEQG 551
Cdd:cd03235 142 LLARA-LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLvLEYFDRVLLL-NRTVVASG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
333-556 |
2.63e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 101.30 E-value: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYpdGQQPAaLKDINFLVR--GFakVAVVGLSGSGKTTLLSSLAG---INSGRgdISIN-----------RN 396
Cdd:COG3839 4 LELENVSKSY--GGVEA-LKDIDLDIEdgEF--LVLLGPSGCGKSTLLRMIAGledPTSGE--ILIGgrdvtdlppkdRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 397 KFLNFQNtswqkqiiYI--PqkpyifHTSLRENIAFY-----QPDAP-KEQVVKAAKAAGIYELAsglfngfDTMIGEse 468
Cdd:COG3839 77 IAMVFQS--------YAlyP------HMTVYENIAFPlklrkVPKAEiDRRVREAAELLGLEDLL-------DRKPKQ-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 469 qsLSGGQAQRIALARAfLASDRHILLFDEPTAHLD----IQTEYDLKQ-------TMLpllenhlvfFATHRlhwlkQ-- 535
Cdd:COG3839 134 --LSGGQRQRVALGRA-LVREPKVFLLDEPLSNLDaklrVEMRAEIKRlhrrlgtTTI---------YVTHD-----Qve 196
|
250 260
....*....|....*....|....*
gi 488907140 536 -M---DYVLVMDNGHIIEQGRPREL 556
Cdd:COG3839 197 aMtlaDRIAVMNDGRIQQVGTPEEL 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
333-557 |
3.71e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 98.29 E-value: 3.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDgqqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFLN----------- 400
Cdd:COG3840 2 LRLDDLTYRYGD-----FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGfLPPDSGRILWNGQDLTAlppaerpvsml 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 401 FQNTSwqkqiiyipqkpyIF-HTSLRENIAF-YQPD-----APKEQVVKAAKAAGIYELASGLfngfdtmigesEQSLSG 473
Cdd:COG3840 77 FQENN-------------LFpHLTVAQNIGLgLRPGlkltaEQRAQVEQALERVGLAGLLDRL-----------PGQLSG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 474 GQAQRIALARAFLaSDRHILLFDEPTAHLDIQteydLKQTMLPLLE------NHLVFFATHrlHW---LKQMDYVLVMDN 544
Cdd:COG3840 133 GQRQRVALARCLV-RKRPILLLDEPFSALDPA----LRQEMLDLVDelcrerGLTVLMVTH--DPedaARIADRVLLVAD 205
|
250
....*....|...
gi 488907140 545 GHIIEQGRPRELL 557
Cdd:COG3840 206 GRIAADGPTAALL 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
335-558 |
4.58e-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: 98.18 E-value: 4.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 335 VHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSG-RGDIsinrnkFLNFQNTS----WQKQ 409
Cdd:cd03296 5 VRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdSGTI------LFGGEDATdvpvQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 410 IIYIPQKPYIF-HTSLRENIAFYQPDAPKEQVV-KAAKAAGIYEL-----ASGLFNGFDTmigeseqSLSGGQAQRIALA 482
Cdd:cd03296 76 VGFVFQHYALFrHMTVFDNVAFGLRVKPRSERPpEAEIRAKVHELlklvqLDWLADRYPA-------QLSGGQRQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488907140 483 RAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLE--NHLVFFATH-RLHWLKQMDYVLVMDNGHIIEQGRPRELLE 558
Cdd:cd03296 149 RA-LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
351-558 |
4.81e-23 |
|
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: 98.18 E-value: 4.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISINRNKFLNFQNTswQKQIIYIPQKPYIF-HTSLRENI 428
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKpDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 429 AFyqpDAPKEQVVKAAKAAGIYELASGLfnGFDTMIGESEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEY 508
Cdd:cd03299 93 AY---GLKKRKVDKKEIERKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARA-LVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488907140 509 DLKQTMLPLLENHLVFF--ATHRLHWLKQM-DYVLVMDNGHIIEQGRPRELLE 558
Cdd:cd03299 167 KLREELKKIRKEFGVTVlhVTHDFEEAWALaDKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
24-303 |
5.59e-23 |
|
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: 99.15 E-value: 5.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 24 FLQAVSILFQ---AFFLSKSIVILWHQSAF-SSAVPYIFGFAISLLCRHFFSLIKEGSANSFSVTASEGLRDQLLGKYLS 99
Cdd:cd18781 3 LLQWISLLANiafVFSIANLLQKLLEGKLTtASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 100 FGDQTIFKTGTGHAVSLLHAGIDNVQNYF-----QLIFikiidlSII-PWLLLIYMFFLRWQEALFLLLIFPVIIFFFVI 173
Cdd:cd18781 83 LGPSYQEKVSTAEVVQLSVEGVEQLEIYFgrylpQFFY------SMLaPLTLFVVLAPINWKAALVLLICVPLIPISIIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 174 LGLAAQKRADNEYRNFTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSIA 253
Cdd:cd18781 157 VQKIAKKLLSKYWGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVAYGGAA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488907140 254 VIAVFLGFSLMEGKMSLFPALTLLVLAPEYFLPLRTFSEDYHATLDGKNA 303
Cdd:cd18781 237 LGIILALLQFANGSISLAGALFIILLSAEFFLPLRLLGSFFHIAMNGMAA 286
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
337-567 |
1.20e-22 |
|
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: 96.99 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 337 NFSFQYPDGQqpAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFLNFQNTSWQKQIIYIPQ 415
Cdd:cd03295 5 NVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRlIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 416 KPYIF-HTSLRENIAFyqpdAPK-EQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAfLASDRHIL 493
Cdd:cd03295 83 QIGLFpHMTVEENIAL----VPKlLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARA-LAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 494 LFDEPTAHLDIQTEYDLKQTMLPLLE--NHLVFFATHRL-HWLKQMDYVLVMDNGHIIEQGRPRELL--------EDFDG 562
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILrspandfvAEFVG 237
|
....*
gi 488907140 563 KLNEL 567
Cdd:cd03295 238 ADRLL 242
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
328-558 |
1.37e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 97.78 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 328 DSETVLSVHNFSFQYPDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINrNKFLNfQNTSW 406
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATYA-LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGlLLPEAGTITVG-GMVLS-EETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 407 Q--KQIIYIPQKP--YIFHTSLRENIAFYQPD--APKEQVVKAAKAA----GIYELASglfngfdtmigESEQSLSGGQA 476
Cdd:PRK13635 78 DvrRQVGMVFQNPdnQFVGATVQDDVAFGLENigVPREEMVERVDQAlrqvGMEDFLN-----------REPHRLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 477 QRIALArAFLASDRHILLFDEPTAHLD-------IQTEYDLK-QTMLPLLEnhlvffATHRLHWLKQMDYVLVMDNGHII 548
Cdd:PRK13635 147 QRVAIA-GVLALQPDIIILDEATSMLDprgrrevLETVRQLKeQKGITVLS------ITHDLDEAAQADRVIVMNKGEIL 219
|
250
....*....|
gi 488907140 549 EQGRPRELLE 558
Cdd:PRK13635 220 EEGTPEEIFK 229
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
351-547 |
1.56e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 102.55 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG---INSGRgdisinrnkflnfqntSW-QKQIIYIPQKPYIFHTSLRE 426
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSqfeISEGR----------------VWaERSIAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 427 NIAFYQPD--APKEQVVKAAK-AAGIYELASGLfngfDTMIGESEQSLSGGQAQRIALARAFLAsDRHILLFDEPTAHLD 503
Cdd:PTZ00243 740 NILFFDEEdaARLADAVRVSQlEADLAQLGGGL----ETEIGEKGVNLSGGQKARVSLARAVYA-NRDVYLLDDPLSALD 814
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488907140 504 IQT-EYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHI 547
Cdd:PTZ00243 815 AHVgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
333-547 |
3.55e-22 |
|
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: 96.46 E-value: 3.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQQpAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGRGDISINRNKFLNFQNTSWQKQIIY 412
Cdd:cd03289 3 MTVKDLTAKYTEGGN-AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 413 IPQKPYIFHTSLRENIAFYQPDApKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLASDRhI 492
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYGKWS-DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK-I 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488907140 493 LLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHI 547
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
325-556 |
5.16e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 95.49 E-value: 5.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 325 PAIDSETVLSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGIN--------SGR---GDISI 393
Cdd:COG1117 4 PASTLEPKIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipgarvEGEillDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 394 NRNKF----LnfqntswQKQIIYIPQKPYIFHTSLRENIAFyqpdAPK-----------EQVVKAAKAAGIYE-----L- 452
Cdd:COG1117 81 YDPDVdvveL-------RRRVGMVFQKPNPFPKSIYDNVAY----GLRlhgikskseldEIVEESLRKAALWDevkdrLk 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 453 ASGLfngfdtmigeseqSLSGGQAQRIALARAfLASDRHILLFDEPTAHLD-IQTeydLK--QTMLPLLENHLVFFATHR 529
Cdd:COG1117 150 KSAL-------------GLSGGQQQRLCIARA-LAVEPEVLLMDEPTSALDpIST---AKieELILELKKDYTIVIVTHN 212
|
250 260 270
....*....|....*....|....*....|.
gi 488907140 530 LHwlkQM----DYVLVMDNGHIIEQGRPREL 556
Cdd:COG1117 213 MQ---QAarvsDYTAFFYLGELVEFGPTEQI 240
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-557 |
5.43e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 100.82 E-value: 5.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 15 ILSWLVLLTFLQA------VSILFQAFFLSKSIVIL-------W-HQSAFSSAVPYIFGFAISLLCrhfFSLIKEGSANS 80
Cdd:PLN03232 895 IISWNVLMRYNKAvgglwvVMILLVCYLTTEVLRVSsstwlsiWtDQSTPKSYSPGFYIVVYALLG---FGQVAVTFTNS 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 81 F-----SVTASEGLRDQLLGKYLSfGDQTIFKTG-TGHAVSLLHAGID----NVQNYFQLiFIKIIdlsiipWLLLIYMF 150
Cdd:PLN03232 972 FwlissSLHAAKRLHDAMLNSILR-APMLFFHTNpTGRVINRFSKDIGdidrNVANLMNM-FMNQL------WQLLSTFA 1043
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 151 FLRWQEALFLLLIFPVIIFFFVILgLAAQ------KRADNEYRnfTVLNNRFADTLRGMQTLkqlglsriftkRIYETSE 224
Cdd:PLN03232 1044 LIGTVSTISLWAIMPLLILFYAAY-LYYQstsrevRRLDSVTR--SPIYAQFGEALNGLSSI-----------RAYKAYD 1109
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 225 RYRKSTMRSL------TIAMTS-----TFSLDFFTTLSIAVIAVF--LGFSLMEGKMSLFPALTLLVlapEYFLPLRTF- 290
Cdd:PLN03232 1110 RMAKINGKSMdnnirfTLANTSsnrwlTIRLETLGGVMIWLTATFavLRNGNAENQAGFASTMGLLL---SYTLNITTLl 1186
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 291 SEDYHATLDGKNAFTEVLSVINQ-KKTSEISAL-----KVPAIDSETVLSVHNFSFQYPDGQqPAALKDINFLVRGFAKV 364
Cdd:PLN03232 1187 SGVLRQASKAENSLNSVERVGNYiDLPSEATAIiennrPVSGWPSRGSIKFEDVHLRYRPGL-PPVLHGLSFFVSPSEKV 1265
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 365 AVVGLSGSGKTTLLSSLAGI-NSGRGDISINRNKFLNFQNTSWQKQIIYIPQKPYIFHTSLRENIAFYQP--DApkeQVV 441
Cdd:PLN03232 1266 GVVGRTGAGKSSMLNALFRIvELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEhnDA---DLW 1342
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 442 KAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLASDRhILLFDEPTAHLDIQTEYDLKQTMLPLLENH 521
Cdd:PLN03232 1343 EALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSK-ILVLDEATASVDVRTDSLIQRTIREEFKSC 1421
|
570 580 590
....*....|....*....|....*....|....*.
gi 488907140 522 LVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELL 557
Cdd:PLN03232 1422 TMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
333-562 |
5.57e-22 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 100.87 E-value: 5.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSL------------AGINSGRGDIS-------- 392
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhiVFKNEHTNDMTneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 393 -------INRNKF-LNFQNTSWQKQIIY---------------------------IPQKPYIFHTSLRENIAFYQPDAPK 437
Cdd:PTZ00265 1246 eeqnvgmKNVNEFsLTKEGGSGEDSTVFknsgkilldgvdicdynlkdlrnlfsiVSQEPMLFNMSIYENIKFGKEDATR 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 438 EQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLASDRhILLFDEPTAHLDIQTEYDLKQTMLPL 517
Cdd:PTZ00265 1326 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK-ILLLDEATSSLDSNSEKLIEKTIVDI 1404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 488907140 518 LE--NHLVFFATHRLHWLKQMDYVLVMDN----GHIIE-QGRPRELLEDFDG 562
Cdd:PTZ00265 1405 KDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSVQDG 1456
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
332-559 |
6.02e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.84 E-value: 6.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYpDGQQPAALKDINFLVRGFAK---VAVVGLSGSGKTTLLSSLAG-INSGRGDISINrnKFLNFQNTSWQ 407
Cdd:PRK13631 21 ILRVKNLYCVF-DEKQENELVALNNISYTFEKnkiYFIIGNSGSGKSTLVTHFNGlIKSKYGTIQVG--DIYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 408 KQIIYIPQKPYIFHTSLRENIAF------YQ-------------PDAPKEQVVKAAKAAGIYELASGLFngfDTMIGESE 468
Cdd:PRK13631 98 ELITNPYSKKIKNFKELRRRVSMvfqfpeYQlfkdtiekdimfgPVALGVKKSEAKKLAKFYLNKMGLD---DSYLERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 469 QSLSGGQAQRIALArAFLASDRHILLFDEPTAHLDIQTEYDLKQTMLPL-LENHLVFFATHRL-HWLKQMDYVLVMDNGH 546
Cdd:PRK13631 175 FGLSGGQKRRVAIA-GILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMeHVLEVADEVIVMDKGK 253
|
250
....*....|...
gi 488907140 547 IIEQGRPRELLED 559
Cdd:PRK13631 254 ILKTGTPYEIFTD 266
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
293-516 |
6.61e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 99.50 E-value: 6.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 293 DYHATLDGKNAFTEVLsvinQKKTSEISALKVPAIDSETVLSVHNFSFQYPDGQqpAALKDINFLVRGFAKVAVVGLSGS 372
Cdd:COG4178 327 EWRATVDRLAGFEEAL----EAADALPEAASRIETSEDGALALEDLTLRTPDGR--PLLEDLSLSLKPGERLLITGPSGS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 373 GKTTLLSSLAGI-NSGRGDISINRNkflnfqntswqKQIIYIPQKPYIFHTSLRENIAF-YQPDAPKEQVVKAA-KAAGI 449
Cdd:COG4178 401 GKSTLLRAIAGLwPYGSGRIARPAG-----------ARVLFLPQRPYLPLGTLREALLYpATAEAFSDAELREAlEAVGL 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 450 YELASGLFNGFDTmigesEQSLSGGQAQRIALARAFLASDRHILLfDEPTAHLDIQTE---YDLKQTMLP 516
Cdd:COG4178 470 GHLAERLDEEADW-----DQVLSLGEQQRLAFARLLLHKPDWLFL-DEATSALDEENEaalYQLLREELP 533
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
351-556 |
1.63e-21 |
|
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: 93.72 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISINRNKFLNFQNTSWQ---KQIIYIPQKPYIFhTSL-- 424
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRpDSGEVLIDGEDISGLSEAELYrlrRRMGMLFQSGALF-DSLtv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 425 RENIAF---YQPDAPKEQVvkAAKAAGIYELAsGLFNGFDTMIGEseqsLSGGQAQRIALARAfLASDRHILLFDEPTAH 501
Cdd:cd03261 95 FENVAFplrEHTRLSEEEI--REIVLEKLEAV-GLRGAEDLYPAE----LSGGMKKRVALARA-LALDPELLLYDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488907140 502 LDIQTEYDLKQTMLPLLE--NHLVFFATHRLHWLKQM-DYVLVMDNGHIIEQGRPREL 556
Cdd:cd03261 167 LDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEEL 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
328-558 |
3.03e-21 |
|
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: 93.12 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 328 DSETVLSVHNFSFQYpdGQQPAaLKDINFLV-RGfaKV-AVVGLSGSGKTTLLSSLAGI---NSGRgdISIN-------- 394
Cdd:COG1127 1 MSEPMIEVRNLTKSF--GDRVV-LDGVSLDVpRG--EIlAIIGGSGSGKSVLLKLIIGLlrpDSGE--ILVDgqditgls 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 395 -------RNKF--LnFQN----TSwqkqiiyipqkpyifhTSLRENIAF---YQPDAPKEQVVKAAKAAgiyeLAS-GLF 457
Cdd:COG1127 74 ekelyelRRRIgmL-FQGgalfDS----------------LTVFENVAFplrEHTDLSEAEIRELVLEK----LELvGLP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 458 NGFDTMIGEseqsLSGGQAQRIALARAfLASDRHILLFDEPTAHLD-------------IQTEYDLkqTmlpllenhlVF 524
Cdd:COG1127 133 GAADKMPSE----LSGGMRKRVALARA-LALDPEILLYDEPTAGLDpitsavidelireLRDELGL--T---------SV 196
|
250 260 270
....*....|....*....|....*....|....*
gi 488907140 525 FATHRLHWLKQM-DYVLVMDNGHIIEQGRPRELLE 558
Cdd:COG1127 197 VVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
332-557 |
3.21e-21 |
|
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: 92.64 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPDGQQPA-ALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI-NSGRGDISINR---NKFLNFQNTSW 406
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPTSGSVLVDGtdlTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 407 QKQIIYIPQKPYIFHT-SLRENIAFyqpdaPKE--QVVKAAKAAGIYELAS--GLFNGFDTMIGEseqsLSGGQAQRIAL 481
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENVAL-----PLEiaGVPKAEIEERVLELLElvGLEDKADAYPAQ----LSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 482 ARAfLASDRHILLFDEPTAHLDIQTeydlKQTMLPLLE------NHLVFFATHRLHWLKQM-DYVLVMDNGHIIEQGRPR 554
Cdd:cd03258 152 ARA-LANNPKVLLCDEATSALDPET----TQSILALLRdinrelGLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVE 226
|
...
gi 488907140 555 ELL 557
Cdd:cd03258 227 EVF 229
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
325-564 |
4.32e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 98.27 E-value: 4.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 325 PAIdsetvlSVHNFSFQY-PDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGRGDISInrnkflnfqn 403
Cdd:PLN03130 613 PAI------SIKNGYFSWdSKAERPT-LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASV---------- 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 404 tSWQKQIIYIPQKPYIFHTSLRENIAFYQP-DAPKEQvvKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALA 482
Cdd:PLN03130 676 -VIRGTVAYVPQVSWIFNATVRDNILFGSPfDPERYE--RAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMA 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 483 RAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLP-LLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLEdfD 561
Cdd:PLN03130 753 RA-VYSNSDVYIFDDPLSALDAHVGRQVFDKCIKdELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN--N 829
|
...
gi 488907140 562 GKL 564
Cdd:PLN03130 830 GPL 832
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
351-559 |
4.64e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 92.46 E-value: 4.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLL---SSLAGINSGR---GDISINRNKfLNFQNTSWQKQIIYipQKPYIF-HTS 423
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKLEEITSGDlivDGLKVNDPK-VDERLIRQEAGMVF--QQFYLFpHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 424 LRENIAFyqpdAPKeQVVKAAKAAGiYELASGLFngfdTMIGESEQS------LSGGQAQRIALARAfLASDRHILLFDE 497
Cdd:PRK09493 94 ALENVMF----GPL-RVRGASKEEA-EKQARELL----AKVGLAERAhhypseLSGGQQQRVAIARA-LAVKPKLMLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488907140 498 PTAHLDIQTEYDLKQTMLPLLENHL-VFFATHRLHWLKQMDYVLV-MDNGHIIEQGRPRELLED 559
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMtMVIVTHEIGFAEKVASRLIfIDKGRIAEDGDPQVLIKN 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
333-567 |
6.48e-21 |
|
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: 91.86 E-value: 6.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQQpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG---INSGRGDIS-INRNKFLNFQNTSWQK 408
Cdd:cd03256 1 IEVENLSKTYPNGKK--ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlvePTSGSVLIDgTDINKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 409 QIIYIPQK-PYIFHTSLRENI--------AFYQPDA---PKEQVVKAAKA---AGIYELASglfngfdTMIGEseqsLSG 473
Cdd:cd03256 79 QIGMIFQQfNLIERLSVLENVlsgrlgrrSTWRSLFglfPKEEKQRALAAlerVGLLDKAY-------QRADQ----LSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 474 GQAQRIALARAfLASDRHILLFDEPTAHLDIQTEydlKQTMLPLLEN------------HLVFFAthrlhwLKQMDYVLV 541
Cdd:cd03256 148 GQQQRVAIARA-LMQQPKLILADEPVASLDPASS---RQVMDLLKRInreegitvivslHQVDLA------REYADRIVG 217
|
250 260
....*....|....*....|....*.
gi 488907140 542 MDNGHIIEQGRPRELLEDfdgKLNEL 567
Cdd:cd03256 218 LKDGRIVFDGPPAELTDE---VLDEI 240
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
333-543 |
7.14e-21 |
|
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: 97.29 E-value: 7.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQQpAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGRGDISINRNKFLNFQNTSWQKQIIY 412
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 413 IPQKPYIFHTSLRENIAFYQpDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLASDRhI 492
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNLDPYE-QWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAK-I 1374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488907140 493 LLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMD 543
Cdd:TIGR01271 1375 LLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIE 1425
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
145-544 |
1.16e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 96.64 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 145 LLIYMFFLRWQEALFLLLIFPVIifffVILGLAAQKRADNEYRNFTVLNNR----FADTLRGMQTLKQLGLSRIFTKRIY 220
Cdd:PTZ00265 188 LYIWSLFKNARLTLCITCVFPLI----YICGVICNKKVKINKKTSLLYNNNtmsiIEEALVGIRTVVSYCGEKTILKKFN 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 221 ETSERYRKST-----MRSLTIAMTSTFSL-----DFFTTLSIAVIAV--------FLGFSLMEGKMSLFPALTLLVLape 282
Cdd:PTZ00265 264 LSEKLYSKYIlkanfMESLHIGMINGFILasyafGFWYGTRIIISDLsnqqpnndFHGGSVISILLGVLISMFMLTI--- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 283 yFLPLRTfseDYHATLDGKNAFTEVlsvINQKKTSEIS--ALKVPAIDSetvLSVHNFSFQYPDGQQPAALKDINFLVRG 360
Cdd:PTZ00265 341 -ILPNIT---EYMKSLEATNSLYEI---INRKPLVENNddGKKLKDIKK---IQFKNVRFHYDTRKDVEIYKDLNFTLTE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 361 FAKVAVVGLSGSGKTTLLSSLAGI-NSGRGDISINRNKFLNFQNTSW-QKQIIYIPQKPYIFHTSLRENIAF-------- 430
Cdd:PTZ00265 411 GKTYAFVGESGCGKSTILKLIERLyDPTEGDIIINDSHNLKDINLKWwRSKIGVVSQDPLLFSNSIKNNIKYslyslkdl 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 431 ------YQPDAPKEQ-------------------------------------------VVKAAKAAGIYELASGLFNGFD 461
Cdd:PTZ00265 491 ealsnyYNEDGNDSQenknkrnscrakcagdlndmsnttdsneliemrknyqtikdseVVDVSKKVLIHDFVSALPDKYE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 462 TMIGESEQSLSGGQAQRIALARAFLASDRhILLFDEPTAHLDIQTEYDLKQTMLPLL--ENHLVFFATHRLHWLKQMDYV 539
Cdd:PTZ00265 571 TLVGSNASKLSGGQKQRISIARAIIRNPK-ILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTI 649
|
....*
gi 488907140 540 LVMDN 544
Cdd:PTZ00265 650 FVLSN 654
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
345-559 |
1.29e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 91.35 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 345 GQQpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGR---GDISINRNKFLNFQNT---SWQKQIIYIPQ 415
Cdd:PRK11264 15 GQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLeqpEAGTirvGDITIDTARSLSQQKGlirQLRQHVGFVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 416 KPYIF-HTSLRENIaFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTmigESEQSLSGGQAQRIALARAfLASDRHILL 494
Cdd:PRK11264 93 NFNLFpHRTVLENI-IEGPVIVKGEPKEEATARARELLAKVGLAGKET---SYPRRLSGGQQQRVAIARA-LAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488907140 495 FDEPTAHLDIQTEYDLKQTMLPLL-ENHLVFFATHRLHWLKQM-DYVLVMDNGHIIEQGRPRELLED 559
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALFAD 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
332-552 |
1.85e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 90.11 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPDGQQpaALKDINF-LVRG-FakVAVVGLSGSGKTTLLSSLAGI---NSGR---GDISINRNKFlnfqn 403
Cdd:COG2884 1 MIRFENVSKRYPGGRE--ALSDVSLeIEKGeF--VFLTGPSGAGKSTLLKLLYGEerpTSGQvlvNGQDLSRLKR----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 404 tswqKQIIYIPQK-PYIF-------HTSLRENIAF------YQPDAPKEQVVKAAKAAGIYELAsglfngfDTMIGEseq 469
Cdd:COG2884 72 ----REIPYLRRRiGVVFqdfrllpDRTVYENVALplrvtgKSRKEIRRRVREVLDLVGLSDKA-------KALPHE--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 470 sLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLkqtmLPLLE--NHL---VFFATHRLHWLKQMDY-VLVMD 543
Cdd:COG2884 138 -LSGGEQQRVAIARA-LVNRPELLLADEPTGNLDPETSWEI----MELLEeiNRRgttVLIATHDLELVDRMPKrVLELE 211
|
....*....
gi 488907140 544 NGHIIEQGR 552
Cdd:COG2884 212 DGRLVRDEA 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
330-568 |
2.47e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 91.34 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 330 ETVLSVHNFSFQYPDGQQpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGIN-SGRGDISInRNKFLNFQNTSW-Q 407
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYlPQRGRVKV-MGREVNAENEKWvR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 408 KQIIYIPQKP--YIFHTSLRENIAF------YQPDAPKEQVVKAAKAAGIYELASglfngfdtmigESEQSLSGGQAQRI 479
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAFgpvnmgLDKDEVERRVEEALKAVRMWDFRD-----------KPPYHLSYGQKKRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 480 ALArAFLASDRHILLFDEPTAHLDIQTEYDLkQTMLPLLENH--LVFFATHRLHWLKQ-MDYVLVMDNGHIIEQGRPREL 556
Cdd:PRK13647 148 AIA-GVLAMDPDVIVLDEPMAYLDPRGQETL-MEILDRLHNQgkTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLL 225
|
250
....*....|..
gi 488907140 557 LEDFDGKLNELR 568
Cdd:PRK13647 226 TDEDIVEQAGLR 237
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
333-544 |
3.21e-20 |
|
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: 87.98 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQqpAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI-NSGRGDISInrnkflnfqntSWQKQII 411
Cdd:cd03223 1 IELENLSLATPDGR--VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwPWGSGRIGM-----------PEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 412 YIPQKPYIFHTSLRENIAFyqpdaPKEQVvkaakaagiyelasglfngfdtmigeseqsLSGGQAQRIALARAFLASDRH 491
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY-----PWDDV------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488907140 492 ILLfDEPTAHLDIQTEydlkQTMLPLLENHL--VFFATHRLHWLKQMDYVLVMDN 544
Cdd:cd03223 113 VFL-DEATSALDEESE----DRLYQLLKELGitVISVGHRPSLWKFHDRVLDLDG 162
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
333-547 |
6.25e-20 |
|
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: 88.36 E-value: 6.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG---INSgrGDISINrNKFLNFQNTSW--- 406
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLleePDS--GTIIID-GLKLTDDKKNInel 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 407 QKQIIYIPQKPYIF-HTSLRENIAFyqpdAP---KEQVVKAAKAAGIYELAS-GLFNGFDTMIGEseqsLSGGQAQRIAL 481
Cdd:cd03262 75 RQKVGMVFQQFNLFpHLTVLENITL----APikvKGMSKAEAEERALELLEKvGLADKADAYPAQ----LSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488907140 482 ARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHL-VFFATHRLHWLKQM-DYVLVMDNGHI 547
Cdd:cd03262 147 ARA-LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMtMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
333-559 |
8.68e-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: 88.26 E-value: 8.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG---INSGR-----GDIS------INRnkf 398
Cdd:cd03224 1 LEVENLNAGYGKSQ---ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGllpPRSGSirfdgRDITglppheRAR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 399 lnfqntswqKQIIYIPQKPYIFHT-SLRENI---AFYQPDAPKEQVVKAakaagIYELasglFNGFDTMIGESEQSLSGG 474
Cdd:cd03224 75 ---------AGIGYVPEGRRIFPElTVEENLllgAYARRRAKRKARLER-----VYEL----FPRLKERRKQLAGTLSGG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 475 QAQRIALARAfLASDRHILLFDEPTAHL----------DIQTEYDLKQTMLpLLENHlVFFAthrlhwLKQMDYVLVMDN 544
Cdd:cd03224 137 EQQMLAIARA-LMSRPKLLLLDEPSEGLapkiveeifeAIRELRDEGVTIL-LVEQN-ARFA------LEIADRAYVLER 207
|
250
....*....|....*
gi 488907140 545 GHIIEQGRPRELLED 559
Cdd:cd03224 208 GRVVLEGTAAELLAD 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
331-559 |
9.74e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.06 E-value: 9.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 331 TVLSVHNFSFQYpdGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINrNKFLnfqnTSWQ-- 407
Cdd:PRK13548 1 AMLEARNLSVRL--GGRTL-LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDSGEVRLN-GRPL----ADWSpa 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 408 ---KQIIYIPQkpyifHTSL------RENIA-----FYQPDAPKEQVVKAA-KAAGIYELASGLFngfdtmigeseQSLS 472
Cdd:PRK13548 73 elaRRRAVLPQ-----HSSLsfpftvEEVVAmgrapHGLSRAEDDALVAAAlAQVDLAHLAGRDY-----------PQLS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 473 GGQAQRIALARAfLA------SDRHILLFDEPTAHLDIQTEydlkQTMLPLLENhlvfFATHR-------LHWLKQM--- 536
Cdd:PRK13548 137 GGEQQRVQLARV-LAqlwepdGPPRWLLLDEPTSALDLAHQ----HHVLRLARQ----LAHERglavivvLHDLNLAary 207
|
250 260
....*....|....*....|....
gi 488907140 537 -DYVLVMDNGHIIEQGRPRELLED 559
Cdd:PRK13548 208 aDRIVLLHQGRLVADGTPAEVLTP 231
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
330-559 |
1.42e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 88.74 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 330 ETVLSVHNFSFQYPDG------QQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGIN-SGRGDISINRNKfLNFQ 402
Cdd:COG4167 2 SALLEVRNLSKTFKYRtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIePTSGEILINGHK-LEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 403 NTSWQ-KQIIYIPQKPYifhTSL--RENIAfYQPDAP------------KEQVVKAAKAAGIY-ELAsgLFNgfdtmige 466
Cdd:COG4167 81 DYKYRcKHIRMIFQDPN---TSLnpRLNIG-QILEEPlrlntdltaeerEERIFATLRLVGLLpEHA--NFY-------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 467 sEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENH-LVF-FATHRLHWLKQM-DYVLVMD 543
Cdd:COG4167 147 -PHMLSSGQKQRVALARA-LILQPKIIIADEALAALDMSVRSQIINLMLELQEKLgISYiYVSQHLGIVKHIsDKVLVMH 224
|
250
....*....|....*.
gi 488907140 544 NGHIIEQGRPRELLED 559
Cdd:COG4167 225 QGEVVEYGKTAEVFAN 240
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
333-562 |
1.51e-19 |
|
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: 88.43 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTL-LSSLAGINSGRGDISINRNKFLNFQNTSWQKQII 411
Cdd:cd03288 20 IKIHDLCVRYENNLKPV-LKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 412 YIPQKPYIFHTSLRENIafyQPD--APKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLASD 489
Cdd:cd03288 99 IILQDPILFSGSIRFNL---DPEckCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488907140 490 RhILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLEDFDG 562
Cdd:cd03288 176 S-ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDG 247
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
354-557 |
1.62e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 88.07 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 354 INFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGRGDISINRNKFLNFQNTSWQKQIIYIPQK---PYI---FHTslren 427
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqtpPFAmpvFQY----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 428 IAFYQPDapkeQVVKAAKAAGIYELASGLfnGFDTMIGESEQSLSGGQAQRIALARAFLASDRHI------LLFDEPTAH 501
Cdd:PRK03695 90 LTLHQPD----KTRTEAVASALNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpagqlLLLDEPMNS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488907140 502 LDIQteydlKQTMLPLLENHL------VFFATHRL-HWLKQMDYVLVMDNGHIIEQGRPRELL 557
Cdd:PRK03695 164 LDVA-----QQAALDRLLSELcqqgiaVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
330-571 |
3.18e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 87.92 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 330 ETVLSVHNFS--FQYPDG----QQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINrNKFLNFQ 402
Cdd:PRK15112 2 ETLLEVRNLSktFRYRTGwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGmIEPTSGELLID-DHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 403 NTSWQKQII-YIPQKP-----------YIFHTSLRENIAFyQPDAPKEQVVKAAKAAGIYELASGLFngfdtmigesEQS 470
Cdd:PRK15112 81 DYSYRSQRIrMIFQDPstslnprqrisQILDFPLRLNTDL-EPEQREKQIIETLRQVGLLPDHASYY----------PHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 471 LSGGQAQRIALARAFLASDRhILLFDEPTAHLDIQTEYDLKQTMLPLLENHLV--FFATHRLHWLKQM-DYVLVMDNGHI 547
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPK-VIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHIsDQVLVMHQGEV 228
|
250 260
....*....|....*....|....
gi 488907140 548 IEQGRPRELLEdfdGKLNELRKEL 571
Cdd:PRK15112 229 VERGSTADVLA---SPLHELTKRL 249
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
350-550 |
3.79e-19 |
|
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: 86.15 E-value: 3.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 350 ALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISIN-----------RNKFLNFQNTSwqkqiIYipqkP 417
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEpTSGRIYIGgrdvtdlppkdRDIAMVFQNYA-----LY----P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 418 yifHTSLRENIAF------YQPDAPKEQVVKAAKAAGIYELasglfngfdtmIGESEQSLSGGQAQRIALARAfLASDRH 491
Cdd:cd03301 86 ---HMTVYDNIAFglklrkVPKDEIDERVREVAELLQIEHL-----------LDRKPKQLSGGQRQRVALGRA-IVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488907140 492 ILLFDEPTAHLDIQTEYDLKQTMLPLLENH--LVFFATH-RLHWLKQMDYVLVMDNGhIIEQ 550
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLgtTTIYVTHdQVEAMTMADRIAVMNDG-QIQQ 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
333-551 |
7.19e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 86.22 E-value: 7.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGR-GDISINRNKFlNFQNTSWQKQII 411
Cdd:PRK11124 3 IQLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRsGTLNIAGNHF-DFSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 412 YIPQK-PYIF-------HTSLRENIAfyqpDAP-------KEQVVKAAKaagiyELASGL-FNGFdtmIGESEQSLSGGQ 475
Cdd:PRK11124 79 ELRRNvGMVFqqynlwpHLTVQQNLI----EAPcrvlglsKDQALARAE-----KLLERLrLKPY---ADRFPLHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 476 AQRIALARAfLASDRHILLFDEPTAHLD--IQTE-----YDLKQT-MLPLLENHLVFFAThrlhwlKQMDYVLVMDNGHI 547
Cdd:PRK11124 147 QQRVAIARA-LMMEPQVLLFDEPTAALDpeITAQivsiiRELAETgITQVIVTHEVEVAR------KTASRVVYMENGHI 219
|
....
gi 488907140 548 IEQG 551
Cdd:PRK11124 220 VEQG 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
351-571 |
8.29e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.22 E-value: 8.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGRgdisinrnkfLNFQNT------SWQKQIIYIPQKPYIF- 420
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLehqTSGH----------IRFHGTdvsrlhARDRKVGFVFQHYALFr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 421 HTSLRENIAFYQPDAPKEQVVKAA----KAAGIYELA--SGLFNGFDTmigeseqSLSGGQAQRIALARAfLASDRHILL 494
Cdd:PRK10851 88 HMTVFDNIAFGLTVLPRRERPNAAaikaKVTQLLEMVqlAHLADRYPA-------QLSGGQKQRVALARA-LAVEPQILL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 495 FDEPTAHLDIQTEYDLKQtMLPLLENHLVF---FATH-RLHWLKQMDYVLVMDNGHIIEQGRPRELLED--------FDG 562
Cdd:PRK10851 160 LDEPFGALDAQVRKELRR-WLRQLHEELKFtsvFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWREpatrfvleFMG 238
|
....*....
gi 488907140 563 KLNELRKEL 571
Cdd:PRK10851 239 EVNRLQGTI 247
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
326-555 |
1.17e-18 |
|
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: 85.18 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 326 AIDSETVLSVHNFSFQYPDGQQP-AALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSG-RGDISIN--------- 394
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPtSGTVRLAgqdlfalde 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 395 --RNKFLN------FQNtswqkqiiyipqkpyiFH-----TSLrENIAFyqpdaPKEQV-VKAAKAAGIYELAS-GLfng 459
Cdd:COG4181 82 daRARLRArhvgfvFQS----------------FQllptlTAL-ENVML-----PLELAgRRDARARARALLERvGL--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 460 fdtmiGESEQ----SLSGGQAQRIALARAFlASDRHILLFDEPTAHLDIQTeydlKQTMLPLL-----ENH--LVfFATH 528
Cdd:COG4181 137 -----GHRLDhypaQLSGGEQQRVALARAF-ATEPAILFADEPTGNLDAAT----GEQIIDLLfelnrERGttLV-LVTH 205
|
250 260
....*....|....*....|....*..
gi 488907140 529 RLHWLKQMDYVLVMDNGHIIEQGRPRE 555
Cdd:COG4181 206 DPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
337-559 |
1.38e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 86.29 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 337 NFSFQYPD---GQQPAALKDINFLVRGFAKVAVVGLSGSGKTTL---LSSLAGINSGRG-----DIS-------INRNKF 398
Cdd:PRK13633 9 NVSYKYESneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPSEGKVyvdglDTSdeenlwdIRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 399 LNFQNTSWQkqiiyipqkpyIFHTSLRENIAF------YQPDAPKEQVVKAAKAAGIYELASglfngfdtmigESEQSLS 472
Cdd:PRK13633 89 MVFQNPDNQ-----------IVATIVEEDVAFgpenlgIPPEEIRERVDESLKKVGMYEYRR-----------HAPHLLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 473 GGQAQRIALArAFLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENH--LVFFATHRLHWLKQMDYVLVMDNGHIIEQ 550
Cdd:PRK13633 147 GGQKQRVAIA-GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVME 225
|
....*....
gi 488907140 551 GRPRELLED 559
Cdd:PRK13633 226 GTPKEIFKE 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
364-551 |
1.74e-18 |
|
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: 84.27 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 364 VAVVGLSGSGKTTLLSSLAGI-NSGRGDISINrnkflnfqNTSW---QKQIIYIPQK---PYIF-------HTSLRENIA 429
Cdd:cd03297 26 TGIFGASGAGKSTLLRCIAGLeKPDGGTIVLN--------GTVLfdsRKKINLPPQQrkiGLVFqqyalfpHLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 430 F-YQPDAPKEQVVKAAKAagiyelaSGLFnGFDTMIGESEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEY 508
Cdd:cd03297 98 FgLKRKRNREDRISVDEL-------LDLL-GLDHLLNRYPAQLSGGEKQRVALARA-LAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488907140 509 DLKQTMLPLLE--NHLVFFATHRLHWLKQM-DYVLVMDNGHIIEQG 551
Cdd:cd03297 169 QLLPELKQIKKnlNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
16-295 |
1.99e-18 |
|
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: 86.07 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 16 LSWLVLLTFLQAVSILFQAFFLSKSIVILWHQSAFSSAVPYIFGFAISLLCRHFFSLIKEGSANSFSVTASEGLRDQLLG 95
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 96 KYLSFGDQTIFKTGTGHAVSLLHAGIDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLRWQEALFLLLIFPVIIFFFVILG 175
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 176 LAAQKRADNEYRNFTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVI 255
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 488907140 256 AVFLGFSLMEGKMSLFPALTLLVLAPEYFLPLRTFSEDYH 295
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYN 280
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
332-556 |
2.37e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.24 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPDGQQpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSG----RGDISINRN-----KF- 398
Cdd:PRK13652 3 LIETRDLCYSYSGSKE--ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIlkpTSGsvliRGEPITKENirevrKFv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 399 -LNFQNTSWQkqiiyipqkpyIFHTSLRENIAF------YQPDAPKEQVVKAAKAAGIYELASglfngfdtmigESEQSL 471
Cdd:PRK13652 81 gLVFQNPDDQ-----------IFSPTVEQDIAFgpinlgLDEETVAHRVSSALHMLGLEELRD-----------RVPHHL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 472 SGGQAQRIALArAFLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENH--LVFFATHRLHWLKQM-DYVLVMDNGHII 548
Cdd:PRK13652 139 SGGEKKRVAIA-GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVPEMaDYIYVMDKGRIV 217
|
....*...
gi 488907140 549 EQGRPREL 556
Cdd:PRK13652 218 AYGTVEEI 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
332-559 |
3.70e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.65 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPDGQqpAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI-NSGRGDISINRNKFLNFQNTSWQKQI 410
Cdd:PRK13644 1 MIRLENVSYSYPDGT--PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLlRPQKGKVLVSGIDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 411 IYI----PQKPYIFHTsLRENIAFyQPD---APKEQVVKAAKAAgiyeLASglfNGFDTMIGESEQSLSGGQAQRIALAr 483
Cdd:PRK13644 79 VGIvfqnPETQFVGRT-VEEDLAF-GPEnlcLPPIEIRKRVDRA----LAE---IGLEKYRHRSPKTLSGGQGQCVALA- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488907140 484 AFLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLEN-HLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLED 559
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
328-559 |
4.21e-18 |
|
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: 87.43 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 328 DSETVLSVHNFSFQYPDG----QQPA----ALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGRGDISinrnkfl 399
Cdd:COG4172 271 DAPPLLEARDLKVWFPIKrglfRRTVghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIR------- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 400 nFQNTSWQK-------------QIIYipQKPYifhTSL----------RENIAFYQPDAPKEQVVKAAKAAgiyeLAS-G 455
Cdd:COG4172 344 -FDGQDLDGlsrralrplrrrmQVVF--QDPF---GSLsprmtvgqiiAEGLRVHGPGLSAAERRARVAEA----LEEvG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 456 LfngfdtmigeSEQSL-------SGGQAQRIALARAfLASDRHILLFDEPTAHLD-------------IQTEYDLkqTML 515
Cdd:COG4172 414 L----------DPAARhryphefSGGQRQRIAIARA-LILEPKLLVLDEPTSALDvsvqaqildllrdLQREHGL--AYL 480
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 488907140 516 pllenhlvfFATHRLHWLKQM-DYVLVMDNGHIIEQGRPRELLED 559
Cdd:COG4172 481 ---------FISHDLAVVRALaHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
347-558 |
6.52e-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: 83.85 E-value: 6.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 347 QPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFLNFQNTSWQ----KQIIYIPQKPYIF- 420
Cdd:cd03294 36 QTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRlIEPTSGKVLIDGQDIAAMSRKELRelrrKKISMVFQSFALLp 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 421 HTSLRENIAF---YQPDAPKEQVVKAAKAagiYELAsGLFNGFDTMIGEseqsLSGGQAQRIALARAfLASDRHILLFDE 497
Cdd:cd03294 116 HRTVLENVAFgleVQGVPRAEREERAAEA---LELV-GLEGWEHKYPDE----LSGGMQQRVGLARA-LAVDPDILLMDE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488907140 498 PTAHLDIQTEYDLKQTMLPLLENH--LVFFATHRL-HWLKQMDYVLVMDNGHIIEQGRPRELLE 558
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLQAELqkTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
364-528 |
1.72e-17 |
|
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: 81.00 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 364 VAVVGLSGSGKTTLLSSLAGINS-GRGDISINrNKFLNFQNTSWQKQIIYIPQKPYIFHT-SLRENIAFYQPDAPKEQVV 441
Cdd:cd03231 29 LQVTGPNGSGKTTLLRILAGLSPpLAGRVLLN-GGPLDFQRDSIARGLLYLGHAPGIKTTlSVLENLRFWHADHSDEQVE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 442 KAAKAAGIyelasglfNGFDTMIGeseQSLSGGQAQRIALARAFLaSDRHILLFDEPTAHLDIQTEYDLKQTMLPLLE-N 520
Cdd:cd03231 108 EALARVGL--------NGFEDRPV---AQLSAGQQRRVALARLLL-SGRPLWILDEPTTALDKAGVARFAEAMAGHCArG 175
|
....*...
gi 488907140 521 HLVFFATH 528
Cdd:cd03231 176 GMVVLTTH 183
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
333-559 |
2.21e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 82.09 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYpdGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISinrnkfLNFQN-TSWQ--- 407
Cdd:COG4559 2 LEAENLSVRL--GGRTL-LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTPSSGEVR------LNGRPlAAWSpwe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 408 --KQIIYIPQkpyifHTSL------RENIAF-----YQPDAPKEQVVKAA-KAAGIYELASGLFngfdtmigeseQSLSG 473
Cdd:COG4559 73 laRRRAVLPQ-----HSSLafpftvEEVVALgraphGSSAAQDRQIVREAlALVGLAHLAGRSY-----------QTLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 474 GQAQRIALARAfLA-------SDRHILLFDEPTAHLDI--QteydlkQTMLPLLENhlvfFATHRLHWLKQM-------- 536
Cdd:COG4559 137 GEQQRVQLARV-LAqlwepvdGGPRWLFLDEPTSALDLahQ------HAVLRLARQ----LARRGGGVVAVLhdlnlaaq 205
|
250 260
....*....|....*....|....*
gi 488907140 537 --DYVLVMDNGHIIEQGRPRELLED 559
Cdd:COG4559 206 yaDRILLLHQGRLVAQGTPEEVLTD 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
333-556 |
3.34e-17 |
|
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: 80.63 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGR---GDISINRNKFLNFQNTSw 406
Cdd:cd03263 1 LQIRNLTKTYKKGTKPA-VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGElrpTSGTayiNGYSIRTDRKAARQSLG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 407 qkqiiYIPQKPYIFHT-SLRENIAFYQPdapkeqvVKAAKAAGIYELASGLFNGF------DTMIGEseqsLSGGQAQRI 479
Cdd:cd03263 79 -----YCPQFDALFDElTVREHLRFYAR-------LKGLPKSEIKEEVELLLRVLgltdkaNKRART----LSGGMKRKL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 480 ALARAFLAsDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHrlhwlkQM-------DYVLVMDNGHIIEQGR 552
Cdd:cd03263 143 SLAIALIG-GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH------SMdeaealcDRIAIMSDGKLRCIGS 215
|
....
gi 488907140 553 PREL 556
Cdd:cd03263 216 PQEL 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
329-559 |
3.53e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 82.16 E-value: 3.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 329 SETVLSVHNFSFQYPDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI--NSGRGDISINRNKFLNFQNTSW 406
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDSKKPA-LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllPDDNPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 407 QkqiiyipqkpyifhtsLREN--IAFYQPDapkEQVVKAAKAAgiyELASGLFN-------------------GFDTMIG 465
Cdd:PRK13640 81 D----------------IREKvgIVFQNPD---NQFVGATVGD---DVAFGLENravprpemikivrdvladvGMLDYID 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 466 ESEQSLSGGQAQRIALArAFLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLL-ENHL-VFFATHRLHWLKQMDYVLVMD 543
Cdd:PRK13640 139 SEPANLSGGQKQRVAIA-GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLtVISITHDIDEANMADQVLVLD 217
|
250
....*....|....*.
gi 488907140 544 NGHIIEQGRPRELLED 559
Cdd:PRK13640 218 DGKLLAQGSPVEIFSK 233
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
345-545 |
3.69e-17 |
|
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: 80.45 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 345 GQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG---INSGRGDISINRNKFLNFQNTSWQKQ--IIYIPQKPYI 419
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGemqTLEGKVHWSNKNESEPSFEATRSRNRysVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 420 FHTSLRENIAFYQPdAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAfLASDRHILLFDEPT 499
Cdd:cd03290 91 LNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARA-LYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488907140 500 AHLDIQ-TEYDLKQTMLPLLEN--HLVFFATHRLHWLKQMDYVLVMDNG 545
Cdd:cd03290 169 SALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
333-551 |
3.70e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 81.21 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYpdGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGR-GDISINRNKFlNFQNTSWQKQII 411
Cdd:COG4161 3 IQLKNINCFY--GSHQA-LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDsGQLNIAGHQF-DFSQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 412 YIPQK-PYIF-------HTSLRENIAfyqpDAPKeQVVKAAKAAGIyELASGLFN--GFDTMIGESEQSLSGGQAQRIAL 481
Cdd:COG4161 79 LLRQKvGMVFqqynlwpHLTVMENLI----EAPC-KVLGLSKEQAR-EKAMKLLArlRLTDKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488907140 482 ARAfLASDRHILLFDEPTAHLD--IQTEY-----DLKQT-MLPLLENHLVFFAThrlhwlKQMDYVLVMDNGHIIEQG 551
Cdd:COG4161 153 ARA-LMMEPQVLLFDEPTAALDpeITAQVveiirELSQTgITQVIVTHEVEFAR------KVASQVVYMEKGRIIEQG 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
333-558 |
3.82e-17 |
|
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: 80.74 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISINRNKFLNFqnTSWQKQII 411
Cdd:cd03300 1 IELENVSKFYGGFV---ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETpTSGEILLDGKDITNL--PPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 412 YIPQKPYIF-HTSLRENIAF------YQPDAPKEQVVKAAKAAGIYELAsglfngfDTMIGEseqsLSGGQAQRIALARA 484
Cdd:cd03300 76 TVFQNYALFpHLTVFENIAFglrlkkLPKAEIKERVAEALDLVQLEGYA-------NRKPSQ----LSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 485 fLASDRHILLFDEPTAHLDIQteydLKQTM-LPLLENH----LVF-FATH-RLHWLKQMDYVLVMDNGHIIEQGRPRELL 557
Cdd:cd03300 145 -LVNEPKVLLLDEPLGALDLK----LRKDMqLELKRLQkelgITFvFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
.
gi 488907140 558 E 558
Cdd:cd03300 220 E 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
351-557 |
5.25e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 80.65 E-value: 5.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGRGDIsinrnkFLNFQN-TSWQKQII-----YIPQKPY------ 418
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEI------LLNGRPlSDWSAAELarhraYLSQQQSppfamp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 419 IFHTslrenIAFYQPDAPKEQVVKAAkaagIYELASGLfnGFDTMIGESEQSLSGGQAQRIALARAFLASDRHI------ 492
Cdd:COG4138 86 VFQY-----LALHQPAGASSEAVEQL----LAQLAEAL--GLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTInpegql 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488907140 493 LLFDEPTAHLDIQteydlKQTMLPLLENHL------VFFATHRL-HWLKQMDYVLVMDNGHIIEQGRPRELL 557
Cdd:COG4138 155 LLLDEPMNSLDVA-----QQAALDRLLRELcqqgitVVMSSHDLnHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
332-561 |
5.72e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 81.28 E-value: 5.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPDGQQpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI-NSGRGDISINRNKfLNFQNTSW---Q 407
Cdd:PRK13639 1 ILETRDLKYSYPDGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGIlKPTSGEVLIKGEP-IKYDKKSLlevR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 408 KQIIYIPQKP--YIFHTSLRENIAF--YQPDAPKEQVVKAAKAAgiyeLASGLFNGFDTmigESEQSLSGGQAQRIALAr 483
Cdd:PRK13639 78 KTVGIVFQNPddQLFAPTVEEDVAFgpLNLGLSKEEVEKRVKEA----LKAVGMEGFEN---KPPHHLSGGQKKRVAIA- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 484 AFLASDRHILLFDEPTAHLD-------IQTEYDL-KQTMLPLLENHLVFFAThrlhwlKQMDYVLVMDNGHIIEQGRPRE 555
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDpmgasqiMKLLYDLnKEGITIIISTHDVDLVP------VYADKVYVMSDGKIIKEGTPKE 223
|
....*.
gi 488907140 556 LLEDFD 561
Cdd:PRK13639 224 VFSDIE 229
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
342-557 |
6.00e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 82.43 E-value: 6.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 342 YPDGQQP-AALKDINFLV-RG--FAkvaVVGLSGSGKTTLLSSLAGIN---SGRgdISIN------------RNKflnfq 402
Cdd:COG1135 11 FPTKGGPvTALDDVSLTIeKGeiFG---IIGYSGAGKSTLIRCINLLErptSGS--VLVDgvdltalserelRAA----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 403 ntswQKQIIYIPQkpyifHTSL------RENIAFyqpdaPKEQ--VVKAAKAAGIYELAS--GLfngfdtmiGESEQS-- 470
Cdd:COG1135 81 ----RRKIGMIFQ-----HFNLlssrtvAENVAL-----PLEIagVPKAEIRKRVAELLElvGL--------SDKADAyp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 471 --LSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTeydlKQTMLPLLEN-----HL-VFFATHRLHWLKQM-DYVLV 541
Cdd:COG1135 139 sqLSGGQKQRVGIARA-LANNPKVLLCDEATSALDPET----TRSILDLLKDinrelGLtIVLITHEMDVVRRIcDRVAV 213
|
250
....*....|....*.
gi 488907140 542 MDNGHIIEQGRPRELL 557
Cdd:COG1135 214 LENGRIVEQGPVLDVF 229
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
351-564 |
8.87e-17 |
|
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: 84.58 E-value: 8.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDIsinrnkflnfqntSWQKQIIYIPQKPYIFHTSLRENIA 429
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEGKI-------------KHSGRISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 430 F-YQPDAPKEQVVkaAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEY 508
Cdd:TIGR01271 509 FgLSYDEYRYTSV--IKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARA-VYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 509 DLKQTML-PLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLE---DFDGKL 564
Cdd:TIGR01271 586 EIFESCLcKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAkrpDFSSLL 645
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
337-559 |
9.07e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 81.03 E-value: 9.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 337 NFSFQYPDGQ--QPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGRGDI---SIN---RNKFLNfqntS 405
Cdd:PRK13641 7 NVDYIYSPGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALlkpSSGTITIagyHITpetGNKNLK----K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 406 WQKQIIYIPQKP--YIFHTSLRENIAF------YQPDAPKEQVVKAAKAAGIYElasglfngfdTMIGESEQSLSGGQAQ 477
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVLKDVEFgpknfgFSEDEAKEKALKWLKKVGLSE----------DLISKSPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 478 RIALArAFLASDRHILLFDEPTAHLDIQTEYDLKQTMLPL-LENHLVFFATHRLHWLKQ-MDYVLVMDNGHIIEQGRPRE 555
Cdd:PRK13641 153 RVAIA-GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKE 231
|
....
gi 488907140 556 LLED 559
Cdd:PRK13641 232 IFSD 235
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
332-551 |
9.20e-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: 78.75 E-value: 9.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPDGQQPAA---LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSG---RGDISINRnkfLNFQNTS 405
Cdd:cd03213 3 TLSFRNLTVTVKSSPSKSGkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgvSGEVLING---RPLDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 406 WQKQIIYIPQKPyIFHTSL--RENIAFyqpdapkeqvvkaakAAGIyelasglfngfdtmigeseQSLSGGQAQRIALAR 483
Cdd:cd03213 80 FRKIIGYVPQDD-ILHPTLtvRETLMF---------------AAKL-------------------RGLSGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488907140 484 AfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPL-LENHLVFFATHRLHWL--KQMDYVLVMDNGHIIEQG 551
Cdd:cd03213 125 E-LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIHQPSSEifELFDKLLLLSQGRVIYFG 194
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
332-559 |
9.60e-17 |
|
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: 81.25 E-value: 9.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPDGQQPA-ALKDINF-LVRGfAKVAVVGLSGSGKTTLLSSLAGINSGR----GDISINRNKFLNFQNTS 405
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVkAVDGVSFdVRRG-ETLGLVGESGSGKSTLARAILGLLPPPgitsGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 406 WQ----KQIIYIPQKPYifhTSL----------RENIAFYQP---DAPKEQVVKAAKAAGIyelasglfngfdtmiGESE 468
Cdd:COG0444 80 LRkirgREIQMIFQDPM---TSLnpvmtvgdqiAEPLRIHGGlskAEARERAIELLERVGL---------------PDPE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 469 Q-------SLSGGQAQRIALARAfLASDRHILLFDEPTAHLD-------------IQTEYDLkqTMLpllenhlvfFATH 528
Cdd:COG0444 142 RrldryphELSGGMRQRVMIARA-LALEPKLLIADEPTTALDvtiqaqilnllkdLQRELGL--AIL---------FITH 209
|
250 260 270
....*....|....*....|....*....|..
gi 488907140 529 RLHWLKQM-DYVLVMDNGHIIEQGRPRELLED 559
Cdd:COG0444 210 DLGVVAEIaDRVAVMYAGRIVEEGPVEELFEN 241
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
335-528 |
1.14e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.81 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 335 VHNFSFQYPDgqqPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNkflnfqntswqKQIIYI 413
Cdd:COG0488 1 LENLSKSFGG---RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGeLEPDSGEVSIPKG-----------LRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 414 PQKPYIF------------HTSLRENIAFY-----QPDAPKEQVVKAAKAAGIYE-------------LASGLfnGFDTM 463
Cdd:COG0488 67 PQEPPLDddltvldtvldgDAELRALEAELeeleaKLAEPDEDLERLAELQEEFEalggweaearaeeILSGL--GFPEE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488907140 464 IGESE-QSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQT-EYdlkqtmlplLENHL------VFFATH 528
Cdd:COG0488 145 DLDRPvSELSGGWRRRVALARA-LLSEPDLLLLDEPTNHLDLESiEW---------LEEFLknypgtVLVVSH 207
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
331-528 |
1.48e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 79.91 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 331 TVLSVHNFSFQYP-DGQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFLN-------- 400
Cdd:COG4525 2 SMLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGfLAPSSGEITLDGVPVTGpgadrgvv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 401 FQNTS---WQkqiiyipqkpyifhtSLRENIAFyqpdAPKEQ-VVKAAKAAGIYELAS--GLFNGFDTMIGEseqsLSGG 474
Cdd:COG4525 82 FQKDAllpWL---------------NVLDNVAF----GLRLRgVPKAERRARAEELLAlvGLADFARRRIWQ----LSGG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488907140 475 QAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPL--LENHLVFFATH 528
Cdd:COG4525 139 MRQRVGIARA-LAADPRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITH 193
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
333-551 |
1.86e-16 |
|
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: 78.39 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQqpaALKDINF-LVRGFakVAVVGLSGSGKTTLLSSLAGI---NSGR-----GDISINRNKFlnfqn 403
Cdd:cd03264 1 LQLENLTKRYGKKR---ALDGVSLtLGPGM--YGLLGPNGAGKTTLMRILATLtppSSGTiridgQDVLKQPQKL----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 404 tswQKQIIYIPQKP-YIFHTSLRENIAFY-------QPDApKEQVVKAAKAAGIYELASglfngfdtmigESEQSLSGGQ 475
Cdd:cd03264 71 ---RRRIGYLPQEFgVYPNFTVREFLDYIawlkgipSKEV-KARVDEVLELVNLGDRAK-----------KKIGSLSGGM 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488907140 476 AQRIALARAFLAsDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQM-DYVLVMDNGHIIEQG 551
Cdd:cd03264 136 RRRVGIAQALVG-DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
351-557 |
4.46e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.27 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFLNFQNTSWQKQIIYIPQKPYI-FHTSLRENI 428
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGtLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 429 A---------FYQPDAPKEQVVKAAKAAGiyelasglfnGFDTMIGESEQSLSGGQAQRIALARAfLASDRHILLFDEPT 499
Cdd:PRK09536 99 EmgrtphrsrFDTWTETDRAAVERAMERT----------GVAQFADRPVTSLSGGERQRVLLARA-LAQATPVLLLDEPT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 500 AHLDIQTEYDLKQTMLPLLEN-HLVFFATHRLHWLKQM-DYVLVMDNGHIIEQGRPRELL 557
Cdd:PRK09536 168 ASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPADVL 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
330-559 |
5.23e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 78.74 E-value: 5.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 330 ETVLSVHNFSFQYPDGQQpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGR-----GDISINRNKFLNF 401
Cdd:PRK13636 3 DYILKVEELNYNYSDGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGIlkpSSGRilfdgKPIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 402 qntswQKQIIYIPQKP--YIFHTSLRENIAF------YQPDAPKEQVVKAAKAAGIYELASglfngfdtmigESEQSLSG 473
Cdd:PRK13636 81 -----RESVGMVFQDPdnQLFSASVYQDVSFgavnlkLPEDEVRKRVDNALKRTGIEHLKD-----------KPTHCLSF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 474 GQAQRIALArAFLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENH--LVFFATHRLHWLK-QMDYVLVMDNGHIIEQ 550
Cdd:PRK13636 145 GQKKRVAIA-GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPlYCDNVFVMKEGRVILQ 223
|
....*....
gi 488907140 551 GRPRELLED 559
Cdd:PRK13636 224 GNPKEVFAE 232
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
335-557 |
5.99e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.75 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 335 VHNFSFQYPDGQqpaalkdinflvrgfaKVAVVGLSGSGKTTLLSSLAGINSGR-GDISINRNKFLNFQNTSWQKQIIYI 413
Cdd:PRK11231 18 LNDLSLSLPTGK----------------ITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 414 PQKPYIFH-TSLRENIAF----YQP------DAPKEQVVKAAKAAGIYELASGLFNgfdtmigeseqSLSGGQAQRIALA 482
Cdd:PRK11231 82 PQHHLTPEgITVRELVAYgrspWLSlwgrlsAEDNARVNQAMEQTRINHLADRRLT-----------DLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488907140 483 RAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFAThrLHWLKQM----DYVLVMDNGHIIEQGRPRELL 557
Cdd:PRK11231 151 MV-LAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTV--LHDLNQAsrycDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
328-562 |
6.67e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.87 E-value: 6.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 328 DSETVLSVHNFSFQYpDGQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGRGDISINRNKFLNFQNTSWQ 407
Cdd:PRK13648 3 DKNSIIVFKNVSFQY-QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 408 KQIIYI----PQKPYIFHTsLRENIAF------YQPDAPKEQVVKAAKAAGIYELAsglfngfdtmigESE-QSLSGGQA 476
Cdd:PRK13648 82 RKHIGIvfqnPDNQFVGSI-VKYDVAFglenhaVPYDEMHRRVSEALKQVDMLERA------------DYEpNALSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 477 QRIALArAFLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFA--THRLHWLKQMDYVLVMDNGHIIEQGRPR 554
Cdd:PRK13648 149 QRVAIA-GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIIsiTHDLSEAMEADHVIVMNKGTVYKEGTPT 227
|
....*...
gi 488907140 555 ELLEDFDG 562
Cdd:PRK13648 228 EIFDHAEE 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
329-573 |
7.43e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.51 E-value: 7.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 329 SETVLSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGRGDISINRNKFLNFQN----- 403
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNiyspr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 404 ---TSWQKQIIYIPQKPYIFHTSLRENIAF-------YQPDAPKEQVVKAAKAAGIYELASGLFNgfDTMIGeseqsLSG 473
Cdd:PRK14239 79 tdtVDLRKEIGMVFQQPNPFPMSIYENVVYglrlkgiKDKQVLDEAVEKSLKGASIWDEVKDRLH--DSALG-----LSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 474 GQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQM-DYVLVMDNGHIIEQGR 552
Cdd:PRK14239 152 GQQQRVCIARV-LATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRIsDRTGFFLDGDLIEYND 230
|
250 260
....*....|....*....|.
gi 488907140 553 PRELLedfdgkLNELRKELTD 573
Cdd:PRK14239 231 TKQMF------MNPKHKETED 245
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
350-561 |
7.97e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.14 E-value: 7.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 350 ALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFlnfQNTSWQKQIIYIPQKPYI--------- 419
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGlLQPTSGTVTIGERVI---TAGKKNKKLKPLRKKVGIvfqfpehql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 420 FHTSLRENIAFyqpdAPKEQVVKAAKAAgiyELASGLFNgfdtMIGESEQ-------SLSGGQAQRIALArAFLASDRHI 492
Cdd:PRK13634 99 FEETVEKDICF----GPMNFGVSEEDAK---QKAREMIE----LVGLPEEllarspfELSGGQMRRVAIA-GVLAMEPEV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 493 LLFDEPTAHLDIQTEYDLKQtmlpllenhlVFFATHRLHWLK------QM-------DYVLVMDNGHIIEQGRPRELLED 559
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMME----------MFYKLHKEKGLTtvlvthSMedaaryaDQIVVMHKGTVFLQGTPREIFAD 236
|
..
gi 488907140 560 FD 561
Cdd:PRK13634 237 PD 238
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
351-551 |
8.34e-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: 76.93 E-value: 8.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSG----RGDISIN---RNKFLnfqntsWQKQIIYIPQKPyIFHTS 423
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggttSGQILFNgqpRKPDQ------FQKCVAYVRQDD-ILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 424 L--RENIAFYQPDA-----PKEQVVKAAKAAGIYELAsglfngfDTMIGESE-QSLSGGQAQRIALARAFLaSDRHILLF 495
Cdd:cd03234 96 LtvRETLTYTAILRlprksSDAIRKKRVEDVLLRDLA-------LTRIGGNLvKGISGGERRRVSIAVQLL-WDPKVLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488907140 496 DEPTAHLDIQTEYDLKQTMLPLL-ENHLVFFATH--RLHWLKQMDYVLVMDNGHIIEQG 551
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQLArRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
348-559 |
1.87e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 80.17 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 348 PAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI-NSGRGDISINRNKFLNFQNTSWQKQIIYIPQKPYIFHTSLRE 426
Cdd:PLN03130 1252 PPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIvELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 427 NIAFY--QPDApkeQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAFLASDRhILLFDEPTAHLDI 504
Cdd:PLN03130 1332 NLDPFneHNDA---DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSK-ILVLDEATAAVDV 1407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488907140 505 QTEYDLKQTMLPLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLED 559
Cdd:PLN03130 1408 RTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
335-561 |
1.96e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 77.01 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 335 VHNFSFQYPDGQ--QPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGR---GDISINRNKflnFQNTSW 406
Cdd:PRK13637 5 IENLTHIYMEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLlkpTSGKiiiDGVDITDKK---VKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 407 QKQIIYIPQKP--YIFHTSLRENIAF------YQPDAPKEQVVKAAKAAGIyelasglfnGFDTMIGESEQSLSGGQAQR 478
Cdd:PRK13637 82 RKKVGLVFQYPeyQLFEETIEKDIAFgpinlgLSEEEIENRVKRAMNIVGL---------DYEDYKDKSPFELSGGQKRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 479 IALArAFLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLE--NHLVFFATHRLHWL-KQMDYVLVMDNGHIIEQGRPRE 555
Cdd:PRK13637 153 VAIA-GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
....*.
gi 488907140 556 LLEDFD 561
Cdd:PRK13637 232 VFKEVE 237
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
353-556 |
2.08e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 77.84 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 353 DINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI-NSGRGDISINRNkflNFQNTSWQKQIIYIPQKPY-IF-HTSLRENIA 429
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLeKPTEGQIFIDGE---DVTHRSIQQRDICMVFQSYaLFpHMSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 430 F-----YQPDAPKEQVVKAAKAagIYELAsglfnGF-DTMIGEseqsLSGGQAQRIALARAFLASDRhILLFDEPTAHLD 503
Cdd:PRK11432 101 YglkmlGVPKEERKQRVKEALE--LVDLA-----GFeDRYVDQ----ISGGQQQRVALARALILKPK-VLLFDEPLSNLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488907140 504 IQTEYDLKQTMLPLLE--NHLVFFATH-RLHWLKQMDYVLVMDNGHIIEQGRPREL 556
Cdd:PRK11432 169 ANLRRSMREKIRELQQqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
330-547 |
2.86e-15 |
|
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: 74.01 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 330 ETVLSVHNFSFqypdgqqPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSG-RGDISINRNKFLNFQNTSWQK 408
Cdd:cd03215 2 EPVLEVRGLSV-------KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPaSGEITLDGKPVTRRSPRDAIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 409 Q-IIYIP---QKPYIFHT-SLRENIAFyqpdapkeqvvkaakaagiyelasglfngfdtmigesEQSLSGGQAQRIALAR 483
Cdd:cd03215 75 AgIAYVPedrKREGLVLDlSVAENIAL-------------------------------------SSLLSGGNQQKVVLAR 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488907140 484 AfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLL-ENHLVFFATHRLHWLKQM-DYVLVMDNGHI 547
Cdd:cd03215 118 W-LARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdAGKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
333-548 |
3.62e-15 |
|
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: 73.23 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGRgdisinrnkflnfqntswqkq 409
Cdd:cd03216 1 LELRGITKRFGGVK---ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLykpDSGE--------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 410 iIYIPQKPYIFHTslreniafyqpdapkeqvVKAAKAAGIYelasglfngfdtMIgeseQSLSGGQAQRIALARAfLASD 489
Cdd:cd03216 57 -ILVDGKEVSFAS------------------PRDARRAGIA------------MV----YQLSVGERQMVEIARA-LARN 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488907140 490 RHILLFDEPTAHLDIQTEYDLKQTMLPLLENHL-VFFATHRLHWLKQM-DYVLVMDNGHII 548
Cdd:cd03216 101 ARLLILDEPTAALTPAEVERLFKVIRRLRAQGVaVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
332-559 |
3.76e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.17 E-value: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYpdgQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGIN-SGRGDISINRNKFLNFQNTSWQKQI 410
Cdd:PRK15439 11 LLCARSISKQY---SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVpPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 411 IY-IPQKPYIF-HTSLRENIAFyqpDAPKEQVVKAAKAAGIYELASGLfnGFDTMIGeseqSLSGGQAQRIALARAfLAS 488
Cdd:PRK15439 88 IYlVPQEPLLFpNLSVKENILF---GLPKRQASMQKMKQLLAALGCQL--DLDSSAG----SLEVADRQIVEILRG-LMR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488907140 489 DRHILLFDEPTAHLD-IQTEYDLKQTMLPLLENHLVFFATHRLHWLKQM-DYVLVMDNGHIIEQGRPRELLED 559
Cdd:PRK15439 158 DSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQLaDRISVMRDGTIALSGKTADLSTD 230
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
20-287 |
3.94e-15 |
|
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: 75.76 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 20 VLLTFLQAVSILFQAFFLSKSIVILWHQSAFSSAVPYIFGFAISLLCrhFFSLIKEGSANSFSVTASEG----LRDQLLG 95
Cdd:pfam00664 5 ILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLG--LAQFILSFLQSYLLNHTGERlsrrLRRKLFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 96 KYLSFGDQTIFKTGTGHAVSLLHAGIDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLRWQEALFLLLIFPVIIFFFVILG 175
Cdd:pfam00664 83 KILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 176 LAAQKRADNEYRNFTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVI 255
Cdd:pfam00664 163 KILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALA 242
|
250 260 270
....*....|....*....|....*....|..
gi 488907140 256 AVFLGFSLMEGKMSLFPALTLLVLAPEYFLPL 287
Cdd:pfam00664 243 LWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
331-559 |
4.27e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 77.29 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 331 TVLSVHNFSFQYpDGQQpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI-NSGRGDIsinrnkFLNFQNTS---- 405
Cdd:PRK09452 13 PLVELRGISKSF-DGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFeTPDSGRI------MLDGQDIThvpa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 406 WQKQIIYIPQKPYIF-HTSLRENIAF-----YQPDAP-KEQVVKAAKAAGIYELAsglfngfdtmiGESEQSLSGGQAQR 478
Cdd:PRK09452 84 ENRHVNTVFQSYALFpHMTVFENVAFglrmqKTPAAEiTPRVMEALRMVQLEEFA-----------QRKPHQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 479 IALARAFLASDRhILLFDEPTAHLDiqteYDLKQTM---LPLLENHL--VF-FATH-RLHWLKQMDYVLVMDNGHIIEQG 551
Cdd:PRK09452 153 VAIARAVVNKPK-VLLLDESLSALD----YKLRKQMqneLKALQRKLgiTFvFVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
....*...
gi 488907140 552 RPRELLED 559
Cdd:PRK09452 228 TPREIYEE 235
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
351-564 |
5.37e-15 |
|
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: 75.66 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDIsinrnkflnfqntSWQKQIIYIPQKPYIFHTSLRENIA 429
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEPSEGKI-------------KHSGRISFSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 430 F---YQPDAPKeQVVKAAKaagIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQT 506
Cdd:cd03291 120 FgvsYDEYRYK-SVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARA-VYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488907140 507 EYDLKQTML-PLLENHLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRELLE---DFDGKL 564
Cdd:cd03291 195 EKEIFESCVcKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSlrpDFSSKL 256
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
337-561 |
5.68e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 75.54 E-value: 5.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 337 NFSFQYPDGQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRnkfLNFQNTSWQKQIIYIPQ 415
Cdd:PRK13643 8 NYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGlLQPTEGKVTVGD---IVVSSTSKQKEIKPVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 416 K---------PYIFHTSLRENIAFyqpdAPKEQVVKAAKAAGIyeLASGLfngfdTMIGESEQ-------SLSGGQAQRI 479
Cdd:PRK13643 85 KvgvvfqfpeSQLFEETVLKDVAF----GPQNFGIPKEKAEKI--AAEKL-----EMVGLADEfwekspfELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 480 ALArAFLASDRHILLFDEPTAHLDIQTEYDlkqtMLPLLEN-----HLVFFATHRLHWLKQ-MDYVLVMDNGHIIEQGRP 553
Cdd:PRK13643 154 AIA-GILAMEPEVLVLDEPTAGLDPKARIE----MMQLFESihqsgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
....*...
gi 488907140 554 RELLEDFD 561
Cdd:PRK13643 229 SDVFQEVD 236
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
365-557 |
7.72e-15 |
|
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: 74.47 E-value: 7.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 365 AVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFLNFQNTSWQKQIIYIPQK-PYIFHTSLRENIAF----------YQ 432
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGaLRPDAGTVDLAGVDLHGLSRRARARRVALVEQDsDTAVPLTVRDVVALgriphrslwaGD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 433 PDAPKEQVVKAAKAAGIYELASglfngfdtmigESEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQ 512
Cdd:TIGR03873 111 SPHDAAVVDRALARTELSHLAD-----------RDMSTLSGGERQRVHVARA-LAQEPKLLLLDEPTNHLDVRAQLETLA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488907140 513 TMLPLLENHL-VFFATHRL-HWLKQMDYVLVMDNGHIIEQGRPRELL 557
Cdd:TIGR03873 179 LVRELAATGVtVVAALHDLnLAASYCDHVVVLDGGRVVAAGPPREVL 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
331-549 |
1.15e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 331 TVLSVHNFSFQYPDgqqPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINrnkflnfQNTswqkQ 409
Cdd:COG0488 314 KVLELEGLSKSYGD---KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGeLEPDSGTVKLG-------ETV----K 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 410 IIYIPQKPYIFHT--SLRENIAFYQPDAPKEQVVKAakaagiyeLASGLFNGFD--TMIGeseqSLSGGQAQRIALARAF 485
Cdd:COG0488 380 IGYFDQHQEELDPdkTVLDELRDGAPGGTEQEVRGY--------LGRFLFSGDDafKPVG----VLSGGEKARLALAKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488907140 486 LaSDRHILLFDEPTAHLDIQTeydlkqtmLPLLENHL------VFFATHRLHWLKQM-DYVLVMDNGHIIE 549
Cdd:COG0488 448 L-SPPNVLLLDEPTNHLDIET--------LEALEEALddfpgtVLLVSHDRYFLDRVaTRILEFEDGGVRE 509
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-536 |
1.29e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.92 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 324 VPAIdsetvlSVHNFSFQYpDGQQpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGRGDISIN-RNKFLNfQ 402
Cdd:PRK14258 5 IPAI------KVNNLSFYY-DTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEgRVEFFN-Q 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 403 N--------TSWQKQIIYIPQKPYIFHTSLRENIAF------YQPDAPKEQVVKAA-KAAGiyelasgLFNGFDTMIGES 467
Cdd:PRK14258 75 NiyerrvnlNRLRRQVSMVHPKPNLFPMSVYDNVAYgvkivgWRPKLEIDDIVESAlKDAD-------LWDEIKHKIHKS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488907140 468 EQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTM--LPLLENHLVFFATHRLHWLKQM 536
Cdd:PRK14258 148 ALDLSGGQQQRLCIARA-LAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRL 217
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
333-528 |
2.09e-14 |
|
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: 70.56 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKflnfqntswqkQII 411
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGeLEPDEGIVTWGSTV-----------KIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 412 YIPQkpyifhtslreniafyqpdapkeqvvkaakaagiyelasglfngfdtmigeseqsLSGGQAQRIALARAFLaSDRH 491
Cdd:cd03221 67 YFEQ-------------------------------------------------------LSGGEKMRLALAKLLL-ENPN 90
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488907140 492 ILLFDEPTAHLDIQTeydlkqtmLPLLENHL------VFFATH 528
Cdd:cd03221 91 LLLLDEPTNHLDLES--------IEALEEALkeypgtVILVSH 125
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
364-528 |
2.42e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.01 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 364 VAVVGLSGSGKTTLLSSLAGI-NSGRGDISINrNKFLNFQNTSWQKQIIYIPQKPYIFHT-SLRENIAFYQPDAPKEQ-- 439
Cdd:TIGR01189 29 LQVTGPNGIGKTTLLRILAGLlRPDSGEVRWN-GTPLAEQRDEPHENILYLGHLPGLKPElSALENLHFWAAIHGGAQrt 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 440 VVKAAKAAGIYELASGLFNgfdtmigeseqSLSGGQAQRIALARAFLaSDRHILLFDEPTAHLDIQTeydlkQTMLP-LL 518
Cdd:TIGR01189 108 IEDALAAVGLTGFEDLPAA-----------QLSAGQQRRLALARLWL-SRRPLWILDEPTTALDKAG-----VALLAgLL 170
|
170
....*....|....*
gi 488907140 519 ENHL-----VFFATH 528
Cdd:TIGR01189 171 RAHLarggiVLLTTH 185
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
20-292 |
2.71e-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: 73.61 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 20 VLLTFLQAVSILFQAFFLSKSIVILWHQSAFSSAVPYIFGFAISLLCRHFFSLIKEGSANSFSVTASEGLRDQLLGKYLS 99
Cdd:cd18552 5 ILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 100 FGDQTIFKTGTGHAVSLLHAGIDNVQNYFQLIFIKIID--LSIIpwLLLIYMFFLRWQEALFLLLIFPVIIFFFVILGLA 177
Cdd:cd18552 85 LPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRdpLTVI--GLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 178 AQKRADNEYRNFTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAV 257
Cdd:cd18552 163 LRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVLW 242
|
250 260 270
....*....|....*....|....*....|....*...
gi 488907140 258 FLGFSLMEGKMS---LFPALTLLVLAPEyflPLRTFSE 292
Cdd:cd18552 243 YGGYQVISGELTpgeFISFITALLLLYQ---PIKRLSN 277
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
351-554 |
2.86e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.79 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGIN--------SGRGDISINRNKF-LNFQNTS---WQKQIiyipqkpy 418
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLEtpsagellAGTAPLAEAREDTrLMFQDARllpWKKVI-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 419 ifhtslrENIAFYQPDAPKEQVVKAAKAAGIYELAsglfngfdtmiGESEQSLSGGQAQRIALARAFLASDRhILLFDEP 498
Cdd:PRK11247 100 -------DNVGLGLKGQWRDAALQALAAVGLADRA-----------NEWPAALSGGQKQRVALARALIHRPG-LLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488907140 499 TAHLDIQTEYDLKQTMLPLLENH--LVFFATHRLHWLKQM-DYVLVMDNGHI-----IEQGRPR 554
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAMaDRVLLIEEGKIgldltVDLPRPR 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
363-557 |
3.54e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 72.31 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 363 KVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNkflNFQNTSWQKQIIYIP-QKPYIF-HTSLRENIAF-YQP----- 433
Cdd:PRK10771 27 RVAILGPSGAGKSTLLNLIAGfLTPASGSLTLNGQ---DHTTTPPSRRPVSMLfQENNLFsHLTVAQNIGLgLNPglkln 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 434 DAPKEQVVKAAKAAGIYELASGLfngfdtmigesEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQteydLKQT 513
Cdd:PRK10771 104 AAQREKLHAIARQMGIEDLLARL-----------PGQLSGGQRQRVALARC-LVREQPILLLDEPFSALDPA----LRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488907140 514 MLPLL-----ENHL-VFFATHRLH-WLKQMDYVLVMDNGHIIEQGRPRELL 557
Cdd:PRK10771 168 MLTLVsqvcqERQLtLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
330-559 |
5.33e-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: 71.55 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 330 ETVLSVHNFSFQYPDGQqpaALKDINFLV-RGFAkVAVVGLSGSGKTTLLSSLAGINSGR-GDISinrnkflnFQNTSWQ 407
Cdd:COG0410 1 MPMLEVENLHAGYGGIH---VLHGVSLEVeEGEI-VALLGRNGAGKTTLLKAISGLLPPRsGSIR--------FDGEDIT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 408 KQ---------IIYIPQKPYIFHT-SLRENI---AFYQPDAPKeqvVKAAKAAgIYELasglfngF---DTMIGESEQSL 471
Cdd:COG0410 69 GLpphriarlgIGYVPEGRRIFPSlTVEENLllgAYARRDRAE---VRADLER-VYEL-------FprlKERRRQRAGTL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 472 SGGQAQRIALARAfLASDRHILLFDEPTAHL-------------DIQTEydlKQTMLpLLENHlVFFAthrlhwLKQMDY 538
Cdd:COG0410 138 SGGEQQMLAIGRA-LMSRPKLLLLDEPSLGLapliveeifeiirRLNRE---GVTIL-LVEQN-ARFA------LEIADR 205
|
250 260
....*....|....*....|.
gi 488907140 539 VLVMDNGHIIEQGRPRELLED 559
Cdd:COG0410 206 AYVLERGRIVLEGTAAELLAD 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
328-559 |
5.40e-14 |
|
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: 74.72 E-value: 5.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 328 DSETVLSVHNFS--FQYPDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKT-TLLSSL----AGINSGRGDISINRNKFLN 400
Cdd:COG4172 2 MSMPLLSVEDLSvaFGQGGGTVEA-VKGVSFDIAAGETLALVGESGSGKSvTALSILrllpDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 401 FQNTSWQK----QIIYIPQKPYifhTSL----------RENIAFYQ---PDAPKEQVVKAAKAAGIYELASglfngfdtM 463
Cdd:COG4172 81 LSERELRRirgnRIAMIFQEPM---TSLnplhtigkqiAEVLRLHRglsGAAARARALELLERVGIPDPER--------R 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 464 IGESEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLD--IQTEY-----DLKQTM-LPLLenhlvfFATHRLHWLKQ 535
Cdd:COG4172 150 LDAYPHQLSGGQRQRVMIAMA-LANEPDLLIADEPTTALDvtVQAQIldllkDLQRELgMALL------LITHDLGVVRR 222
|
250 260
....*....|....*....|....*
gi 488907140 536 M-DYVLVMDNGHIIEQGRPRELLED 559
Cdd:COG4172 223 FaDRVAVMRQGEIVEQGPTAELFAA 247
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
350-559 |
5.44e-14 |
|
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: 71.70 E-value: 5.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 350 ALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGR----G-DIS-----------INRnkflNFQNTSwqkqi 410
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFlrpTSGSvlfdGeDITglppheiarlgIGR----TFQIPR----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 411 iyipqkpyIFHT-SLRENI----------AFYQPDAPKEQVVKAAKAAGIYELAsGLFNGFDTMIGEseqsLSGGQAQRI 479
Cdd:cd03219 86 --------LFPElTVLENVmvaaqartgsGLLLARARREEREARERAEELLERV-GLADLADRPAGE----LSYGQQRRL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 480 ALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHL-VFFATHRLHWLKQM-DYVLVMDNGHIIEQGRPRELL 557
Cdd:cd03219 153 EIARA-LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGItVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVR 231
|
..
gi 488907140 558 ED 559
Cdd:cd03219 232 NN 233
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
329-558 |
8.26e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 71.74 E-value: 8.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 329 SETVLSVHNFSFQYPDGQ--QPAALkdiNFLVrgfAKV-AVVGLSGSGKTTLLSSLaginsGR------GDISINRNKFL 399
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRTllHPLSL---TFPA---GKVtGLIGHNGSGKSTLLKML-----GRhqppseGEILLDAQPLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 400 NFQNTSWQKQIIYIPQK-PYIFHTSLRENIA------------FYQPDapKEQVVKAAKAAGIYELASGLFNgfdtmige 466
Cdd:PRK10575 77 SWSSKAFARKVAYLPQQlPAAEGMTVRELVAigrypwhgalgrFGAAD--REKVEEAISLVGLKPLAHRLVD-------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 467 seqSLSGGQAQRIALArAFLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENH-LVFFAThrLHWL----KQMDYVLV 541
Cdd:PRK10575 147 ---SLSGGERQRAWIA-MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERgLTVIAV--LHDInmaaRYCDYLVA 220
|
250
....*....|....*..
gi 488907140 542 MDNGHIIEQGRPRELLE 558
Cdd:PRK10575 221 LRGGEMIAQGTPAELMR 237
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
341-506 |
9.03e-14 |
|
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: 70.51 E-value: 9.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 341 QYPDGQqpAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISINRNKFLNFQntswQKQIIYIPQK--- 416
Cdd:cd03292 9 TYPNGT--AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTIRVNGQDVSDLR----GRAIPYLRRKigv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 417 -----PYIFHTSLRENIAFYQP--DAPKEQVVKAAKAAgiYELAsGLFNGFDTMIGEseqsLSGGQAQRIALARAfLASD 489
Cdd:cd03292 83 vfqdfRLLPDRNVYENVAFALEvtGVPPREIRKRVPAA--LELV-GLSHKHRALPAE----LSGGEQQRVAIARA-IVNS 154
|
170
....*....|....*..
gi 488907140 490 RHILLFDEPTAHLDIQT 506
Cdd:cd03292 155 PTILIADEPTGNLDPDT 171
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
332-550 |
9.78e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.00 E-value: 9.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPDGQ-QPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGRGDISINRNKFLNFQNTSWQ--- 407
Cdd:PRK11629 5 LLQCDNLCKRYQEGSvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKael 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 408 --KQIIYIpqkpYIFH------TSLrENIAF------YQPDAPKEQVVKAAKAAGIYELASglfngfdtmigESEQSLSG 473
Cdd:PRK11629 85 rnQKLGFI----YQFHhllpdfTAL-ENVAMplligkKKPAEINSRALEMLAAVGLEHRAN-----------HRPSELSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488907140 474 GQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFF--ATHRLHWLKQMDYVLVMDNGHIIEQ 550
Cdd:PRK11629 149 GERQRVAIARA-LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFlvVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
330-556 |
1.62e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 71.30 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 330 ETVLSVHNFSFQYPDGQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI-NSGRGDISINRNKfLNFQNTsWQK 408
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLlEAESGQIIIDGDL-LTEENV-WDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 409 --QIIYIPQKP--YIFHTSLRENIAF------YQPDAPKEQVVKAAKAAGIYELAsglfngfdtmigESEQS-LSGGQAQ 477
Cdd:PRK13650 80 rhKIGMVFQNPdnQFVGATVEDDVAFglenkgIPHEEMKERVNEALELVGMQDFK------------EREPArLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 478 RIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENH--LVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRE 555
Cdd:PRK13650 148 RVAIAGA-VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRE 226
|
.
gi 488907140 556 L 556
Cdd:PRK13650 227 L 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
333-559 |
1.63e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 71.66 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHnfsFQYPDG-----QQPAALK---DINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFLNFQN 403
Cdd:PRK15079 14 LKVH---FDIKDGkqwfwQPPKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGlVKATDGEVAWLGKDLLGMKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 404 TSW---QKQIIYIPQKPYifhTSL--RENIA--------FYQPDAPKEQVVKAAKAAgiyELASGLFngfDTMIGESEQS 470
Cdd:PRK15079 91 DEWravRSDIQMIFQDPL---ASLnpRMTIGeiiaeplrTYHPKLSRQEVKDRVKAM---MLKVGLL---PNLINRYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 471 LSGGQAQRIALARAFLASDRHILLfDEPTAHLD--IQTE-YDLKQTMLPLLENHLVFFAtHRLHWLKQM-DYVLVMDNGH 546
Cdd:PRK15079 162 FSGGQCQRIGIARALILEPKLIIC-DEPVSALDvsIQAQvVNLLQQLQREMGLSLIFIA-HDLAVVKHIsDRVLVMYLGH 239
|
250
....*....|...
gi 488907140 547 IIEQGRPRELLED 559
Cdd:PRK15079 240 AVELGTYDEVYHN 252
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
364-551 |
2.14e-13 |
|
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: 69.44 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 364 VAVVGLSGSGKTTLLSSLAGINSGR-GDISINRNKFlNFQNTSwQKQIIYIPQKPYIF-HTSLRENIAF-----YQPDAP 436
Cdd:cd03298 27 TAIVGPSGSGKSTLLNLIAGFETPQsGRVLINGVDV-TAAPPA-DRPVSMLFQENNLFaHLTVEQNVGLglspgLKLTAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 437 KEQVVKAAKA-AGIYELASGLfngfdtmigesEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQteydLKQTML 515
Cdd:cd03298 105 DRQAIEVALArVGLAGLEKRL-----------PGELSGGERQRVALARV-LVRDKPVLLLDEPFAALDPA----LRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488907140 516 PL-LENH-----LVFFATHRLHWLKQM-DYVLVMDNGHIIEQG 551
Cdd:cd03298 169 DLvLDLHaetkmTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
350-559 |
2.24e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.27 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 350 ALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGRGDISINRNKFLNFQNTSWQKQIIYIPQKPY-------- 418
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKTRfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 419 ----------------IFHTSLRENIAF--YQPDAPKEQVVKaaKAAGIYELAsGLFNGFdtmIGESEQSLSGGQAQRIA 480
Cdd:PRK13651 102 eirrrvgvvfqfaeyqLFEQTIEKDIIFgpVSMGVSKEEAKK--RAAKYIELV-GLDESY---LQRSPFELSGGQKRRVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 481 LArAFLASDRHILLFDEPTAHLDIQTEYDlkqtMLPLLEN-----HLVFFATHRL-HWLKQMDYVLVMDNGHIIEQGRPR 554
Cdd:PRK13651 176 LA-GILAMEPDFLVFDEPTAGLDPQGVKE----ILEIFDNlnkqgKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGDTY 250
|
....*
gi 488907140 555 ELLED 559
Cdd:PRK13651 251 DILSD 255
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
365-552 |
3.40e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.06 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 365 AVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFLNFQNTSW----QKQIIYIPQKPYIF-HTSLRENIAFYQPDAPKE 438
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGlTRPQKGRIVLNGRVLFDAEKGIClppeKRRIGYVFQDARLFpHYKVRGNLRYGMAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 439 QVVKAAKAAGIYELASGLfngfdtmigesEQSLSGGQAQRIALARAFLaSDRHILLFDEPTAHLDIQTeydlKQTMLPLL 518
Cdd:PRK11144 108 QFDKIVALLGIEPLLDRY-----------PGSLSGGEKQRVAIGRALL-TAPELLLMDEPLASLDLPR----KRELLPYL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488907140 519 E------NHLVFFATHRLHWLKQM-DYVLVMDNGHIIEQGR 552
Cdd:PRK11144 172 ErlareiNIPILYVSHSLDEILRLaDRVVVLEQGKVKAFGP 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
337-573 |
3.75e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.19 E-value: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 337 NFSFQYPDGQ--QPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRnkfLNFQNTSWQKQIIYI 413
Cdd:PRK13646 7 NVSYTYQKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAlLKPTTGTVTVDD---ITITHKTKDKYIRPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 414 PQK---------PYIFHTSLRENIAFyqpdAPK------EQVVKAAkaagiYELASGLfnGFD-TMIGESEQSLSGGQAQ 477
Cdd:PRK13646 84 RKRigmvfqfpeSQLFEDTVEREIIF----GPKnfkmnlDEVKNYA-----HRLLMDL--GFSrDVMSQSPFQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 478 RIALArAFLASDRHILLFDEPTAHLDIQTEYdlkQTM-----LPLLENHLVFFATHRLHWL-KQMDYVLVMDNGHIIEQG 551
Cdd:PRK13646 153 KIAIV-SILAMNPDIIVLDEPTAGLDPQSKR---QVMrllksLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQT 228
|
250 260
....*....|....*....|..
gi 488907140 552 RPRELLEDfDGKLNELRKELTD 573
Cdd:PRK13646 229 SPKELFKD-KKKLADWHIGLPE 249
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
329-551 |
3.88e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.91 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 329 SETVLSVHNFSFQYPDGQqpAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISI---NRNKFLNfqnt 404
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGH--TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGfVRLASGKISIlgqPTRQALQ---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 405 swQKQIIYIPQKPYIFHT--SLRENIAFY----------QPDAPKEQVVKAAKA-AGIYELASglfngfdTMIGEseqsL 471
Cdd:PRK15056 77 --KNLVAYVPQSEEVDWSfpVLVEDVVMMgryghmgwlrRAKKRDRQIVTAALArVDMVEFRH-------RQIGE----L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 472 SGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLL-ENHLVFFATHRLHWLKQM-DYVlVMDNGHIIE 549
Cdd:PRK15056 144 SGGQKKRVFLARA-IAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFcDYT-VMVKGTVLA 221
|
..
gi 488907140 550 QG 551
Cdd:PRK15056 222 SG 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
335-566 |
4.30e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 69.69 E-value: 4.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 335 VHNFSFQYPDGQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINrNKFLNFQNTSWQ------ 407
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlIEIYDSKIKVD-GKVLYFGKDIFQidaikl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 408 -KQIIYIPQKPYIF-HTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAf 485
Cdd:PRK14246 89 rKEVGMVFQQPNPFpHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARA- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 486 LASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQM-DYVLVMDNGHIIEQGRPRELLEDFDGKL 564
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIFTSPKNEL 247
|
..
gi 488907140 565 NE 566
Cdd:PRK14246 248 TE 249
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
362-557 |
4.82e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.74 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 362 AKVAVVGLSGSGKTTLLSSLAGIN---SG---RGDISINRNKFLNFQNT-SWQKQIIYIPQKPYIFHTSLRENI---AFY 431
Cdd:PRK14271 48 AVTSLMGPTGSGKTTFLRTLNRMNdkvSGyrySGDVLLGGRSIFNYRDVlEFRRRVGMLFQRPNPFPMSIMDNVlagVRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 432 QPDAPKEQVVKAAKAAgIYELasGLFNGFDTMIGESEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLK 511
Cdd:PRK14271 128 HKLVPRKEFRGVAQAR-LTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLART-LAVNPEVLLLDEPTSALDPTTTEKIE 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488907140 512 QTMLPLLENHLVFFATHRLHWLKQM-DYVLVMDNGHIIEQGRPRELL 557
Cdd:PRK14271 204 EFIRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLF 250
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
331-566 |
5.20e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 69.17 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 331 TVLSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI------NSGRGDISINRNKFLNFQNT 404
Cdd:PRK14247 2 NKIEIRDLKVSFGQVE---VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypeARVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 405 SWQKQIIYIPQKPY-IFHTSLRENIAFyqpdAPK------------EQVVKAAKAAGIYELASglfNGFDTMIGeseqSL 471
Cdd:PRK14247 79 ELRRRVQMVFQIPNpIPNLSIFENVAL----GLKlnrlvkskkelqERVRWALEKAQLWDEVK---DRLDAPAG----KL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 472 SGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRLHWLKQM-DYVLVMDNGHIIEQ 550
Cdd:PRK14247 148 SGGQQQRLCIARA-LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEW 226
|
250
....*....|....*.
gi 488907140 551 GRPRELLEDFDGKLNE 566
Cdd:PRK14247 227 GPTREVFTNPRHELTE 242
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
358-561 |
5.35e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.62 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 358 VRGFAK----VAVVGLSGSGKTTLLSSLAGINS----GRGDISINRNKFlnfqnTSWQKQII--YIPQKP-YIFHTSLRE 426
Cdd:TIGR00955 44 VSGVAKpgelLAVMGSSGAGKTTLMNALAFRSPkgvkGSGSVLLNGMPI-----DAKEMRAIsaYVQQDDlFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 427 NIAFYQPDAPKEQVVKAAKAAGIYEL--ASGLFNGFDTMIGESEQ--SLSGGQAQRIALARAFLaSDRHILLFDEPTAHL 502
Cdd:TIGR00955 119 HLMFQAHLRMPRRVTKKEKRERVDEVlqALGLRKCANTRIGVPGRvkGLSGGERKRLAFASELL-TDPPLLFCDEPTSGL 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488907140 503 DIQTEYDLKQTMLPLLEN-HLVFFATHR--LHWLKQMDYVLVMDNGHIIEQGRPRELLEDFD 561
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQKgKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQAVPFFS 259
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
329-548 |
7.01e-13 |
|
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: 71.12 E-value: 7.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 329 SETVLSVHNFSFQYPDGQQpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSgrgdisinrnkflNFQNTSWQK 408
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPPKKE--ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK-------------DFNGEARPQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 409 QII---YIPQKPYIFHT-SLRENI-------------------AFYQPDAPKEQVV-KAAK------AAGIYELASGLFN 458
Cdd:TIGR03719 66 PGIkvgYLPQEPQLDPTkTVRENVeegvaeikdaldrfneisaKYAEPDADFDKLAaEQAElqeiidAADAWDLDSQLEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 459 GFDTM---IGESE-QSLSGGQAQRIALARaFLASDRHILLFDEPTAHLDIQTeydlkqtmLPLLENHL------VFFATH 528
Cdd:TIGR03719 146 AMDALrcpPWDADvTKLSGGERRRVALCR-LLLSKPDMLLLDEPTNHLDAES--------VAWLERHLqeypgtVVAVTH 216
|
250 260
....*....|....*....|.
gi 488907140 529 RLHWLKQM-DYVLVMDNGHII 548
Cdd:TIGR03719 217 DRYFLDNVaGWILELDRGRGI 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
332-558 |
7.21e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 70.25 E-value: 7.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYpDGQqpAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDIsinrnkFLNFQNTS----W 406
Cdd:PRK11607 19 LLEIRNLTKSF-DGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQpTAGQI------MLDGVDLShvppY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 407 QKQIIYIPQKPYIF-HTSLRENIAF--YQPDAPKEQVvkAAKAAGIYELASglfngFDTMIGESEQSLSGGQAQRIALAR 483
Cdd:PRK11607 90 QRPINMMFQSYALFpHMTVEQNIAFglKQDKLPKAEI--ASRVNEMLGLVH-----MQEFAKRKPHQLSGGQRQRVALAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488907140 484 AfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLV--FFATHRLHWLKQM-DYVLVMDNGHIIEQGRPRELLE 558
Cdd:PRK11607 163 S-LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVtcVMVTHDQEEAMTMaGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
330-557 |
7.31e-13 |
|
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: 68.57 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 330 ETVLSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGIN---SG---------RGDISInrnk 397
Cdd:COG1119 1 DPLLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptYGndvrlfgerRGGEDV---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 398 flnfqntsWQ--KQIIYI-P--QKPYIFHTSLRENI--AFY-------QPDApkEQVVKAA---KAAGIYELASGLFngf 460
Cdd:COG1119 74 --------WElrKRIGLVsPalQLRFPRDETVLDVVlsGFFdsiglyrEPTD--EQRERARellELLGLAHLADRPF--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 461 dtmigeseQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLEN---HLVfFATHRLH-WLKQM 536
Cdd:COG1119 141 --------GTLSQGEQRRVLIARA-LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgapTLV-LVTHHVEeIPPGI 210
|
250 260
....*....|....*....|.
gi 488907140 537 DYVLVMDNGHIIEQGRPRELL 557
Cdd:COG1119 211 THVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
351-528 |
7.80e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.59 E-value: 7.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNkflNFQNTSWQKQIIYI----PQKPyifHTSLR 425
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGlLPPAAGTIKLDGG---DIDDPDVAEACHYLghrnAMKP---ALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 426 ENIAFYQP--DAPKEQVVKAAKAAGIYELASGLFNgfdtmigeseqSLSGGQAQRIALARaFLASDRHILLFDEPTAHLD 503
Cdd:PRK13539 92 ENLEFWAAflGGEELDIAAALEAVGLAPLAHLPFG-----------YLSAGQKRRVALAR-LLVSNRPIWILDEPTAALD 159
|
170 180 190
....*....|....*....|....*....|.
gi 488907140 504 IQTeydlkQTMLP-LLENHL-----VFFATH 528
Cdd:PRK13539 160 AAA-----VALFAeLIRAHLaqggiVIAATH 185
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
337-559 |
8.35e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 69.27 E-value: 8.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 337 NFSFQYPDgQQPAALKDINFLVRGFAK---VAVVGLSGSGKTTLLSSLAGI---NSGR---GDISINRNKFLNFQNTSWQ 407
Cdd:PRK13645 11 NVSYTYAK-KTPFEFKALNNTSLTFKKnkvTCVIGTTGSGKSTMIQLTNGLiisETGQtivGDYAIPANLKKIKEVKRLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 408 KQIIYIPQKP--YIFHTSLRENIAF--YQPDAPKEQVVKAakaagIYELASgLFNGFDTMIGESEQSLSGGQAQRIALAr 483
Cdd:PRK13645 90 KEIGLVFQFPeyQLFQETIEKDIAFgpVNLGENKQEAYKK-----VPELLK-LVQLPEDYVKRSPFELSGGQKRRVALA- 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488907140 484 AFLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENH--LVFFATHRL-HWLKQMDYVLVMDNGHIIEQGRPRELLED 559
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYkkRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
351-566 |
9.72e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.33 E-value: 9.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLLSS---LAGINSG---RGDISI-NRNKFL-NFQNTSWQKQIIYIPQKPYIF-H 421
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEarvEGEVRLfGRNIYSpDVDPIEVRREVGMVFQYPNPFpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 422 TSLRENIA-------FYQPDAPKEQVVK-AAKAAGIYELASGLFNGFDTmigeseqSLSGGQAQRIALARAfLASDRHIL 493
Cdd:PRK14267 100 LTIYDNVAigvklngLVKSKKELDERVEwALKKAALWDEVKDRLNDYPS-------NLSGGQRQRLVIARA-LAMKPKIL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488907140 494 LFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHR-LHWLKQMDYVLVMDNGHIIEQGRPRELLEDFDGKLNE 566
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTE 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
317-552 |
1.02e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.50 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 317 SEISALKVP-AIDSETVLSVHNFSFQYPDGQ--------QPAALKDINFLVRGFAKVAVVGLSGSGK-TTLLSSLAGINS 386
Cdd:PRK15134 259 SEPSGDPVPlPEPASPLLDVEQLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKsTTGLALLRLINS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 387 gRGDI--------SINRNKFLNFQNtswQKQIIYipQKPYifhTSLR----------ENIAFYQPD---APKEQVVKAAk 445
Cdd:PRK15134 339 -QGEIwfdgqplhNLNRRQLLPVRH---RIQVVF--QDPN---SSLNprlnvlqiieEGLRVHQPTlsaAQREQQVIAV- 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 446 aagIYELasglfnGFDTmigESEQ----SLSGGQAQRIALARAFLASDRHILLfDEPTAHLDIQTEYDLKQTMLPLLENH 521
Cdd:PRK15134 409 ---MEEV------GLDP---ETRHrypaEFSGGQRQRIAIARALILKPSLIIL-DEPTSSLDKTVQAQILALLKSLQQKH 475
|
250 260 270
....*....|....*....|....*....|....
gi 488907140 522 LV--FFATHRLHWLKQMDY-VLVMDNGHIIEQGR 552
Cdd:PRK15134 476 QLayLFISHDLHVVRALCHqVIVLRQGEVVEQGD 509
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
333-561 |
1.06e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 68.62 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQ--QPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGIN---SGR---GDISINrnkflnfqNT 404
Cdd:PRK13649 3 INLQNVSYTYQAGTpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHvptQGSvrvDDTLIT--------ST 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 405 SWQKQIIYIPQK---------PYIFHTSLRENIAFyqpdAPKEQVVKAAKAAGIYELASGLFNGFDTMIGESEQSLSGGQ 475
Cdd:PRK13649 75 SKNKDIKQIRKKvglvfqfpeSQLFEETVLKDVAF----GPQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 476 AQRIALArAFLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHL-VFFATHRLHWLKQM-DYVLVMDNGHIIEQGRP 553
Cdd:PRK13649 151 MRRVAIA-GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMtIVLVTHLMDDVANYaDFVYVLEKGKLVLSGKP 229
|
....*...
gi 488907140 554 RELLEDFD 561
Cdd:PRK13649 230 KDIFQDVD 237
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
329-530 |
1.07e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 68.27 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 329 SETVLSVHNFSFQYPDGqqpAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG----INSGRGDISIN-RNKFLNFQN 403
Cdd:PRK14243 7 TETVLRTENLNVYYGSF---LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndlIPGFRVEGKVTfHGKNLYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 404 ---TSWQKQIIYIPQKPYIFHTSLRENIAF------YQPDApKEQVVKAAKAAGiyelasgLFNGFDTMIGESEQSLSGG 474
Cdd:PRK14243 84 vdpVEVRRRIGMVFQKPNPFPKSIYDNIAYgaringYKGDM-DELVERSLRQAA-------LWDEVKDKLKQSGLSLSGG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488907140 475 QAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFATHRL 530
Cdd:PRK14243 156 QQQRLCIARA-IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
332-557 |
1.40e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.11 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGRGDISINRNKFLNFQNT---SWQK 408
Cdd:PRK13638 1 MLATSDLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllALRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 409 QIIYIPQKP--YIFHTSLRENIAFYQPD--APKEQVVKAAKAAGIYELASGLFNgfdtmigESEQSLSGGQAQRIALARA 484
Cdd:PRK13638 78 QVATVFQDPeqQIFYTDIDSDIAFSLRNlgVPEAEITRRVDEALTLVDAQHFRH-------QPIQCLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 485 FLASDRHILLfDEPTAHLDIQTeydlKQTMLPLLE------NHLVfFATHRLHWLKQM-DYVLVMDNGHIIEQGRPRELL 557
Cdd:PRK13638 151 LVLQARYLLL-DEPTAGLDPAG----RTQMIAIIRrivaqgNHVI-ISSHDIDLIYEIsDAVYVLRQGQILTHGAPGEVF 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
341-558 |
1.47e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.10 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 341 QYPDGQQpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG---INSGrgDISI-----------NRNKFLNFQNTSw 406
Cdd:PRK11650 12 SYDGKTQ--VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGlerITSG--EIWIggrvvnelepaDRDIAMVFQNYA- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 407 qkqiIYipqkPyifHTSLRENIAFYQPDA--PKEQV-VKAAKAAGIYELasglfngfDTMIGESEQSLSGGQAQRIALAR 483
Cdd:PRK11650 87 ----LY----P---HMSVRENMAYGLKIRgmPKAEIeERVAEAARILEL--------EPLLDRKPRELSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 484 AFLasdRH--ILLFDEPTAHLD----------IQT-EYDLKQTMLpllenhlvfFATHrlhwlKQM------DYVLVMDN 544
Cdd:PRK11650 148 AIV---REpaVFLFDEPLSNLDaklrvqmrleIQRlHRRLKTTSL---------YVTH-----DQVeamtlaDRVVVMNG 210
|
250
....*....|....*
gi 488907140 545 GHiIEQ-GRPRELLE 558
Cdd:PRK11650 211 GV-AEQiGTPVEVYE 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
350-551 |
1.73e-12 |
|
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: 66.86 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 350 ALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFLNfqNTSWQKQIIYIPQKPYIF-HTSLREN 427
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGlIKPDSGEITFDGKSYQK--NIEALRRIGALIEAPGFYpNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 428 IAFYQ--PDAPKEQVVKAAKAAGIYELASGLFNGFdtmigeseqSLsgGQAQRIALARAFLaSDRHILLFDEPTAHLDIQ 505
Cdd:cd03268 93 LRLLArlLGIRKKRIDEVLDVVGLKDSAKKKVKGF---------SL--GMKQRLGIALALL-GNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488907140 506 TEYDLKQTMLPLL-ENHLVFFATHRLHWLKQM-DYVLVMDNGHIIEQG 551
Cdd:cd03268 161 GIKELRELILSLRdQGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
327-551 |
2.94e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 327 IDSETVLSVHNFSFQYPDGQQP-AALKDINFLVRGFAKVAVVGLSGSGKT-TLLSSLAGINSGRGDISIN------RNKF 398
Cdd:PRK10261 7 LDARDVLAVENLNIAFMQEQQKiAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGLVQCDkmllrrRSRQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 399 LNFQNTSWQKQ--------IIYIPQKPYifhTSLR----------ENIAFYQPDAPKEQVVKAAKAAGIYELASGlfngf 460
Cdd:PRK10261 87 VIELSEQSAAQmrhvrgadMAMIFQEPM---TSLNpvftvgeqiaESIRLHQGASREEAMVEAKRMLDQVRIPEA----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 461 DTMIGESEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQtMLPLLENHL---VFFATHRLHWLKQM- 536
Cdd:PRK10261 159 QTILSRYPHQLSGGMRQRVMIAMA-LSCRPAVLIADEPTTALDVTIQAQILQ-LIKVLQKEMsmgVIFITHDMGVVAEIa 236
|
250
....*....|....*
gi 488907140 537 DYVLVMDNGHIIEQG 551
Cdd:PRK10261 237 DRVLVMYQGEAVETG 251
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
336-552 |
3.37e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 67.90 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 336 HNFSFQYPDGQQP-AALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGIN---SGR----G-DISINRNKFLnfqnTSW 406
Cdd:PRK11153 5 KNISKVFPQGGRTiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLErptSGRvlvdGqDLTALSEKEL----RKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 407 QKQIIYIPQkpyifHTSL---R---ENIAFyqP----DAPKEQVvkAAKAAGIYELasglfngfdtmIGESEQ------S 470
Cdd:PRK11153 81 RRQIGMIFQ-----HFNLlssRtvfDNVAL--PlelaGTPKAEI--KARVTELLEL-----------VGLSDKadrypaQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 471 LSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTeydlKQTMLPLL-----ENHL-VFFATHRLHWLKQM-DYVLVMD 543
Cdd:PRK11153 141 LSGGQKQRVAIARA-LASNPKVLLCDEATSALDPAT----TRSILELLkdinrELGLtIVLITHEMDVVKRIcDRVAVID 215
|
....*....
gi 488907140 544 NGHIIEQGR 552
Cdd:PRK11153 216 AGRLVEQGT 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
329-557 |
5.28e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.15 E-value: 5.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 329 SETVLSVHNFSFQYpdGQQpAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISINRNKFLNFQNTSWQ 407
Cdd:PRK10619 2 SENKLNVIDLHKRY--GEH-EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKpSEGSIVVNGQTINLVRDKDGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 408 ------KQIIYIPQK-PYIF-------HTSLRENIAfyqpDAP-----------KEQVVKAAKAAGIYELASGLFngfdt 462
Cdd:PRK10619 79 lkvadkNQLRLLRTRlTMVFqhfnlwsHMTVLENVM----EAPiqvlglskqeaRERAVKYLAKVGIDERAQGKY----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 463 migesEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLEN-HLVFFATHRLHWLKQM-DYVL 540
Cdd:PRK10619 150 -----PVHLSGGQQQRVSIARA-LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVsSHVI 223
|
250
....*....|....*..
gi 488907140 541 VMDNGHIIEQGRPRELL 557
Cdd:PRK10619 224 FLHQGKIEEEGAPEQLF 240
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
332-557 |
6.18e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 66.27 E-value: 6.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPDGQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI-NSGRGDISINRNKFLNFQNTSWQKQI 410
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLfEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 411 IYIPQKP--YIFHTSLRENIAFYQPDA--PKEQVVKAAKAAgiyELASGLFNgFDTmigESEQSLSGGQAQRIALArAFL 486
Cdd:PRK13642 84 GMVFQNPdnQFVGATVEDDVAFGMENQgiPREEMIKRVDEA---LLAVNMLD-FKT---REPARLSGGQKQRVAVA-GII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488907140 487 ASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLEN-HLVFFA-THRLHWLKQMDYVLVMDNGHIIEQGRPRELL 557
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSiTHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
349-551 |
6.28e-12 |
|
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: 65.08 E-value: 6.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 349 AALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGRGDIS---INRNKFlnfqntSWQKQIIYIPQKPYIF-H 421
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLlepDAGFATVDgfdVVKEPA------EARRRLGFVSDSTGLYdR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 422 TSLRENIAFY------QPDAPKEQVVKAAKAAGIYELASGLFNGFDTmigeseqslsgGQAQRIALARAfLASDRHILLF 495
Cdd:cd03266 93 LTARENLEYFaglyglKGDELTARLEELADRLGMEELLDRRVGGFST-----------GMRQKVAIARA-LVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488907140 496 DEPTAHLDIQTEYDLKQTMLPLLE-NHLVFFATHRLHWLKQM-DYVLVMDNGHIIEQG 551
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
350-559 |
1.27e-11 |
|
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: 67.13 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 350 ALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGR-----GDISINRNKfLNFQNTSWQKQIIYIPQKPYIFH 421
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVlepTSGEvnvrvGDEWVDMTK-PGPDGRGRAKRYIGILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 422 T------SLRENIAFYQPDapkeqvvKAAKAAGIYELASGlfnGFDTMIGES-----EQSLSGGQAQRIALARAfLASDR 490
Cdd:TIGR03269 378 PhrtvldNLTEAIGLELPD-------ELARMKAVITLKMV---GFDEEKAEEildkyPDELSEGERHRVALAQV-LIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488907140 491 HILLFDEPTAHLDIQTEYDLKQTMLPLLE--NHLVFFATHrlhwlkQMDYVL-------VMDNGHIIEQGRPRELLED 559
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSH------DMDFVLdvcdraaLMRDGKIVKIGDPEEIVEE 518
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
331-549 |
1.35e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.09 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 331 TVLSVHNFSFQYPDG------QQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGR-GDIS--------INR 395
Cdd:PRK10419 2 TLLNVSGLSHHYAHGglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSqGNVSwrgeplakLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 396 NKFLNFQNTSwqkQIIYI-------PQKpyifhtSLRENIAfyQPDAPKEQVVKAAKAAGIYEL--ASGLFngfDTMIGE 466
Cdd:PRK10419 82 AQRKAFRRDI---QMVFQdsisavnPRK------TVREIIR--EPLRHLLSLDKAERLARASEMlrAVDLD---DSVLDK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 467 SEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQteydLKQTMLPLLE------NHLVFFATHRLHWLKQM-DYV 539
Cdd:PRK10419 148 RPPQLSGGQLQRVCLARA-LAVEPKLLILDEAVSNLDLV----LQAGVIRLLKklqqqfGTACLFITHDLRLVERFcQRV 222
|
250
....*....|
gi 488907140 540 LVMDNGHIIE 549
Cdd:PRK10419 223 MVMDNGQIVE 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
350-570 |
1.39e-11 |
|
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: 67.13 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 350 ALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGR---GDI-----------SINRNKFLNFQ----NTSWQKQII 411
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptsGRIiyhvalcekcgYVERPSKVGEPcpvcGGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 412 --YIPQKPYIFHTSLRENI------AFYQPDAPKEQVVKAAKAAGiYELASGLFNGFDTM--------IGESEQSLSGGQ 475
Cdd:TIGR03269 95 dfWNLSDKLRRRIRKRIAImlqrtfALYGDDTVLDNVLEALEEIG-YEGKEAVGRAVDLIemvqlshrITHIARDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 476 AQRIALARAfLASDRHILLFDEPTAHLDIQTEyDLKQTML--PLLENHLVFFATHrlHWLKQM----DYVLVMDNGHIIE 549
Cdd:TIGR03269 174 KQRVVLARQ-LAKEPFLFLADEPTGTLDPQTA-KLVHNALeeAVKASGISMVLTS--HWPEVIedlsDKAIWLENGEIKE 249
|
250 260
....*....|....*....|.
gi 488907140 550 QGRPRELLEDFDGKLNELRKE 570
Cdd:TIGR03269 250 EGTPDEVVAVFMEGVSEVEKE 270
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
365-557 |
2.36e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.62 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 365 AVVGLSGSGKTTLLSSLAGINS-GRGDISINRNKFLNFQNTSWQKQIIYIPQKPYI-FHTSLRENIAF----YQP----- 433
Cdd:PRK10253 37 AIIGPNGCGKSTLLRTLSRLMTpAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQELVARgrypHQPlftrw 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 434 -DAPKEQVVKAAKAAGIYELAsglfngfdtmiGESEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQ 512
Cdd:PRK10253 117 rKEDEEAVTKAMQATGITHLA-----------DQSVDTLSGGQRQRAWIAMV-LAQETAIMLLDEPTTWLDISHQIDLLE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488907140 513 tMLPLLENHLVFFATHRLHWLKQ----MDYVLVMDNGHIIEQGRPRELL 557
Cdd:PRK10253 185 -LLSELNREKGYTLAAVLHDLNQacryASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
329-506 |
2.89e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 63.64 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 329 SETVLSVHNFSFQYPDG-QQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGR-GDISI---NRNKFLNFQN 403
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGeHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSsGEVSLvgqPLHQMDEEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 404 TSWQ-KQIIYIPQKPYIFHT-SLRENIAFyqPDAPKEQVVKAAKAAGIYELAS-GLFNGFDTMIGEseqsLSGGQAQRIA 480
Cdd:PRK10584 83 AKLRaKHVGFVFQSFMLIPTlNALENVEL--PALLRGESSRQSRNGAKALLEQlGLGKRLDHLPAQ----LSGGEQQRVA 156
|
170 180
....*....|....*....|....*..
gi 488907140 481 LARAFlaSDRHILLF-DEPTAHLDIQT 506
Cdd:PRK10584 157 LARAF--NGRPDVLFaDEPTGNLDRQT 181
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
351-503 |
3.48e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.19 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINF-LVRGFAKVaVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFLNFQNTSWQKQIIYIPQKPYIFHTSLRENI 428
Cdd:PRK10247 23 LNNISFsLRAGEFKL-ITGPSGCGKSTLLKIVASlISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 429 AF-YQ--PDAPKEQVVKAakaagiyELASglFNGFDTMIGESEQSLSGGQAQRIALAR--AFLAsdrHILLFDEPTAHLD 503
Cdd:PRK10247 102 IFpWQirNQQPDPAIFLD-------DLER--FALPDTILTKNIAELSGGEKQRISLIRnlQFMP---KVLLLDEITSALD 169
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
331-557 |
4.94e-11 |
|
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: 63.29 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 331 TVLSVHNFSFQYPDG------QQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDIS--------INR 395
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKpAQGTVSfrgqdlyqLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 396 NKFLNFQNTSwqkQIIYI-------PQKpyifhtSLRENIAfyQPDAPKEQVVKAAKAAGIYELASGLfnGFDTMIGES- 467
Cdd:TIGR02769 81 KQRRAFRRDV---QLVFQdspsavnPRM------TVRQIIG--EPLRHLTSLDESEQKARIAELLDMV--GLRSEDADKl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 468 EQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQteydLKQTMLPLLE------NHLVFFATHRLHWLKQM-DYVL 540
Cdd:TIGR02769 148 PRQLSGGQLQRINIARA-LAVKPKLIVLDEAVSNLDMV----LQAVILELLRklqqafGTAYLFITHDLRLVQSFcQRVA 222
|
250
....*....|....*..
gi 488907140 541 VMDNGHIIEQGRPRELL 557
Cdd:TIGR02769 223 VMDKGQIVEECDVAQLL 239
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
364-557 |
8.11e-11 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 62.51 E-value: 8.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 364 VAVVGLSGSGKTTLLSSlagIN----SGRGDISIN-------RNKFLNFQNTSWqKQIIYIPQK-PYIF-------HTSL 424
Cdd:COG4598 37 ISIIGSSGSGKSTFLRC---INlletPDSGEIRVGgeeirlkPDRDGELVPADR-RQLQRIRTRlGMVFqsfnlwsHMTV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 425 RENIAfyqpDAP-------KEQVVKAAKA----AGIYELAsglfngfDTMIGEseqsLSGGQAQRIALARAfLASDRHIL 493
Cdd:COG4598 113 LENVI----EAPvhvlgrpKAEAIERAEAllakVGLADKR-------DAYPAH----LSGGQQQRAAIARA-LAMEPEVM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 494 LFDEPTAHLD----------IQteyDLKQ---TMLpllenhLVffaTHrlhwlkQMDY-------VLVMDNGHIIEQGRP 553
Cdd:COG4598 177 LFDEPTSALDpelvgevlkvMR---DLAEegrTML------VV---TH------EMGFardvsshVVFLHQGRIEEQGPP 238
|
....
gi 488907140 554 RELL 557
Cdd:COG4598 239 AEVF 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
329-559 |
1.05e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.27 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 329 SETVLSVHNFSFQYPdGQQpaALKDINFLVR-GfaKV-AVVGLSGSGKTTLLSSLAGINS-GRGDISINRNKfLNFQNT- 404
Cdd:COG1129 1 AEPLLEMRGISKSFG-GVK--ALDGVSLELRpG--EVhALLGENGAGKSTLMKILSGVYQpDSGEILLDGEP-VRFRSPr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 405 -SWQKQIIYIPQKPYIF-HTSLRENIAFYQPDApKEQVVKAAKaagIYELASGLFNGF------DTMIGEseqsLSGGQA 476
Cdd:COG1129 75 dAQAAGIAIIHQELNLVpNLSVAENIFLGREPR-RGGLIDWRA---MRRRARELLARLgldidpDTPVGD----LSVAQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 477 QRIALARAfLASDRHILLFDEPTAHLDIQ-TEY------DLKQtmlpllENHLVFFATHRLHWLKQM-DYVLVMDNGHII 548
Cdd:COG1129 147 QLVEIARA-LSRDARVLILDEPTASLTEReVERlfriirRLKA------QGVAIIYISHRLDEVFEIaDRVTVLRDGRLV 219
|
250
....*....|.
gi 488907140 549 EQGRPRELLED 559
Cdd:COG1129 220 GTGPVAELTED 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
351-559 |
1.76e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.45 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGRGDISINRNKFLNFQNTSwQKQIIYIPQKPYIFHT-SLRE 426
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvprDAGNIIIDDEDISLLPLHARA-RRGIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 427 NI-AFYQ--PDAPKEQvvKAAKAAGIYEL--ASGLFNGFDtmigeseQSLSGGQAQRIALARAFLASDRHILLfDEPTAH 501
Cdd:PRK10895 98 NLmAVLQirDDLSAEQ--REDRANELMEEfhIEHLRDSMG-------QSLSGGERRRVEIARALAANPKFILL-DEPFAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 502 LDIQTEYDLKQTMLPLLENHL-VFFATHRL-HWLKQMDYVLVMDNGHIIEQGRPRELLED 559
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRDSGLgVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
318-504 |
1.87e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.50 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 318 EISAL--KVPAIDSETVLSVHNFSfqypdgqQPAALKDINFLVR-----GFAkvavvGLSGSGKTTLLSSLAGINSG-RG 389
Cdd:COG1129 240 ELEDLfpKRAAAPGEVVLEVEGLS-------VGGVVRDVSFSVRageilGIA-----GLVGAGRTELARALFGADPAdSG 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 390 DISINrNKFLNFQNTS--WQKQIIYIP----QKPYIFHTSLRENIA-----------FYQPDAPKEQVVKAA-----KAA 447
Cdd:COG1129 308 EIRLD-GKPVRIRSPRdaIRAGIAYVPedrkGEGLVLDLSIRENITlasldrlsrggLLDRRRERALAEEYIkrlriKTP 386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488907140 448 GIYELASglfngfdtmigeseqSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDI 504
Cdd:COG1129 387 SPEQPVG---------------NLSGGNQQKVVLAKW-LATDPKVLILDEPTRGIDV 427
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
332-548 |
1.99e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.05 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFLNFQNTSWQKQI 410
Cdd:PRK11614 5 MLSFDKVSAHYGKIQ---ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGdPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 411 IYI-PQKPYIF-HTSLRENIAFYQPDAPKEQVVKaaKAAGIYELASGLFNGFDTMIGeseqSLSGGQAQRIALARAFLAS 488
Cdd:PRK11614 82 VAIvPEGRRVFsRMTVEENLAMGGFFAERDQFQE--RIKWVYELFPRLHERRIQRAG----TMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488907140 489 DRhILLFDEPT---AHLDIQTEYDlkqTMLPLLENHLVFFATHR--LHWLKQMDYVLVMDNGHII 548
Cdd:PRK11614 156 PR-LLLLDEPSlglAPIIIQQIFD---TIEQLREQGMTIFLVEQnaNQALKLADRGYVLENGHVV 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
329-557 |
2.80e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.80 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 329 SETVLSVHNFSFQYPD-GQQPAALKDINFLVRGFAKVAVVGLSGSGKT-TLLSSLAGINSG-----RGDISINRNKFLNF 401
Cdd:PRK15134 2 TQPLLAIENLSVAFRQqQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvypSGDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 402 QNTSWQK----QIIYIPQKPYI----FHT---SLRENIAFYQ---PDAPKEQVVKAAKAAGIYELASGLfNGFdtmiges 467
Cdd:PRK15134 82 SEQTLRGvrgnKIAMIFQEPMVslnpLHTlekQLYEVLSLHRgmrREAARGEILNCLDRVGIRQAAKRL-TDY------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 468 EQSLSGGQAQRIALARAFLASDRhILLFDEPTAHLDI-------QTEYDLKQTMlplleNHLVFFATHRLHWLKQM-DYV 539
Cdd:PRK15134 154 PHQLSGGERQRVMIAMALLTRPE-LLIADEPTTALDVsvqaqilQLLRELQQEL-----NMGLLFITHNLSIVRKLaDRV 227
|
250
....*....|....*...
gi 488907140 540 LVMDNGHIIEQGRPRELL 557
Cdd:PRK15134 228 AVMQNGRCVEQNRAATLF 245
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
146-270 |
3.06e-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: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 146 LIYMFFLRWQEALFLLLIFPVIIFFFVILglaaQKRADNEYRNF----TVLNNRFADTLRGMQTLKQLGLSRIFTKRIYE 221
Cdd:cd18544 133 LIAMFLLNWRLALISLLVLPLLLLATYLF----RKKSRKAYREVreklSRLNAFLQESISGMSVIQLFNREKREFEEFDE 208
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 488907140 222 TSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVFLGFSLMEGKMSL 270
Cdd:cd18544 209 INQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTL 257
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
350-559 |
3.39e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 62.36 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 350 ALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFLNFQNTSWQ----KQIIYIPQKPYIF-HTS 423
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRlIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMpHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 424 LRENIAF------YQPDAPKEQVVKAAKAAGIYELASGLfngfdtmigesEQSLSGGQAQRIALARAfLASDRHILLFDE 497
Cdd:PRK10070 123 VLDNTAFgmelagINAEERREKALDALRQVGLENYAHSY-----------PDELSGGMRQRVGLARA-LAINPDILLMDE 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488907140 498 PTAHLDIQTEYDLKQTMLPLLENH--LVFFATHRL-HWLKQMDYVLVMDNGHIIEQGRPRELLED 559
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHqrTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
352-556 |
4.22e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 61.58 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 352 KDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG---INSGR---GDISIN------RNKFLNFQNTSwqkqiIYiPqkpyi 419
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGledITSGDlfiGEKRMNdvppaeRGVGMVFQSYA-----LY-P----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 420 fHTSLRENIAF--YQPDAPKEQVVKAAK-AAGIYELASglfngfdtMIGESEQSLSGGQAQRIALARAfLASDRHILLFD 496
Cdd:PRK11000 89 -HLSVAENMSFglKLAGAKKEEINQRVNqVAEVLQLAH--------LLDRKPKALSGGQRQRVAIGRT-LVAEPSVFLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488907140 497 EPTAHLD----IQTEYD-------LKQTMLpllenhlvfFATH-RLHWLKQMDYVLVMDNGHIIEQGRPREL 556
Cdd:PRK11000 159 EPLSNLDaalrVQMRIEisrlhkrLGRTMI---------YVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
333-528 |
6.38e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.10 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDgqQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKF--------LNFQN 403
Cdd:PRK11248 2 LQISHLYADYGG--KPA-LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGfVPYQHGSITLDGKPVegpgaergVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 404 TS---WQkqiiyipqkpyifhtSLRENIAFYQPDA--PKEQVVKAAKAAgiyeLASGLFNGFDT-MIGEseqsLSGGQAQ 477
Cdd:PRK11248 79 EGllpWR---------------NVQDNVAFGLQLAgvEKMQRLEIAHQM----LKKVGLEGAEKrYIWQ----LSGGQRQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488907140 478 RIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLEN--HLVFFATH 528
Cdd:PRK11248 136 RVGIARA-LAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITH 187
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
333-555 |
7.17e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 61.66 E-value: 7.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQQP-AALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGIN---------SGRGDISINRNKFLNFQ 402
Cdd:PRK10535 5 LELKDIRRSYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDkptsgtyrvAGQDVATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 403 ntswQKQIIYIPQKPYIF-HTSLRENI---AFYQPDAPKEQVVKAAkaagiyELASGLfnGFDTMIGESEQSLSGGQAQR 478
Cdd:PRK10535 85 ----REHFGFIFQRYHLLsHLTAAQNVevpAVYAGLERKQRLLRAQ------ELLQRL--GLEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488907140 479 IALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLEN-HLVFFATHRLHWLKQMDYVLVMDNGHIIEQGRPRE 555
Cdd:PRK10535 153 VSIARA-LMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQE 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
329-572 |
7.98e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.20 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 329 SETVLSVHNFSFQYPDgqqPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISI------NRNKFLnf 401
Cdd:PRK13537 4 SVAPIDFRNVEKRYGD---KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHpDAGSISLcgepvpSRARHA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 402 qntswQKQIIYIPQkpyiFHT-----SLRENIAFYQPDAPKEQVVKAAKAAGIYELASgLFNGFDTMIGEseqsLSGGQA 476
Cdd:PRK13537 79 -----RQRVGVVPQ----FDNldpdfTVRENLLVFGRYFGLSAAAARALVPPLLEFAK-LENKADAKVGE----LSGGMK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 477 QRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLL-ENHLVFFATHRLHWLKQM-DYVLVMDNGHIIEQGRPR 554
Cdd:PRK13537 145 RRLTLARA-LVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPH 223
|
250 260
....*....|....*....|....*..
gi 488907140 555 ELLED---------FDGKLNELRKELT 572
Cdd:PRK13537 224 ALIESeigcdvieiYGPDPVALRDELA 250
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
329-556 |
1.72e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 59.35 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 329 SETVLSVHNF--SFQYPDGQQpAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGRGDIS----INRNKFLNFQ 402
Cdd:PRK09473 9 ADALLDVKDLrvTFSTPDGDV-TAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGgsatFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 403 NTSWQK----QIIYIPQ------KPY-----------IFHTSLRENIAFYQP----DAPKeqVVKAAKAAGIYElasglf 457
Cdd:PRK09473 88 EKELNKlraeQISMIFQdpmtslNPYmrvgeqlmevlMLHKGMSKAEAFEESvrmlDAVK--MPEARKRMKMYP------ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 458 ngfdtmigeseQSLSGGQAQRIALARAFLASDRhILLFDEPTAHLDIQTEydlKQTMLPLLE-----NHLVFFATHRLHW 532
Cdd:PRK09473 160 -----------HEFSGGMRQRVMIAMALLCRPK-LLIADEPTTALDVTVQ---AQIMTLLNElkrefNTAIIMITHDLGV 224
|
250 260
....*....|....*....|....*
gi 488907140 533 LKQM-DYVLVMDNGHIIEQGRPREL 556
Cdd:PRK09473 225 VAGIcDKVLVMYAGRTMEYGNARDV 249
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
364-561 |
1.77e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.66 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 364 VAVVGLSGSGKTTLLSSLAG---INSGRGDISINRNKFlnfqNTSWQKQIIYIPQKPYIF-HTSLRENIAFYQ----PDA 435
Cdd:PLN03211 97 LAVLGPSGSGKSTLLNALAGriqGNNFTGTILANNRKP----TKQILKRTGFVTQDDILYpHLTVRETLVFCSllrlPKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 436 PKEQVVKAAKAAGIYELasGLFNGFDTMIGES-EQSLSGGQAQRIALARAFLASDRhILLFDEPTAHLDIQTEYDLKQTM 514
Cdd:PLN03211 173 LTKQEKILVAESVISEL--GLTKCENTIIGNSfIRGISGGERKRVSIAHEMLINPS-LLILDEPTSGLDATAAYRLVLTL 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488907140 515 LPLLEN-HLVFFATHR-LHWLKQM-DYVLVMDNGHIIEQGRPRELLEDFD 561
Cdd:PLN03211 250 GSLAQKgKTIVTSMHQpSSRVYQMfDSVLVLSEGRCLFFGKGSDAMAYFE 299
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
351-559 |
2.65e-09 |
|
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: 57.94 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGRgdISINRNKFlnfqnTSW------QKQIIYIPQKPYIFH 421
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLvkpDSGK--ILLDGQDI-----TKLpmhkraRLGIGYLPQEASIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 422 T-SLRENI--AFYQPDAPKEQVVKAAKAA----GIYELASGLfngfdtmigesEQSLSGGQAQRIALARAfLASDRHILL 494
Cdd:cd03218 89 KlTVEENIlaVLEIRGLSKKEREEKLEELleefHITHLRKSK-----------ASSLSGGERRRVEIARA-LATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488907140 495 FDEPTAHLDIQTEYDLKQTMLPLLENHL-VFFATHRLH-WLKQMDYVLVMDNGHIIEQGRPRELLED 559
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIgVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
48-270 |
2.65e-09 |
|
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: 58.60 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 48 SAFSSAVPYIFGFAI----------------------SLLcRHFFSLIKEGSANSFSVTASEGLRDQLLGK--YLSFGdq 103
Cdd:cd18542 12 TALNLLIPLLIRRIIdsviggglrellwllallilgvALL-RGVFRYLQGYLAEKASQKVAYDLRNDLYDHlqRLSFS-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 104 tiF--KTGTGHAVSLLHAGIDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLRWQEALFLLLIFPVIIFFFVILGLAAQK- 180
Cdd:cd18542 89 --FhdKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPa 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 181 --RADNEyrnFTVLNNRFADTLRGMQTLKQlglsriFTKRIYET------SERYRKSTMRSLTIAMTSTFSLDFFTTLSI 252
Cdd:cd18542 167 feEIREQ---EGELNTVLQENLTGVRVVKA------FAREDYEIekfdkeNEEYRDLNIKLAKLLAKYWPLMDFLSGLQI 237
|
250
....*....|....*...
gi 488907140 253 AVIAVFLGFSLMEGKMSL 270
Cdd:cd18542 238 VLVLWVGGYLVINGEITL 255
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
323-504 |
2.79e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.66 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 323 KVPAIDSETVLSVHNFSfqYPDGQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG---INSGRgdISINRNkfl 399
Cdd:COG3845 248 KAPAEPGEVVLEVENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGlrpPASGS--IRLDGE--- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 400 NFQNTS----WQKQIIYIPQKPyifHT-------SLRENIAFYQPDapKEQVVKAA--KAAGIYELASGLFNGFDTMIGE 466
Cdd:COG3845 321 DITGLSprerRRLGVAYIPEDR---LGrglvpdmSVAENLILGRYR--RPPFSRGGflDRKAIRAFAEELIEEFDVRTPG 395
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488907140 467 SEQ---SLSGGQAQRIALARAfLASDRHILLFDEPTAHLDI 504
Cdd:COG3845 396 PDTparSLSGGNQQKVILARE-LSRDPKLLIAAQPTRGLDV 435
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
344-529 |
4.43e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 344 DGQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGRGDISINRNKFLNFqntswqkqiiyiPQKpyifhTS 423
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQF------------GRE-----AS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 424 LRENIAfyqPDAPKEQVVKAAKAAGIYElASGLFNGFDTmigeseqsLSGGQAQRIALARAfLASDRHILLFDEPTAHLD 503
Cdd:COG2401 102 LIDAIG---RKGDFKDAVELLNAVGLSD-AVLWLRRFKE--------LSTGQKFRFRLALL-LAERPKLLVIDEFCSHLD 168
|
170 180
....*....|....*....|....*...
gi 488907140 504 IQTEYDLKQTMLPLLENHLVFF--ATHR 529
Cdd:COG2401 169 RQTAKRVARNLQKLARRAGITLvvATHH 196
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
333-505 |
5.17e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 333 LSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGinsgrgDISINRNKFLNFQNTSwqkqIIY 412
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG------ELEPDSGTVKWSENAN----IGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 413 IPQKpyifHT-------SLRENIAFYQPDAPKEQVVKAAkaagiyeLASGLFNGFDtmIGESEQSLSGGQAQRIALARAF 485
Cdd:PRK15064 387 YAQD----HAydfendlTLFDWMSQWRQEGDDEQAVRGT-------LGRLLFSQDD--IKKSVKVLSGGEKGRMLFGKLM 453
|
170 180
....*....|....*....|
gi 488907140 486 LAsDRHILLFDEPTAHLDIQ 505
Cdd:PRK15064 454 MQ-KPNVLVMDEPTNHMDME 472
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
350-554 |
1.01e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 57.28 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 350 ALKDINF-LVRGfAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISINRNKFLN----------------FQNT----SWQ 407
Cdd:PRK11308 30 ALDGVSFtLERG-KTLAVVGESGCGKSTLARLLTMIETpTGGELYYQGQDLLKadpeaqkllrqkiqivFQNPygslNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 408 KQIIYIPQKPYIFHTSLreniafyqpdAPKEQVVKAAKAAGIYELASGLFNGFDTMigeseqsLSGGQAQRIALARAfLA 487
Cdd:PRK11308 109 KKVGQILEEPLLINTSL----------SAAERREKALAMMAKVGLRPEHYDRYPHM-------FSGGQRQRIAIARA-LM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 488 SDRHILLFDEPTAHLD--IQTE-----YDLKQTMlpllenHLVF-FATHRLHWLKQM-DYVLVMDNGHIIEQG------- 551
Cdd:PRK11308 171 LDPDVVVADEPVSALDvsVQAQvlnlmMDLQQEL------GLSYvFISHDLSVVEHIaDEVMVMYLGRCVEKGtkeqifn 244
|
...
gi 488907140 552 RPR 554
Cdd:PRK11308 245 NPR 247
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
351-528 |
1.04e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDIN--FLvRGfAKVAVVGLSGSGKTTLLSSLAGINSgrgdisinrnkflNFQNTSWQKQ---IIYIPQKPYIFHT-SL 424
Cdd:PRK11819 23 LKDISlsFF-PG-AKIGVLGLNGAGKSTLLRIMAGVDK-------------EFEGEARPAPgikVGYLPQEPQLDPEkTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 425 RENIAfyqpDAPKEQVVKAAKAAGIYELASGLFNGFDTMIGES-------------------EQS--------------- 470
Cdd:PRK11819 88 RENVE----EGVAEVKAALDRFNEIYAAYAEPDADFDALAAEQgelqeiidaadawdldsqlEIAmdalrcppwdakvtk 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488907140 471 LSGGQAQRIALARAFLaSDRHILLFDEPTAHLDIQTeydlkqtmLPLLENHLVFFA------TH 528
Cdd:PRK11819 164 LSGGERRRVALCRLLL-EKPDMLLLDEPTNHLDAES--------VAWLEQFLHDYPgtvvavTH 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
351-551 |
1.06e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 55.35 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGR----GDISINRNKFLNFQNTsWQKQIIYIPQKPYIFHT-SLR 425
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsveGDIHYNGIPYKEFAEK-YPGEIIYVSEEDVHFPTlTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 426 ENIAFyqpdapkeqvvkAAKAAGiyelasglfngfdtmiGESEQSLSGGQAQRIALARAFLASDRhILLFDEPTAHLDIQ 505
Cdd:cd03233 102 ETLDF------------ALRCKG----------------NEFVRGISGGERKRVSIAEALVSRAS-VLCWDNSTRGLDSS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488907140 506 TEYDLKQTMLPLL-ENHLVFFAT-----HRLhwLKQMDYVLVMDNGHIIEQG 551
Cdd:cd03233 153 TALEILKCIRTMAdVLKTTTFVSlyqasDEI--YDLFDKVLVLYEGRQIYYG 202
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
364-528 |
1.45e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.20 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 364 VAVVGLSGSGKTTLLSSLAGINSGR-GDISINrNKFLNFQNTSWQKQIIYIPQKPYIfHTSL--RENIAFYQP---DAPK 437
Cdd:PRK13538 30 VQIEGPNGAGKTSLLRILAGLARPDaGEVLWQ-GEPIRRQRDEYHQDLLYLGHQPGI-KTELtaLENLRFYQRlhgPGDD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 438 EQVVKAAKAAGiyeLAsglfnGF-DTMIGeseqSLSGGQAQRIALARAFLaSDRHILLFDEP-TAhLDIQTEYDLKQtml 515
Cdd:PRK13538 108 EALWEALAQVG---LA-----GFeDVPVR----QLSAGQQRRVALARLWL-TRAPLWILDEPfTA-IDKQGVARLEA--- 170
|
170
....*....|....*...
gi 488907140 516 pLLENHL-----VFFATH 528
Cdd:PRK13538 171 -LLAQHAeqggmVILTTH 187
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
351-559 |
1.46e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 55.81 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLV-RGfakvAVVGL---SGSGKTTLLSSLAGI---NSGRgdisInrnkFLNFQN-TSW------QKQIIYIPQK 416
Cdd:COG1137 19 VKDVSLEVnQG----EIVGLlgpNGAGKTTTFYMIVGLvkpDSGR----I----FLDGEDiTHLpmhkraRLGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 417 PYIF-HTSLRENIAfyqpdAPKEQVVKAAKAagIYELASGLFNGFD-TMIGESE-QSLSGGQAQRIALARAfLASDRHIL 493
Cdd:COG1137 87 ASIFrKLTVEDNIL-----AVLELRKLSKKE--REERLEELLEEFGiTHLRKSKaYSLSGGERRRVEIARA-LATNPKFI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488907140 494 LFDEPTAHLD------IQTE-YDLKQTMLP-LLENHLVfFAThrlhwLKQMDYVLVMDNGHIIEQGRPRELLED 559
Cdd:COG1137 159 LLDEPFAGVDpiavadIQKIiRHLKERGIGvLITDHNV-RET-----LGICDRAYIISEGKVLAEGTPEEILNN 226
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-270 |
1.48e-08 |
|
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: 56.36 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 19 LVLLTFLQAVSILFQAFFLSKSIVILWHQSAFSSAVPYIFGFAISLLCRHFFSLIKE--GSANSFSVTASegLRDQLLGK 96
Cdd:cd18563 8 MLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGrlLARLGERITAD--LRRDLYEH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 97 Y----LSFGDqtifKTGTGHAVSLLHAGIDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLRWQEALFLLLIFPVIIFFFV 172
Cdd:cd18563 86 LqrlsLSFFD----KRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 173 ILGLAAQKRADNEYRNFTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSI 252
Cdd:cd18563 162 FFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGT 241
|
250
....*....|....*...
gi 488907140 253 AVIAVFLGFSLMEGKMSL 270
Cdd:cd18563 242 LIVWYFGGRQVLSGTMTL 259
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
330-551 |
1.58e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.79 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 330 ETVLSVHNFSFQYpdgQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGRGDI---------SINRNKFLN 400
Cdd:PRK09984 2 QTIIRVEKLAKTF---NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshiellgrTVQREGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 401 FQNTSWQKQIIYIPQK-PYIFHTSLRENI---------------AFYQPdAPKEQVVKAAKAAGIYELASglfngfdtmi 464
Cdd:PRK09984 79 RDIRKSRANTGYIFQQfNLVNRLSVLENVligalgstpfwrtcfSWFTR-EQKQRALQALTRVGMVHFAH---------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 465 gESEQSLSGGQAQRIALARAFLASDRhILLFDEPTAHLDIQTEYDLKQTMLPLLENH--LVFFATHRLHW-LKQMDYVLV 541
Cdd:PRK09984 148 -QRVSTLSGGQQQRVAIARALMQQAK-VILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYaLRYCERIVA 225
|
250
....*....|
gi 488907140 542 MDNGHIIEQG 551
Cdd:PRK09984 226 LRQGHVFYDG 235
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
89-270 |
1.90e-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: 55.88 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 89 LRDQLLGKYLSFgDQTIF-KTGTGHAVSLLHAGIDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLRWQEALFLLLIFPVI 167
Cdd:cd18541 75 LRNDLFAHLLTL-SPSFYqKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 168 IFFFVILGlaaqKRADNEYRN----FTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRsltIAMTSTF- 242
Cdd:cd18541 154 ALLVYRLG----KKIHKRFRKvqeaFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLR---LARVDALf 226
|
170 180 190
....*....|....*....|....*....|
gi 488907140 243 --SLDFFTTLSIAVIAVFLGFSLMEGKMSL 270
Cdd:cd18541 227 fpLIGLLIGLSFLIVLWYGGRLVIRGTITL 256
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
349-557 |
1.97e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.60 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 349 AALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSG---------RGDISINRNKFLNFQNTSWQKQIIYIPQ--KP 417
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQaaQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 418 yIFHTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLfNGFDTMIGESEQSLSGGQAQRIALARAFL--------ASD 489
Cdd:PRK13547 95 -AFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALAL-AGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaAQP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488907140 490 RHILLFDEPTAHLDIQTEYDLKQTMLPLL-ENHL-VFFATHRLHW-LKQMDYVLVMDNGHIIEQGRPRELL 557
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLArDWNLgVLAIVHDPNLaARHADRIAMLADGAIVAHGAPADVL 243
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
318-547 |
2.12e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.86 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 318 EISAL--KVPAIDSETVLSVHNFSFQYPDGQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGR--GDISI 393
Cdd:PRK13549 243 ELTALypREPHTIGEVILEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRweGEIFI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 394 NrNKFLNFQNT--SWQKQIIYIPQ--KPY--IFHTSLRENIA------FYQP---DAPKEQV----------VKAAKAag 448
Cdd:PRK13549 323 D-GKPVKIRNPqqAIAQGIAMVPEdrKRDgiVPVMGVGKNITlaaldrFTGGsriDDAAELKtilesiqrlkVKTASP-- 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 449 iyELASGlfngfdtmigeseqSLSGGQAQRIALARAFLASDRhILLFDEPTAHLDIQTEYDLKQTMLPLLENH--LVFFA 526
Cdd:PRK13549 400 --ELAIA--------------RLSGGNQQKAVLAKCLLLNPK-ILILDEPTRGIDVGAKYEIYKLINQLVQQGvaIIVIS 462
|
250 260
....*....|....*....|.
gi 488907140 527 THRLHWLKQMDYVLVMDNGHI 547
Cdd:PRK13549 463 SELPEVLGLSDRVLVMHEGKL 483
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
350-566 |
2.55e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 55.09 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 350 ALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGRgdisINRNK----FLNFqNTSwqkqiiyipqkpyiFHT 422
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGIlepTSGR----VEVNGrvsaLLEL-GAG--------------FHP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 423 SL--RENIAFYqpdA-----PKEQVvkAAKAAGIYELAsGLFNGFDTMIGeseqSLSGGQAQRIALARAfLASDRHILLF 495
Cdd:COG1134 102 ELtgRENIYLN---GrllglSRKEI--DEKFDEIVEFA-ELGDFIDQPVK----TYSSGMRARLAFAVA-TAVDPDILLV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 496 DEPTAHLD----------IQteyDLKQtmlpllENHLVFFATHRLHWLKQM-DYVLVMDNGHIIEQGRPRELLEDFDGKL 564
Cdd:COG1134 171 DEVLAVGDaafqkkclarIR---ELRE------SGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEEVIAAYEALL 241
|
..
gi 488907140 565 NE 566
Cdd:COG1134 242 AG 243
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
330-503 |
2.75e-08 |
|
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: 54.75 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 330 ETVLSVHNFS--F----QypDGQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG---INSGRgdISINRNkfln 400
Cdd:COG4778 2 TTLLEVENLSktFtlhlQ--GGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnylPDSGS--ILVRHD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 401 fqnTSW-------QKQIIYipqkpyifhtsLRENIAFY--Q-----PDAPKEQVV-KAAKAAGI-----YELASGLFNGF 460
Cdd:COG4778 74 ---GGWvdlaqasPREILA-----------LRRRTIGYvsQflrviPRVSALDVVaEPLLERGVdreeaRARARELLARL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488907140 461 DtmIGESEQSL-----SGGQAQRIALARAFLAsDRHILLFDEPTAHLD 503
Cdd:COG4778 140 N--LPERLWDLppatfSGGEQQRVNIARGFIA-DPPLLLLDEPTASLD 184
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
350-551 |
2.99e-08 |
|
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: 54.46 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 350 ALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGRgdISINRnkflnfqntswqkQIIYIPQKPYIFHTSL-- 424
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIyppDSGT--VTVRG-------------RVSSLLGLGGGFNPELtg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 425 RENIAFY------QPDAPKEqvvkaaKAAGIYELaSGLFNGFDTMIGEseqsLSGGQAQRIALARAfLASDRHILLFDEP 498
Cdd:cd03220 102 RENIYLNgrllglSRKEIDE------KIDEIIEF-SELGDFIDLPVKT----YSSGMKARLAFAIA-TALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488907140 499 TAHLDIQTEYDLKQTMLPLLENH-LVFFATHRLHWLKQM-DYVLVMDNGHIIEQG 551
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
332-538 |
3.15e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPDgqQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI-NSGRGDISINRNKfLNFQNTSWQKQI 410
Cdd:PRK13540 1 MLDVIELDFDYHD--QPL-LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLlNPEKGEILFERQS-IKKDLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 411 IYIPQK----PYIfhtSLRENIAFyqpdapkeQVVKAAKAAGIYELASgLFNgFDTMIGESEQSLSGGQAQRIALARAFL 486
Cdd:PRK13540 77 CFVGHRsginPYL---TLRENCLY--------DIHFSPGAVGITELCR-LFS-LEHLIDYPCGLLSSGQKRQVALLRLWM 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488907140 487 aSDRHILLFDEPTAHLDiqtEYDLkQTMLPLLENH-----LVFFATHRLHWLKQMDY 538
Cdd:PRK13540 144 -SKAKLWLLDEPLVALD---ELSL-LTIITKIQEHrakggAVLLTSHQDLPLNKADY 195
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
364-505 |
3.39e-08 |
|
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: 54.72 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 364 VAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKflnfqntswqkqIIYIPQkpYI---FHTSLRENIA-----FYQPD 434
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGvLKPDEGDIEIELDT------------VSYKPQ--YIkadYEGTVRDLLSsitkdFYTHP 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488907140 435 APKEQVVKAAKAAGIYElasglfngfdtmigESEQSLSGGQAQRIALArAFLASDRHILLFDEPTAHLDIQ 505
Cdd:cd03237 94 YFKTEIAKPLQIEQILD--------------REVPELSGGELQRVAIA-ACLSKDADIYLLDEPSAYLDVE 149
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
331-553 |
4.13e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.35 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 331 TVLSVHNFSFQYpdGQQpAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGrgdiSINRNKFLnfqntswq 407
Cdd:PRK09544 3 SLVSLENVSVSF--GQR-RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLvapDEG----VIKRNGKL-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 408 kQIIYIPQKPYIfHTSLRENIAFY---QPDAPKEQVVKAAKAAGIYELasglfngfdtmIGESEQSLSGGQAQRIALARA 484
Cdd:PRK09544 68 -RIGYVPQKLYL-DTTLPLTVNRFlrlRPGTKKEDILPALKRVQAGHL-----------IDAPMQKLSGGETQRVLLARA 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488907140 485 FLASDRhILLFDEPTAHLDIQTE---YDLKQTMLPLLeNHLVFFATHRLHW-LKQMDYVLVMdNGHIIEQGRP 553
Cdd:PRK09544 135 LLNRPQ-LLVLDEPTQGVDVNGQvalYDLIDQLRREL-DCAVLMVSHDLHLvMAKTDEVLCL-NHHICCSGTP 204
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
326-557 |
4.14e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 55.12 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 326 AIDSETVLSVHNFSFQYP-----DGQQPAALK---DINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGRgdISIN 394
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFPvrgglFGRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLeepTSGE--ILFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 395 RNKFLNFQNTSWQK-----QIIYipQKPYifhTSL------RENIAF---YQPDAPKEQvvKAAKAAGIYELaSGLfngf 460
Cdd:COG4608 79 GQDITGLSGRELRPlrrrmQMVF--QDPY---ASLnprmtvGDIIAEplrIHGLASKAE--RRERVAELLEL-VGL---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 461 dtmigESEQS------LSGGQAQRIALARAfLASDRHILLFDEPTAHLD-------------IQTEYDLkqTMLpllenh 521
Cdd:COG4608 147 -----RPEHAdrypheFSGGQRQRIGIARA-LALNPKLIVCDEPVSALDvsiqaqvlnlledLQDELGL--TYL------ 212
|
250 260 270
....*....|....*....|....*....|....*..
gi 488907140 522 lvfFATHRLHWLKQM-DYVLVMDNGHIIEQGrPRELL 557
Cdd:COG4608 213 ---FISHDLSVVRHIsDRVAVMYLGKIVEIA-PRDEL 245
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
339-551 |
4.86e-08 |
|
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: 53.88 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 339 SFQYPDGQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI-NSGRGDISIN-------RNKFLnfqntswqKQI 410
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLlQPTSGEVRVAglvpwkrRKKFL--------RRI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 411 -IYIPQK-------PYIfhTSLRENIAFYQ--PDAPKEQVVKAAKAAGIYELasglfngFDTMIgeseQSLSGGQAQRIA 480
Cdd:cd03267 97 gVVFGQKtqlwwdlPVI--DSFYLLAAIYDlpPARFKKRLDELSELLDLEEL-------LDTPV----RQLSLGQRMRAE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488907140 481 LARAFLaSDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENH--LVFFATHRLHWLKQM-DYVLVMDNGHIIEQG 551
Cdd:cd03267 164 IAAALL-HEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
299-547 |
5.69e-08 |
|
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: 55.60 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 299 DGKNAFTEVLS------VINQKKTSEISAL--KVPAIDSETVLSVHNFSFQYPDGQQPAALKDINFLVRGFAKVAVVGLS 370
Cdd:TIGR02633 216 DGQHVATKDMStmseddIITMMVGREITSLypHEPHEIGDVILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLV 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 371 GSGKTTLLSSLAGINSGR--GDISINrNKFLNFQN--TSWQKQIIYIPQK-------------PYIFHTSLRENIAFYQP 433
Cdd:TIGR02633 296 GAGRTELVQALFGAYPGKfeGNVFIN-GKPVDIRNpaQAIRAGIAMVPEDrkrhgivpilgvgKNITLSVLKSFCFKMRI 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 434 DAPKEQvvkAAKAAGIYELASGLFNGFdTMIGeseqSLSGGQAQRIALARAFLASDRhILLFDEPTAHLDIQTEYDLKQT 513
Cdd:TIGR02633 375 DAAAEL---QIIGSAIQRLKVKTASPF-LPIG----RLSGGNQQKAVLAKMLLTNPR-VLILDEPTRGVDVGAKYEIYKL 445
|
250 260 270
....*....|....*....|....*....|....*.
gi 488907140 514 MLPLLEN--HLVFFATHRLHWLKQMDYVLVMDNGHI 547
Cdd:TIGR02633 446 INQLAQEgvAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
470-506 |
8.60e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 8.60e-08
10 20 30
....*....|....*....|....*....|....*..
gi 488907140 470 SLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQT 506
Cdd:PRK11147 156 SLSGGWLRKAALGRA-LVSNPDVLLLDEPTNHLDIET 191
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
110-292 |
1.00e-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: 54.11 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 110 TGHAVSLLHAGIDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLRWQEALFLLLIFPVIIFFFVILglaaQKRADNEYRNF 189
Cdd:cd18565 110 TGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWF----QRRIEPRYRAV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 190 --TV--LNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVFLGFSLME 265
Cdd:cd18565 186 reAVgdLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLD 265
|
170 180 190
....*....|....*....|....*....|...
gi 488907140 266 GKMSLFPALT------LLVLAPEYFLPLRTFSE 292
Cdd:cd18565 266 GPPLFTGTLTvgtlvtFLFYTQRLLWPLTRLGD 298
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
339-547 |
1.13e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.95 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 339 SFQYPDGQQpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS--------GRGDISINRNKFLNFqntsWQKQI 410
Cdd:PRK10908 8 SKAYLGGRQ--ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERpsagkiwfSGHDITRLKNREVPF----LRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 411 IYIPQKPYIF-HTSLRENIAF------YQPDAPKEQVVKAAKAAGIYELASGLfngfdtmigesEQSLSGGQAQRIALAR 483
Cdd:PRK10908 82 GMIFQDHHLLmDRTVYDNVAIpliiagASGDDIRRRVSAALDKVGLLDKAKNF-----------PIQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 484 AfLASDRHILLFDEPTAHLDIQteydLKQTMLPLLENH-----LVFFATHRLHWLKQMDY-VLVMDNGHI 547
Cdd:PRK10908 151 A-VVNKPAVLLADEPTGNLDDA----LSEGILRLFEEFnrvgvTVLMATHDIGLISRRSYrMLTLSDGHL 215
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
331-547 |
1.22e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.29 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 331 TVLSVHNFSfqypdGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGRGDisinrNKFLNFQNTS----- 405
Cdd:PRK15439 267 PVLTVEDLT-----GE---GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGG-----RIMLNGKEINalsta 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 406 --WQKQIIYIP---QKPYIF-HTSLRENIAFYQPDAPKEQVVKAAKAAGI--YELASGL-FNGFDTMIGeseqSLSGGQA 476
Cdd:PRK15439 334 qrLARGLVYLPedrQSSGLYlDAPLAWNVCALTHNRRGFWIKPARENAVLerYRRALNIkFNHAEQAAR----TLSGGNQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488907140 477 QRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHL-VFFATHRLHWLKQM-DYVLVMDNGHI 547
Cdd:PRK15439 410 QKVLIAKC-LEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMaDRVLVMHQGEI 481
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
471-562 |
2.20e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 52.91 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 471 LSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLL-ENHLVFFATHRLHWLKQM-DYVLVMDNGHII 548
Cdd:PRK13536 173 LSGGMKRRLTLARA-LINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERLcDRLCVLEAGRKI 251
|
90
....*....|....
gi 488907140 549 EQGRPRELLEDFDG 562
Cdd:PRK13536 252 AEGRPHALIDEHIG 265
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
353-543 |
2.41e-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: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 353 DINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSGR-GDISINRnkflnfqntswQKQIIYIPQKPYIFHTSLRENIAFy 431
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYgGRLTKPA-----------KGKLFYVPQRPYMTLGTLRDQIIY- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 432 qPDAPKEQVVKAAKAAgiyELASGLFN-----------GFDTMIGESEQsLSGGQAQRIALARAFLASDRHILLfDEPTA 500
Cdd:TIGR00954 538 -PDSSEDMKRRGLSDK---DLEQILDNvqlthileregGWSAVQDWMDV-LSGGEKQRIAMARLFYHKPQFAIL-DECTS 611
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488907140 501 HLDIqteyDLKQTMLPLLENHLV--FFATHRLHWLKQMDYVLVMD 543
Cdd:TIGR00954 612 AVSV----DVEGYMYRLCREFGItlFSVSHRKSLWKYHEYLLYMD 652
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
332-556 |
2.70e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.82 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPDGQQP-AALKDINFLVRGFAKVAVVGLSGSGKTtlLSSLA--GINSGRGDISINRnkfLNFQNTSWQK 408
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPfRAVDRISYSVKQGEVVGIVGESGSGKS--VSSLAimGLIDYPGRVMAEK---LEFNGQDLQR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 409 ------------QIIYIPQKPYifhTSLR----------ENIAFYQPDAPKEQVVKAA---KAAGIYELASGLFNgfdtm 463
Cdd:PRK11022 78 isekerrnlvgaEVAMIFQDPM---TSLNpcytvgfqimEAIKVHQGGNKKTRRQRAIdllNQVGIPDPASRLDV----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 464 igeSEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLL--ENHLVFFATHRLHWLKQM-DYVL 540
Cdd:PRK11022 150 ---YPHQLSGGMSQRVMIAMA-IACRPKLLIADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVAEAaHKII 225
|
250
....*....|....*.
gi 488907140 541 VMDNGHIIEQGRPREL 556
Cdd:PRK11022 226 VMYAGQVVETGKAHDI 241
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
464-556 |
4.51e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 53.09 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 464 IGESEQSLSGGQAQRIALARAFLASDRH--ILLFDEPTA--HLDiqteyDLKQtmlpLLE--------NHLVFFATHRLH 531
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKRSTGrtLYILDEPTTglHFD-----DIKK----LLEvlqrlvdkGNTVVVIEHNLD 893
|
90 100 110
....*....|....*....|....*....|.
gi 488907140 532 WLKQMDYVLVM------DNGHIIEQGRPREL 556
Cdd:TIGR00630 894 VIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
464-553 |
4.61e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 51.46 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 464 IGESEQSLSGGQAQRIALARAFL--ASDRHILLFDEPTAHL---DIQTeydLKQTMLPLLEN-HLVFFATHRLHWLKQMD 537
Cdd:cd03271 163 LGQPATTLSGGEAQRIKLAKELSkrSTGKTLYILDEPTTGLhfhDVKK---LLEVLQRLVDKgNTVVVIEHNLDVIKCAD 239
|
90 100
....*....|....*....|..
gi 488907140 538 YVLVM------DNGHIIEQGRP 553
Cdd:cd03271 240 WIIDLgpeggdGGGQVVASGTP 261
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
365-552 |
9.29e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 52.32 E-value: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 365 AVVGLSGSGKTTLLSSLAGINSGRGDISINRNKFLNFQNTSWQKQIIYIPQKPYIF-HTSLRENIAFYQPDAPKEQVVKA 443
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFhHLTVAEHILFYAQLKGRSWEEAQ 1039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 444 AKAAGIYElASGLFNGFDtmigESEQSLSGGQAQRIALARAFLAsDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLV 523
Cdd:TIGR01257 1040 LEMEAMLE-DTGLHHKRN----EEAQDLSGGMQRKLSVAIAFVG-DAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTI 1113
|
170 180 190
....*....|....*....|....*....|
gi 488907140 524 FFATHrlhwlkQMDYV-LVMDNGHIIEQGR 552
Cdd:TIGR01257 1114 IMSTH------HMDEAdLLGDRIAIISQGR 1137
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
332-504 |
1.00e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPDGqqPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDIsinrnkflnFQNTswqKQI 410
Cdd:PLN03073 508 IISFSDASFGYPGG--PLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGeLQPSSGTV---------FRSA---KVR 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 411 IYIPQKPYIFHTSLRENIAFYQ----PDAPkEQVVKAakaagiyELASglFNGFDTMIGESEQSLSGGQAQRIALARAFL 486
Cdd:PLN03073 574 MAVFSQHHVDGLDLSSNPLLYMmrcfPGVP-EQKLRA-------HLGS--FGVTGNLALQPMYTLSGGQKSRVAFAKITF 643
|
170
....*....|....*...
gi 488907140 487 ASDrHILLFDEPTAHLDI 504
Cdd:PLN03073 644 KKP-HILLLDEPSNHLDL 660
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
183-556 |
1.02e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.51 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 183 DNEYRNF-TVLNNRfadtlrgmqtlKQLGLSRIFTKRIYET-----SERYRKSTMRSLT----------IAMTSTFSLDF 246
Cdd:PRK10522 183 DKLYNDYqTVLEGR-----------KELTLNRERAEYVFENeyepdAQEYRHHIIRADTfhlsavnwsnIMMLGAIGLVF 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 247 FTTLSI--------AVIAVFLGFsLMEGKMSLFPALTLLVLAPEYFLPLRTFS-EDYHATLDGKNAFTEVlsvinQKkts 317
Cdd:PRK10522 252 YMANSLgwadtnvaATYSLTLLF-LRTPLLSAVGALPTLLSAQVAFNKLNKLAlAPYKAEFPRPQAFPDW-----QT--- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 318 eisalkvpaidsetvLSVHNFSFQYPDgqQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISINRN 396
Cdd:PRK10522 323 ---------------LELRNVTFAYQD--NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQpQSGEILLDGK 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 397 KFLNFQNTSWQKQIIYIPQKPYIFhTSLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLFngfdtmigeSEQSLSGGQA 476
Cdd:PRK10522 386 PVTAEQPEDYRKLFSAVFTDFHLF-DQLLGPEGKPANPALVEKWLERLKMAHKLELEDGRI---------SNLKLSKGQK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 477 QRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLL--ENHLVFFATHRLHWLKQMDYVLVMDNGHIIE-QGRP 553
Cdd:PRK10522 456 KRLALLLA-LAEERDILLLDEWAADQDPHFRREFYQVLLPLLqeMGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEE 534
|
...
gi 488907140 554 REL 556
Cdd:PRK10522 535 RDA 537
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
364-504 |
1.20e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 364 VAVVGLSGSGKTTLLSSLAGI---NSGRGDISINRNKFLN-FQNTSWQ---KQI----IYIPQKP-YIfhtslrENIafy 431
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGElipNLGDYEEEPSWDEVLKrFRGTELQnyfKKLyngeIKVVHKPqYV------DLI--- 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488907140 432 qPDAPK---EQVVKAAKAAGIY-ELASGLfnGFDTMIGESEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDI 504
Cdd:PRK13409 173 -PKVFKgkvRELLKKVDERGKLdEVVERL--GLENILDRDISELSGGELQRVAIAAA-LLRDADFYFFDEPTSYLDI 245
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
20-270 |
1.68e-06 |
|
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: 50.09 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 20 VLLTFLQAVSILFQAFFLSKSIVILWH------QSAFSSAVPYIFGFAISLLCRHFFSLIKEGSANSFSVTASEGLRDQL 93
Cdd:cd18547 5 IILAIISTLLSVLGPYLLGKAIDLIIEglggggGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 94 LGKY----LSFGDQTifktGTGHAVSLLHAGIDNVQNYFQLIFIKIID--LSIIpwLLLIYMFFLRWQEALFLLLIFPVI 167
Cdd:cd18547 85 FEKLqrlpLSYFDTH----SHGDIMSRVTNDVDNISQALSQSLTQLISsiLTIV--GTLIMMLYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 168 IFFFVILGLAAQKRADNEYRNFTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFF 247
Cdd:cd18547 159 LLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFI 238
|
250 260
....*....|....*....|...
gi 488907140 248 TTLSIAVIAVFLGFSLMEGKMSL 270
Cdd:cd18547 239 NNLGYVLVAVVGGLLVINGALTV 261
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
364-504 |
1.68e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 364 VAVVGLSGSGKTTLLSSLAG-INSGRGDISinrnkflnfqntsWQKQIIYIPQkpYIFHtslreniafyQPDAPKEQVVk 442
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGvLKPDEGEVD-------------PELKISYKPQ--YIKP----------DYDGTVEDLL- 421
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488907140 443 aAKAAGIY-------ELAS--GLFNGFDTMIGEseqsLSGGQAQRIALArAFLASDRHILLFDEPTAHLDI 504
Cdd:PRK13409 422 -RSITDDLgssyyksEIIKplQLERLLDKNVKD----LSGGELQRVAIA-ACLSRDADLYLLDEPSAHLDV 486
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
121-270 |
1.83e-06 |
|
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: 49.84 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 121 IDNVQNyFQLIFIKIIDLSIIPWLLL----IYMFFLRWQEALFLLLIFPVIIFFFVILGLAAQKRADNEYRNFTVLNNRF 196
Cdd:cd18778 104 INDVAN-VERLIADGIPQGITNVLTLvgvaIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALL 182
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488907140 197 ADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVFLGFSLMEGKMSL 270
Cdd:cd18778 183 QDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLAGELTI 256
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
327-519 |
1.83e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.55 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 327 IDSETVLSVHNFSfqypdGQQPAALKDINFLVR-----GFAkvavvGLSGSGKTTLLSSLAGINSGR-GDISINRNKF-L 399
Cdd:PRK09700 260 LAHETVFEVRNVT-----SRDRKKVRDISFSVCrgeilGFA-----GLVGSGRTELMNCLFGVDKRAgGEIRLNGKDIsP 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 400 NFQNTSWQKQIIYIPQKPY---IFHT-SLRENIAfyqpdapkeqVVKAAKAAGiYELASGLFNGFDTM-IGESEQS---- 470
Cdd:PRK09700 330 RSPLDAVKKGMAYITESRRdngFFPNfSIAQNMA----------ISRSLKDGG-YKGAMGLFHEVDEQrTAENQREllal 398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 471 -----------LSGGQAQRIALARaFLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLE 519
Cdd:PRK09700 399 kchsvnqniteLSGGNQQKVLISK-WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD 457
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
364-551 |
2.82e-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: 47.70 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 364 VAVVGLSGSGKTTLLSSlaginsgrgdisinrnkflnfqntswqkqiiyipqkpyIFHTSLRENIAFYQPDAPKEQVVKA 443
Cdd:cd03238 24 VVVTGVSGSGKSTLVNE--------------------------------------GLYASGKARLISFLPKFSRNKLIFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 444 AKAAGIYELasGLfnGFDTmIGESEQSLSGGQAQRIALARaFLASDRH--ILLFDEPTAHLDIQTEYDLKQTMLPLL-EN 520
Cdd:cd03238 66 DQLQFLIDV--GL--GYLT-LGQKLSTLSGGELQRVKLAS-ELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLG 139
|
170 180 190
....*....|....*....|....*....|....*..
gi 488907140 521 HLVFFATHRLHWLKQMDYVLVM------DNGHIIEQG 551
Cdd:cd03238 140 NTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
146-270 |
3.74e-06 |
|
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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 49.01 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 146 LIYMFFLRWQEALFLLLIFPVIIFFFVILglaaQKRADNEYRNFTVLNNR----FADTLRGMQTLKQLGLSRIFTKRIYE 221
Cdd:cd18540 134 LIVMLILNWKLALIVLAVVPVLAVVSIYF----QKKILKAYRKVRKINSRitgaFNEGITGAKTTKTLVREEKNLREFKE 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 488907140 222 TSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVFLGFSLMEGKMSL 270
Cdd:cd18540 210 LTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITI 258
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
327-559 |
4.00e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.38 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 327 IDSETVLSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISinrnkflnFQNTS 405
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRK---GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSArLAPDAGEVH--------YRMRD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 406 WQKQIIYI---PQKPYIFHTS---LRENIAfyqpDAPKEQVVKAAK------AAG------IYELASglfngfDTM---- 463
Cdd:PRK11701 70 GQLRDLYAlseAERRRLLRTEwgfVHQHPR----DGLRMQVSAGGNigerlmAVGarhygdIRATAG------DWLerve 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 464 -----IGESEQSLSGGQAQRIALARAFLASDRhiLLF-DEPTAHLDIQTEYDLkqtmLPLL-----ENHL-VFFATH--- 528
Cdd:PRK11701 140 idaarIDDLPTTFSGGMQQRLQIARNLVTHPR--LVFmDEPTGGLDVSVQARL----LDLLrglvrELGLaVVIVTHdla 213
|
250 260 270
....*....|....*....|....*....|...
gi 488907140 529 --RLhwlkQMDYVLVMDNGHIIEQGRPRELLED 559
Cdd:PRK11701 214 vaRL----LAHRLLVMKQGRVVESGLTDQVLDD 242
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
18-277 |
4.08e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 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 type 3 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 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. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 48.64 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 18 WLVLLTFLQAVSILFQAFFLSKSI--VILWHQSAFSSAVPYIFGFAI-----SLLCRHFFSLIkegsaNSFSVTASEGLR 90
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLIsyLSSYPDEPLSEGYLLALALFLvsllqSLLLHQYFFLS-----FRLGMRVRSALS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 91 DQLLGKYLSFGDQTIFKTGTGHAVSLLHAGIDNVQNYFQLIFikiiDLSIIPWLLLIYMFFLrWQE--------ALFLLL 162
Cdd:cd18579 76 SLIYRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLH----YLWSAPLQIIVALYLL-YRLlgwaalagLGVLLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 163 IFPVIIFFFVILG---LAAQKRADNEYRnftVLNnrfaDTLRGMQTLKQLGLSRIFTKRIyetsERYRKSTMRSLTIA-- 237
Cdd:cd18579 151 LIPLQAFLAKLISklrKKLMKATDERVK---LTN----EILSGIKVIKLYAWEKPFLKRI----EELRKKELKALRKFgy 219
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 488907140 238 MTSTFSLDFFTTLSIAVIAVFLGFSLMEGKMSL---FPALTLL 277
Cdd:cd18579 220 LRALNSFLFFSTPVLVSLATFATYVLLGNPLTAakvFTALSLF 262
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
364-504 |
4.10e-06 |
|
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: 49.78 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 364 VAVVGLSGSGKTTLLSSLAGI---NSGRGDISINRNKFLN-FQNTSWQ---KQI----IYIPQKP-YIfhtslrENIafy 431
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGElkpNLGDYDEEPSWDEVLKrFRGTELQdyfKKLangeIKVAHKPqYV------DLI--- 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488907140 432 qPDAPK---EQVVKAAKAAGIY-ELASGLfnGFDTMIGESEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDI 504
Cdd:COG1245 173 -PKVFKgtvRELLEKVDERGKLdELAEKL--GLENILDRDISELSGGELQRVAIAAA-LLRDADFYFFDEPSSYLDI 245
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
358-514 |
4.34e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 358 VRGFAK----VAVVGLSGSGKTTLLSSLAG-INSG---RGDISINRNKFlnfqNTSWQKQIIYIPQKP-YIFHTSLRENI 428
Cdd:TIGR00956 782 VDGWVKpgtlTALMGASGAGKTTLLNVLAErVTTGvitGGDRLVNGRPL----DSSFQRSIGYVQQQDlHLPTSTVRESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 429 AFY----QPDA-PKEQ----VVKAAKAAGIYELAsglfngfDTMIGESEQSLSGGQAQRIALARAFLASDRHILLFDEPT 499
Cdd:TIGR00956 858 RFSaylrQPKSvSKSEkmeyVEEVIKLLEMESYA-------DAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLFLDEPT 930
|
170
....*....|....*
gi 488907140 500 AHLDIQTEYDLKQTM 514
Cdd:TIGR00956 931 SGLDSQTAWSICKLM 945
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
364-504 |
4.75e-06 |
|
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: 49.40 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 364 VAVVGLSGSGKTTLLSSLAGI---NSGrgdisinrnkflnfqNTSWQKQIIYIPQkpYIfhtslreniafyQPDAPKEqv 440
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVlkpDEG---------------EVDEDLKISYKPQ--YI------------SPDYDGT-- 417
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488907140 441 VKAAkaagiyeLASGLFNGFDTMIGESE---------------QSLSGGQAQRIALArAFLASDRHILLFDEPTAHLDI 504
Cdd:COG1245 418 VEEF-------LRSANTDDFGSSYYKTEiikplgleklldknvKDLSGGELQRVAIA-ACLSRDADLYLLDEPSAHLDV 488
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
332-514 |
5.34e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 47.24 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPD-GQQPAALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAG-INSG--RGDISIN-RNKFLNFqntsw 406
Cdd:cd03232 3 VLTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrKTAGviTGEILINgRPLDKNF----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 407 QKQIIYIPQKPYIFHTS-LRENIAFyqpdapkeqvvkaakaagiyelaSGLFNGfdtmigeseqsLSGGQAQRIALARAf 485
Cdd:cd03232 78 QRSTGYVEQQDVHSPNLtVREALRF-----------------------SALLRG-----------LSVEQRKRLTIGVE- 122
|
170 180
....*....|....*....|....*....
gi 488907140 486 LASDRHILLFDEPTAHLDIQTEYDLKQTM 514
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
350-555 |
7.56e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.48 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 350 ALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGI---NSGRgdISINRNKfLNFQNTswqKQ-----IIYIPQKPYIFH 421
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLyqpDSGE--ILIDGKP-VRIRSP---RDaialgIGMVHQHFMLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 422 T-SLRENIAFYQPDAPKEQVVKAAKAAGIYELASGLfnGF----DTMIGEseqsLSGGQAQRIALARAfLASDRHILLFD 496
Cdd:COG3845 94 NlTVAENIVLGLEPTKGGRLDRKAARARIRELSERY--GLdvdpDAKVED----LSVGEQQRVEILKA-LYRGARILILD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488907140 497 EPTAHLDIQ-TEyDLKQTMLPLLENHL-VFFATHRLHWLKQM-DYVLVMDNGHIIEQGRPRE 555
Cdd:COG3845 167 EPTAVLTPQeAD-ELFEILRRLAAEGKsIIFITHKLREVMAIaDRVTVLRRGKVVGTVDTAE 227
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
121-270 |
8.63e-06 |
|
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: 47.96 E-value: 8.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 121 IDNVQNYF--QLIFIkIIDLsiiPWLL--LIYMFFLRWQEALFLLLIFPVIIFFFVILG------LAAQKRADNEYRNFT 190
Cdd:cd18566 108 LEQIREFLtgQALLA-LLDL---PFVLifLGLIWYLGGKLVLVPLVLLGLFVLVAILLGpilrraLKERSRADERRQNFL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 191 VlnnrfaDTLRGMQTLKQLGLSRIFTKRiYEtsERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVFLGF---SLMEGK 267
Cdd:cd18566 184 I------ETLTGIHTIKAMAMEPQMLRR-YE--RLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFgalLVINGD 254
|
...
gi 488907140 268 MSL 270
Cdd:cd18566 255 LTV 257
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
353-561 |
8.80e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.45 E-value: 8.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 353 DINFLV-RGfaKV-AVVGLSGSGKTTLLSSLAG-INSGRGDI--------SINRNKFLNFQntswqKQIIYIPQKPYIFh 421
Cdd:PRK11831 25 NISLTVpRG--KItAIMGPSGIGKTTLLRLIGGqIAPDHGEIlfdgenipAMSRSRLYTVR-----KRMSMLFQSGALF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 422 TSLR--ENIAFyqPDAPKEQVVKAA-KAAGIYEL-ASGLFNGFDTMIGEseqsLSGGQAQRIALARAfLASDRHILLFDE 497
Cdd:PRK11831 97 TDMNvfDNVAY--PLREHTQLPAPLlHSTVMMKLeAVGLRGAAKLMPSE----LSGGMARRAALARA-IALEPDLIMFDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488907140 498 PTAHLDIQTEYDLKQTMLPLleNHLV----FFATHRL-HWLKQMDYVLVMDNGHIIEQGRPRELLEDFD 561
Cdd:PRK11831 170 PFVGQDPITMGVLVKLISEL--NSALgvtcVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQALQANPD 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
350-545 |
1.48e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.86 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 350 ALKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISINRNKFLNFQNT-SWQKQIIYIPQK-PYIFHTSLRE 426
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEpTKGTITINNINYNKLDHKlAAQLGIGIIYQElSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 427 NIafYQPDAPKEQVV--------KAAKAAGIYELASGLFNGFDTMIGEseqsLSGGQAQRIALARAfLASDRHILLFDEP 498
Cdd:PRK09700 100 NL--YIGRHLTKKVCgvniidwrEMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKT-LMLDAKVIIMDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488907140 499 TAHL-DIQTEYdlkqtmLPLLENHL------VFFATHRLHWLKQM-DYVLVMDNG 545
Cdd:PRK09700 173 TSSLtNKEVDY------LFLIMNQLrkegtaIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
464-557 |
1.80e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 464 IGESEQSLSGGQAQRIALARAFLASDRHILLF--DEPTAHLDIQTEYDLKQTMLPLL-ENHLVFFATHRLHWLKQMDYVL 540
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAYELLAPSKKPTLYvlDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVVKVADYVL 882
|
90 100
....*....|....*....|...
gi 488907140 541 VMD------NGHIIEQGRPRELL 557
Cdd:PRK00635 883 ELGpeggnlGGYLLASCSPEELI 905
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
146-270 |
2.34e-05 |
|
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: 46.28 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 146 LIYMFFLRWQeaLFLLLIFPVIIFFFVILGLaaQKRADNEYR----NFTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYE 221
Cdd:cd18570 133 GIILFFYNWK--LFLITLLIIPLYILIILLF--NKPFKKKNRevmeSNAELNSYLIESLKGIETIKSLNAEEQFLKKIEK 208
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 488907140 222 TSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVFLGFSLMEGKMSL 270
Cdd:cd18570 209 KFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSL 257
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
471-551 |
2.49e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 46.23 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 471 LSGGQAQRIALARAFLAsDRHILLFDEPTAHLDIqteydLKQT-MLPLLENHL------VFFATHRLHWLKQM-DYVLVM 542
Cdd:PRK10418 141 MSGGMLQRMMIALALLC-EAPFIIADEPTTDLDV-----VAQArILDLLESIVqkralgMLLVTHDMGVVARLaDDVAVM 214
|
....*....
gi 488907140 543 DNGHIIEQG 551
Cdd:PRK10418 215 SHGRIVEQG 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
302-526 |
2.82e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 46.85 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 302 NAFTEVLSVINQKK--TSEIsalKVPAID--SETVLSVHNFSFQYPDGQqpaALKDINFLVRGFAKVAVVGLSGSGKTTL 377
Cdd:TIGR03719 291 ARYEELLSQEFQKRneTAEI---YIPPGPrlGDKVIEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 378 LSSLAGI---NSGRgdisinrnkfLNFQNTSwqkQIIYIPQkpyiFHTSLRENIAFYQPDAPKEQVVKAAKaagiYELAS 454
Cdd:TIGR03719 365 FRMITGQeqpDSGT----------IEIGETV---KLAYVDQ----SRDALDPNKTVWEEISGGLDIIKLGK----REIPS 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 455 ----GLFN--GFDT--MIGEseqsLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTeydlkqtmLPLLENHLVFFA 526
Cdd:TIGR03719 424 rayvGRFNfkGSDQqkKVGQ----LSGGERNRVHLAKT-LKSGGNVLLLDEPTNDLDVET--------LRALEEALLNFA 490
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
364-504 |
2.82e-05 |
|
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: 45.82 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 364 VAVVGLSGSGKTTLLSSLAGI---NSGRGDISINRNKFLN-FQNTSWQ-----------KQII---YIPQKPYIFHTSLR 425
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKlkpNLGKFDDPPDWDEILDeFRGSELQnyftkllegdvKVIVkpqYVDLIPKAVKGKVG 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488907140 426 ENIAFYQPDAPKEQVVKAAKAAGIYElasglfngfdtmigESEQSLSGGQAQRIALArAFLASDRHILLFDEPTAHLDI 504
Cdd:cd03236 109 ELLKKKDERGKLDELVDQLELRHVLD--------------RNIDQLSGGELQRVAIA-AALARDADFYFFDEPSSYLDI 172
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
115-270 |
3.49e-05 |
|
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: 45.94 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 115 SLLHAGIDN-VQNYFQLIFIkiidlsiipwllLIYMFFLRWQEALFLLLIFPVIifffVILGLAAQKRADNEYR----NF 189
Cdd:cd18546 111 ELLQTGLVQlVVSLLTLVGI------------AVVLLVLDPRLALVALAALPPL----ALATRWFRRRSSRAYRrareRI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 190 TVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVFLGFSLMEGKMS 269
Cdd:cd18546 175 AAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLT 254
|
.
gi 488907140 270 L 270
Cdd:cd18546 255 V 255
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
110-270 |
4.29e-05 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. 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 I 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. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 45.57 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 110 TGHAVSLLhagIDNVqnyFQLIFikiidlsiipwllLIYMFFLRWQEALFLLLIFPVIIFFFVILGLAAQKRADNEYrNF 189
Cdd:cd18588 116 TGSALTLV---LDLV---FSVVF-------------LAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKF-QR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 190 TVLNNRF-ADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVFLGFSLMEGKM 268
Cdd:cd18588 176 GAENQSFlVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGEL 255
|
..
gi 488907140 269 SL 270
Cdd:cd18588 256 TI 257
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
327-559 |
4.70e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.39 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 327 IDSETVLSVHNFSFQYP--DG------QQPAALKDINFLVRGFAKVAVVGLSGSGK-TTLLSSLAGINSGRGDISINRNK 397
Cdd:PRK10261 308 VDGEPILQVRNLVTRFPlrSGllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKsTTGRALLRLVESQGGEIIFNGQR 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 398 FLNFQNTSWQ---KQIIYIPQKPYifhTSL--RENIAF-----------YQPDAPKEQVVKAAKAAGIYELASGLFngfd 461
Cdd:PRK10261 388 IDTLSPGKLQalrRDIQFIFQDPY---ASLdpRQTVGDsimeplrvhglLPGKAAAARVAWLLERVGLLPEHAWRY---- 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 462 tmigesEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHLV--FFATHRLHWLKQMDY- 538
Cdd:PRK10261 461 ------PHEFSGGQRQRICIARA-LALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHr 533
|
250 260
....*....|....*....|.
gi 488907140 539 VLVMDNGHIIEQGRPRELLED 559
Cdd:PRK10261 534 VAVMYLGQIVEIGPRRAVFEN 554
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
351-563 |
6.68e-05 |
|
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: 44.05 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGiNSG----RGDISinrnkflnFQNTSwqkqIIYIPqkPY------IF 420
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKyevtEGEIL--------FKGED----ITDLP--PEerarlgIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 421 htslrenIAFYQPdaPKEQVVKAAkaagiyELASGLFNGFdtmigeseqslSGGQAQRIALARAfLASDRHILLFDEPTA 500
Cdd:cd03217 81 -------LAFQYP--PEIPGVKNA------DFLRYVNEGF-----------SGGEKKRNEILQL-LLLEPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488907140 501 HLDIQTEYDLKQTMLPLL-ENHLVFFATHRLHWLKQM--DYVLVMDNGHIIEQGrPRELLEDFDGK 563
Cdd:cd03217 134 GLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSG-DKELALEIEKK 198
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
121-284 |
7.90e-05 |
|
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: 44.78 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 121 IDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLRWQEALFLLLIFPVIIFFFVILGLAAQKRADNEYRNF-TVLNNRFADT 199
Cdd:cd18585 102 IDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLGKKIGQQLVQLrAELRTELVDG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 200 LRGMQTLKQLGLSRIFTKRIYETSERY-----RKSTMRSLTIAMTSTFSldFFTTLSIAVIAVFLGFS-LMEGK------ 267
Cdd:cd18585 182 LQGMAELLIFGALERQRQQLEQLSDALikeqrRLARLSGLSQALMILLS--GLTVWLVLWLGAPLVQNgALDGAllamlv 259
|
170 180
....*....|....*....|
gi 488907140 268 ---MSLFPALTLLVLAPEYF 284
Cdd:cd18585 260 favLASFEAVAPLPLAFQYL 279
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
146-270 |
8.25e-05 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis 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: 349993 [Multi-domain] Cd Length: 295 Bit Score: 44.75 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 146 LIYMFFLRWQEALFLLLIFPVIIFFFVILGLAAQKRADNEYRNFTVLNNRFADTLRGMQTLKQLGLSRIFTKRIYETSER 225
Cdd:cd18549 134 FIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDR 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 488907140 226 YRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVFLGFSLMEGKMSL 270
Cdd:cd18549 214 FLESKKKAYKAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITL 258
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
459-547 |
1.32e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 459 GFDTMIGeseqSLSGGQAQRIALARaFLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENH--LVFFATHRLHWLKQM 536
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGR-WLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDkgIIIISSEMPELLGIT 458
|
90
....*....|.
gi 488907140 537 DYVLVMDNGHI 547
Cdd:PRK10982 459 DRILVMSNGLV 469
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
363-536 |
1.67e-04 |
|
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: 41.98 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 363 KVAVVGLSGSGKTTLLSSLAGINSGRGdisinrnkflnfqntswqKQIIYIpqkpyifhtslreniafyqpdapkeqvvk 442
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPG------------------GGVIYI----------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 443 aakaAGIYELASGLFNGFDTMIGESEQSLSGGQAQRIALARAfLASDRHILLFDEPTAHLDIQTEYDLKQ-------TML 515
Cdd:smart00382 37 ----DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALA-RKLKPDVLILDEITSLLDAEQEALLLLleelrllLLL 111
|
170 180
....*....|....*....|.
gi 488907140 516 PLLENHLVFFATHRLHWLKQM 536
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLGPA 132
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
146-281 |
2.04e-04 |
|
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: 43.70 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 146 LIYMFFLRWQEALFLLLIFPVIIFFfVILGLAAQKRADNEYRNFTV-LNNRFADTLRGMQTLKQLGLSRIFTKRIYETSE 224
Cdd:cd18568 133 LGLMFYYNLQLTLIVLAFIPLYVLL-TLLSSPKLKRNSREIFQANAeQQSFLVEALTGIATIKALAAERPIRWRWENKFA 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488907140 225 RYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIaVFLGFSL-MEGKMSL-----FPALTLLVLAP 281
Cdd:cd18568 212 KALNTRFRGQKLSIVLQLISSLINHLGTIAV-LWYGAYLvISGQLTIgqlvaFNMLFGSVINP 273
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
363-504 |
2.39e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 363 KVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFLNFQNTswQKQIIYIPQKPYIFHTSlRE--------NIAFYQP 433
Cdd:PRK10636 29 KVGLVGKNGCGKSTLLALLKNeISADGGSYTFPGNWQLAWVNQ--ETPALPQPALEYVIDGD-REyrqleaqlHDANERN 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488907140 434 D----APKEQVVKAAKAAGIYELASGLFNGF---DTMIGESEQSLSGGQAQRIALARAFLA-SDrhILLFDEPTAHLDI 504
Cdd:PRK10636 106 DghaiATIHGKLDAIDAWTIRSRAASLLHGLgfsNEQLERPVSDFSGGWRMRLNLAQALICrSD--LLLLDEPTNHLDL 182
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
469-556 |
2.58e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 469 QS---LSGGQAQRIALARaFLA---SDRHILLFDEPTA--HLDiqteyDLKQtmlpLLEnhlVFfatHRL---------- 530
Cdd:COG0178 822 QPattLSGGEAQRVKLAS-ELSkrsTGKTLYILDEPTTglHFH-----DIRK----LLE---VL---HRLvdkgntvvvi 885
|
90 100 110
....*....|....*....|....*....|....*.
gi 488907140 531 -HWL---KQMDYVLVM-----DN-GHIIEQGRPREL 556
Cdd:COG0178 886 eHNLdviKTADWIIDLgpeggDGgGEIVAEGTPEEV 921
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
470-505 |
2.82e-04 |
|
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: 42.17 E-value: 2.82e-04
10 20 30
....*....|....*....|....*....|....*.
gi 488907140 470 SLSGGQAQRIALArAFLASDRHILLFDEPTAHLDIQ 505
Cdd:cd03222 71 DLSGGELQRVAIA-AALLRNATFYLFDEPSAYLDIE 105
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
110-269 |
2.83e-04 |
|
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: 43.24 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 110 TGHAVSLLHAGIDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLRWQEALFLLLIFPVIIFFFVILGLAAQKRADNEYRNF 189
Cdd:cd18576 92 VGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDEL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 190 TVLNNRFADTLRGMQTLKqlglsrIFTKRIYEtSERYRKSTMRSLTIAMT-----STFS--LDFFTTLSIAVIAVFLGFS 262
Cdd:cd18576 172 AEANTIVEETLQGIRVVK------AFTREDYE-IERYRKALERVVKLALKrarirALFSsfIIFLLFGAIVAVLWYGGRL 244
|
....*..
gi 488907140 263 LMEGKMS 269
Cdd:cd18576 245 VLAGELT 251
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
357-573 |
3.48e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 357 LVRGfAKVAVVGLSGSGKTTLLSSLAG-INSGRGDISINRNKFLNFQNtswQKQIIYipqkpyifhtsLRENiafyqpDA 435
Cdd:PRK10636 335 LVPG-SRIGLLGRNGAGKSTLIKLLAGeLAPVSGEIGLAKGIKLGYFA---QHQLEF-----------LRAD------ES 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 436 PKEQVVKAAKAAGIYELASGL----FNGfDTMIGESEQsLSGGQAQRIALAraFLASDR-HILLFDEPTAHLDIqteyDL 510
Cdd:PRK10636 394 PLQHLARLAPQELEQKLRDYLggfgFQG-DKVTEETRR-FSGGEKARLVLA--LIVWQRpNLLLLDEPTNHLDL----DM 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488907140 511 KQTMLPLL---ENHLVfFATHRLHWLKQmdyvlVMDNGHIIEQGRprelLEDFDGKLNELRKELTD 573
Cdd:PRK10636 466 RQALTEALidfEGALV-VVSHDRHLLRS-----TTDDLYLVHDGK----VEPFDGDLEDYQQWLSD 521
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
332-519 |
3.53e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPDGQqpaALKDINFLV-RGfAKVAVVGLSGSGKTTLLSSLAG---INSGRgdisINRNKFLN---FQnt 404
Cdd:PRK11147 319 VFEMENVNYQIDGKQ---LVKDFSAQVqRG-DKIALIGPNGCGKTTLLKLMLGqlqADSGR----IHCGTKLEvayFD-- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 405 swQKQIIYIPQKpyifhtSLRENIAfyqpDAPKEQVVKAAKAAGIYELASGLFNGFDTMIgeSEQSLSGGQAQRIALARA 484
Cdd:PRK11147 389 --QHRAELDPEK------TVMDNLA----EGKQEVMVNGRPRHVLGYLQDFLFHPKRAMT--PVKALSGGERNRLLLARL 454
|
170 180 190
....*....|....*....|....*....|....*
gi 488907140 485 FLASDrHILLFDEPTAHLDIQTeydlkqtmLPLLE 519
Cdd:PRK11147 455 FLKPS-NLLILDEPTNDLDVET--------LELLE 480
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
107-270 |
5.49e-04 |
|
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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 42.08 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 107 KTGTGHAVSLLHAGIDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLRWQEALFLLLIFPVIIFFFVILGLAAQKRADNEY 186
Cdd:cd18550 92 RTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 187 RNFTVLNNRFADTLR--GMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVFLGFSLM 264
Cdd:cd18550 172 EKLAELNSIMQETLSvsGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVI 251
|
....*.
gi 488907140 265 EGKMSL 270
Cdd:cd18550 252 GGGLTI 257
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
469-504 |
8.82e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 8.82e-04
10 20 30
....*....|....*....|....*....|....*..
gi 488907140 469 QSLSGGQAQRIALARA-FLASDrhILLFDEPTAHLDI 504
Cdd:PLN03073 343 KTFSGGWRMRIALARAlFIEPD--LLLLDEPTNHLDL 377
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
129-281 |
9.75e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. 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 I 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). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 41.34 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 129 QLIFIkIIDLSIIPwLLLIYMFFLRWQEALFLLLIFPVIIFFFVILGLAAQKRADNEYRNFTVLNNRFADTLRGMQTLKQ 208
Cdd:cd18555 118 QVISL-IIDLLLLV-IYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKS 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 209 LGLSRIFTKR---IYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVFLgfsLMEGKMSL-----FPALTLLVLA 280
Cdd:cd18555 196 LGSEKNIYKKwenLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYL---VINGELTLgeliaFSSLAGSFLT 272
|
.
gi 488907140 281 P 281
Cdd:cd18555 273 P 273
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
332-530 |
1.75e-03 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 41.54 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 332 VLSVHNFSFQYPDGQQPAaLKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINS-GRGDISINRNKFLNfqNTSWQKQI 410
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSPA-VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTvTSGDATVAGKSILT--NISDVHQN 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 411 I-YIPQKPYIFHT-SLRENIAFYQP--DAPKEQVVKAAKAaGIYELASGLFNgfDTMIGeseqSLSGGQAQRIALARAFL 486
Cdd:TIGR01257 2014 MgYCPQFDAIDDLlTGREHLYLYARlrGVPAEEIEKVANW-SIQSLGLSLYA--DRLAG----TYSGGNKRKLSTAIALI 2086
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488907140 487 ASDRhILLFDEPTAHLDIQTEYDLKQTMLPLL-ENHLVFFATHRL 530
Cdd:TIGR01257 2087 GCPP-LVLLDEPTTGMDPQARRMLWNTIVSIIrEGRAVVLTSHSM 2130
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
471-553 |
1.84e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 40.36 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 471 LSGGQAQRIALARAFLASDRhILLFDEPTAHLDIQTEYDLKQTMLPLLENHLVFFAthrlhwLKQMDYVLVM---DNGHI 547
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPE-ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVL------LIEHDMKLVMgisDRIYV 226
|
....*.
gi 488907140 548 IEQGRP 553
Cdd:PRK11300 227 VNQGTP 232
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
146-269 |
2.73e-03 |
|
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: 350019 [Multi-domain] Cd Length: 289 Bit Score: 40.16 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 146 LIYMFFLRWQEALFLLLIFPVIIFFFVILG-------LAAQKR-ADneyrnftvLNNRFADTLRGMQTLKqlglsrIFTK 217
Cdd:cd18575 128 LVMLFITSPKLTLLVLLVIPLVVLPIILFGrrvrrlsRASQDRlAD--------LSAFAEETLSAIKTVQ------AFTR 193
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488907140 218 RIYEtSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVFLGFSL-------MEGKMS 269
Cdd:cd18575 194 EDAE-RQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLwlgahdvLAGRMS 251
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
464-557 |
2.75e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 464 IGESEQSLSGGQAQRIALARAFLASDRHILLF--DEPTAHLDIQTEYDLKQTMLPLL-ENHLVFFATHRLHWLKQMDYVL 540
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYLPPKHPTLFllDEIATSLDNQQKSALLVQLRTLVsLGHSVIYIDHDPALLKQADYLI 1772
|
90 100
....*....|....*....|...
gi 488907140 541 VMD------NGHIIEQGRPRELL 557
Cdd:PRK00635 1773 EMGpgsgktGGKILFSGPPKDIS 1795
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
351-503 |
3.74e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.21 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 351 LKDINFLVRGFAKVAVVGLSGSGKTTLLSSLAGINSG---RGDISInrNKFLNFQNT------SWQKQIIYIPQkpyifh 421
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyiEGDIRI--SGFPKKQETfarisgYCEQNDIHSPQ------ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 422 TSLRENI---AFYQpdAPKEqVVKAAKAAGIYELAS--GLFNGFDTMIG-ESEQSLSGGQAQRIALARAFLASDRhILLF 495
Cdd:PLN03140 968 VTVRESLiysAFLR--LPKE-VSKEEKMMFVDEVMElvELDNLKDAIVGlPGVTGLSTEQRKRLTIAVELVANPS-IIFM 1043
|
....*...
gi 488907140 496 DEPTAHLD 503
Cdd:PLN03140 1044 DEPTSGLD 1051
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
116-270 |
3.99e-03 |
|
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: 39.37 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 116 LLHAGIDN-VQNYFQLIFIKIIdlsiipwllliyMFFLRWQEALFLLLIFPVIIFFFVILGLAAQKRADNEYRNFTVLNN 194
Cdd:cd18545 113 LLSNGLINlIPDLLTLVGIVII------------MFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNA 180
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488907140 195 RFADTLRGMQTLKQLGLSRIFTKRIYETSERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVFLGFSLMEGKMSL 270
Cdd:cd18545 181 YLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGGAITV 256
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
364-528 |
5.48e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.22 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 364 VAVVGLSGSGKTTLLSSLAGINSGRGDISINRNKFLNFQNTSWQKQIIYIpqkpyIFHTSLRENIAFYQPDAPKEQVVKA 443
Cdd:COG3593 26 TVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIEL-----TFGSLLSRLLRLLLKEEDKEELEEA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 444 AK------AAGIYELASGLFNGFDTMIGESE-----------------------------QSLSGGQAQRI------ALA 482
Cdd:COG3593 101 LEelneelKEALKALNELLSEYLKELLDGLDlelelsldeledllkslslriedgkelplDRLGSGFQRLIllallsALA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488907140 483 RAFLASDRHILLFDEPTAHLDIQTEYDLKQTMLPLLENHL-VFFATH 528
Cdd:COG3593 181 ELKRAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNqVIITTH 227
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
465-568 |
5.55e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 39.33 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 465 GESEQSLSGGQAQRIALARAFLASDRhILLFDEPTAHLDIQTEYDLKQTMLPLLEN-HLVFFATHRLHWLKQMDYVL-VM 542
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPA-VLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLAHELtVI 217
|
90 100
....*....|....*....|....*.
gi 488907140 543 DNGHIIEQGRPRELLEDFDGKLNELR 568
Cdd:NF000106 218 DRGRVIADGKVDELKTKVGGRTLQIR 243
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
146-270 |
6.32e-03 |
|
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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 39.03 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 146 LIYMFFLRWQEALFLLLIFPViiFFFVILGLAAQ-KRADNEYRNFT-VLNNRFADTLRGMQTLKQLGLSRIFTKRIYETS 223
Cdd:cd18564 146 LGVMFWLDWQLALIALAVAPL--LLLAARRFSRRiKEASREQRRREgALASVAQESLSAIRVVQAFGREEHEERRFAREN 223
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 488907140 224 ERYRKSTMRSLTIAMTSTFSLDFFTTLSIAVIAVFLGFSLMEGKMSL 270
Cdd:cd18564 224 RKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTP 270
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
18-279 |
7.84e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350037 [Multi-domain] Cd Length: 291 Bit Score: 38.74 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 18 WLVLLTFLQAVSILFQAFFLSKSIVILWH-QSAFSSAVPYIFGFAISLLC--------RHFFSLIKEGsaNSFSVTASeG 88
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRYFEGnGSSISLTEAYLYAGGVSLCSflfiithhPYFFGMQRIG--MRLRVACS-S 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 89 LrdqLLGKYLSFGDQTIFKTGTGHAVSLLhagiDNVQNYFQLIFIKIIDLSIIPWLLLIYMFFLrWQE--------ALFL 160
Cdd:cd18593 78 L---IYRKALRLSQAALGKTTVGQIVNLL----SNDVNRFDQAVLFLHYLWVAPLQLIAVIYIL-WFEigwsclagLAVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488907140 161 LLIFPVIIFF---FVILGLAAQKRADNEYRnftVLNnrfaDTLRGMQTLKQLGLSRIFTKRIyetsERYRKSTMRSLtia 237
Cdd:cd18593 150 LILIPLQSFFgklFSKLRRKTAARTDKRIR---IMN----EIINGIRVIKMYAWEKAFAKLV----DDLRRKEIKKV--- 215
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 488907140 238 MTSTFsldffttlsiaVIAVFLGFSLMEGKMSLFPALTLLVL 279
Cdd:cd18593 216 RRTSF-----------LRALNMGLFFVSSKLILFLTFLAYIL 246
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
478-506 |
8.22e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.10 E-value: 8.22e-03
10 20
....*....|....*....|....*....
gi 488907140 478 RIALARAfLASDRHILLFDEPTAHLDIQT 506
Cdd:PRK15064 163 RVLLAQA-LFSNPDILLLDEPTNNLDINT 190
|
|
| |
