|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-492 |
1.34e-87 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 278.10 E-value: 1.34e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 6 IQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQET-YQGKISKD----VEFIK----FPPNISd 76
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEpDSGEVSIPkglrIGYLPqeppLDDDLT- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 77 tsklgidLYKELISDDEE-WKLFRELNL----------------------------------------LNVDENLVYREF 115
Cdd:COG0488 78 -------VLDTVLDGDAElRALEAELEEleaklaepdedlerlaelqeefealggweaearaeeilsgLGFPEEDLDRPV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 116 KTLSKGEQTKILLA-ILFTKEDgFLLIDEPTNHLDMNGRKILSEYLKSKKG-FLLISHDRNFLDGCINHVISINRNSIDV 193
Cdd:COG0488 151 SELSGGWRRRVALArALLSEPD-LLLLDEPTNHLDLESIEWLEEFLKNYPGtVLVVSHDRYFLDRVATRILELDRGKLTL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 194 QSGNFTSWYENKLMKDKFEISKNEKLRKDIKRLKEAARQSKiwsdkientkngVKVSGIKPDKGRIghqsakmmkksknl 273
Cdd:COG0488 230 YPGNYSAYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFR------------AKARKAKQAQSRI-------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 274 ehrqnKAIEEkqslLKDIEIKESLLLHPLHHHK-----NPLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGK 348
Cdd:COG0488 284 -----KALEK----LEREEPPRRDKTVEIRFPPperlgKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGK 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 349 STLIKILLGINHEYTGEIKLASNLKISYIPQDTSNLSGSLN--EYIhsQDVDETLCKTILRKL--DFareLFEMDMI--- 421
Cdd:COG0488 355 STLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTvlDEL--RDGAPGGTEQEVRGYlgRF---LFSGDDAfkp 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493786691 422 --DYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKPTLIFVEHDKRFVEDIANKIIQF 492
Cdd:COG0488 430 vgVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEF 502
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
310-492 |
3.94e-40 |
|
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: 141.43 E-value: 3.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIPQdtsnLSGsln 389
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----LSG--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 390 eyihsqdvdetlcktilrkldfarelfemdmidysdGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAK 469
Cdd:cd03221 74 ------------------------------------GEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYP 117
|
170 180
....*....|....*....|...
gi 493786691 470 PTLIFVEHDKRFVEDIANKIIQF 492
Cdd:cd03221 118 GTVILVSHDRYFLDQVATKIIEL 140
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-189 |
2.20e-38 |
|
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: 136.81 E-value: 2.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLnqetyqGKISKDVEFIKFPPNIsdtsklgid 83
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIA------GELEPDEGIVTWGSTV--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 84 lykelisddeewklfrelnllnvdeNLVYreFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGRKILSEYLKSK 163
Cdd:cd03221 64 -------------------------KIGY--FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEY 116
|
170 180
....*....|....*....|....*..
gi 493786691 164 KG-FLLISHDRNFLDGCINHVISINRN 189
Cdd:cd03221 117 PGtVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-492 |
7.90e-37 |
|
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: 142.77 E-value: 7.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 14 YGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL--LNQEtYQGKI-------------------SKDVEfikfpP 72
Cdd:TIGR03719 14 VPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagVDKD-FNGEArpqpgikvgylpqepqldpTKTVR-----E 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 73 NISDTSKLGIDLYKEL--IS------DDEEWKLFRE----------LNLLNVDENL-----VYR------EFKTLSKGEQ 123
Cdd:TIGR03719 88 NVEEGVAEIKDALDRFneISakyaepDADFDKLAAEqaelqeiidaADAWDLDSQLeiamdALRcppwdaDVTKLSGGER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 124 TKILLAILFTKEDGFLLIDEPTNHLDMNGRKILSEYLKSKKG-FLLISHDRNFLDGCINHVISINRNSIDVQSGNFTSWY 202
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGtVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 203 ENKLMKDKFEISKNEKLRKDIKRLKEAARQSKiwsdkientkngvkvsgikpdKGRIGHQSAKMMKKSKNLEHRQNKAIE 282
Cdd:TIGR03719 248 EQKQKRLEQEEKEESARQKTLKRELEWVRQSP---------------------KGRQAKSKARLARYEELLSQEFQKRNE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 283 EKQsllkdIEIKESlllhplHHHKNPLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEY 362
Cdd:TIGR03719 307 TAE-----IYIPPG------PRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 363 TGEIKLASNLKISYIPQDTSNLSGSLNEYihsQDVDETLCKTILRKldfarelFEMDMIDY--------SDGQKK----- 429
Cdd:TIGR03719 376 SGTIEIGETVKLAYVDQSRDALDPNKTVW---EEISGGLDIIKLGK-------REIPSRAYvgrfnfkgSDQQKKvgqls 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493786691 430 -----KVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKPTLIFVEHDKRFVEDIANKIIQF 492
Cdd:TIGR03719 446 ggernRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAF 513
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-479 |
6.54e-36 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 141.08 E-value: 6.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 17 VKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLlnqetyQGKISKDVEFIKFPPNIS------DTSKLGIDLYKELIS 90
Cdd:PRK10636 13 VRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL------KNEISADGGSYTFPGNWQlawvnqETPALPQPALEYVID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 91 DDEEWK-LFRELNLLNV--DENLV---------------------------------YREFKTLSKGEQTKILLAILFTK 134
Cdd:PRK10636 87 GDREYRqLEAQLHDANErnDGHAIatihgkldaidawtirsraasllhglgfsneqlERPVSDFSGGWRMRLNLAQALIC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 135 EDGFLLIDEPTNHLDMNGRKILSEYLKSKKGFL-LISHDRNFLDGCINHVISINRNSIDVQSGNFTSwyenklmkdkFEI 213
Cdd:PRK10636 167 RSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLiLISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSS----------FEV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 214 SKNEKLRKdikrlKEAARQSKiwSDKIENTKNGVKVSGIKPDKGRIGHQSAKMMKKSKNLE--HRQNK---AIEEKQSLL 288
Cdd:PRK10636 237 QRATRLAQ-----QQAMYESQ--QERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIApaHVDNPfhfSFRAPESLP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 289 kdieikeslllhplhhhkNPLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL 368
Cdd:PRK10636 310 ------------------NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 369 ASNLKISYIPQDTSnlsgslnEYIHSqdvDETLCKTILRkldFARELFEMDMIDY------------------SDGQKKK 430
Cdd:PRK10636 372 AKGIKLGYFAQHQL-------EFLRA---DESPLQHLAR---LAPQELEQKLRDYlggfgfqgdkvteetrrfSGGEKAR 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 493786691 431 VLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKPTLIFVEHDK 479
Cdd:PRK10636 439 LVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDR 487
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-490 |
7.17e-35 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 136.95 E-value: 7.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 18 KPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL------------LNQETYQGKISKD-VEFIKFppNISDTSKLGidl 84
Cdd:PRK15064 14 KPLFENISVKFGGGNRYGLIGANGCGKSTFMKILggdlepsagnvsLDPNERLGKLRQDqFAFEEF--TVLDTVIMG--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 85 YKEL---------------ISDDEEWKL------FRELN-----------LLNV--DENLVYREFKTLSKGEQTKILLA- 129
Cdd:PRK15064 89 HTELwevkqerdriyalpeMSEEDGMKVadlevkFAEMDgytaearagelLLGVgiPEEQHYGLMSEVAPGWKLRVLLAq 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 130 ILFTKEDgFLLIDEPTNHLDMNGRKILSEYLKSKKG-FLLISHDRNFLDGCINHVISINRNSIDVQSGNFTSWYE----- 203
Cdd:PRK15064 169 ALFSNPD-ILLLDEPTNNLDINTIRWLEDVLNERNStMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTaatqa 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 204 -NKLMKDkfeiskNEKLRKDIKRLKE-AARQSKIWSDKIENTKNGVKVSGIKPDKgrighqsakmMKKSKnlehRQNKAI 281
Cdd:PRK15064 248 rERLLAD------NAKKKAQIAELQSfVSRFSANASKAKQATSRAKQIDKIKLEE----------VKPSS----RQNPFI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 282 EEKQSllkdieikeslllhpLHHHKNPLIsVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHE 361
Cdd:PRK15064 308 RFEQD---------------KKLHRNALE-VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 362 YTGEIKLASNLKISYIPQDTS-------NLSGSLNEYIHSQDvDETLCKTILRKLdfareLFEMDMID-----YSDGQKK 429
Cdd:PRK15064 372 DSGTVKWSENANIGYYAQDHAydfendlTLFDWMSQWRQEGD-DEQAVRGTLGRL-----LFSQDDIKksvkvLSGGEKG 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493786691 430 KVLIA-LSLSKPAHLfIWDEPLNYIDVISriqIEEI---IKEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:PRK15064 446 RMLFGkLMMQKPNVL-VMDEPTNHMDMES---IESLnmaLEKYEGTLIFVSHDREFVSSLATRII 506
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
310-490 |
1.65e-34 |
|
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: 127.13 E-value: 1.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL----------ASNLKISYIPQ 379
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkdikkepeEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 380 DTS---NLSGslneyihsqdvdetlcktilrkldfarelfeMDMIDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVI 456
Cdd:cd03230 81 EPSlyeNLTV-------------------------------RENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190
....*....|....*....|....*....|....*..
gi 493786691 457 SRIQIEEIIKEAK---PTLIFVEHDKRFVEDIANKII 490
Cdd:cd03230 130 SRREFWELLRELKkegKTILLSSHILEEAERLCDRVA 166
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
306-490 |
3.47e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 128.67 E-value: 3.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 306 KNPLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL------ASNLKISYIPQ 379
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 380 dtsnlsgslneyihSQDVDETLCKT-----------------ILRKLDFAR--ELFE-MDMIDYSD--------GQKKKV 431
Cdd:COG1121 83 --------------RAEVDWDFPITvrdvvlmgrygrrglfrRPSRADREAvdEALErVGLEDLADrpigelsgGQQQRV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493786691 432 LIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKE---AKPTLIFVEHDKRFVEDIANKII 490
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElrrEGKTILVVTHDLGAVREYFDRVL 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
311-490 |
2.10e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 120.33 E-value: 2.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 311 SVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA------SNLKISYIPQDTS-- 382
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFgkplekERKRIGYVPQRRSid 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 383 ---NLSG----SLNEYIHS-----------QDVDETLCKTILrkLDFA-RELFEMdmidySDGQKKKVLIALSLSKPAHL 443
Cdd:cd03235 81 rdfPISVrdvvLMGLYGHKglfrrlskadkAKVDEALERVGL--SELAdRQIGEL-----SGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493786691 444 FIWDEPLNYIDVISRIQIEEIIKEAKP---TLIFVEHDKRFVEDIANKII 490
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVL 203
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-483 |
2.74e-30 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 124.29 E-value: 2.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 1 MSAIKIQN--LTFSYYgyvkPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL---------------------LNQ--- 54
Cdd:PRK11147 1 MSLISIHGawLSFSDA----PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILngevllddgriiyeqdlivarLQQdpp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 55 ----------------------ETYQgKISKDVEFIKFPPNISDTSKLgidlyKELISDDEEWKLFRELN----LLNVDE 108
Cdd:PRK11147 77 rnvegtvydfvaegieeqaeylKRYH-DISHLVETDPSEKNLNELAKL-----QEQLDHHNLWQLENRINevlaQLGLDP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 109 NlvyREFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGRKILSEYLKSKKGFLL-ISHDRNFLDGCINHVISIN 187
Cdd:PRK11147 151 D---AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIfISHDRSFIRNMATRIVDLD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 188 RnsidvqsGNFTSWYENklmKDKFEISKNEKLRkdIKRLKEAA-----RQSKIWsdkienTKNGVKVSGIKpDKGRIGHQ 262
Cdd:PRK11147 228 R-------GKLVSYPGN---YDQYLLEKEEALR--VEELQNAEfdrklAQEEVW------IRQGIKARRTR-NEGRVRAL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 263 SAKMMKKSKNLEhRQNKAieekqsllkDIEIKESLLLHPLhhhknpLISVSELSAHYGERQILSNLSFEIEQGDIVAISG 342
Cdd:PRK11147 289 KALRRERSERRE-VMGTA---------KMQVEEASRSGKI------VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 343 RNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIPQdtsnlsgslneyiHSQDVDETlcKTILRKL------------- 409
Cdd:PRK11147 353 PNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQ-------------HRAELDPE--KTVMDNLaegkqevmvngrp 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 410 --------DFareLFE----MDMID-YSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKPTLIFVE 476
Cdd:PRK11147 418 rhvlgylqDF---LFHpkraMTPVKaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVS 494
|
....*..
gi 493786691 477 HDKRFVE 483
Cdd:PRK11147 495 HDRQFVD 501
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-203 |
2.99e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 123.25 E-value: 2.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQET-YQGKIskdvefikfppNISDTSKLGi 82
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEpDSGTV-----------KLGETVKIG- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 83 dlY--KELISDDEEWKLFRELNLLNVDEN-------L---------VYREFKTLSKGEQTKILLAILFTKEDGFLLIDEP 144
Cdd:COG0488 382 --YfdQHQEELDPDKTVLDELRDGAPGGTeqevrgyLgrflfsgddAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 145 TNHLDMNGRKILSEYLKSKKG-FLLISHDRNFLDGCINHVISINRNSIDVQSGNFTSWYE 203
Cdd:COG0488 460 TNHLDIETLEALEEALDDFPGtVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
311-492 |
5.91e-30 |
|
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: 114.26 E-value: 5.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 311 SVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIklasnlkisyipqdtsnlsgslne 390
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 391 YIHSQDVDETLCKTILRKLDFARELfemdmidySDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEA-- 468
Cdd:cd00267 57 LIDGKDIAKLPLEELRRRIGYVPQL--------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELae 128
|
170 180
....*....|....*....|....*
gi 493786691 469 -KPTLIFVEHDKRFVEDIANKIIQF 492
Cdd:cd00267 129 eGRTVIIVTHDPELAELAADRVIVL 153
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
310-490 |
4.50e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 114.39 E-value: 4.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL--------ASNLK--ISYIPQ 379
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgedvardPAEVRrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 380 DTS---NLSGSLN-EYI-----HSQDVDETLCKTILRKL---DFARELFEmdmiDYSDGQKKKVLIALSLSKPAHLFIWD 447
Cdd:COG1131 81 EPAlypDLTVRENlRFFarlygLPRKEARERIDELLELFgltDAADRKVG----TLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493786691 448 EPLNYIDVISRIQIEEIIKEAKP---TLIFVEHDKRFVEDIANKII 490
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCDRVA 202
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
309-490 |
6.67e-29 |
|
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: 114.18 E-value: 6.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEI----------KLASNLKISYIP 378
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedvrkePREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 379 QDT---SNLSGSlnEYI------HSQDVDEtlcktILRKLDFARELFEMDMI------DYSDGQKKKVLIALSLSKPAHL 443
Cdd:COG4555 81 DERglyDRLTVR--ENIryfaelYGLFDEE-----LKKRIEELIELLGLEEFldrrvgELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493786691 444 FIWDEPLNYIDVISRIQIEEIIKEAKP---TLIFVEHDKRFVEDIANKII 490
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRVV 203
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
309-490 |
1.09e-28 |
|
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: 112.98 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHY----GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNL------------ 372
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 373 --KISYIPQDTSNlsgSLN----------E--YIHSQDVDETLCKTILRKLDFARELFEmDMIDY-----SDGQKKKVLI 433
Cdd:cd03257 81 rkEIQMVFQDPMS---SLNprmtigeqiaEplRIHGKLSKKEARKEAVLLLLVGVGLPE-EVLNRyphelSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493786691 434 ALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKP----TLIFVEHDKRFVEDIANKII 490
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelglTLLFITHDLGVVAKIADRVA 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
309-478 |
2.06e-26 |
|
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: 107.44 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA----SNL-------KISYI 377
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgrdlASLsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 378 PQDTSNLSG-------SLNEYIHS------QDVDETLCKTILRKLD---FA-RELFEMdmidySDGQKKKVLIALSLSKP 440
Cdd:COG1120 81 PQEPPAPFGltvrelvALGRYPHLglfgrpSAEDREAVEEALERTGlehLAdRPVDEL-----SGGERQRVLIARALAQE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493786691 441 AHLFIWDEPLNYIDVISRIQIEEIIK----EAKPTLIFVEHD 478
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRrlarERGRTVVMVLHD 197
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-492 |
1.21e-25 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 110.28 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 34 TGLIGRNGIGKSTLFKLLLNQET-----YQGKISKDvEFIKFppnISDT------SKLG------------IDLY----- 85
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIpnlgdYEEEPSWD-EVLKR---FRGTelqnyfKKLYngeikvvhkpqyVDLIpkvfk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 86 ---KELISDDEEWKLFREL-NLLNVdENLVYREFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLD----MNGRKILS 157
Cdd:PRK13409 178 gkvRELLKKVDERGKLDEVvERLGL-ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqrLNVARLIR 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 158 EYLKSKKgFLLISHDRNFLD----------------GCINHVISiNRNSIdvqsgnftswyenklmkdkfeiskNEKLRK 221
Cdd:PRK13409 257 ELAEGKY-VLVVEHDLAVLDyladnvhiaygepgayGVVSKPKG-VRVGI------------------------NEYLKG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 222 dikRLKEaarqskiwsdkiENTkngvkvsgikpdkgRIghqsakmmkksknlehrqnkaieekqsllKDIEIKESLLLHP 301
Cdd:PRK13409 311 ---YLPE------------ENM--------------RI-----------------------------RPEPIEFEERPPR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 302 LHHHKNPLISVSELSAHYGERQiLSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKlaSNLKISYIPQD- 380
Cdd:PRK13409 333 DESERETLVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--PELKISYKPQYi 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 381 TSNLSGSLNEYIHSQ--DVDETLCKT-ILRKLDFAReLFEMDMIDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVIS 457
Cdd:PRK13409 410 KPDYDGTVEDLLRSItdDLGSSYYKSeIIKPLQLER-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 488
|
490 500 510
....*....|....*....|....*....|....*....
gi 493786691 458 RIQ----IEEIIKEAKPTLIFVEHDKRFVEDIANKIIQF 492
Cdd:PRK13409 489 RLAvakaIRRIAEEREATALVVDHDIYMIDYISDRLMVF 527
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-490 |
1.81e-25 |
|
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: 109.22 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 1 MS-AIKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQETYQGKISKDVEFikfppNISDTSK 79
Cdd:COG1123 1 MTpLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLL-----DGRDLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 80 LGIDLYKELIS----------------------------DDEEWK-----LFRELNLlnvdENLVYREFKTLSKGEQTKI 126
Cdd:COG1123 76 LSEALRGRRIGmvfqdpmtqlnpvtvgdqiaealenlglSRAEARarvleLLEAVGL----ERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 127 LLAILFTKEDGFLLIDEPTNHLDMNGRKILSEYLKS-----KKGFLLISHDRNFLDGCINHVISINRNSIdvqsgnftsw 201
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqrerGTTVLLITHDLGVVAEIADRVVVMDDGRI---------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 202 yenklmkdkFEISKNEKLRKDIKRLKEAarqskiwsdkientkngvkvsgikPDKGRIGHQSAKMMKKSKnlehrqnkai 281
Cdd:COG1123 222 ---------VEDGPPEEILAAPQALAAV------------------------PRLGAARGRAAPAAAAAE---------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 282 eekqsllkdieikeslllhplhhhknPLISVSELSAHY-----GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILL 356
Cdd:COG1123 259 --------------------------PLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLL 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 357 GINHEYTGEIKLA----SNL----------KISYIPQDTsnlSGSLNEYiHS--QDVDETLckTILRKLDFA------RE 414
Cdd:COG1123 313 GLLRPTSGSILFDgkdlTKLsrrslrelrrRVQMVFQDP---YSSLNPR-MTvgDIIAEPL--RLHGLLSRAerrervAE 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 415 LFEM-----DMIDY-----SDGQKKKVLIA--LSLsKPAhLFIWDEPLNYIDVISRIQIEEIIKEAKP----TLIFVEHD 478
Cdd:COG1123 387 LLERvglppDLADRyphelSGGQRQRVAIAraLAL-EPK-LLILDEPTSALDVSVQAQILNLLRDLQRelglTYLFISHD 464
|
570
....*....|..
gi 493786691 479 KRFVEDIANKII 490
Cdd:COG1123 465 LAVVRYIADRVA 476
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
307-485 |
2.14e-25 |
|
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: 104.40 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 307 NPLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTG----------------EIK--- 367
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvrlfgerrggedvwELRkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 368 -LASNLKISYIPQDTSN----LSG---SLNEYIHSQDVDETLCKTILRKLDFArELFEMDMIDYSDGQKKKVLIALSLSK 439
Cdd:COG1119 81 gLVSPALQLRFPRDETVldvvLSGffdSIGLYREPTDEQRERARELLELLGLA-HLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493786691 440 PAHLFIWDEPLNYIDVISRIQ----IEEIIKEAKPTLIFVEHdkrFVEDI 485
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELllalLDKLAAEGAPTLVLVTH---HVEEI 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
308-484 |
2.85e-25 |
|
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: 102.94 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLkisyIPQDTSNLSGS 387
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP----IRDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 388 LNeYI-HSQDVDETLckTILRKLDFARELF--------------EMDMIDYSD--------GQKKKVLIALSLSKPAHLF 444
Cdd:COG4133 77 LA-YLgHADGLKPEL--TVRENLRFWAALYglradreaidealeAVGLAGLADlpvrqlsaGQKRRVALARLLLSPAPLW 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493786691 445 IWDEPLNYIDVISRIQIEEIIKE---AKPTLIFVEHDKRFVED 484
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAhlaRGGAVLLTTHQPLELAA 196
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
311-478 |
2.93e-25 |
|
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: 102.13 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 311 SVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA----SNLK-------ISYIPQ 379
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDgkdlASLSpkelarkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 380 dtsnlsgslneyihsqdvdetlcktILRKLDfARELFEMDMIDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRI 459
Cdd:cd03214 81 -------------------------ALELLG-LAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180
....*....|....*....|...
gi 493786691 460 QIEEIIKEAKP----TLIFVEHD 478
Cdd:cd03214 135 ELLELLRRLARergkTVVMVLHD 157
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
311-492 |
3.58e-25 |
|
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: 102.93 E-value: 3.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 311 SVSELSAHY--GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLAS-----------NLKISYI 377
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 378 PQDTSN-LSGSlneyihsqDVDETLC----------KTILRKLDFAreLFEMDMIDY--------SDGQKKKVLIALSLS 438
Cdd:cd03225 81 FQNPDDqFFGP--------TVEEEVAfglenlglpeEEIEERVEEA--LELVGLEGLrdrspftlSGGQKQRVAIAGVLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493786691 439 -KPAHLfIWDEPLNYIDVISRIQIEEIIKE---AKPTLIFVEHDKRFVEDIANKIIQF 492
Cdd:cd03225 151 mDPDIL-LLDEPTAGLDPAGRRELLELLKKlkaEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-492 |
3.87e-25 |
|
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: 108.72 E-value: 3.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 3 AIKIQNL---------------TFSYYGYVKPIFENVsfsfdtnwkTGLIGRNGIGKSTLFKLLLNQET-----YQGKIS 62
Cdd:COG1245 65 AISIVNLpeeleedpvhrygenGFRLYGLPVPKKGKV---------TGILGPNGIGKSTALKILSGELKpnlgdYDEEPS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 63 KDvEFIKFppnISDT------SKLG------------IDLY--------KELISDDEEWKLFRELN-LLNVdENLVYREF 115
Cdd:COG1245 136 WD-EVLKR---FRGTelqdyfKKLAngeikvahkpqyVDLIpkvfkgtvRELLEKVDERGKLDELAeKLGL-ENILDRDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 116 KTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGR----KILSEYLKSKKGFLLISHDRNFLDgcinhvisinrnsi 191
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRlnvaRLIRELAEEGKYVLVVEHDLAILD-------------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 192 dvqsgnftswyenkLMKDKFEISKNEklrkdikrlkEAARqskiwsdkientknGVkVSGIKPDKGRIGHqsakMMK--- 268
Cdd:COG1245 277 --------------YLADYVHILYGE----------PGVY--------------GV-VSKPKSVRVGINQ----YLDgyl 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 269 KSKNLEHRQnKAIEEKQSLLKDIEIKEslllhplhhhknPLISVSELSAHYGERQiLSNLSFEIEQGDIVAISGRNGSGK 348
Cdd:COG1245 314 PEENVRIRD-EPIEFEVHAPRREKEEE------------TLVEYPDLTKSYGGFS-LEVEGGEIREGEVLGIVGPNGIGK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 349 STLIKILLGINHEYTGEIKlaSNLKISYIPQD-TSNLSGSLNEYIHS---QDVDETLCKT-ILRKLDFAReLFEMDMIDY 423
Cdd:COG1245 380 TTFAKILAGVLKPDEGEVD--EDLKISYKPQYiSPDYDGTVEEFLRSantDDFGSSYYKTeIIKPLGLEK-LLDKNVKDL 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493786691 424 SDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIK----EAKPTLIFVEHDKRFVEDIANKIIQF 492
Cdd:COG1245 457 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRrfaeNRGKTAMVVDHDIYLIDYISDRLMVF 529
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-492 |
1.37e-24 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 106.74 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 14 YGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL--LNQEtYQGKIskdvefiKFPPNIS----------DTSK-- 79
Cdd:PRK11819 16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagVDKE-FEGEA-------RPAPGIKvgylpqepqlDPEKtv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 80 LGI----------------DLYKELISDDEEW-KLFRE----------LNLLNVDENL---------------VyrefKT 117
Cdd:PRK11819 88 RENveegvaevkaaldrfnEIYAAYAEPDADFdALAAEqgelqeiidaADAWDLDSQLeiamdalrcppwdakV----TK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 118 LSKGEQTKILLA-ILFTKEDgFLLIDEPTNHLDMNGRKILSEYLKSKKG-FLLISHDRNFLDGCINHVISINRNSIDVQS 195
Cdd:PRK11819 164 LSGGERRRVALCrLLLEKPD-MLLLDEPTNHLDAESVAWLEQFLHDYPGtVVAVTHDRYFLDNVAGWILELDRGRGIPWE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 196 GNFTSWYENKLMKDKFEISKNEKLRKDIKRLKEAARQSKiwsdkientkngvkvsgikpdKGRighQSakmmkKSK---- 271
Cdd:PRK11819 243 GNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWVRQSP---------------------KAR---QA-----KSKarla 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 272 NLEHRQNKAIEEKQSLLkDIEIkeslllhplhhhknP--------LISVSELSAHYGERQILSNLSFEIEQGDIVAISGR 343
Cdd:PRK11819 294 RYEELLSEEYQKRNETN-EIFI--------------PpgprlgdkVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 344 NGSGKSTLIKILLGINHEYTGEIKLASNLKISYIPQDTSNLsgslneyihsqDVDETLCKTILRKLDFAR-ELFEMDMID 422
Cdd:PRK11819 359 NGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDAL-----------DPNKTVWEEISGGLDIIKvGNREIPSRA 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 423 Y--------SDGQKK----------KVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKPTLIFVEHDKRFVED 484
Cdd:PRK11819 428 YvgrfnfkgGDQQKKvgvlsggernRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDR 507
|
....*...
gi 493786691 485 IANKIIQF 492
Cdd:PRK11819 508 IATHILAF 515
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
310-490 |
9.35e-24 |
|
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: 99.33 E-value: 9.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHY-GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL------ASNL-----KISYI 377
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdgkditKKNLrelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 378 PQDTSNlsgslneYIHSQDVDETLC----------KTILRKLDFARELFEMDmiDYSD--------GQKKKVLIA--LSL 437
Cdd:COG1122 81 FQNPDD-------QLFAPTVEEDVAfgpenlglprEEIRERVEEALELVGLE--HLADrpphelsgGQKQRVAIAgvLAM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493786691 438 sKPAHLfIWDEPLNYIDVISRIQIEEIIKE---AKPTLIFVEHDKRFVEDIANKII 490
Cdd:COG1122 152 -EPEVL-VLDEPTAGLDPRGRRELLELLKRlnkEGKTVIIVTHDLDLVAELADRVI 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
309-490 |
1.02e-23 |
|
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: 99.88 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGE----RQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNL-----------K 373
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPvtrrrrkafrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 374 ISYIPQD--TS-----NLSGSLNE--YIHSQDVDETLCKTILRKLDFARELFEMDMIDYSDGQKKKVLIALSLS-KPAhL 443
Cdd:COG1124 81 VQMVFQDpyASlhprhTVDRILAEplRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALIlEPE-L 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493786691 444 FIWDEPLNYIDVISRIQI----EEIIKEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:COG1124 160 LLLDEPTSALDVSVQAEIlnllKDLREERGLTYLFVSHDLAVVAHLCDRVA 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-188 |
1.71e-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: 98.37 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 5 KIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQET-YQGKISKDVEFIK-------------- 69
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKpTSGSIRVFGKPLEkerkrigyvpqrrs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 70 ----FPPNISDTSKLGIDLYKELIS--DDEEWKLFRELnLLNVD-ENLVYREFKTLSKGEQTKILLA-ILFTKEDgFLLI 141
Cdd:cd03235 79 idrdFPISVRDVVLMGLYGHKGLFRrlSKADKAKVDEA-LERVGlSELADRQIGELSGGQQQRVLLArALVQDPD-LLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493786691 142 DEPTNHLDMNGRKILSEYLKS----KKGFLLISHDRNFLDGCINHVISINR 188
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRElrreGMTILVVTHDLGLVLEYFDRVLLLNR 207
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
310-490 |
2.40e-23 |
|
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: 96.68 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGER--QILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL----ASNL-------KISY 376
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIdgvdLRDLdleslrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 377 IPQDTSNLSGSLNEyihsqdvdetlckTILrkldfarelfemdmidySDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVI 456
Cdd:cd03228 81 VPQDPFLFSGTIRE-------------NIL-----------------SGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180 190
....*....|....*....|....*....|....*.
gi 493786691 457 SRIQIEEIIKEAKP--TLIFVEHDKRFVEDiANKII 490
Cdd:cd03228 131 TEALILEALRALAKgkTVIVIAHRLSTIRD-ADRII 165
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
325-451 |
4.54e-23 |
|
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: 95.02 E-value: 4.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 325 LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL-----------ASNLKISYIPQDTS---------NL 384
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdltdderkSLRKEIGYVFQDPQlfprltvreNL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 385 SGSLNEYIHSQDVDETLCKTILRKL---DFARELFEMDMIDYSDGQKKKVLIALSLSKPAHLFIWDEPLN 451
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLglgDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
310-490 |
4.57e-23 |
|
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: 102.99 E-value: 4.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQ--ILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIK-------------LASNlkI 374
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqidpasLRRQ--I 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 375 SYIPQDTSNLSGSLNEYI--HSQDVDETLCKTILRK---LDFAREL---FEMDMID----YSDGQKKKVLIALSLSKPAH 442
Cdd:COG2274 552 GVVLQDVFLFSGTIRENItlGDPDATDEEIIEAARLaglHDFIEALpmgYDTVVGEggsnLSGGQRQRLAIARALLRNPR 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493786691 443 LFIWDEPLNYIDVISRIQIEEIIKEAKP--TLIFVEHDKRFVEDiANKII 490
Cdd:COG2274 632 ILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL-ADRII 680
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
310-490 |
6.16e-22 |
|
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: 92.64 E-value: 6.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIklasnlkisyipqdtsnlsgsln 389
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 390 eYIHSQDVD--ETLCKTILRKL-----DFAreLFE----MDMIDY--SDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVI 456
Cdd:cd03229 58 -LIDGEDLTdlEDELPPLRRRIgmvfqDFA--LFPhltvLENIALglSGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 493786691 457 SRIQIEEIIKEAKP----TLIFVEHDKRFVEDIANKII 490
Cdd:cd03229 135 TRREVRALLKSLQAqlgiTVVLVTHDLDEAARLADRVV 172
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-174 |
4.35e-21 |
|
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: 90.57 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 5 KIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLN-QETYQGKISKDVEFIKFPPNISDTSKLGId 83
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGlLKPSSGEILLDGKDLASLSPKELARKIAY- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 84 lykelisddeewkLFRELNLLNVdENLVYREFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGRKILSEYLKS- 162
Cdd:cd03214 78 -------------VPQALELLGL-AHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRl 143
|
170
....*....|....*.
gi 493786691 163 ----KKGFLLISHDRN 174
Cdd:cd03214 144 arerGKTVVMVLHDLN 159
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-455 |
7.29e-21 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 96.08 E-value: 7.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGYVKPIFENVSFSFDTNWktGLIGRNGIGKSTLFK---------------------------------- 49
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHY--GLVGRNGTGKTTFLRymamhaidgipkncqilhveqevvgddttalqcv 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 50 --------LLLNQETYQGKISKDVEFIKFPPNISDTSKLGID----------LYK--ELI-SDDEEWKLFRELNLLNVDE 108
Cdd:PLN03073 256 lntdiertQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDkdavsqrleeIYKrlELIdAYTAEARAASILAGLSFTP 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 109 NLVYREFKTLSKGEQTKILLA-ILFTKEDgFLLIDEPTNHLDMNGRKILSEYL-KSKKGFLLISHDRNFLDGCINHVISI 186
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALArALFIEPD-LLLLDEPTNHLDLHAVLWLETYLlKWPKTFIVVSHAREFLNTVVTDILHL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 187 NRNSIDVQSGNFtswyenklmkDKFEISKNEKLRKDIKRLK--EAARQS-KIWSDKIE-NTKNGVKV-SGIKPDKgRIGH 261
Cdd:PLN03073 415 HGQKLVTYKGDY----------DTFERTREEQLKNQQKAFEsnERSRSHmQAFIDKFRyNAKRASLVqSRIKALD-RLGH 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 262 QSAKMMKKSKNLEHrqnKAIEEKQSLlkdieikeslllhplhhhknPLISVSELSAHY-GERQILSNLSFEIEQGDIVAI 340
Cdd:PLN03073 484 VDAVVNDPDYKFEF---PTPDDRPGP--------------------PIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAM 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 341 SGRNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIPQ---DTSNLSGSLNEYIHS--QDVDETLCKTILRKLDFAREL 415
Cdd:PLN03073 541 VGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQhhvDGLDLSSNPLLYMMRcfPGVPEQKLRAHLGSFGVTGNL 620
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 493786691 416 FEMDMIDYSDGQKKKVLIA-LSLSKPaHLFIWDEPLNYIDV 455
Cdd:PLN03073 621 ALQPMYTLSGGQKSRVAFAkITFKKP-HILLLDEPSNHLDL 660
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-188 |
7.93e-21 |
|
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: 88.84 E-value: 7.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 5 KIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQET-YQGKIskdvEFikfppNISDTSKLGID 83
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEI----LI-----DGKDIAKLPLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 84 LYKELISddeewklfrelnllnvdenlvYREfkTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGRKILSEYLK-- 161
Cdd:cd00267 70 ELRRRIG---------------------YVP--QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRel 126
|
170 180
....*....|....*....|....*....
gi 493786691 162 SKKG--FLLISHDRNFLDGCINHVISINR 188
Cdd:cd00267 127 AEEGrtVIIVTHDPELAELAADRVIVLKD 155
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
307-490 |
1.06e-20 |
|
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: 95.21 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 307 NPLISVSELSAHY-GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA----SNL-------KI 374
Cdd:COG4988 334 PPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINgvdlSDLdpaswrrQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 375 SYIPQDTSNLSGSLNEYIH--SQDVDETLCKTILRK---LDFARELFemDMIDY---------SDGQKKKVLIALSLSKP 440
Cdd:COG4988 414 AWVPQNPYLFAGTIRENLRlgRPDASDEELEAALEAaglDEFVAALP--DGLDTplgeggrglSGGQAQRLALARALLRD 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493786691 441 AHLFIWDEPLNYIDVISRIQIEEIIKEAKP--TLIFVEHDKRFVEDiANKII 490
Cdd:COG4988 492 APLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALLAQ-ADRIL 542
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-188 |
5.55e-20 |
|
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: 89.15 E-value: 5.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQET-YQGKISKDVEFIKFPPNiSDTSKLGI 82
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKpDSGSILIDGEDVRKEPR-EARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 83 -----DLYKEL--------------ISDDEEWKLFRELN-LLNVDENLVYReFKTLSKGEQTKILLAILFTKEDGFLLID 142
Cdd:COG4555 79 lpderGLYDRLtvreniryfaelygLFDEELKKRIEELIeLLGLEEFLDRR-VGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493786691 143 EPTNHLDMNG----RKILSEYLKSKKGFLLISHDRNFLDGCINHVISINR 188
Cdd:COG4555 158 EPTNGLDVMArrllREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHK 207
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
310-490 |
5.96e-20 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 87.95 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNL-----------KISYIP 378
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 379 QDTSNLSGSLNEY------IHSQDVDETLCKTILRKLDFARELFEMDMIDYSDGQKKKV--LIALSLSKPAHLFiwDEPL 450
Cdd:COG4619 81 QEPALWGGTVRDNlpfpfqLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLalIRALLLQPDVLLL--DEPT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493786691 451 NYIDVISRIQIEEII----KEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:COG4619 159 SALDPENTRRVEELLreylAEEGRAVLWVSHDPEQIERVADRVL 202
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
310-486 |
1.94e-19 |
|
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: 86.72 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA------------SNLKISYI 377
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditglppherARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 378 PQDtSNLSGSLNeyihsqdVDETL--------CKTILRKLDFARELF----EM------DMidySDGQKKKVLIALSLSK 439
Cdd:cd03224 81 PEG-RRIFPELT-------VEENLllgayarrRAKRKARLERVYELFprlkERrkqlagTL---SGGEQQMLAIARALMS 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493786691 440 PAHLFIWDEPL-----NYIDVISRIqIEEiIKEAKPTLIFVEHDKRFVEDIA 486
Cdd:cd03224 150 RPKLLLLDEPSeglapKIVEEIFEA-IRE-LRDEGVTILLVEQNARFALEIA 199
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
308-482 |
2.79e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 87.09 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIPQDtsnlsgs 387
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 388 lneyIHsqdVDETLCKTI---------LRKLDF--------ARELFEMDMIDYSDGQKKKVLIALSLSKPAHLFIWDEPL 450
Cdd:PRK09544 76 ----LY---LDTTLPLTVnrflrlrpgTKKEDIlpalkrvqAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 493786691 451 NYIDVISRIQIEEIIKEAKPTL----IFVEHDKRFV 482
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRELdcavLMVSHDLHLV 184
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
331-492 |
5.07e-19 |
|
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: 86.31 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 331 EIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIkLASNLKISYIPQD-TSNLSGSLNEYIHSQDVDETLC---KT-I 405
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-EIELDTVSYKPQYiKADYEGTVRDLLSSITKDFYTHpyfKTeI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 406 LRKLDFAReLFEMDMIDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIK----EAKPTLIFVEHDKRF 481
Cdd:cd03237 100 AKPLQIEQ-ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRrfaeNNEKTAFVVEHDIIM 178
|
170
....*....|.
gi 493786691 482 VEDIANKIIQF 492
Cdd:cd03237 179 IDYLADRLIVF 189
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
310-490 |
1.25e-18 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 83.42 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQ--ILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL--------ASNLK---ISY 376
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgadisqwDPNELgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 377 IPQDTSNLSGSLNEYIhsqdvdetlcktilrkldfarelfemdmidYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVI 456
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190
....*....|....*....|....*....|....*..
gi 493786691 457 SRIQIEEIIKEAK---PTLIFVEHDKRFVEdIANKII 490
Cdd:cd03246 131 GERALNQAIAALKaagATRIVIAHRPETLA-SADRIL 166
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-191 |
3.94e-18 |
|
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: 81.68 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQET-YQGKIS-KDVEFIKFPPNISdtSKLG 81
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKpDSGEIKvLGKDIKKEPEEVK--RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 82 IdlykeLIsddEEWKLFRElnlLNVDENLVYrefktlSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGR----KILS 157
Cdd:cd03230 77 Y-----LP---EEPSLYEN---LTVRENLKL------SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRrefwELLR 139
|
170 180 190
....*....|....*....|....*....|....
gi 493786691 158 EYLKSKKGFLLISHDRNFLDGCINHVISINRNSI 191
Cdd:cd03230 140 ELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
310-490 |
1.19e-17 |
|
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: 81.49 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEI--------KLASNLK-----ISY 376
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItfdgksyqKNIEALRrigalIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 377 iPQDTSNLSGSLNEYIHS-------QDVDETLCKTILRklDFARELFEmdmiDYSDGQKKKVLIALS-LSKPAHLfIWDE 448
Cdd:cd03268 81 -PGFYPNLTARENLRLLArllgirkKRIDEVLDVVGLK--DSAKKKVK----GFSLGMKQRLGIALAlLGNPDLL-ILDE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493786691 449 PLNYIDVISRIQIEEII---KEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:cd03268 153 PTNGLDPDGIKELRELIlslRDQGITVLISSHLLSEIQKVADRIG 197
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
310-490 |
1.54e-17 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 81.15 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSelsaHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL-ASNLK-------ISYIPQD- 380
Cdd:cd03226 5 ISFS----YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLnGKPIKakerrksIGYVMQDv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 381 TSNLSGS--LNE-YIHSQDVDETLCK--TILRKLDFArELFEMDMIDYSDGQKKKVLIALS-LSKPaHLFIWDEPLNYID 454
Cdd:cd03226 81 DYQLFTDsvREElLLGLKELDAGNEQaeTVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAAlLSGK-DLLIFDEPTSGLD 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 493786691 455 VISRIQIEEIIKE---AKPTLIFVEHDKRFVEDIANKII 490
Cdd:cd03226 159 YKNMERVGELIRElaaQGKAVIVITHDYEFLAKVCDRVL 197
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-146 |
1.91e-17 |
|
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: 79.23 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 21 FENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQET-YQGKISKDVEFIKFPPNISDTSKLG------------------ 81
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTILLDGQDLTDDERKSLRKEIGyvfqdpqlfprltvrenl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 82 -----IDLYKELISDDEEWKLFRELNLLNVDENLVYREFKTLSKGEQTKILLAILFTKEDGFLLIDEPTN 146
Cdd:pfam00005 81 rlgllLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
310-490 |
1.94e-17 |
|
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: 81.03 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA----SNL-----KISYIPQD 380
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdvTGVpperrNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 381 TSNlsgslneYIHsQDVDETLC----------KTILRKLDFARELFEMDMIDY------SDGQKKKVLIALSLSKPAHLF 444
Cdd:cd03259 81 YAL-------FPH-LTVAENIAfglklrgvpkAEIRARVRELLELVGLEGLLNryphelSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493786691 445 IWDEPLNYIDVISRIQ----IEEIIKEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:cd03259 153 LLDEPLSALDAKLREElreeLKELQRELGITTIYVTHDQEEALALADRIA 202
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
310-490 |
2.41e-17 |
|
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: 81.01 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL--------------ASNLKIS 375
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdgedisglseaelyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 376 YIPQD----TS-----NLSGSLNEyiHSQDVDETLCKTILRKLDFA----------RELfemdmidySDGQKKKVLIALS 436
Cdd:cd03261 81 MLFQSgalfDSltvfeNVAFPLRE--HTRLSEEEIREIVLEKLEAVglrgaedlypAEL--------SGGMKKRVALARA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493786691 437 L-SKPAHLFiWDEPLNYIDVISRIQIEEIIKEAKPTL----IFVEHDKRFVEDIANKII 490
Cdd:cd03261 151 LaLDPELLL-YDEPTAGLDPIASGVIDDLIRSLKKELgltsIMVTHDLDTAFAIADRIA 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-188 |
2.46e-17 |
|
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: 80.59 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 5 KIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL--LNQET-----YQGKISKDVEFIKFPPNI--- 74
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLngLLGPTsgevlVDGKDLTKLSLKELRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 75 ---SDTSKLGIDLYKEL--------ISDDEEWK-LFRELNLLNvDENLVYREFKTLSKGEQTKILLAILFTKEDGFLLID 142
Cdd:cd03225 81 fqnPDDQFFGPTVEEEVafglenlgLPEEEIEErVEEALELVG-LEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493786691 143 EPTNHLDMNGRKILSEYLK----SKKGFLLISHDRNFLDGCINHVISINR 188
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKklkaEGKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
310-490 |
3.39e-17 |
|
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: 84.26 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHY-GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNL-----------KISYI 377
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPladadadswrdQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 378 PQDTSNLSGSLNEYI-HSQ-DVDETLCKTILRK---LDFARELFEM--DMID-----YSDGQKKKVLIALSLSKPAHLFI 445
Cdd:TIGR02857 402 PQHPFLFAGTIAENIrLARpDASDAEIREALERaglDEFVAALPQGldTPIGeggagLSGGQAQRLALARAFLRDAPLLL 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493786691 446 WDEPLNYIDVISRIQIEEIIKEAKP--TLIFVEHDKRFVEDiANKII 490
Cdd:TIGR02857 482 LDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALAAL-ADRIV 527
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-206 |
4.59e-17 |
|
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: 83.83 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQET-YQGKISkdvefikfppnISDTSKLG- 81
Cdd:TIGR03719 323 IEAENLTKAFGD--KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQpDSGTIE-----------IGETVKLAy 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 82 -------IDLYK---ELISDDEEwklfrELNLLNVDEN---LVYR-EFK---------TLSKGEQTKILLAILFTKEDGF 138
Cdd:TIGR03719 390 vdqsrdaLDPNKtvwEEISGGLD-----IIKLGKREIPsraYVGRfNFKgsdqqkkvgQLSGGERNRVHLAKTLKSGGNV 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 139 LLIDEPTNHLDMNGRKILSEYLKSKKG-FLLISHDRNFLDGCINHVISINRNS-IDVQSGNFTSWYENKL 206
Cdd:TIGR03719 465 LLLDEPTNDLDVETLRALEEALLNFAGcAVVISHDRWFLDRIATHILAFEGDShVEWFEGNFSEYEEDKK 534
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
320-466 |
5.78e-17 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 79.13 E-value: 5.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 320 GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLG--INHEYTGEIKL------ASNLK--ISYIPQDtsnlsgsln 389
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLIngrpldKRSFRkiIGYVPQD--------- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493786691 390 EYIHSQD-VDETlcktilrkLDFARELFEMdmidySDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIK 466
Cdd:cd03213 91 DILHPTLtVRET--------LMFAAKLRGL-----SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLR 155
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
310-467 |
8.40e-17 |
|
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: 78.55 E-value: 8.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLAsnlkisyiPQDTSNLSGSLN 389
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWN--------GTPLAEQRDEPH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 390 EYI----HSQDVDETLckTILRKLDFARELF------------EMDMIDYSD--------GQKKKVLIALSLSKPAHLFI 445
Cdd:TIGR01189 73 ENIlylgHLPGLKPEL--SALENLHFWAAIHggaqrtiedalaAVGLTGFEDlpaaqlsaGQQRRLALARLWLSRRPLWI 150
|
170 180
....*....|....*....|..
gi 493786691 446 WDEPLNYIDVISRIQIEEIIKE 467
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRA 172
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
318-490 |
1.09e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 79.36 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 318 HYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLasNLKISYI--------PQdtsnLSGS-- 387
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV--NGRVSALlelgagfhPE----LTGRen 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 388 --LNEYIHSQDVDEtlcktILRKLDFARELFEM-DMID-----YSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDV---- 455
Cdd:COG1134 109 iyLNGRLLGLSRKE-----IDEKFDEIVEFAELgDFIDqpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqk 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 493786691 456 --ISRiqIEEIIKEAKpTLIFVEHDKRFVEDIANKII 490
Cdd:COG1134 184 kcLAR--IRELRESGR-TVIFVSHSMGAVRRLCDRAI 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
310-490 |
1.28e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 78.48 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL-------ASNLKISYIP---- 378
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkpldiAARNRIGYLPeerg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 379 -------QDTSNLSGSLNEYIHSQ---DVDEtlcktILRKLDFaRELFEMDMIDYSDGQKKKV-LIALSLSKPAhLFIWD 447
Cdd:cd03269 81 lypkmkvIDQLVYLAQLKGLKKEEarrRIDE-----WLERLEL-SEYANKRVEELSKGNQQKVqFIAAVIHDPE-LLILD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493786691 448 EPLNYIDVISRIQIEEII---KEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIrelARAGKTVILSTHQMELVEELCDRVL 199
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
310-489 |
1.47e-16 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 78.57 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLAS----------NLKISYIPQ 379
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 380 DTS---NLSGSLNEYIHS-----------QDVDETLCKTILrkLDFARELFEMdmidYSDGQKKKVLIALSL-SKPAHLF 444
Cdd:cd03265 81 DLSvddELTGWENLYIHArlygvpgaerrERIDELLDFVGL--LEAADRLVKT----YSGGMRRRLEIARSLvHRPEVLF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493786691 445 IwDEPLNYIDVISRIQIEEIIKEAKP----TLIFVEHDKRFVEDIANKI 489
Cdd:cd03265 155 L-DEPTIGLDPQTRAHVWEYIEKLKEefgmTILLTTHYMEEAEQLCDRV 202
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
308-380 |
1.81e-16 |
|
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: 78.49 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA----SNLK--------IS 375
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgediTGLPphriarlgIG 81
|
....*
gi 493786691 376 YIPQD 380
Cdd:COG0410 82 YVPEG 86
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-488 |
2.05e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.77 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQETYQ---GKISKDV------EFIKFPPNI 74
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptsGRIIYHValcekcGYVERPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 75 SDT-SKLGIDLYKELIS----DDEEWKLFRELN----------------LLNVDENL----------VYREFK------- 116
Cdd:TIGR03269 79 GEPcPVCGGTLEPEEVDfwnlSDKLRRRIRKRIaimlqrtfalygddtvLDNVLEALeeigyegkeaVGRAVDliemvql 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 117 ---------TLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGRKILSEYLKskkgfllishdrnflDGCINHVISIN 187
Cdd:TIGR03269 159 shrithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALE---------------EAVKASGISMV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 188 RNSidvqsgnftSWYENklmkdkfeiskneklrkdIKRLKEAArqskIWSDKIENTKNGvkvsgiKPDKgrighQSAKMM 267
Cdd:TIGR03269 224 LTS---------HWPEV------------------IEDLSDKA----IWLENGEIKEEG------TPDE-----VVAVFM 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 268 KKSKNLEHRQNkaieekqsllkdIEIKEslllhplhhhknPLISVSELSAHY-----GERQILSNLSFEIEQGDIVAISG 342
Cdd:TIGR03269 262 EGVSEVEKECE------------VEVGE------------PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVG 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 343 RNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIPQDTSNLSGSLNEYI---HSQ-------DVDETLCKTIlrKLDFA 412
Cdd:TIGR03269 318 TSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPDGRGRAKRYIgilHQEydlyphrTVLDNLTEAI--GLELP 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 413 RELFEMDMI----------------------DYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEII----K 466
Cdd:TIGR03269 396 DELARMKAVitlkmvgfdeekaeeildkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarE 475
|
570 580
....*....|....*....|..
gi 493786691 467 EAKPTLIFVEHDKRFVEDIANK 488
Cdd:TIGR03269 476 EMEQTFIIVSHDMDFVLDVCDR 497
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
310-490 |
2.72e-16 |
|
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: 76.31 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL------------ASNLKISYI 377
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVdgkevsfasprdARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 378 PQdtsnLSGslneyihsqdvdetlcktilrkldfarelfemdmidysdGQKKKVLIALSLSKPAHLFIWDEPLNYIDVIS 457
Cdd:cd03216 81 YQ----LSV---------------------------------------GERQMVEIARALARNARLLILDEPTAALTPAE 117
|
170 180 190
....*....|....*....|....*....|....*.
gi 493786691 458 RIQIEEIIKEAKP---TLIFVEHDKRFVEDIANKII 490
Cdd:cd03216 118 VERLFKVIRRLRAqgvAVIFISHRLDEVFEIADRVT 153
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
310-478 |
3.02e-16 |
|
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: 77.51 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYG----ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL------ASNLKISYIPQ 379
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 380 DTS---------NLSGSLNeyihSQDVDETlcktilRKLDFARELFEM----DMIDY-----SDGQKKKVLIALSLSKPA 441
Cdd:cd03293 81 QDAllpwltvldNVALGLE----LQGVPKA------EARERAEELLELvglsGFENAyphqlSGGMRQRVALARALAVDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493786691 442 HLFIWDEPLNYIDVISRIQIEE----IIKEAKPTLIFVEHD 478
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEelldIWRETGKTVLLVTHD 191
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
319-490 |
3.78e-16 |
|
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: 77.57 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 319 YGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASnlKISYIPQDTS----NLSGSLNEY--- 391
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--RVSSLLGLGGgfnpELTGRENIYlng 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 392 -IHSQDVDEtlcktILRKLDFARELFEM-DMID-----YSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQ---- 460
Cdd:cd03220 110 rLLGLSRKE-----IDEKIDEIIEFSELgDFIDlpvktYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKcqrr 184
|
170 180 190
....*....|....*....|....*....|
gi 493786691 461 IEEIIKEAKpTLIFVEHDKRFVEDIANKII 490
Cdd:cd03220 185 LRELLKQGK-TVILVSHDPSSIKRLCDRAL 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-172 |
4.31e-16 |
|
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: 77.78 E-value: 4.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 3 AIKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLN-QETYQGKIS---KDV------EFIK--- 69
Cdd:COG1120 1 MLEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGlLKPSSGEVLldgRDLaslsrrELARria 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 70 -------FPPNIS--DTSKLG----IDLYKELISDDEE--WKLFRELNLlnvdENLVYREFKTLSKGEQTKILLAILFTK 134
Cdd:COG1120 79 yvpqeppAPFGLTvrELVALGryphLGLFGRPSAEDREavEEALERTGL----EHLADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493786691 135 EDGFLLIDEPTNHLDMNGRKILSEYLKS-----KKGFLLISHD 172
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRlarerGRTVVMVLHD 197
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-198 |
4.57e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 80.71 E-value: 4.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 3 AIKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLnqetyqGKISKDVEFIKFppniSDTSKLGI 82
Cdd:PRK15064 319 ALEVENLTKGFDN--GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV------GELEPDSGTVKW----SENANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 83 ---DLYKELISD--------------DEEWKLFRELNLLNVDENLVYREFKTLSKGEQTKILLAILFTKEDGFLLIDEPT 145
Cdd:PRK15064 387 yaqDHAYDFENDltlfdwmsqwrqegDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493786691 146 NHLDMNGRKILSEYLKSKKGFLL-ISHDRNFLDGCINHVISINRNSIDVQSGNF 198
Cdd:PRK15064 467 NHMDMESIESLNMALEKYEGTLIfVSHDREFVSSLATRIIEITPDGVVDFSGTY 520
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-186 |
5.36e-16 |
|
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: 76.36 E-value: 5.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQET-YQGKISKDVEFIKFPPNISDTS---- 78
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPpSAGEVLWNGEPIRDAREDYRRRlayl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 79 --KLGI--------------DLYKELISDDEEWKLFRELNLlnvdENLVYREFKTLSKGEQTKILLAILFTKEDGFLLID 142
Cdd:COG4133 81 ghADGLkpeltvrenlrfwaALYGLRADREAIDEALEAVGL----AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493786691 143 EPTNHLDMNGRK----ILSEYLKSKKGFLLISHDRNFLDGCinHVISI 186
Cdd:COG4133 157 EPFTALDAAGVAllaeLIAAHLARGGAVLLTTHQPLELAAA--RVLDL 202
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-171 |
7.32e-16 |
|
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: 75.11 E-value: 7.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQ-ETYQGKISKDvefikfppnisdtsklGI 82
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLyDPTSGEILID----------------GV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 83 DLYKeliSDDEEWK-----LFRELNLLN--VDENLvyrefktLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGRKI 155
Cdd:cd03228 65 DLRD---LDLESLRkniayVPQDPFLFSgtIRENI-------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170
....*....|....*....
gi 493786691 156 LSEYLKS---KKGFLLISH 171
Cdd:cd03228 135 ILEALRAlakGKTVIVIAH 153
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
309-490 |
7.76e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 80.38 E-value: 7.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIPQD-TSNLSGS 387
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDpPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 388 LNEYI--------------H--SQDVDETLCKTILRKLDFARELFE-----------------------MDMIDYSDGQK 428
Cdd:PRK11147 83 VYDFVaegieeqaeylkryHdiSHLVETDPSEKNLNELAKLQEQLDhhnlwqlenrinevlaqlgldpdAALSSLSGGWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493786691 429 KKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIV 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
310-492 |
9.74e-16 |
|
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: 75.99 E-value: 9.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYG----ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA----SNL--------- 372
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdiSKLsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 373 --KISYIPQDTsNLSGSLN--EYI--------HSQDVDETLCKTILRKLD-------FARELfemdmidySDGQKKKVLI 433
Cdd:cd03255 81 rrHIGFVFQSF-NLLPDLTalENVelplllagVPKKERRERAEELLERVGlgdrlnhYPSEL--------SGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493786691 434 ALSLSKPAHLFIWDEPLNYIDVISRIQIEEII----KEAKPTLIFVEHDKRFVEdIANKIIQF 492
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLrelnKEAGTTIVVVTHDPELAE-YADRIIEL 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
319-478 |
1.23e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.96 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 319 YGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIPQDTSnlsgslneyihsqdVD 398
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSE--------------VP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 399 ETLCKTI--------------LRKLD------FARELFEMDMIDY--------SDGQKKKVLIALSLSKPAHLFIWDEPL 450
Cdd:NF040873 68 DSLPLTVrdlvamgrwarrglWRRLTrddraaVDDALERVGLADLagrqlgelSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|.
gi 493786691 451 NYIDVISRIQIEEIIKEA---KPTLIFVEHD 478
Cdd:NF040873 148 TGLDAESRERIIALLAEEharGATVVVVTHD 178
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
310-478 |
1.52e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.21 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASN-----------LKISYIP 378
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlaRRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 379 QDTS-------------------NLSGSLNEYIHsQDVDETLCKTilRKLDFARELFEmdmiDYSDGQKKKVLIALSLSK 439
Cdd:PRK11231 83 QHHLtpegitvrelvaygrspwlSLWGRLSAEDN-ARVNQAMEQT--RINHLADRRLT----DLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493786691 440 PAHLFIWDEPLNYIDvISRiQIE-----EIIKEAKPTLIFVEHD 478
Cdd:PRK11231 156 DTPVVLLDEPTTYLD-INH-QVElmrlmRELNTQGKTVVTVLHD 197
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-184 |
2.51e-15 |
|
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: 75.51 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 1 MSAIKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLlNQETYQGKiSKDVEF------------I 68
Cdd:COG1119 1 DPLLELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLI-TGDLPPTY-GNDVRLfgerrggedvweL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 69 K-------------FPPNIS----------DTsklgIDLYKELisDDEEWKLFRE-LNLLNVDEnLVYREFKTLSKGEQT 124
Cdd:COG1119 77 RkriglvspalqlrFPRDETvldvvlsgffDS----IGLYREP--TDEQRERARElLELLGLAH-LADRPFGTLSQGEQR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493786691 125 KILLAILFTKEDGFLLIDEPTNHLDMNGRKILSEYL-----KSKKGFLLISHDRNFLDGCINHVI 184
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLdklaaEGAPTLVLVTHHVEEIPPGITHVL 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
310-489 |
2.97e-15 |
|
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: 74.85 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQ--ILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIK-----LASNLK-----ISYI 377
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYingysIRTDRKaarqsLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 378 PQDTSNLSG--------------SLNEYIHSQDVDETLCKTILRKL--DFARelfemdmiDYSDGQKKKVLIALSLSKPA 441
Cdd:cd03263 81 PQFDALFDEltvrehlrfyarlkGLPKSEIKEEVELLLRVLGLTDKanKRAR--------TLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493786691 442 HLFIWDEPLNYIDVISRIQIEEIIKEAKP--TLIFVEHDKRFVEDIANKI 489
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRI 202
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-198 |
3.37e-15 |
|
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: 78.34 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 3 AIKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQET-YQGKIS---KDVEFIkfppNISD-T 77
Cdd:COG2274 473 DIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEpTSGRILidgIDLRQI----DPASlR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 78 SKLG----------------IDLYKELISDDEEWKLFRELNLLNVDENL-------VYREFKTLSKGEQTKILLAILFTK 134
Cdd:COG2274 549 RQIGvvlqdvflfsgtirenITLGDPDATDEEIIEAARLAGLHDFIEALpmgydtvVGEGGSNLSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493786691 135 EDGFLLIDEPTNHLDMNGRKILSEYLKS---KKGFLLISHDRNFLDGCiNHVISINRNSIdVQSGNF 198
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRllkGRTVIIIAHRLSTIRLA-DRIIVLDKGRI-VEDGTH 693
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
310-478 |
4.01e-15 |
|
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: 74.52 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEY-----TGEIKLA-----------SNLK 373
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDgkdiydldvdvLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 374 --------------------ISYIPQdtsnLSGSLNEYIHSQDVDETLCKTIL-----RKLDfARELfemdmidySDGQK 428
Cdd:cd03260 81 rrvgmvfqkpnpfpgsiydnVAYGLR----LHGIKLKEELDERVEEALRKAALwdevkDRLH-ALGL--------SGGQQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493786691 429 KKVLIALSLS-KPAHLFIwDEPLNYIDVISRIQIEEIIKEAK--PTLIFVEHD 478
Cdd:cd03260 148 QRLCLARALAnEPEVLLL-DEPTSALDPISTAKIEELIAELKkeYTIVIVTHN 199
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
309-490 |
6.33e-15 |
|
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: 75.47 E-value: 6.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHY----GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGI---NHEYTGEIKLA-SNL-------- 372
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDgEDLlklsekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 373 ------KISYIPQDTSNlsgSLNEY--IHSQdVDETLckTILRKLDF------ARELFEM-------DMID-Y----SDG 426
Cdd:COG0444 81 rkirgrEIQMIFQDPMT---SLNPVmtVGDQ-IAEPL--RIHGGLSKaearerAIELLERvglpdpeRRLDrYphelSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493786691 427 QKKKVLIALSLS-KPAhLFIWDEPLNYIDVISRIQI----EEIIKEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:COG0444 155 MRQRVMIARALAlEPK-LLIADEPTTALDVTIQAQIlnllKDLQRELGLAILFITHDLGVVAEIADRVA 222
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
321-490 |
7.26e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.84 E-value: 7.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 321 ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILlginheyTGEIKLASNLKISYIPQDTSNLSGSLNEYI-HSQDVDE 399
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL-------AGALKGTPVAGCVDVPDNQFGREASLIDAIgRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 400 -----TLCK-----TILRKLDfarelfemdmiDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYID-----VISRIqIEEI 464
Cdd:COG2401 115 avellNAVGlsdavLWLRRFK-----------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtakRVARN-LQKL 182
|
170 180
....*....|....*....|....*..
gi 493786691 465 IKEAKPTLIFVEHDKRFVEDIA-NKII 490
Cdd:COG2401 183 ARRAGITLVVATHHYDVIDDLQpDLLI 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
319-490 |
2.03e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 72.75 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 319 YGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNL----------KISYIPQDTSNL---- 384
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrrkkflrRIGVVFGQKTQLwwdl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 385 ----SGSLNEYIHsqDVDETLCKTILRKLDfarELFEMDMIDY------SDGQKKKVLIALSL-SKPAHLFIwDEPLNYI 453
Cdd:cd03267 111 pvidSFYLLAAIY--DLPPARFKKRLDELS---ELLDLEELLDtpvrqlSLGQRMRAEIAAALlHEPEILFL-DEPTIGL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493786691 454 DVISRIQIEEIIKEA----KPTLIFVEHDKRFVEDIANKII 490
Cdd:cd03267 185 DVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVL 225
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
309-465 |
2.49e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.76 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL------------ASNLkiSY 376
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqgepirrqrdeyHQDL--LY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 377 I-------PQDTS--NLSGSLNeyiHSQDVDETLCKTILRKLDFARelFEMDMIDY-SDGQKKKVLIA-LSLSKPAhLFI 445
Cdd:PRK13538 79 LghqpgikTELTAleNLRFYQR---LHGPGDDEALWEALAQVGLAG--FEDVPVRQlSAGQQRRVALArLWLTRAP-LWI 152
|
170 180
....*....|....*....|
gi 493786691 446 WDEPLNYIDVISRIQIEEII 465
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALL 172
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
310-490 |
2.61e-14 |
|
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: 71.85 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQI--LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL---------ASNLK--ISY 376
Cdd:cd03245 3 IEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirqldPADLRrnIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 377 IPQDTSNLSGSLNEYIHS--QDVDETLcktILRKL------DFAREL---FEMdMI-----DYSDGQKKKVLIA-LSLSK 439
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLgaPLADDER---ILRAAelagvtDFVNKHpngLDL-QIgergrGLSGGQRQAVALArALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493786691 440 PAHLFIwDEPLNYIDVISRIQIEEIIKEAKP--TLIFVEHDKRFVeDIANKII 490
Cdd:cd03245 159 PPILLL-DEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLL-DLVDRII 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
307-490 |
2.94e-14 |
|
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: 72.32 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 307 NPLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASnlkisyipQDTSNLSG 386
Cdd:COG1127 3 EPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDG--------QDITGLSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 387 S-LNEYIH-------------SQDVDE----------TLCKTILRKLdfARELFEM----DMIDY-----SDGQKKKVLI 433
Cdd:COG1127 75 KeLYELRRrigmlfqggalfdSLTVFEnvafplrehtDLSEAEIREL--VLEKLELvglpGAADKmpselSGGMRKRVAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493786691 434 A--LSLsKPAHLFiWDEP---LnyiDVISRIQIEEIIKEAKPTL----IFVEHDKRFVEDIANKII 490
Cdd:COG1127 153 AraLAL-DPEILL-YDEPtagL---DPITSAVIDELIRELRDELgltsVVVTHDLDSAFAIADRVA 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
307-492 |
3.08e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 72.00 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 307 NPLISVSELSAHYG----ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA----SNL------ 372
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgqdiSSLserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 373 -----KISYIPQDtSNLSGSLN---------EYIH-SQDVDETLCKTILRKLD-------FARELfemdmidySDGQKKK 430
Cdd:COG1136 82 rlrrrHIGFVFQF-FNLLPELTalenvalplLLAGvSRKERRERARELLERVGlgdrldhRPSQL--------SGGQQQR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493786691 431 VLIALSLSKPAHLFIWDEPLNYIDVISRIQI----EEIIKEAKPTLIFVEHDKRfVEDIANKIIQF 492
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVlellRELNRELGTTIVMVTHDPE-LAARADRVIRL 217
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
308-478 |
3.49e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.40 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLIsVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIkLASNLKISYIPQDTSnlsgs 387
Cdd:PRK11247 12 PLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTR----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 388 lneyIHSQDVDETLCKTILRKL---------DFARE-LFEMDMID--------YSDGQKKKVLIALSLSKPAHLFIWDEP 449
Cdd:PRK11247 85 ----LMFQDARLLPWKKVIDNVglglkgqwrDAALQaLAAVGLADranewpaaLSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190
....*....|....*....|....*....|...
gi 493786691 450 LNYIDVISRIQIEEII----KEAKPTLIFVEHD 478
Cdd:PRK11247 161 LGALDALTRIEMQDLIeslwQQHGFTVLLVTHD 193
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
307-449 |
3.97e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.28 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 307 NPLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL------------ASNLKI 374
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdgepvrfrsprdAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 375 SYIPQDTS---NLS-------GslNEYIHSQDVDEtlcKTILRKldfARELFEM-------DMI--DYSDGQKKKVLIAL 435
Cdd:COG1129 82 AIIHQELNlvpNLSvaeniflG--REPRRGGLIDW---RAMRRR---ARELLARlgldidpDTPvgDLSVAQQQLVEIAR 153
|
170
....*....|....
gi 493786691 436 SLSKPAHLFIWDEP 449
Cdd:COG1129 154 ALSRDARVLILDEP 167
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
310-490 |
5.84e-14 |
|
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: 70.03 E-value: 5.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGE--RQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASnlkisyipQDTSNLSGS 387
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG--------VPVSDLEKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 388 LNEYIH--SQDV---DETLCKTILRKLdfarelfemdmidySDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIE 462
Cdd:cd03247 73 LSSLISvlNQRPylfDTTLRNNLGRRF--------------SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL 138
|
170 180 190
....*....|....*....|....*....|
gi 493786691 463 EIIKEA--KPTLIFVEHDKRFVEDiANKII 490
Cdd:cd03247 139 SLIFEVlkDKTLIWITHHLTGIEH-MDKIL 167
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-477 |
1.28e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 72.74 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 1 MSAIKIQNLTFSYYGYVKPIFENVSFSFDTNWktGLIGRNGIGKSTLFKLLLNQET-YQGKISKD------VEFIKFPPN 73
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSW--AFVGANGSGKSALARALAGELPlLSGERQSQfshitrLSFEQLQKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 74 ISDTSKlgiDLYKELISDDEE--WKLFRELNLLNVDEN--------------LVYREFKTLSKGEQTKILLAILFTKEDG 137
Cdd:PRK10938 79 VSDEWQ---RNNTDMLSPGEDdtGRTTAEIIQDEVKDParceqlaqqfgitaLLDRRFKYLSTGETRKTLLCQALMSEPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 138 FLLIDEPTNHLDMNGRKILSEYLKS--KKGFLLishdrnfldgcinhVISINRnsidvqsgnftswyenklmkdkFEisk 215
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASlhQSGITL--------------VLVLNR----------------------FD--- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 216 neklrkDIkrlKEAARQSKIWSDKiENTKNGvkvsgikpDKGRIGHQS-AKMMKKSKNLEhrqNKAIEEKQSLLKDIEIK 294
Cdd:PRK10938 197 ------EI---PDFVQFAGVLADC-TLAETG--------EREEILQQAlVAQLAHSEQLE---GVQLPEPDEPSARHALP 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 295 ESlllhplhhhkNPLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLG------INH-------- 360
Cdd:PRK10938 256 AN----------EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgySNDltlfgrrr 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 361 ---EYTGEIK-----LASNLKISY-IPQDTSN--LSG---SLNEYIHSQDVDETLCKTILRKLDFARELFEMDMIDYSDG 426
Cdd:PRK10938 326 gsgETIWDIKkhigyVSSSLHLDYrVSTSVRNviLSGffdSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPFHSLSWG 405
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 493786691 427 QKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQ----IEEIIKEAKPTLIFVEH 477
Cdd:PRK10938 406 QQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLvrrfVDVLISEGETQLLFVSH 460
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
308-467 |
1.35e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.52 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNlkisyiPQDTSNLSGS 387
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG------DIDDPDVAEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 388 LNeYIHSQDVdetlCK---TILRKLDF--------------ARELFEMDMI------DYSDGQKKKVLIALSLSKPAHLF 444
Cdd:PRK13539 75 CH-YLGHRNA----MKpalTVAENLEFwaaflggeeldiaaALEAVGLAPLahlpfgYLSAGQKRRVALARLLVSNRPIW 149
|
170 180
....*....|....*....|...
gi 493786691 445 IWDEPLNYIDVISRIQIEEIIKE 467
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIRA 172
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
322-477 |
1.57e-13 |
|
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: 68.33 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 322 RQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIPQDTSNLSGSLNeyihsqdvdETL 401
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLGTLR---------EQL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493786691 402 CKTILRKLdfarelfemdmidySDGQKKKVLIA-LSLSKPAHLFIwDEPLNYIDVISRIQIEEIIKEAKPTLIFVEH 477
Cdd:cd03223 85 IYPWDDVL--------------SGGEQQRLAFArLLLHKPKFVFL-DEATSALDEESEDRLYQLLKELGITVISVGH 146
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
310-478 |
1.88e-13 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 70.54 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHY--GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL-------ASNL-----KIS 375
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVdgldtldEENLweirkKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 376 YIPQDTSN-LSGSLNEYihsqDVD---ETLC---KTILRKLDFAreLFEMDMIDY--------SDGQKKKVLIA--LSLs 438
Cdd:TIGR04520 81 MVFQNPDNqFVGATVED----DVAfglENLGvprEEMRKRVDEA--LKLVGMEDFrdrephllSGGQKQRVAIAgvLAM- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493786691 439 KPAHLfIWDEPLNYIDVISRIQIEEII----KEAKPTLIFVEHD 478
Cdd:TIGR04520 154 RPDII-ILDEATSMLDPKGRKEVLETIrklnKEEGITVISITHD 196
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
309-490 |
2.79e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 72.12 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIPQDTSNLSGSL 388
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 389 NEYIHSQDV----------------DETLCKTILRKLD-------------------FARELFEMDMIDYSDGQKKKVLI 433
Cdd:PRK10636 81 LEYVIDGDReyrqleaqlhdanernDGHAIATIHGKLDaidawtirsraasllhglgFSNEQLERPVSDFSGGWRMRLNL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493786691 434 ALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKII 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
332-478 |
4.66e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.38 E-value: 4.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 332 IEQGDIVAISGRNGSGKSTLIKILLGI------NHE------------------------YTGEIKLAsnLKISYIPQDT 381
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGElipnlgDYEeepswdevlkrfrgtelqnyfkklYNGEIKVV--HKPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 382 SNLSGSLNEYIhsQDVDETlcktilRKLDFARELFEMDMI------DYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDV 455
Cdd:PRK13409 174 KVFKGKVRELL--KKVDER------GKLDEVVERLGLENIldrdisELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180
....*....|....*....|....*
gi 493786691 456 ISRIQIEEIIKE--AKPTLIFVEHD 478
Cdd:PRK13409 246 RQRLNVARLIRElaEGKYVLVVEHD 270
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
310-490 |
4.73e-13 |
|
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: 67.99 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGdIVAISGRNGSGKSTLIKILLGINHEYTGEIKL--------ASNL--KISYIPQ 379
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvlkqPQKLrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 380 DTS-----------NLSGSLNEyIHSQDVDETLCKTI--LRKLDFARELfemdMIDYSDGQKKKVLIALSLSKPAHLFIW 446
Cdd:cd03264 80 EFGvypnftvreflDYIAWLKG-IPSKEVKARVDEVLelVNLGDRAKKK----IGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493786691 447 DEPLNYIDVISRIQIEEIIKE--AKPTLIFVEHDKRFVEDIANKII 490
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSElgEDRIVILSTHIVEDVESLCNQVA 200
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-198 |
5.34e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 71.43 E-value: 5.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGyvKPI-FENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQ-ETYQGKI--SKDVEFIKFPPNISDtsk 79
Cdd:PLN03073 509 ISFSDASFGYPG--GPLlFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGElQPSSGTVfrSAKVRMAVFSQHHVD--- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 80 lGIDL-------YKELISDDEEWKLFRELNLLNVDENLVYREFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNG 152
Cdd:PLN03073 584 -GLDLssnpllyMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA 662
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493786691 153 RKILSEYLKS-KKGFLLISHDRNFLDGCINHVISINRNSIDVQSGNF 198
Cdd:PLN03073 663 VEALIQGLVLfQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTF 709
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
310-490 |
5.54e-13 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 67.82 E-value: 5.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGER--QILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL-----------ASNLKISY 376
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdgidistipleDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 377 IPQDTSNLSGS----LNEYIHSQDVdetlcktilrkldfarELFEMDMI-----DYSDGQKKKVLIALSLSKPAHLFIWD 447
Cdd:cd03369 87 IPQDPTLFSGTirsnLDPFDEYSDE----------------EIYGALRVsegglNLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493786691 448 EPLNYIDVISRIQIEEIIKE--AKPTLIFVEHDKRFVEDIANKII 490
Cdd:cd03369 151 EATASIDYATDALIQKTIREefTNSTILTIAHRLRTIIDYDKILV 195
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
310-490 |
6.75e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 69.73 E-value: 6.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL---------ASNLKISYIPQD 380
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhgtdvsrlhARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 381 TS---------NLSGSL---------NEYIHSQDVDETLCKTILRKL--DFARELfemdmidySDGQKKKVLIALSLSKP 440
Cdd:PRK10851 83 YAlfrhmtvfdNIAFGLtvlprrerpNAAAIKAKVTQLLEMVQLAHLadRYPAQL--------SGGQKQRVALARALAVE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493786691 441 AHLFIWDEPLNYIDVISRIQ----IEEIIKEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKElrrwLRQLHEELKFTSVFVTHDQEEAMEVADRVV 208
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-235 |
7.55e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.53 E-value: 7.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGYVkpIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQET-YQGKISkdvefikfppnISDTSKLG- 81
Cdd:PRK11819 325 IEAENLSKSFGDRL--LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQpDSGTIK-----------IGETVKLAy 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 82 -------IDLYK---ELISDDEEWklfreLNLLNVDEN---LVYR-EFK---------TLSKGEQTKILLAILFTKEDGF 138
Cdd:PRK11819 392 vdqsrdaLDPNKtvwEEISGGLDI-----IKVGNREIPsraYVGRfNFKggdqqkkvgVLSGGERNRLHLAKTLKQGGNV 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 139 LLIDEPTNHLDMNGRKILSEYLKSKKG-FLLISHDRNFLDGCINHVISINRNSidvQ----SGNFTSWYENKlmkdkfei 213
Cdd:PRK11819 467 LLLDEPTNDLDVETLRALEEALLEFPGcAVVISHDRWFLDRIATHILAFEGDS---QvewfEGNFQEYEEDK-------- 535
|
250 260
....*....|....*....|...
gi 493786691 214 skneklrkdIKRL-KEAARQSKI 235
Cdd:PRK11819 536 ---------KRRLgADAARPHRI 549
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-171 |
8.26e-13 |
|
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: 66.47 E-value: 8.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLL-NQETYQGKISKDVEfikfppnisDTSKLGI 82
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILgLLRPTSGRVRLDGA---------DISQWDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 83 DLYKELI----SDDEewkLFRElnllNVDENLvyrefktLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGRKILSE 158
Cdd:cd03246 72 NELGDHVgylpQDDE---LFSG----SIAENI-------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQ 137
|
170
....*....|....*..
gi 493786691 159 YLKSKKGF----LLISH 171
Cdd:cd03246 138 AIAALKAAgatrIVIAH 154
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
310-469 |
8.69e-13 |
|
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: 67.95 E-value: 8.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASN------------LKISYI 377
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 378 PQDTS---------NLSGSLNEyihsQDVDEtlcKTILRKLDFARELFEMDMI------DYSDGQKKKVLIALSLS-KPA 441
Cdd:cd03218 81 PQEASifrkltveeNILAVLEI----RGLSK---KEREEKLEELLEEFHITHLrkskasSLSGGERRRVEIARALAtNPK 153
|
170 180
....*....|....*....|....*...
gi 493786691 442 HLFIwDEPLNYIDVISRIQIEEIIKEAK 469
Cdd:cd03218 154 FLLL-DEPFAGVDPIAVQDIQKIIKILK 180
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
308-490 |
8.91e-13 |
|
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: 70.57 E-value: 8.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHY--GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGiNHEYT-GEIKLA---------SNL--K 373
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR-FLDPQsGSITLGgvdlrdldeDDLrrR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 374 ISYIPQDTSNLSGSLNEYIH--SQDVDETLCKTILRKL---DFARELFE-MD-MID-----YSDGQKKKVLIALSLSKPA 441
Cdd:COG4987 411 IAVVPQRPHLFDTTLRENLRlaRPDATDEELWAALERVglgDWLAALPDgLDtWLGeggrrLSGGERRRLALARALLRDA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493786691 442 HLFIWDEPLNYIDVISRIQIEEIIKEAKP--TLIFVEHDKRFVEDiANKII 490
Cdd:COG4987 491 PILLLDEPTEGLDAATEQALLADLLEALAgrTVLLITHRLAGLER-MDRIL 540
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
310-490 |
1.09e-12 |
|
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: 67.17 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKIllgINH--EYT-GEIkLASNLKISYIPQDTSNLSG 386
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRC---INLleEPDsGTI-IIDGLKLTDDKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 387 -------SLNEYIHsQDVDE--TLCKTILRKLD------FARELFE----MDMIDY-----SDGQKKKVLIALSLSKPAH 442
Cdd:cd03262 77 kvgmvfqQFNLFPH-LTVLEniTLAPIKVKGMSkaeaeeRALELLEkvglADKADAypaqlSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493786691 443 LFIWDEPLNYID---------VISRIQIEEIikeakpTLIFVEHDKRFVEDIANKII 490
Cdd:cd03262 156 VMLFDEPTSALDpelvgevldVMKDLAEEGM------TMVVVTHEMGFAREVADRVI 206
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
308-369 |
1.31e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.87 E-value: 1.31e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493786691 308 PLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA 369
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLN 62
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
308-467 |
1.39e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.10 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA----SNL-------KISY 376
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvEALsaraasrRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 377 IPQDTS---NLSGS----------LNEYIHSQDVDETLCKTILRKLDFAReLFEMDMIDYSDGQKKKVLIALSLSKPAHL 443
Cdd:PRK09536 82 VPQDTSlsfEFDVRqvvemgrtphRSRFDTWTETDRAAVERAMERTGVAQ-FADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180
....*....|....*....|....
gi 493786691 444 FIWDEPLNYIDVISRIQIEEIIKE 467
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRR 184
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
306-478 |
1.44e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 67.71 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 306 KNPLISVSELSAHYG--ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL------ASNL----- 372
Cdd:PRK13632 4 KSVMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdgitisKENLkeirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 373 KISYIPQDTSnlsgslNEYIHSQDVD------ETLC---KTILRKLDFARElfEMDMIDY--------SDGQKKKVLIAL 435
Cdd:PRK13632 84 KIGIIFQNPD------NQFIGATVEDdiafglENKKvppKKMKDIIDDLAK--KVGMEDYldkepqnlSGGQKQRVAIAS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493786691 436 SLSKPAHLFIWDEPLNYIDVISRIQIEEIIKE----AKPTLIFVEHD 478
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrktRKKTLISITHD 202
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
310-491 |
2.63e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 66.23 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHY-GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA----SNLK----------I 374
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqdlSRLKrreipylrrrI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 375 SYIPQDT---SNLS------------GSLNEYIHsQDVDETLCKT-ILRKLD-FARELfemdmidySDGQKKKVLIALSL 437
Cdd:COG2884 82 GVVFQDFrllPDRTvyenvalplrvtGKSRKEIR-RRVREVLDLVgLSDKAKaLPHEL--------SGGEQQRVAIARAL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493786691 438 -SKPAhLFIWDEPLNYIDVISRIQIEEIIKE---AKPTLIFVEHDKRFVEDIANKIIQ 491
Cdd:COG2884 153 vNRPE-LLLADEPTGNLDPETSWEIMELLEEinrRGTTVLIATHDLELVDRMPKRVLE 209
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
33-229 |
2.92e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 69.04 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 33 KTGLIGRNGIGKSTLFKLLLNQ-ETYQGKI--SKDV----------EFIKfppniSDTSKLgiDLYKELISDDEEWKLFR 99
Cdd:PRK10636 340 RIGLLGRNGAGKSTLIKLLAGElAPVSGEIglAKGIklgyfaqhqlEFLR-----ADESPL--QHLARLAPQELEQKLRD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 100 ELNLLNVDENLVYREFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGRKILSEYLKSKKGFL-LISHDRNFLDG 178
Cdd:PRK10636 413 YLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALvVVSHDRHLLRS 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493786691 179 CINHVISINRNSIDVQSG---NFTSWY------ENKLMKDKFEISKNE-KLRKDIKRlKEA 229
Cdd:PRK10636 493 TTDDLYLVHDGKVEPFDGdleDYQQWLsdvqkqENQTDEAPKENNANSaQARKDQKR-REA 552
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
310-490 |
2.98e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 68.65 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHY-GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGInHEYT-GEIKL---------ASNL--KISY 376
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF-YDPTsGRILIdgvdirdltLESLrrQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 377 IPQDTSNLSGSLNEYIH--SQDVDETLCKTILRK---LDFARELFEmdmiDY-----------SDGQKKKVLIALSLSKP 440
Cdd:COG1132 419 VPQDTFLFSGTIRENIRygRPDATDEEVEEAAKAaqaHEFIEALPD----GYdtvvgergvnlSGGQRQRIAIARALLKD 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493786691 441 AHLFIWDEPLNYIDVIS--RIQ--IEEIIKEAkpTLIFVEHdkRF--VEDiANKII 490
Cdd:COG1132 495 PPILILDEATSALDTETeaLIQeaLERLMKGR--TTIVIAH--RLstIRN-ADRIL 545
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-187 |
3.34e-12 |
|
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: 64.90 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQETyqgKISKDVEFikfppnisdtskLGID 83
Cdd:cd03229 1 LELKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE---PDSGSILI------------DGED 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 84 LYKELISDDEEWK----LFRELNL---LNVDENLVYRefktLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGRKIL 156
Cdd:cd03229 64 LTDLEDELPPLRRrigmVFQDFALfphLTVLENIALG----LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREV 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 493786691 157 SEYLKS-----KKGFLLISHDRNFLDGCINHVISIN 187
Cdd:cd03229 140 RALLKSlqaqlGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
315-492 |
3.89e-12 |
|
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: 64.52 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 315 LSAHYGERQILSNLSfEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLaSNLKISYIPQdtsnlsgslneyihs 394
Cdd:cd03222 6 CVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVYKPQ--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 395 qdvdetlcktilrkldfarelfemdMIDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIK----EAKP 470
Cdd:cd03222 69 -------------------------YIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRrlseEGKK 123
|
170 180
....*....|....*....|..
gi 493786691 471 TLIFVEHDKRFVEDIANKIIQF 492
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHVF 145
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
319-489 |
5.52e-12 |
|
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: 64.97 E-value: 5.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 319 YGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLkISYIPQDTSNLSGSLNEY------- 391
Cdd:cd03301 10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD-VTDLPPKDRDIAMVFQNYalyphmt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 392 ----------IHSQDVDEtlcktILRKLDFARELFEMDMI------DYSDGQKKKVLIALSLSKPAHLFIWDEPLNYID- 454
Cdd:cd03301 89 vydniafglkLRKVPKDE-----IDERVREVAELLQIEHLldrkpkQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDa 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 493786691 455 ---VISRIQIEEIIKEAKPTLIFVEHDKRFVEDIANKI 489
Cdd:cd03301 164 klrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRI 201
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
306-478 |
5.99e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 66.19 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 306 KNPLISVSELSAHY--GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNL----------- 372
Cdd:PRK13635 2 KEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 373 KISYIPQDTSN-LSGSLNEyihsQDV-----------DEtlcktILRKLDFARELFEM-DMIDY-----SDGQKKKVLIA 434
Cdd:PRK13635 82 QVGMVFQNPDNqFVGATVQ----DDVafglenigvprEE-----MVERVDQALRQVGMeDFLNRephrlSGGQKQRVAIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493786691 435 LSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKP----TLIFVEHD 478
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqkgiTVLSITHD 200
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
308-489 |
6.69e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.78 E-value: 6.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLaSNLKISYIPQDTSNLSGS 387
Cdd:PRK11607 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLSHVPPYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 388 LNEYI---H---SQDVDETLCKTILRKLDFARELFEM----DMIDY--------SDGQKKKVLIALSLSKPAHLFIWDEP 449
Cdd:PRK11607 97 FQSYAlfpHmtvEQNIAFGLKQDKLPKAEIASRVNEMlglvHMQEFakrkphqlSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493786691 450 LNYID--VISRIQIE--EIIKEAKPTLIFVEHDKRFVEDIANKI 489
Cdd:PRK11607 177 MGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQEEAMTMAGRI 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
310-477 |
7.01e-12 |
|
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: 64.82 E-value: 7.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHY--GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEI-------------KLASnlKI 374
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIlidgvdiskiglhDLRS--RI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 375 SYIPQDTSNLSGSLNEYI--HSQDVDETL------------CKTILRKLDFareLFEMDMIDYSDGQKKKVLIALSLSKP 440
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLdpFGEYSDEELwqalervglkefVESLPGGLDT---VVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 493786691 441 AHLFIWDEPLNYIDVISRIQIEEIIKE--AKPTLIFVEH 477
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREafKDCTVLTIAH 196
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-205 |
7.02e-12 |
|
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: 67.48 E-value: 7.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 3 AIKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQ-ETYQGKIS-KDVEFIKFPP-----NIS 75
Cdd:COG4987 333 SLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFlDPQSGSITlGGVDLRDLDEddlrrRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 76 ---------DTS-----KLGidlyKELISDDEEWKLFRELNLLNVDENL-------VYREFKTLSKGEQTKILLAILFTK 134
Cdd:COG4987 413 vvpqrphlfDTTlrenlRLA----RPDATDEELWAALERVGLGDWLAALpdgldtwLGEGGRRLSGGERRRLALARALLR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493786691 135 EDGFLLIDEPTNHLD-MNGRKILSEYLKSKKG--FLLISHDRNFLDGCiNHVISINRNSIdVQSGNFTSWYENK 205
Cdd:COG4987 489 DAPILLLDEPTEGLDaATEQALLADLLEALAGrtVLLITHRLAGLERM-DRILVLEDGRI-VEQGTHEELLAQN 560
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
308-490 |
7.94e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.48 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHY---------GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA----SNLK- 373
Cdd:PRK10419 2 TLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRgeplAKLNr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 374 ---------ISYIPQDTS---NLSGSLNEYI-----HSQDVDET----LCKTILRKLDFARELFEMDMIDYSDGQKKKVL 432
Cdd:PRK10419 82 aqrkafrrdIQMVFQDSIsavNPRKTVREIIreplrHLLSLDKAerlaRASEMLRAVDLDDSVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493786691 433 IALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKPTL----IFVEHDKRFVEDIANKII 490
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFgtacLFITHDLRLVERFCQRVM 223
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
321-466 |
9.82e-12 |
|
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: 64.21 E-value: 9.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 321 ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEY---TGEIKLA--SNLKISYIPQDTSNLSGSLNEYIHSQ 395
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNgiPYKEFAEKYPGEIIYVSEEDVHFPTL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493786691 396 DVDETlcktilrkLDFARELFEMDMI-DYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIK 466
Cdd:cd03233 99 TVRET--------LDFALRCKGNEFVrGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIR 162
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
317-489 |
1.19e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.68 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 317 AHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIPQDTsnlsgSLNEyihSQD 396
Cdd:PRK11819 15 VVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEP-----QLDP---EKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 397 VDETL------CKTILRKLD-----FARELFEMD-----------MIDYSD----------------------------- 425
Cdd:PRK11819 87 VRENVeegvaeVKAALDRFNeiyaaYAEPDADFDalaaeqgelqeIIDAADawdldsqleiamdalrcppwdakvtklsg 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493786691 426 GQKKKV-LIALSLSKPaHLFIWDEPLNYIDVISRIQIEEIIKEAKPTLIFVEHDKRFVEDIANKI 489
Cdd:PRK11819 167 GERRRVaLCRLLLEKP-DMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWI 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
312-463 |
1.31e-11 |
|
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: 63.67 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 312 VSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIPQDTSNLSgslneY 391
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLL-----Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 392 I-HSQDVDETLckTILRKLDFARE----------LFEMDMIDYSD--------GQKKKVLIALSLSKPAHLFIWDEPLNY 452
Cdd:cd03231 78 LgHAPGIKTTL--SVLENLRFWHAdhsdeqveeaLARVGLNGFEDrpvaqlsaGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170
....*....|.
gi 493786691 453 IDVISRIQIEE 463
Cdd:cd03231 156 LDKAGVARFAE 166
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
327-490 |
1.33e-11 |
|
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: 63.85 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 327 NLSFEIEqGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL------ASNLKISYIPQD--TSNLSGSLNEYIHsQDVD 398
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfDSRKKINLPPQQrkIGLVFQQYALFPH-LNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 399 ETLCKTILRKLDFARELFEMDMIDY--------------SDGQKKKVLIALSL-SKPAHLFIwDEPLNYIDVISRIQI-- 461
Cdd:cd03297 94 ENLAFGLKRKRNREDRISVDELLDLlgldhllnrypaqlSGGEKQRVALARALaAQPELLLL-DEPFSALDRALRLQLlp 172
|
170 180 190
....*....|....*....|....*....|.
gi 493786691 462 --EEIIKEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:cd03297 173 elKQIKKNLNIPVIFVTHDLSEAEYLADRIV 203
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
310-490 |
1.48e-11 |
|
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: 64.13 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGE-RQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL---------ASNL-----KI 374
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIdgtdinklkGKALrqlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 375 SYIPQD----------TSNLSGSLNEYihsqdvdeTLCKTILRKLD-----FARELFE-MDMIDY--------SDGQKKK 430
Cdd:cd03256 81 GMIFQQfnlierlsvlENVLSGRLGRR--------STWRSLFGLFPkeekqRALAALErVGLLDKayqradqlSGGQQQR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493786691 431 VLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKP----TLIFVEHDKRFVEDIANKII 490
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReegiTVIVSLHQVDLAREYADRIV 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
310-368 |
2.01e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 64.74 E-value: 2.01e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL 368
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW 60
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
321-490 |
2.15e-11 |
|
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: 63.66 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 321 ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASN-----------LKISYIPQDTSNLSGSLN 389
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlaladpawlrRQVGVVLQENVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 390 EYIHSQDVDETLCKTI-LRKL----DFARELFE-MDMI------DYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVIS 457
Cdd:cd03252 94 DNIALADPGMSMERVIeAAKLagahDFISELPEgYDTIvgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATSALDYES 173
|
170 180 190
....*....|....*....|....*....|....*
gi 493786691 458 RIQIEEIIKE--AKPTLIFVEHDKRFVEDiANKII 490
Cdd:cd03252 174 EHAIMRNMHDicAGRTVIIIAHRLSTVKN-ADRII 207
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-151 |
2.93e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.49 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQETYQ-GKISKDVEFIK------------F 70
Cdd:PRK11231 3 LRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISmlssrqlarrlaL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 71 PPNISDTSKlGIDLyKELI--------------SDDEEWKLFRELNLLNVDEnLVYREFKTLSKGEQTKILLAILFTKED 136
Cdd:PRK11231 81 LPQHHLTPE-GITV-RELVaygrspwlslwgrlSAEDNARVNQAMEQTRINH-LADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170
....*....|....*
gi 493786691 137 GFLLIDEPTNHLDMN 151
Cdd:PRK11231 158 PVVLLDEPTTYLDIN 172
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
324-463 |
3.28e-11 |
|
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: 64.11 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 324 ILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASnlKISYIPQDTSNLSGSLNEYI-HSQDVDETLC 402
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--RISFSSQFSWIMPGTIKENIiFGVSYDEYRY 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493786691 403 KTILRKLDFARELFEMDMIDY----------SDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEE 463
Cdd:cd03291 130 KSVVKACQLEEDITKFPEKDNtvlgeggitlSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFE 200
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-161 |
3.41e-11 |
|
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: 66.09 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 6 IQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQETYQGKISKD-------------VEFIKFPP 72
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDgvswnsvtlqtwrKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 73 NI---SDTSKLGIDLYkELISDDEEWKLFRELNLLNVDENLVYR-EFK------TLSKGEQTKILLAILFTKEDGFLLID 142
Cdd:TIGR01271 1300 KVfifSGTFRKNLDPY-EQWSDEEIWKVAEEVGLKSVIEQFPDKlDFVlvdggyVLSNGHKQLMCLARSILSKAKILLLD 1378
|
170
....*....|....*....
gi 493786691 143 EPTNHLDMNGRKILSEYLK 161
Cdd:TIGR01271 1379 EPSAHLDPVTLQIIRKTLK 1397
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
309-489 |
3.56e-11 |
|
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: 65.23 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGI--NHEYTGEIKL------ASNLK------I 374
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWsgsplkASNIRdteragI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 375 SYIPQDTS---NLSGSLNEYIHSQ--------DVDETL--CKTILRKLDFARELFEMDMIDYSDGQKKKVLIALSLSKPA 441
Cdd:TIGR02633 81 VIIHQELTlvpELSVAENIFLGNEitlpggrmAYNAMYlrAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493786691 442 HLFIWDEPLNyidVISRIQIE---EIIKEAKP---TLIFVEHDKRFVEDIANKI 489
Cdd:TIGR02633 161 RLLILDEPSS---SLTEKETEillDIIRDLKAhgvACVYISHKLNEVKAVCDTI 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
310-468 |
3.58e-11 |
|
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: 63.01 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGE-RQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL---------ASNL--KISYI 377
Cdd:cd03254 3 IEFENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdgidirdisRKSLrsMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 378 PQDTSNLSGSLNEYI-----HSQDVDETLCKTILRKLDFARELFE-MDMI------DYSDGQKKKVLIALSLSKPAHLFI 445
Cdd:cd03254 83 LQDTFLFSGTIMENIrlgrpNATDEEVIEAAKEAGAHDFIMKLPNgYDTVlgenggNLSQGERQLLAIARAMLRDPKILI 162
|
170 180
....*....|....*....|...
gi 493786691 446 WDEPLNYIDVISriqiEEIIKEA 468
Cdd:cd03254 163 LDEATSNIDTET----EKLIQEA 181
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
325-490 |
3.95e-11 |
|
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: 62.43 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 325 LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA----SNLKISYIP----------QDtSNLSGSLNE 390
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvSDLRGRAIPylrrkigvvfQD-FRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 391 Y-----------IHSQDVDETLcKTILRKLDFARELFEMDMiDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRI 459
Cdd:cd03292 96 YenvafalevtgVPPREIRKRV-PAALELVGLSHKHRALPA-ELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTW 173
|
170 180 190
....*....|....*....|....*....|....
gi 493786691 460 QIEEIIKE---AKPTLIFVEHDKRFVEDIANKII 490
Cdd:cd03292 174 EIMNLLKKinkAGTTVVVATHAKELVDTTRHRVI 207
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-184 |
4.65e-11 |
|
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: 62.81 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 35 GLIGRNGIGKSTLFKLLLNQ-ETYQGKISKDVEFIKFPPN--ISDTSKLGIDLYKELISDDEEWKLFRE--LNLLNVdEN 109
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGVlKPDEGDIEIELDTVSYKPQyiKADYEGTVRDLLSSITKDFYTHPYFKTeiAKPLQI-EQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 110 LVYREFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGR----KILSEY-LKSKKGFLLISHDRNFLDGCINHVI 184
Cdd:cd03237 108 ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasKVIRRFaENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
321-490 |
4.96e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.53 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 321 ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL------ASNLKISYIPQDTsnlsGSLNEYIHS 394
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditDKKVKLSDIRKKV----GLVFQYPEY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 395 QDVDETLCKTI--------------LRKLDFARELFEMDMIDYSD--------GQKKKVLIALSLSKPAHLFIWDEPLNY 452
Cdd:PRK13637 95 QLFEETIEKDIafgpinlglseeeiENRVKRAMNIVGLDYEDYKDkspfelsgGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493786691 453 IDVISR----IQIEEIIKEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:PRK13637 175 LDPKGRdeilNKIKELHKEYNMTIILVSHSMEDVAKLADRII 216
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
310-467 |
5.15e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.36 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHY-GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIK---------LASNLkISYIPQ 379
Cdd:PRK15056 7 IVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgqptrqaLQKNL-VAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 380 dTSNLSGS----------LNEYIH-----------SQDVDETLCKtilrkldfarelfeMDMIDY--------SDGQKKK 430
Cdd:PRK15056 86 -SEEVDWSfpvlvedvvmMGRYGHmgwlrrakkrdRQIVTAALAR--------------VDMVEFrhrqigelSGGQKKR 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 493786691 431 VLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKE 467
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRE 187
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
310-485 |
5.53e-11 |
|
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: 61.77 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGiNHEYT---GEIKLASnlkisyipQDTSNLSg 386
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKYEvteGEILFKG--------EDITDLP- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 387 slneyihsqdVDETLCKTI------------LRKLDFARELFEmdmiDYSDGQKKKVLIA-LSLSKPaHLFIWDEPLNYI 453
Cdd:cd03217 71 ----------PEERARLGIflafqyppeipgVKNADFLRYVNE----GFSGGEKKRNEILqLLLLEP-DLAILDEPDSGL 135
|
170 180 190
....*....|....*....|....*....|....*
gi 493786691 454 DVISRIQIEEII---KEAKPTLIFVEHDKRFVEDI 485
Cdd:cd03217 136 DIDALRLVAEVInklREEGKSVLIITHYQRLLDYI 170
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
310-490 |
5.62e-11 |
|
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: 62.45 E-value: 5.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA------------SNLKISYI 377
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgeditglppheiARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 378 PQDTSNLSG-SLNEYI----HSQDVDETLCKTILRKLDFARE-----LFEMDMIDYSD--------GQKKKVLIALSLSK 439
Cdd:cd03219 81 FQIPRLFPElTVLENVmvaaQARTGSGLLLARARREEREAREraeelLERVGLADLADrpagelsyGQQRRLEIARALAT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493786691 440 PAHLFIWDEPLNYIDVISRIQIEEIIKEAKP---TLIFVEHDKRFVEDIANKII 490
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRErgiTVLLVEHDMDVVMSLADRVT 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
324-463 |
5.64e-11 |
|
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: 65.32 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 324 ILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASnlKISYIPQDTSNLSGSLNEYI-HSQDVDETLC 402
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--RISFSPQTSWIMPGTIKDNIiFGLSYDEYRY 518
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493786691 403 KTILRKLDFARELF---EMDM-------IDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEE 463
Cdd:TIGR01271 519 TSVIKACQLEEDIAlfpEKDKtvlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFE 589
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
310-490 |
9.29e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.51 E-value: 9.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLAsNLKISYIPQDTSNL----- 384
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG-EKRMNDVPPAERGVgmvfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 385 SGSLneYIHsQDVDET------LCKT----ILRKLDFARELFEMDMI------DYSDGQKKKVLIALSLSKPAHLFIWDE 448
Cdd:PRK11000 83 SYAL--YPH-LSVAENmsfglkLAGAkkeeINQRVNQVAEVLQLAHLldrkpkALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493786691 449 PLNYID----VISRIQIEEIIKEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:PRK11000 160 PLSNLDaalrVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIV 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
310-490 |
9.59e-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: 64.05 E-value: 9.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLKI----------SYIPQ 379
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 380 DTSNLSGSLNEY-IHSQDVDETLCKTILRK-----------------------------------LDFARELFEMDMI-- 421
Cdd:TIGR03269 81 PCPVCGGTLEPEeVDFWNLSDKLRRRIRKRiaimlqrtfalygddtvldnvlealeeigyegkeaVGRAVDLIEMVQLsh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 422 -------DYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDV----ISRIQIEEIIKEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:TIGR03269 161 rithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPqtakLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
310-478 |
1.30e-10 |
|
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: 61.48 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNlKISYIPQDTSNLSGSLN 389
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK-DITNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 390 EYI---HsQDVDETLC----------KTILRKLDFARELFEMD-----MID-YSDGQKKKVLIALSLSKPAHLFIWDEPL 450
Cdd:cd03300 80 NYAlfpH-LTVFENIAfglrlkklpkAEIKERVAEALDLVQLEgyanrKPSqLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190
....*....|....*....|....*....|..
gi 493786691 451 NYIDVISR--IQIE--EIIKEAKPTLIFVEHD 478
Cdd:cd03300 159 GALDLKLRkdMQLElkRLQKELGITFVFVTHD 190
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
322-477 |
1.37e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.67 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 322 RQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGI-NHeYTGEIKLASNLKISYIPQDTSNLSGSLNEYI----HSQD 396
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwPY-GSGRIARPAGARVLFLPQRPYLPLGTLREALlypaTAEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 397 VDETLCKTILRKL-------------DFARELfemdmidySDGQKKKVLIA-LSLSKPAHLFIwDEPLNYIDVISRIQIE 462
Cdd:COG4178 455 FSDAELREALEAVglghlaerldeeaDWDQVL--------SLGEQQRLAFArLLLHKPDWLFL-DEATSALDEENEAALY 525
|
170
....*....|....*..
gi 493786691 463 EIIKEAKP--TLIFVEH 477
Cdd:COG4178 526 QLLREELPgtTVISVGH 542
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
310-490 |
1.56e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 60.56 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQ-----ILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASnlKISYIPQDTSNL 384
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 385 SGSLNEYI-HSQDVDETLCKTILR----KLDFarELFEM-DM-------IDYSDGQKKKVLIALSLSKPAHLFIWDEPLN 451
Cdd:cd03250 79 NGTIRENIlFGKPFDEERYEKVIKacalEPDL--EILPDgDLteigekgINLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493786691 452 YID--VISRIqIEEII----KEAKpTLIFVEHDKRFVEDiANKII 490
Cdd:cd03250 157 AVDahVGRHI-FENCIlgllLNNK-TRILVTHQLQLLPH-ADQIV 198
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
310-490 |
1.68e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 61.68 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGE-RQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNL-----------KISYI 377
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvnaenekwvrsKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 378 PQDTSN--LSGSLNEYIHSQDVDETLCKT-ILRKLDFAreLFEMDMIDYSD--------GQKKKVLIALSLSKPAHLFIW 446
Cdd:PRK13647 85 FQDPDDqvFSSTVWDDVAFGPVNMGLDKDeVERRVEEA--LKAVRMWDFRDkppyhlsyGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493786691 447 DEPLNYIDVISRIQIEEII----KEAKpTLIFVEHDKRFVEDIANKII 490
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILdrlhNQGK-TVIVATHDVDLAAEWADQVI 209
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-161 |
1.70e-10 |
|
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: 61.79 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQETYQGKISKD-VEFIKFPPN--------- 73
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDgVSWNSVPLQkwrkafgvi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 74 ------ISDTSKLGIDLYKELiSDDEEWKLFRELNLLNVDEN--------LVYREFkTLSKGEQTKILLAILFTKEDGFL 139
Cdd:cd03289 83 pqkvfiFSGTFRKNLDPYGKW-SDEEIWKVAEEVGLKSVIEQfpgqldfvLVDGGC-VLSHGHKQLMCLARSVLSKAKIL 160
|
170 180
....*....|....*....|..
gi 493786691 140 LIDEPTNHLDMNGRKILSEYLK 161
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLK 182
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-171 |
1.91e-10 |
|
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: 60.31 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLnqetyqGKISKD---VEF--IKFPPNISDTS 78
Cdd:cd03268 1 LKTNDLTKTYGK--KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIL------GLIKPDsgeITFdgKSYQKNIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 79 KLG--ID---LYKELiSDDEEWKLFRELNLL---NVDENLVY--------REFKTLSKGEQTKILLAILFTKEDGFLLID 142
Cdd:cd03268 73 RIGalIEapgFYPNL-TARENLRLLARLLGIrkkRIDEVLDVvglkdsakKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190
....*....|....*....|....*....|...
gi 493786691 143 EPTNHLDMNG----RKILSEYLKSKKGFLLISH 171
Cdd:cd03268 152 EPTNGLDPDGikelRELILSLRDQGITVLISSH 184
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
310-490 |
1.92e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.14 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKIL----------LGINHEYT-------GEIKLASNL 372
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsegsIVVNGQTInlvrdkdGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 373 KISYIPQDTSNLSGSLNEYIHSQDVDETLCKTI----LRKLDfARE--LFEMDMI------------DYSDGQKKKVLIA 434
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIqvlgLSKQE-AREraVKYLAKVgideraqgkypvHLSGGQQQRVSIA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493786691 435 LSLSKPAHLFIWDEPLNYID---VISRIQIEEIIKEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVI 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-191 |
2.03e-10 |
|
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: 60.68 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 3 AIKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQ-ETYQGKISKD-VEFIKFPP-----NI- 74
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLyKPTSGSVLLDgTDIRQLDPadlrrNIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 75 ---------SDTSKLGIDLyKELISDDEEwkLFRELNLLNVDE---------NLVYREF-KTLSKGEQTKILLAILFTKE 135
Cdd:cd03245 82 yvpqdvtlfYGTLRDNITL-GAPLADDER--ILRAAELAGVTDfvnkhpnglDLQIGERgRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493786691 136 DGFLLIDEPTNHLDMNGRKILSEYLK---SKKGFLLISHDRNFLDGCiNHVISINRNSI 191
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRqllGDKTLIIITHRPSLLDLV-DRIIVMDSGRI 216
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
310-368 |
2.04e-10 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 62.09 E-value: 2.04e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL 368
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL 61
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
308-478 |
2.15e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 62.04 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA----SNLK-----ISYIP 378
Cdd:COG3842 4 PALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvTGLPpekrnVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 379 QDtsnlsgslneY---------------IHSQDVDEtlcKTILRKldfARELFEM-DMIDYSD--------GQKKKVLIA 434
Cdd:COG3842 84 QD----------YalfphltvaenvafgLRMRGVPK---AEIRAR---VAELLELvGLEGLADryphqlsgGQQQRVALA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493786691 435 LSL-SKPAHLFIwDEPLNYIDVISR--IQIE--EIIKEAKPTLIFVEHD 478
Cdd:COG3842 148 RALaPEPRVLLL-DEPLSALDAKLReeMREElrRLQRELGITFIYVTHD 195
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-171 |
2.38e-10 |
|
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: 60.12 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLN-QETYQGKIS---KDVEFIKF--------- 70
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRfLEAEEGKIEidgIDISTIPLedlrsslti 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 71 ----PPNISDTSKLGIDLYKELisDDEEwkLFRELNLLNVDENlvyrefktLSKGEQTKILLAILFTKEDGFLLIDEPTN 146
Cdd:cd03369 87 ipqdPTLFSGTIRSNLDPFDEY--SDEE--IYGALRVSEGGLN--------LSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180
....*....|....*....|....*...
gi 493786691 147 HLDMNGRKILSEYLK---SKKGFLLISH 171
Cdd:cd03369 155 SIDYATDALIQKTIReefTNSTILTIAH 182
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
309-460 |
2.50e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNlkisYIPQDTSNLSGSL 388
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ----SIKKDLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 389 NEYIHSQDVDE--TLCKTILRKLDFARELFEMD----------MIDY-----SDGQKKKV-LIALSLSKpAHLFIWDEPL 450
Cdd:PRK13540 77 CFVGHRSGINPylTLRENCLYDIHFSPGAVGITelcrlfslehLIDYpcgllSSGQKRQVaLLRLWMSK-AKLWLLDEPL 155
|
170
....*....|....*.
gi 493786691 451 NYID------VISRIQ 460
Cdd:PRK13540 156 VALDelslltIITKIQ 171
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
321-490 |
2.60e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 61.38 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 321 ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASnlkiSYIPQDTSNLS--------GSLNEYI 392
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAG----YHITPETGNKNlkklrkkvSLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 393 HSQDVDETLCKTI---------------------LRKLDFARELFEMDMIDYSDGQKKKVLIALSLSKPAHLFIWDEPLN 451
Cdd:PRK13641 95 EAQLFENTVLKDVefgpknfgfsedeakekalkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493786691 452 YIDVISRIQIEEIIKE---AKPTLIFVEHDKRFVEDIANKII 490
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDyqkAGHTVILVTHNMDDVAEYADDVL 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-171 |
2.70e-10 |
|
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: 59.25 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLL-NQETYQGKISKDVEfikfppnisDTSKLGI 82
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTgDLKPQQGEITLDGV---------PVSDLEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 83 DLYKELISDDEEWKLFrELNLLNvdeNLVYRefktLSKGEQTKILLAILFTKEDGFLLIDEPTNHLD-MNGRKILS---E 158
Cdd:cd03247 72 ALSSLISVLNQRPYLF-DTTLRN---NLGRR----FSGGERQRLALARILLQDAPIVLLDEPTVGLDpITERQLLSlifE 143
|
170
....*....|...
gi 493786691 159 YLKSKKgFLLISH 171
Cdd:cd03247 144 VLKDKT-LIWITH 155
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
325-490 |
3.43e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.26 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 325 LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA---------SNLK-ISYI------------PQDTS 382
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLgyvpfkrrkEFARrIGVVfgqrsqlwwdlpAIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 383 NlsgsLNEYIHsqDVDEtlcKTILRKLDFARELFEMDmiDY--------SDGQKKKVLIALSL-SKPAHLFIwDEPLNYI 453
Cdd:COG4586 118 R----LLKAIY--RIPD---AEYKKRLDELVELLDLG--ELldtpvrqlSLGQRMRCELAAALlHRPKILFL-DEPTIGL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493786691 454 DVISRIQIEEIIKE----AKPTLIFVEHDKRFVEDIANKII 490
Cdd:COG4586 186 DVVSKEAIREFLKEynreRGTTILLTSHDMDDIEALCDRVI 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
310-490 |
3.44e-10 |
|
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: 60.43 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL----ASNLK-----ISYIPQD 380
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFggedATDVPvqernVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 381 TS---------NLSGSLNEYIHSQDVDETlckTILRKldfARELFEMDMIDY---------SDGQKKKVLIALSLSKPAH 442
Cdd:cd03296 83 YAlfrhmtvfdNVAFGLRVKPRSERPPEA---EIRAK---VHELLKLVQLDWladrypaqlSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493786691 443 LFIWDEPLNYIDVISRIQ----IEEIIKEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:cd03296 157 VLLLDEPFGALDAKVRKElrrwLRRLHDELHVTTVFVTHDQEEALEVADRVV 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
306-477 |
4.16e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 62.15 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 306 KNPLISVSELSAHYGERQ--ILSNLSFEIEQGDIVAISGRNGSGKSTLIKILlgiNHEY---TGEIKLA---------SN 371
Cdd:PRK11160 335 DQVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL---TRAWdpqQGEILLNgqpiadyseAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 372 LK--ISYIPQDTSNLSGSL-------NEYIHSQDVDETLCKTILRKL------------DFARELfemdmidySDGQKKK 430
Cdd:PRK11160 412 LRqaISVVSQRVHLFSATLrdnlllaAPNASDEALIEVLQQVGLEKLleddkglnawlgEGGRQL--------SGGEQRR 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493786691 431 VLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKE--AKPTLIFVEH 477
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEhaQNKTVLMITH 532
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
307-366 |
4.35e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.89 E-value: 4.35e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 307 NPLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEI 366
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRI 62
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
325-489 |
4.44e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 325 LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGI--NHEYTGEI------KLASNLK------ISYIPQD---TSNLSGS 387
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIifegeeLQASNIRdteragIAIIHQElalVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 388 LNEYIHSQ-------DVDETL--CKTILRKLdfarelfEMDM------IDYSDGQKKKVLIALSLSKPAHLFIWDEPLNy 452
Cdd:PRK13549 101 ENIFLGNEitpggimDYDAMYlrAQKLLAQL-------KLDInpatpvGNLGLGQQQLVEIAKALNKQARLLILDEPTA- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493786691 453 idVISRIQIE---EIIKEAKP---TLIFVEHDKRFVEDIANKI 489
Cdd:PRK13549 173 --SLTESETAvllDIIRDLKAhgiACIYISHKLNEVKAISDTI 213
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
321-490 |
4.70e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.56 E-value: 4.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 321 ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTG-----EIKLASNLKISYIPQDTSNLsGSLNEYIHSQ 395
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGtvtvdDITITHKTKDKYIRPVRKRI-GMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 396 DVDETLCKTI---------------------LRKLDFARELFEMDMIDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYID 454
Cdd:PRK13646 98 LFEDTVEREIifgpknfkmnldevknyahrlLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493786691 455 VISRIQIEEIIK----EAKPTLIFVEHDKRFVEDIANKII 490
Cdd:PRK13646 178 PQSKRQVMRLLKslqtDENKTIILVSHDMNEVARYADEVI 217
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-177 |
5.62e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.20 E-value: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 18 KPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQET-YQGKISKDVEFIKFPPNISdtsklGID-LYKELISDDEew 95
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgTPVAGCVDVPDNQFGREAS-----LIDaIGRKGDFKDA-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 96 klfreLNLLN----VDENLVYREFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMN-----GRKILSEYLKSKKGF 166
Cdd:COG2401 116 -----VELLNavglSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQtakrvARNLQKLARRAGITL 190
|
170
....*....|.
gi 493786691 167 LLISHDRNFLD 177
Cdd:COG2401 191 VVATHHYDVID 201
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
310-490 |
5.76e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 59.64 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNL----------KISYIPQ 379
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfsktpsdkAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 380 DTSNLSGSLNEYIH---SQDVDETLCKTI-----------------LRKLDFArELFEMDMidySDGQKKKVLIALSLSK 439
Cdd:PRK11124 83 NVGMVFQQYNLWPHltvQQNLIEAPCRVLglskdqalaraekllerLRLKPYA-DRFPLHL---SGGQQQRVAIARALMM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493786691 440 PAHLFIWDEPLNYIDVISRIQIEEIIKEAKPTLI---FVEHDKRFVEDIANKII 490
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHEVEVARKTASRVV 212
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
307-369 |
5.88e-10 |
|
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: 59.37 E-value: 5.88e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493786691 307 NPLISVSELSAHYGER----QILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA 369
Cdd:COG4181 6 APIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLA 72
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
323-477 |
7.30e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.40 E-value: 7.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 323 QILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGiNHEYTGEIKLA----SNL-------KISYIPQDTSNLSGSLNEY 391
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINgielRELdpeswrkHLSWVGQNPQLPHGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 392 I--HSQDVDETLCKTILRK---LDFARELfeMDMIDY---------SDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVIS 457
Cdd:PRK11174 443 VllGNPDASDEQLQQALENawvSEFLPLL--PQGLDTpigdqaaglSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180
....*....|....*....|..
gi 493786691 458 RIQIEEIIKEA--KPTLIFVEH 477
Cdd:PRK11174 521 EQLVMQALNAAsrRQTTLMVTH 542
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
310-478 |
7.37e-10 |
|
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: 59.24 E-value: 7.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQ-ILSNLSFEIEQGDIVAISGRNGSGKSTLIKIllgINH--EYT-GEIKLA---------SNL--KI 374
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKM---INRliEPTsGEIFIDgedireqdpVELrrKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 375 SYIPQDTS---------------NLSGSLNEYIhSQDVDETLCKTILRKLDFA----RELfemdmidySDGQKKKVLIAL 435
Cdd:cd03295 78 GYVIQQIGlfphmtveenialvpKLLKWPKEKI-RERADELLALVGLDPAEFAdrypHEL--------SGGQQQRVGVAR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493786691 436 SLSKPAHLFIWDEPLNYIDVISRIQIEE----IIKEAKPTLIFVEHD 478
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEefkrLQQELGKTIVFVTHD 195
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
310-463 |
7.72e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 60.23 E-value: 7.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL----------ASNLKISYIPQ 379
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvpararLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 380 -DTSNLSGSLNEYI---------HSQDVDEtlckTILRKLDFARELFEMD--MIDYSDGQKKKVLIALSLSKPAHLFIWD 447
Cdd:PRK13536 122 fDNLDLEFTVRENLlvfgryfgmSTREIEA----VIPSLLEFARLESKADarVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170
....*....|....*.
gi 493786691 448 EPLNYIDVISRIQIEE 463
Cdd:PRK13536 198 EPTTGLDPHARHLIWE 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
308-449 |
1.01e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.57 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEI------------KLASNLKIS 375
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinninynkldhKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 376 YIPQDTS---NLSGSLNEYIHSQDVDETL-------------CKTILRKLDFARELFEMdMIDYSDGQKKKVLIALSLSK 439
Cdd:PRK09700 84 IIYQELSvidELTVLENLYIGRHLTKKVCgvniidwremrvrAAMMLLRVGLKVDLDEK-VANLSISHKQMLEIAKTLML 162
|
170
....*....|
gi 493786691 440 PAHLFIWDEP 449
Cdd:PRK09700 163 DAKVIIMDEP 172
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
315-488 |
1.22e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 58.75 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 315 LSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL------------ASNLKISYIPQDTS 382
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplhaRARRGIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 383 ---NLSgSLNEYIHSQDVDETLckTILRKLDFARELFEMDMIDY---------SDGQKKKVLIALSLSKPAHLFIWDEPL 450
Cdd:PRK10895 89 ifrRLS-VYDNLMAVLQIRDDL--SAEQREDRANELMEEFHIEHlrdsmgqslSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493786691 451 NYIDVISRIQIEEIIKEAKPT---LIFVEHDKRFVEDIANK 488
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDSglgVLITDHNVRETLAVCER 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
309-490 |
1.44e-09 |
|
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: 58.15 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHY----GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEI----------KLASNLKI 374
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAtvdgfdvvkePAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 375 SYIPQDTS---NLSGSLN-EY---IHSQDVDETL--CKTILRKLDFaRELFEMDMIDYSDGQKKKVLIALSL-SKPAHLf 444
Cdd:cd03266 81 GFVSDSTGlydRLTARENlEYfagLYGLKGDELTarLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALvHDPPVL- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493786691 445 IWDEPLNYIDVISRIQIEEII---KEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIrqlRALGKCILFSTHIMQEVERLCDRVV 207
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
315-368 |
2.21e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 57.77 E-value: 2.21e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 493786691 315 LSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGI-NHEYT-GEIKL 368
Cdd:COG0396 6 LHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpKYEVTsGSILL 61
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
307-490 |
2.31e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.97 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 307 NPLISVSELSAHY----GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGI---NHEYTGEIKLAS----NL--- 372
Cdd:PRK09473 10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGreilNLpek 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 373 --------KISYIPQDTSNlsgSLNEYIHsqdVDETLCKTIL---------------RKLDF-----ARELFEMDMIDYS 424
Cdd:PRK09473 90 elnklraeQISMIFQDPMT---SLNPYMR---VGEQLMEVLMlhkgmskaeafeesvRMLDAvkmpeARKRMKMYPHEFS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 425 DGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAK----PTLIFVEHDKRFVEDIANKII 490
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrefnTAIIMITHDLGVVAGICDKVL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
321-490 |
2.42e-09 |
|
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: 57.63 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 321 ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILL-------G---INHEYTGEIKLAS-NLKISYIPQDT-------- 381
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFrfydvssGsilIDGQDIREVTLDSlRRAIGVVPQDTvlfndtig 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 382 -----SNLSGSLNEYIHS---QDVDETLCK------TIL--RKLdfarelfemdMIdySDGQKKKVLIALSLSKPAHLFI 445
Cdd:cd03253 93 yniryGRPDATDEEVIEAakaAQIHDKIMRfpdgydTIVgeRGL----------KL--SGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493786691 446 WDEPLNYIDVISRIQIEEIIKE--AKPTLIFVEHDKRFVEDiANKII 490
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDvsKGRTTIVIAHRLSTIVN-ADKII 206
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
306-478 |
2.67e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.84 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 306 KNPLISVSELSAHY--GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIkLASNLKISyiPQDTSN 383
Cdd:PRK13648 4 KNSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAIT--DDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 384 LSGSLNeyIHSQDVDETLCKTILrKLDFA------------------RELFEMDMIDYSD--------GQKKKVLIALSL 437
Cdd:PRK13648 81 LRKHIG--IVFQNPDNQFVGSIV-KYDVAfglenhavpydemhrrvsEALKQVDMLERADyepnalsgGQKQRVAIAGVL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493786691 438 SKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKP----TLIFVEHD 478
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehniTIISITHD 202
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
17-189 |
3.34e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 56.85 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 17 VKPIFENVSFSFDTNWkTGLIGRNGIGKSTLFKLLLNQETYQGKISKDVEFIKFPPNISDTSKLGIDLYKELiSDDEEWK 96
Cdd:cd03240 9 IRSFHERSEIEFFSPL-TLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPKLIREGEVRAQVKLAFEN-ANGKKYT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 97 LFRELN-LLNV------DEN-LVYREFKTLSKGEQTKILLAI------LFTKEDGFLLIDEPTNHLDMNGRKI----LSE 158
Cdd:cd03240 87 ITRSLAiLENVifchqgESNwPLLDMRGRCSGGEKVLASLIIrlalaeTFGSNCGILALDEPTTNLDEENIEEslaeIIE 166
|
170 180 190
....*....|....*....|....*....|...
gi 493786691 159 YLKSKKGFLLI--SHDRNFLDGcINHVISINRN 189
Cdd:cd03240 167 ERKSQKNFQLIviTHDEELVDA-ADHIYRVEKD 198
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
18-184 |
3.38e-09 |
|
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: 57.52 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 18 KPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQE-TYQGKISKDVEFIK---------------------FPPNIS 75
Cdd:TIGR03873 14 RLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALrPDAGTVDLAGVDLHglsrrararrvalveqdsdtaVPLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 76 DTSKLGIDLYKELI--SDDEEWKLFRELNLLNVDENLVYREFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGR 153
Cdd:TIGR03873 94 DVVALGRIPHRSLWagDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQ 173
|
170 180 190
....*....|....*....|....*....|....*
gi 493786691 154 ----KILSEYLKSKKGFLLISHDRNFLDGCINHVI 184
Cdd:TIGR03873 174 letlALVRELAATGVTVVAALHDLNLAASYCDHVV 208
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
310-477 |
3.62e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.54 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGE--RQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGI-NHEytGEIKLASnlkISY---------- 376
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLlSTE--GEIQIDG---VSWnsvtlqtwrk 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 377 ----IPQDTSNLSGSLNEYI--HSQDVDETLCKTI----LR--------KLDFArelfemdMID----YSDGQKKKVLIA 434
Cdd:TIGR01271 1293 afgvIPQKVFIFSGTFRKNLdpYEQWSDEEIWKVAeevgLKsvieqfpdKLDFV-------LVDggyvLSNGHKQLMCLA 1365
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493786691 435 LSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKE--AKPTLIFVEH 477
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQsfSNCTVILSEH 1410
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
335-478 |
3.83e-09 |
|
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: 57.38 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 335 GDIVAISGRNGSGKSTLIKILLG-----------------INHEYTG-----------EIKLASNLKISYIPQDTSNLSG 386
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGklkpnlgkfddppdwdeILDEFRGselqnyftkllEGDVKVIVKPQYVDLIPKAVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 387 SLNEYIHSQDVDETLcKTILRKLDFaRELFEMDMIDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQ----IE 462
Cdd:cd03236 106 KVGELLKKKDERGKL-DELVDQLEL-RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNaarlIR 183
|
170
....*....|....*.
gi 493786691 463 EIIKEAKPTLIfVEHD 478
Cdd:cd03236 184 ELAEDDNYVLV-VEHD 198
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-174 |
4.34e-09 |
|
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: 58.84 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 2 SAIKIQNLTFSYYGyVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQ-ETYQGKIS-KDVEFIKFPPN------ 73
Cdd:TIGR02857 320 SSLEFSGVSVAYPG-RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFvDPTEGSIAvNGVPLADADADswrdqi 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 74 ---------ISDTSKLGIDLYKELISDDEewkLFRELNLLNVDENLVYREFKT----------LSKGEQTKILLAILFTK 134
Cdd:TIGR02857 399 awvpqhpflFAGTIAENIRLARPDASDAE---IREALERAGLDEFVAALPQGLdtpigeggagLSGGQAQRLALARAFLR 475
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493786691 135 EDGFLLIDEPTNHLDMNG----RKILSEYLKSKKGfLLISHDRN 174
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETeaevLEALRALAQGRTV-LLVTHRLA 518
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-177 |
4.94e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 56.00 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQETY---QGKIS-KDVEFIKFPPNisDTSK 79
Cdd:cd03217 1 LEIKDLHVSVGG--KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevtEGEILfKGEDITDLPPE--ERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 80 LGIDL---YKELISDDEEWKLFRELNllnvdenlvyrefKTLSKGEQTKI-LLAILFTKEDgFLLIDEPTNHLDMNGRKI 155
Cdd:cd03217 77 LGIFLafqYPPEIPGVKNADFLRYVN-------------EGFSGGEKKRNeILQLLLLEPD-LAILDEPDSGLDIDALRL 142
|
170 180
....*....|....*....|....*.
gi 493786691 156 LSE----YLKSKKGFLLISHDRNFLD 177
Cdd:cd03217 143 VAEvinkLREEGKSVLIITHYQRLLD 168
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
308-478 |
5.00e-09 |
|
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: 58.53 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHY-GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL-----------ASNLKIS 375
Cdd:TIGR02868 333 PTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLdgvpvssldqdEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 376 YIPQDTSNLSGSL--NEYIHSQDVDETLCKTILRK---LDFARELFE-------MDMIDYSDGQKKKVLIALSLSKPAHL 443
Cdd:TIGR02868 413 VCAQDAHLFDTTVreNLRLARPDATDEELWAALERvglADWLRALPDgldtvlgEGGARLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*..
gi 493786691 444 FIWDEPLNYIDVISRIQIEEIIKEAKP--TLIFVEHD 478
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAALSgrTVVLITHH 529
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
309-490 |
5.45e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.44 E-value: 5.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGERQI----LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINhEYTGEI---KLASN----LKISyi 377
Cdd:PRK11022 3 LLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLI-DYPGRVmaeKLEFNgqdlQRIS-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 378 PQDTSNLSGSLNEYIHsQDVDETL--CKT----ILRKL------------DFARELFEMDMI------------DYSDGQ 427
Cdd:PRK11022 80 EKERRNLVGAEVAMIF-QDPMTSLnpCYTvgfqIMEAIkvhqggnkktrrQRAIDLLNQVGIpdpasrldvyphQLSGGM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493786691 428 KKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKP----TLIFVEHDKRFVEDIANKII 490
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkenmALVLITHDLALVAEAAHKII 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
308-489 |
7.01e-09 |
|
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: 58.16 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHYG----ERQILSNLSFEIEQGDIVAISGRNGSGKS----TLIKILLGINHEYTGEIKLAS-NL------ 372
Cdd:COG4172 5 PLLSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGqDLlglser 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 373 --------KISYIPQD--TsnlsgSLNEY--IHSQdVDETLckTILRKLDF------ARELFEMDMI--------DY--- 423
Cdd:COG4172 85 elrrirgnRIAMIFQEpmT-----SLNPLhtIGKQ-IAEVL--RLHRGLSGaaararALELLERVGIpdperrldAYphq 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493786691 424 -SDGQKKKVLIALSL-SKPAhLFIWDEPLNYIDVISRIQIEEIIKEAKPT----LIFVEHDKRFVEDIANKI 489
Cdd:COG4172 157 lSGGQRQRVMIAMALaNEPD-LLIADEPTTALDVTVQAQILDLLKDLQRElgmaLLLITHDLGVVRRFADRV 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-158 |
9.55e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.27 E-value: 9.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 18 KPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL--LnQETYQGKISKDVEFIKFPPNISDTSKLG-IDLYKELISDDEE 94
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIagL-LPPAAGTIKLDGGDIDDPDVAEACHYLGhRNAMKPALTVAEN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493786691 95 ---WKLFRELNLLNVDE--------NLVYREFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGRKILSE 158
Cdd:PRK13539 94 lefWAAFLGGEELDIAAaleavglaPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAE 168
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
310-490 |
9.88e-09 |
|
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: 55.70 E-value: 9.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYG--ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGInHEYTG-----------EIKLAS-NLKIS 375
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRF-YDVDSgrilidghdvrDYTLASlRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 376 YIPQDTSNLSGSLNEYIHSQDVDETLcKTILR--KLDFARElFEMDM------------IDYSDGQKKKVLIALSLSKPA 441
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATR-EEVEEaaRAANAHE-FIMELpegydtvigergVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493786691 442 HLFIWDEPLNYIDVISRIQIEEIIKE--AKPTLIFVEHDKRFVEDiANKII 490
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERlmKNRTTFVIAHRLSTIEN-ADRIV 207
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
309-490 |
1.02e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 55.87 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKIllgIN--HEYTG------------------EIKL 368
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRC---INklEEITSgdlivdglkvndpkvderLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 369 ASNL---KISYIPQDTS--NLS-GSLNEYIHSQDVDETLCKTILRKLDFAR-------ELfemdmidySDGQKKKVLIAL 435
Cdd:PRK09493 78 EAGMvfqQFYLFPHLTAleNVMfGPLRVRGASKEEAEKQARELLAKVGLAErahhypsEL--------SGGQQQRVAIAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493786691 436 SLSKPAHLFIWDEPLNYIDVISRIQIEEIIK---EAKPTLIFVEHDKRFVEDIANKII 490
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRHEVLKVMQdlaEEGMTMVIVTHEIGFAEKVASRLI 207
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
325-477 |
1.29e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.23 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 325 LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNlkisyiPQDTSNLSGSLNE---YIHSQ------ 395
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ------EMRFASTTAALAAgvaIIYQElhlvpe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 396 -DVDETLC------------KTILRKlDFARELFEMDM-ID-------YSDGQKKKVLIALSLSKPAHLFIWDEPLNY-- 452
Cdd:PRK11288 94 mTVAENLYlgqlphkggivnRRLLNY-EAREQLEHLGVdIDpdtplkyLSIGQRQMVEIAKALARNARVIAFDEPTSSls 172
|
170 180
....*....|....*....|....*...
gi 493786691 453 ---IDVISRIqIEEIIKEAKpTLIFVEH 477
Cdd:PRK11288 173 areIEQLFRV-IRELRAEGR-VILYVSH 198
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-172 |
1.32e-08 |
|
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: 56.99 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGyVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLN----------------QETYQGKISKDVEF 67
Cdd:TIGR02868 335 LELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGlldplqgevtldgvpvSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 68 IKFPPNISDTSKLG-IDLYKELISDDEEWKLFRELNLLNVDENL-------VYREFKTLSKGEQTKILLA-ILFTKEDgF 138
Cdd:TIGR02868 414 CAQDAHLFDTTVREnLRLARPDATDEELWAALERVGLADWLRALpdgldtvLGEGGARLSGGERQRLALArALLADAP-I 492
|
170 180 190
....*....|....*....|....*....|....*..
gi 493786691 139 LLIDEPTNHLDM-NGRKILSEYLK--SKKGFLLISHD 172
Cdd:TIGR02868 493 LLLDEPTEHLDAeTADELLEDLLAalSGRTVVLITHH 529
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
309-490 |
1.35e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGERQ----ILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNL--KISYIPQDTS 382
Cdd:PRK10261 12 VLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLlrRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 383 NLSGSLNEYIHSQD-----------------VDETLCKTILRKLDFARE--LFEMD-MID-----------------YSD 425
Cdd:PRK10261 92 EQSAAQMRHVRGADmamifqepmtslnpvftVGEQIAESIRLHQGASREeaMVEAKrMLDqvripeaqtilsryphqLSG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 426 GQKKKVLIALSLS-KPAHLfIWDEPLNYIDVISRIQIEEIIK----EAKPTLIFVEHDKRFVEDIANKII 490
Cdd:PRK10261 172 GMRQRVMIAMALScRPAVL-IADEPTTALDVTIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEIADRVL 240
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-172 |
1.46e-08 |
|
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: 55.20 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQET------YQGKISKDVEFIKFPPNI--- 74
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRptsgtaYINGYSIRTDRKAARQSLgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 75 --SDTsklgidLYKEL--------------ISDDEEWK----LFRELNLLNVDENLVyrefKTLSKGEQTKILLAILFTK 134
Cdd:cd03263 81 pqFDA------LFDELtvrehlrfyarlkgLPKSEIKEevelLLRVLGLTDKANKRA----RTLSGGMKRKLSLAIALIG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493786691 135 EDGFLLIDEPTNHLDMNGRKILSEYL---KSKKGFLLISHD 172
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLIlevRKGRSIILTTHS 191
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
314-489 |
1.59e-08 |
|
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: 55.28 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 314 ELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA---------SNL-----KISYIPQ 379
Cdd:cd03258 10 VFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtdltllsgKELrkarrRIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 380 DTsNLSGSLNEY--------IHSQDVDEtlcktILRKldfARELFEM----DMID-Y----SDGQKKKVLIALSLSKPAH 442
Cdd:cd03258 90 HF-NLLSSRTVFenvalpleIAGVPKAE-----IEER---VLELLELvgleDKADaYpaqlSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493786691 443 LFIWDEPLNYID------VISRIQieEIIKEAKPTLIFVEHDKRFVEDIANKI 489
Cdd:cd03258 161 VLLCDEATSALDpettqsILALLR--DINRELGLTIVLITHEMEVVKRICDRV 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
308-366 |
1.63e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.21 E-value: 1.63e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493786691 308 PLISVSELSAHYGERQI----LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEI 366
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSVqtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV 66
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-172 |
1.67e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.43 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 1 MSAIKIQNLTFSYYgyVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL--LNQETYQGKISKDVEFIK--------- 69
Cdd:PRK14258 5 IPAIKVNNLSFYYD--TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEVRVEGRVEFFNqniyerrvn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 70 -----------------FPPNISDTSKLGIDL---YKELISDDEEWKLFRELNLLNVDENLVYREFKTLSKGEQTKILLA 129
Cdd:PRK14258 83 lnrlrrqvsmvhpkpnlFPMSVYDNVAYGVKIvgwRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493786691 130 ILFTKEDGFLLIDEPTNHLDMNGRK-----ILSEYLKSKKGFLLISHD 172
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMkveslIQSLRLRSELTMVIVSHN 210
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
309-489 |
1.67e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.44 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASnlKISYIPQDTSNLSG-- 386
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYFGKDIFQIDAik 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 387 ----------SLNEYIHSQDVD-----------------ETLCKTILRKLDFARELFEM---DMIDYSDGQKKKVLIALS 436
Cdd:PRK14246 88 lrkevgmvfqQPNPFPHLSIYDniayplkshgikekreiKKIVEECLRKVGLWKEVYDRlnsPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493786691 437 LSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKP--TLIFVEHDKRFVEDIANKI 489
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYV 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
308-489 |
1.87e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.64 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHY----GERQILSNLSFEIEQGDIVAISGRNGSGKS----TLIKILLGINHEYT-GEIKLASNlkiSYIP 378
Cdd:PRK15134 4 PLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVYPsGDIRFHGE---SLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 379 QDTSNLSG---------------SLNEyIHSqdVDETLCKTILRKLDFARELFEMDMI----------------DY---- 423
Cdd:PRK15134 81 ASEQTLRGvrgnkiamifqepmvSLNP-LHT--LEKQLYEVLSLHRGMRREAARGEILncldrvgirqaakrltDYphql 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 424 SDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKP----TLIFVEHDKRFVEDIANKI 489
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNLSIVRKLADRV 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
310-490 |
2.16e-08 |
|
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: 54.42 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQIlsNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL---------ASNLKISYIPQD 380
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIngvdvtaapPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 381 TS---------NLSGSLNEYIHSQDVDETLCKTILRKLDFARelFEMDMID-YSDGQKKKVLIALSLSKPAHLFIWDEPL 450
Cdd:cd03298 79 NNlfahltveqNVGLGLSPGLKLTAEDRQAIEVALARVGLAG--LEKRLPGeLSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493786691 451 NYIDVISRIQ----IEEIIKEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:cd03298 157 AALDPALRAEmldlVLDLHAETKMTVLMVTHQPEDAKRLAQRVV 200
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
309-478 |
2.35e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.09 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLAsNLKIS-------YIPQD- 380
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLD-GKPVEgpgaergVVFQNe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 381 --------TSNLSGSLNEYIHSQDVDETLCKTILRKLDFARelFEMDMI-DYSDGQKKKVLIALSLSKPAHLFIWDEPLN 451
Cdd:PRK11248 80 gllpwrnvQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEG--AEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190
....*....|....*....|....*....|..
gi 493786691 452 YIDVISRIQIEEII-----KEAKPTLIfVEHD 478
Cdd:PRK11248 158 ALDAFTREQMQTLLlklwqETGKQVLL-ITHD 188
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
308-466 |
2.57e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.58 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA----------SNLKISYI 377
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCgepvpsrarhARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 378 PQdTSNL----SGSLNEYIHSQ--DVDETLCKTILRK-LDFARELFEMD--MIDYSDGQKKKVLIALSLSKPAHLFIWDE 448
Cdd:PRK13537 86 PQ-FDNLdpdfTVRENLLVFGRyfGLSAAAARALVPPlLEFAKLENKADakVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170
....*....|....*...
gi 493786691 449 PLNYIDVISRIQIEEIIK 466
Cdd:PRK13537 165 PTTGLDPQARHLMWERLR 182
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
308-357 |
2.70e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.93 E-value: 2.70e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLG 357
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA 54
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
325-487 |
2.92e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.12 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 325 LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIPQD----TSNLSGSLNEYIHSQDVDET 400
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 401 LCKTI---------------------LRKLDFARELFEMDMIDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRI 459
Cdd:PRK13643 102 VLKDVafgpqnfgipkekaekiaaekLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190
....*....|....*....|....*....|.
gi 493786691 460 QIE---EIIKEAKPTLIFVEHdkrFVEDIAN 487
Cdd:PRK13643 182 EMMqlfESIHQSGQTVVLVTH---LMDDVAD 209
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
318-356 |
3.29e-08 |
|
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: 55.98 E-value: 3.29e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 493786691 318 HY-GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILL 356
Cdd:COG5265 366 GYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLF 405
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
321-487 |
3.38e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 54.75 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 321 ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLAS--------NLKISYIPQDTsnlsGSLNEYI 392
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstskNKDIKQIRKKV----GLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 393 HSQDVDETLCKTI---------------------LRKLDFARELFEMDMIDYSDGQKKKVLIALSLSKPAHLFIWDEPLN 451
Cdd:PRK13649 95 ESQLFEETVLKDVafgpqnfgvsqeeaealarekLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 493786691 452 YIDVISRIQIEEIIK---EAKPTLIFVEHdkrFVEDIAN 487
Cdd:PRK13649 175 GLDPKGRKELMTLFKklhQSGMTIVLVTH---LMDDVAN 210
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
306-357 |
3.57e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 3.57e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 493786691 306 KNPLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLG 357
Cdd:CHL00131 4 NKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-145 |
4.73e-08 |
|
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: 53.59 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTfSYYGYVkPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQET-YQGKIS---KDVEfiKFPPniSDTSK 79
Cdd:cd03224 1 LEVENLN-AGYGKS-QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPpRSGSIRfdgRDIT--GLPP--HERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 80 LGIDLYKelisddEEWKLFRElnlLNVDENL------------------VYREF-----------KTLSKGEQTkiLLAI 130
Cdd:cd03224 75 AGIGYVP------EGRRIFPE---LTVEENLllgayarrrakrkarlerVYELFprlkerrkqlaGTLSGGEQQ--MLAI 143
|
170
....*....|....*...
gi 493786691 131 ---LFTKEDgFLLIDEPT 145
Cdd:cd03224 144 araLMSRPK-LLLLDEPS 160
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
310-490 |
5.29e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 53.99 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL------------ASNLKISYI 377
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 378 PQDTSNLSGSLNEYIH-----------------SQDVDETLCKTILRKLDFA-------RELfemdmidySDGQKKKVLI 433
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHrtvleniiegpvivkgePKEEATARARELLAKVGLAgketsypRRL--------SGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493786691 434 ALSLSKPAHLFIWDEPLNYID------VISRIQieeIIKEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDpelvgeVLNTIR---QLAQEKRTMVIVTHEMSFARDVADRAI 215
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
308-469 |
7.28e-08 |
|
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: 52.43 E-value: 7.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHYGerqiLSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL------------ASNLKIS 375
Cdd:cd03215 3 PVLEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdgkpvtrrsprdAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 376 YIPQDtsNLSGSLneyIHSQDVDETLcktILRKLdfarelfemdmidYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDV 455
Cdd:cd03215 79 YVPED--RKREGL---VLDLSVAENI---ALSSL-------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170
....*....|....
gi 493786691 456 ISRIQIEEIIKEAK 469
Cdd:cd03215 138 GAKAEIYRLIRELA 151
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
307-491 |
8.18e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 54.73 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 307 NPLISVSELSAHY--GERQI--LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASnlkisyipQDTS 382
Cdd:PRK10535 2 TALLELKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAG--------QDVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 383 NLSGS-------------------LNEYIHSQDVD-----ETLCKTilRKLDFARELFEM----DMIDY-----SDGQKK 429
Cdd:PRK10535 74 TLDADalaqlrrehfgfifqryhlLSHLTAAQNVEvpavyAGLERK--QRLLRAQELLQRlgleDRVEYqpsqlSGGQQQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493786691 430 KVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKP---TLIFVEHDKRfVEDIANKIIQ 491
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrghTVIIVTHDPQ-VAAQAERVIE 215
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
321-467 |
8.54e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.98 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 321 ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLG-INHEYTGEIKLASNlkISYIPQDTSNLSGSLNEYI------- 392
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS--VAYVPQVSWIFNATVRENIlfgsdfe 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 393 ---HSQDVDETlckTILRKLDF--ARELFEMDM--IDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDV-ISRIQIEEI 464
Cdd:PLN03232 707 serYWRAIDVT---ALQHDLDLlpGRDLTEIGErgVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQVFDSC 783
|
...
gi 493786691 465 IKE 467
Cdd:PLN03232 784 MKD 786
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
310-477 |
1.02e-07 |
|
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: 53.32 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGE--RQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLG-INHEYTGEIKLASNLKISY---------I 377
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRlLNTEGDIQIDGVSWNSVPLqkwrkafgvI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 378 PQDTSNLSGS----LNEYIHSQD------VDETLCKTILR----KLDFArelfemdMID----YSDGQKKKVLIALSLSK 439
Cdd:cd03289 83 PQKVFIFSGTfrknLDPYGKWSDeeiwkvAEEVGLKSVIEqfpgQLDFV-------LVDggcvLSHGHKQLMCLARSVLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493786691 440 PAHLFIWDEPLNYIDVISRIQIEEIIKE--AKPTLIFVEH 477
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQafADCTVILSEH 195
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-150 |
1.18e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 52.78 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKL---LLNQEtyQGKIS---KDVEFIKFP------ 71
Cdd:COG4604 2 IEIKNVSKRYGG--KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMisrLLPPD--SGEVLvdgLDVATTPSRelakrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 72 ------PNIsdTSKLGIdlyKELIS-------------DDEEwKLFRELNLLNVDEnLVYREFKTLSKGEQTKILLAILF 132
Cdd:COG4604 78 ailrqeNHI--NSRLTV---RELVAfgrfpyskgrltaEDRE-IIDEAIAYLDLED-LADRYLDELSGGQRQRAFIAMVL 150
|
170
....*....|....*...
gi 493786691 133 TKEDGFLLIDEPTNHLDM 150
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDM 168
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
315-478 |
1.21e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.86 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 315 LSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLI-----------------KILLGINHEYTGEIK-LASNLKISY 376
Cdd:PRK14243 16 LNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlndlipgfrvegKVTFHGKNLYAPDVDpVEVRRRIGM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 377 IPQDTSNLSGSLNEYI--------HSQDVDEtLCKTILRKL---DFARELFEMDMIDYSDGQKKKVLIALSLSKPAHLFI 445
Cdd:PRK14243 96 VFQKPNPFPKSIYDNIaygaringYKGDMDE-LVERSLRQAalwDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190
....*....|....*....|....*....|....*
gi 493786691 446 WDEPLNYIDVISRIQIEEIIKEAKP--TLIFVEHD 478
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEqyTIIIVTHN 209
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
328-368 |
1.40e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 54.03 E-value: 1.40e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 493786691 328 LSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL 368
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
308-449 |
1.42e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL------------ASNLKIS 375
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIggnpcarltpakAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 376 YIPQDT---SNLSgslneyihsqdVDETLCKTILRKLDFAREL----------FEMDM----IDYSDGQkkKVLIALSLS 438
Cdd:PRK15439 90 LVPQEPllfPNLS-----------VKENILFGLPKRQASMQKMkqllaalgcqLDLDSsagsLEVADRQ--IVEILRGLM 156
|
170
....*....|.
gi 493786691 439 KPAHLFIWDEP 449
Cdd:PRK15439 157 RDSRILILDEP 167
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
309-489 |
1.53e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.70 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIkLASNLKISY-------IPQDT 381
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPLDYskrgllaLRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 382 SNLSGSLNEYIHSQDVDETLC----------KTILRKLDFARELFEMDMIDY------SDGQKKKVLIALSLSKPAHLFI 445
Cdd:PRK13638 80 ATVFQDPEQQIFYTDIDSDIAfslrnlgvpeAEITRRVDEALTLVDAQHFRHqpiqclSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493786691 446 WDEPLNYIDVISRIQIEEIIKEAKPT---LIFVEHDKRFVEDIANKI 489
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAV 206
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
325-478 |
1.71e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.79 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 325 LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL------ASNL-----KISYIPQDTSN--LSGSLNEY 391
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdgelltAENVwnlrrKIGMVFQNPDNqfVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 392 IHSQDVDETLCK-TILRKLDFAreLFEMDMIDY--------SDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIE 462
Cdd:PRK13642 103 VAFGMENQGIPReEMIKRVDEA--LLAVNMLDFktreparlSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
170 180
....*....|....*....|
gi 493786691 463 EIIKEAKP----TLIFVEHD 478
Cdd:PRK13642 181 RVIHEIKEkyqlTVLSITHD 200
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
320-454 |
1.80e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.18 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 320 GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNlkISYIPQDTSNLSGSLNEYI-HSQDVD 398
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQQAWIQNDSLRENIlFGKALN 726
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493786691 399 ETLCKTILRKLDFARELfEM-----------DMIDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYID 454
Cdd:TIGR00957 727 EKYYQQVLEACALLPDL-EIlpsgdrteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
314-478 |
1.97e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.30 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 314 ELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIPQDTSNLSGSLNE--- 390
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQnat 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 391 ---------------YIHS------QDVDETLCKTILRKLDFArELFEMDMIDYSDGQKKKVLIALSLSKPAHLFIWDEP 449
Cdd:PRK10253 92 tpgditvqelvargrYPHQplftrwRKEDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190
....*....|....*....|....*....|...
gi 493786691 450 LNYIDVISRIQIEEII----KEAKPTLIFVEHD 478
Cdd:PRK10253 171 TTWLDISHQIDLLELLselnREKGYTLAAVLHD 203
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-149 |
1.97e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 52.08 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 3 AIKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKlLLNQE--TYQGKIS---KDVEFIK-------- 69
Cdd:PRK13548 2 MLEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLR-ALSGElsPDSGEVRlngRPLADWSpaelarrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 70 ----------FPPNISDTSKLGidLYKELISDDEEWKLFRE-LNLLNVDEnLVYREFKTLSKGEQTKILLAILFT----- 133
Cdd:PRK13548 79 avlpqhsslsFPFTVEEVVAMG--RAPHGLSRAEDDALVAAaLAQVDLAH-LAGRDYPQLSGGEQQRVQLARVLAqlwep 155
|
170
....*....|....*..
gi 493786691 134 -KEDGFLLIDEPTNHLD 149
Cdd:PRK13548 156 dGPPRWLLLDEPTSALD 172
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
308-454 |
2.12e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.39 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL----ASNLK-------ISY 376
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdgktATRGDrsrfmayLGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 377 IP---QDTSNLSG-----SLNEYIHSQDVDETLckTILRKLDFARELFEmdmiDYSDGQKKKVLIALSLSKPAHLFIWDE 448
Cdd:PRK13543 90 LPglkADLSTLENlhflcGLHGRRAKQMPGSAL--AIVGLAGYEDTLVR----QLSAGQKKRLALARLWLSPAPLWLLDE 163
|
....*.
gi 493786691 449 PLNYID 454
Cdd:PRK13543 164 PYANLD 169
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
306-488 |
2.55e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 51.70 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 306 KNPLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKIL-----LGINHEYTGEIKLasNLKISYIPQ- 379
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVY--NGHNIYSPRt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 380 DTSNLSGSL-------NEY----------------IHSQDVDETLCKTILRKL---DFARELFEMDMIDYSDGQKKKVLI 433
Cdd:PRK14239 80 DTVDLRKEIgmvfqqpNPFpmsiyenvvyglrlkgIKDKQVLDEAVEKSLKGAsiwDEVKDRLHDSALGLSGGQQQRVCI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493786691 434 ALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKP--TLIFVEHDKRFVEDIANK 488
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRSMQQASRISDR 216
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-158 |
2.61e-07 |
|
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: 51.83 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQ-ETYQGKISKD-VEFIKFPPNiSDTSKLG 81
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMvDIFDGKIVIDgIDISKLPLH-TLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 82 IDLYKELI---------------SDDEEWKLFRELNLLNVDENL-------VYREFKTLSKGEQTKILLAILFTKEDGFL 139
Cdd:cd03288 99 IILQDPILfsgsirfnldpeckcTDDRLWEALEIAQLKNMVKSLpggldavVTEGGENFSVGQRQLFCLARAFVRKSSIL 178
|
170
....*....|....*....
gi 493786691 140 LIDEPTNHLDMNGRKILSE 158
Cdd:cd03288 179 IMDEATASIDMATENILQK 197
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
321-490 |
2.86e-07 |
|
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: 51.32 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 321 ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLAS-----------NLKISYIPQDTSNLSGSLN 389
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylHSKVSLVGQEPVLFARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 390 EYIHS--QDVDETLCKTILRKL---DFARELFEMDMID-------YSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVIS 457
Cdd:cd03248 106 DNIAYglQSCSFECVKEAAQKAhahSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190
....*....|....*....|....*....|....*
gi 493786691 458 RIQIEEIIKE--AKPTLIFVEHDKRFVEDiANKII 490
Cdd:cd03248 186 EQQVQQALYDwpERRTVLVIAHRLSTVER-ADQIL 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
306-478 |
3.63e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.72 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 306 KNPLISVSELSAHY--GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGI----NHEYTGEIKLASNL------- 372
Cdd:PRK13640 2 KDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpdDNPNSKITVDGITLtaktvwd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 373 ---KISYIPQDTSN------LSGSLNEYIHSQDVDETLCKTILRKLdfareLFEMDMIDYSD--------GQKKKVLIAL 435
Cdd:PRK13640 82 ireKVGIVFQNPDNqfvgatVGDDVAFGLENRAVPRPEMIKIVRDV-----LADVGMLDYIDsepanlsgGQKQRVAIAG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493786691 436 SLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKP----TLIFVEHD 478
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknnlTVISITHD 203
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
323-489 |
4.35e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 51.23 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 323 QILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNlKISYIPQDTSNLSGSLNEYIHSQDvDETLC 402
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE-PIKYDKKSLLEVRKTVGIVFQNPD-DQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 403 KTILRKLDFA----------------RELFEMDMIDY--------SDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISR 458
Cdd:PRK13639 94 PTVEEDVAFGplnlglskeevekrvkEALKAVGMEGFenkpphhlSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190
....*....|....*....|....*....|....
gi 493786691 459 IQIEEIIKEAKP---TLIFVEHDKRFVEDIANKI 489
Cdd:PRK13639 174 SQIMKLLYDLNKegiTIIISTHDVDLVPVYADKV 207
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-171 |
4.66e-07 |
|
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: 49.73 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYyGYVKpIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL--LNQETyQGKIS---KDVEFikfpPNISDTS 78
Cdd:cd03216 1 LELRGITKRF-GGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILsgLYKPD-SGEILvdgKEVSF----ASPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 79 KLGIdlykelisddeewklfrelnllnvdeNLVYRefktLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGRKILSE 158
Cdd:cd03216 74 RAGI--------------------------AMVYQ----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK 123
|
170
....*....|....*..
gi 493786691 159 YLK----SKKGFLLISH 171
Cdd:cd03216 124 VIRrlraQGVAVIFISH 140
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
310-490 |
4.95e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 50.52 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGErQILsNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLAS-NL--------KISYIPQD 380
Cdd:COG3840 2 LRLDDLTYRYGD-FPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqDLtalppaerPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 381 TsNLSGSLNEY------IHS----QDVDETLCKTILRKLDFArelfemDMIDY-----SDGQKKKVLIALSL--SKPahL 443
Cdd:COG3840 80 N-NLFPHLTVAqniglgLRPglklTAEQRAQVEQALERVGLA------GLLDRlpgqlSGGQRQRVALARCLvrKRP--I 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493786691 444 FIWDEPLNYIDVISRIQ----IEEIIKEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:COG3840 151 LLLDEPFSALDPALRQEmldlVDELCRERGLTVLMVTHDPEDAARIADRVL 201
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-188 |
5.30e-07 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 50.36 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTfSYYGYVKPIfENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLN-QETYQGKIskdvEFIKFPPNISDTSKLGI 82
Cdd:cd03269 1 LEVENVT-KRFGRVTAL-DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiILPDSGEV----LFDGKPLDIAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 83 -----DLYK--------------------ELISDDEEWklFRELNLlnvdENLVYREFKTLSKGEQTKILLAILFTKEDG 137
Cdd:cd03269 75 lpeerGLYPkmkvidqlvylaqlkglkkeEARRRIDEW--LERLEL----SEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493786691 138 FLLIDEPTNHLD-MNGR---KILSEYLKSKKGFLLISHDRNFLDGCINHVISINR 188
Cdd:cd03269 149 LLILDEPFSGLDpVNVEllkDVIRELARAGKTVILSTHQMELVEELCDRVLLLNK 203
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
309-478 |
6.37e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 50.89 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGERQ---ILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNL-----------KI 374
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdirhKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 375 SYIPQDTSN-LSGSLNEyihsQDVDETL------CKTILRKLDFARELfeMDMIDY--------SDGQKKKVLIALSLSK 439
Cdd:PRK13650 84 GMVFQNPDNqFVGATVE----DDVAFGLenkgipHEEMKERVNEALEL--VGMQDFkereparlSGGQKQRVAIAGAVAM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493786691 440 PAHLFIWDEPLNYIDVISRIQ----IEEIIKEAKPTLIFVEHD 478
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLEliktIKGIRDDYQMTVISITHD 200
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
310-477 |
7.02e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.68 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEY-----TGEIKL---------ASNLK-- 373
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLdgqdifkmdVIELRrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 374 ---ISYIPQDTSNLS--------GSLNEYIHSQDVDETLCKTILRKLDFARELfeMDMID-----YSDGQKKKVLIALSL 437
Cdd:PRK14247 84 vqmVFQIPNPIPNLSifenvalgLKLNRLVKSKKELQERVRWALEKAQLWDEV--KDRLDapagkLSGGQQQRLCIARAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493786691 438 SKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKP--TLIFVEH 477
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-174 |
7.41e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 50.76 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 2 SAIKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLN-QETYQGKISKDVEFIKFpPNISDT-SK 79
Cdd:PRK13632 6 VMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGlLKPQSGEIKIDGITISK-ENLKEIrKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 80 LGI--------------------DLYKELISDDEEWKLFRELNLLNVDENLVYREFKTLSKGEQTKILLAILFTKEDGFL 139
Cdd:PRK13632 85 IGIifqnpdnqfigatveddiafGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493786691 140 LIDEPTNHLDMNGRKILSEYLKS-----KKGFLLISHDRN 174
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDlrktrKKTLISITHDMD 204
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-194 |
7.57e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.37 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 7 QNLTFSYYGYVkpIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQET-YQGKISKDVEFIKFPPNISDTSKLGI--- 82
Cdd:PRK10253 11 EQLTLGYGKYT--VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpAHGHVWLDGEHIQHYASKEVARRIGLlaq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 83 ------DL-YKELIS---------------DDEEwKLFRELNLLNVDEnLVYREFKTLSKGEQTKILLAILFTKEDGFLL 140
Cdd:PRK10253 89 nattpgDItVQELVArgryphqplftrwrkEDEE-AVTKAMQATGITH-LADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 141 IDEPTNHLDMNGR----KILSEyLKSKKGFLL--ISHDRNFLDGCINHVISINRNSIDVQ 194
Cdd:PRK10253 167 LDEPTTWLDISHQidllELLSE-LNREKGYTLaaVLHDLNQACRYASHLIALREGKIVAQ 225
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
320-466 |
8.81e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 49.16 E-value: 8.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 320 GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHE--YTGEIKLASNLKISYIPQDTSnlsgslneYIHSQDV 397
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDKNFQRSTG--------YVEQQDV 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493786691 398 DETlCKTILRKLDFA---RELfemdmidySDGQKKKVLIALSL-SKPAHLFIwDEPLNYIDVISRIQIEEIIK 466
Cdd:cd03232 90 HSP-NLTVREALRFSallRGL--------SVEQRKRLTIGVELaAKPSILFL-DEPTSGLDSQAAYNIVRFLK 152
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-52 |
9.07e-07 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 51.32 E-value: 9.07e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 493786691 3 AIKIQNLTFSYYGyVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLL 52
Cdd:COG1132 339 EIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLL 387
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
308-368 |
1.02e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.18 E-value: 1.02e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493786691 308 PLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGInheYT---GEIKL 368
Cdd:COG3845 4 PALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGL---YQpdsGEILI 64
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-175 |
1.19e-06 |
|
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: 49.41 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSY--YGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL--LNQETyqgkiSKDVEFikfppnisdtsk 79
Cdd:cd03255 1 IELKNLSKTYggGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILggLDRPT-----SGEVRV------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 80 LGIDLYKElisDDEEWKLFR---------ELNL---LNVDEN----LVYREFK--------------------------T 117
Cdd:cd03255 64 DGTDISKL---SEKELAAFRrrhigfvfqSFNLlpdLTALENvelpLLLAGVPkkerreraeellervglgdrlnhypsE 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493786691 118 LSKGEQTKILLAILFTKEDGFLLIDEPTNHLDM-NGRKILSEYLK----SKKGFLLISHDRNF 175
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSeTGKEVMELLRElnkeAGTTIVVVTHDPEL 203
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
309-478 |
1.26e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.85 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGE-RQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEI---------------KLASNL 372
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrkglmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 373 KISYIPQDTSNLSGSLNEYIHSQDVDETLCK-TILRKLDFARELFEMDMIDY------SDGQKKKVLIALSLSKPAHLFI 445
Cdd:PRK13636 85 GMVFQDPDNQLFSASVYQDVSFGAVNLKLPEdEVRKRVDNALKRTGIEHLKDkpthclSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 493786691 446 WDEPLNYIDVISRIQIEEIIKEAKP----TLIFVEHD 478
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKelglTIIIATHD 201
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
321-490 |
1.41e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 50.88 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 321 ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLasnlkisyipqDTSNLSGSLNEYIHSQDV--- 397
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL-----------DGVPLVQYDHHYLHRQVAlvg 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 398 ------DETLCKTILRKLDF---------ARELFEMDMI-----DY-----------SDGQKKKVLIALSLSKPAHLFIW 446
Cdd:TIGR00958 562 qepvlfSGSVRENIAYGLTDtpdeeimaaAKAANAHDFImefpnGYdtevgekgsqlSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493786691 447 DEPLNYIDVISRIQIEEIIKEAKPTLIFVEHDKRFVEDiANKII 490
Cdd:TIGR00958 642 DEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVER-ADQIL 684
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
324-466 |
1.45e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.10 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 324 ILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLAS-----------NLKISYIPQDTSNLSGSL--NE 390
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniakiglhdlRFKITIIPQDPVLFSGSLrmNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 391 YIHSQDVDE------------TLCKTILRKLDF-ARELFEmdmiDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVIS 457
Cdd:TIGR00957 1381 DPFSQYSDEevwwalelahlkTFVSALPDKLDHeCAEGGE----NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1456
|
....*....
gi 493786691 458 RIQIEEIIK 466
Cdd:TIGR00957 1457 DNLIQSTIR 1465
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-171 |
1.59e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 50.59 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 3 AIKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLL-NQETYQGKISKDVEFIK------------ 69
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWDPQQGEILLNGQPIAdyseaalrqais 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 70 --------FppniSDTSKLGIDLYKELISDDeewKLFREL------NLLNVDENLVY------REfktLSKGEQTKILLA 129
Cdd:PRK11160 418 vvsqrvhlF----SATLRDNLLLAAPNASDE---ALIEVLqqvgleKLLEDDKGLNAwlgeggRQ---LSGGEQRRLGIA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493786691 130 ILFTKEDGFLLIDEPTNHLDMNG-RKILSEYLKSKKG--FLLISH 171
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETeRQILELLAEHAQNktVLMITH 532
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-177 |
2.02e-06 |
|
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: 49.29 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 34 TGLIGRNGIGKSTLFKLLLNQ------------------ETYQGK---------ISKDVEFIKFPPNISDTSKLGIDLYK 86
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKlkpnlgkfddppdwdeilDEFRGSelqnyftklLEGDVKVIVKPQYVDLIPKAVKGKVG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 87 ELISDDEEWKLFRELnllnVD----ENLVYREFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLD----MNGRKILSE 158
Cdd:cd03236 109 ELLKKKDERGKLDEL----VDqlelRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDikqrLNAARLIRE 184
|
170
....*....|....*....
gi 493786691 159 YLKSKKGFLLISHDRNFLD 177
Cdd:cd03236 185 LAEDDNYVLVVEHDLAVLD 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
325-366 |
2.02e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.17 E-value: 2.02e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 493786691 325 LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGI--NHEYTGEI 366
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEI 60
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
325-490 |
2.03e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 49.32 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 325 LSNLSFEIEQGDIVAISGRNGSGKSTLIKillginheYTGEIKLASNLKISYIPQDTSNLSGSLNeyIHS------QDVD 398
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAK--------HMNALLIPSEGKVYVDGLDTSDEENLWD--IRNkagmvfQNPD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 399 ETLCKTILRKlDFA-------------RE-----LFEMDMIDY--------SDGQKKKVLIALSLSKPAHLFIWDEPLNY 452
Cdd:PRK13633 96 NQIVATIVEE-DVAfgpenlgippeeiRErvdesLKKVGMYEYrrhaphllSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493786691 453 IDVISRIQ----IEEIIKEAKPTLIFVEHdkrFVEDI--ANKII 490
Cdd:PRK13633 175 LDPSGRREvvntIKELNKKYGITIILITH---YMEEAveADRII 215
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
310-469 |
2.03e-06 |
|
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: 49.08 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGER---QILSNLSFEIEQGDIVAISGRNGSGKSTLIKILL-------G---INHEYTGEIKLASNL-KIS 375
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLErfydptsGeilLDGVDIRDLNLRWLRsQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 376 YIPQDTSNLSGSLNEYIHSQDVDETLcKTILR--KLDFARELFEMDMIDY-----------SDGQKKKVLIALSLSKPAH 442
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATD-EEVEEaaKKANIHDFIMSLPDGYdtlvgergsqlSGGQKQRIAIARALLRNPK 159
|
170 180
....*....|....*....|....*..
gi 493786691 443 LFIWDEPLNYIDVISRIQIEEIIKEAK 469
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAM 186
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
3-162 |
2.11e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 49.36 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 3 AIKIQNLTFSYYG---YVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL--LNQETyQGKIS------------KDV 65
Cdd:PRK13649 2 GINLQNVSYTYQAgtpFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLngLHVPT-QGSVRvddtlitstsknKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 66 EFIK--------FPPNisdtsklgiDLYKEL-------------ISDDEEWKLFRE-LNLLNVDENLVYREFKTLSKGEQ 123
Cdd:PRK13649 81 KQIRkkvglvfqFPES---------QLFEETvlkdvafgpqnfgVSQEEAEALAREkLALVGISESLFEKNPFELSGGQM 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 493786691 124 TKILLAILFTKEDGFLLIDEPTNHLDMNGRKILSEYLKS 162
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKK 190
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
309-454 |
2.12e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.72 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELS-AHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA----SNLKISYIP----- 378
Cdd:PRK10908 1 MIRFEHVSkAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghdiTRLKNREVPflrrq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 379 -----QDTSNL---------------SGSLNEYIHSQdVDETLCKTILrkLDFARELfemdMIDYSDGQKKKVLIALS-L 437
Cdd:PRK10908 81 igmifQDHHLLmdrtvydnvaipliiAGASGDDIRRR-VSAALDKVGL--LDKAKNF----PIQLSGGEQQRVGIARAvV 153
|
170
....*....|....*..
gi 493786691 438 SKPAHLFIwDEPLNYID 454
Cdd:PRK10908 154 NKPAVLLA-DEPTGNLD 169
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-179 |
2.49e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 48.74 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 1 MSAIKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLN-QETYQGKISKDVEFIKFPP------- 72
Cdd:PRK10895 1 MATLTAKNLAKAYKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGiVPRDAGNIIIDDEDISLLPlhararr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 73 -------------------NISDTSKLGIDLYKELISDDEEwKLFRELNLLNVDENLvyreFKTLSKGEQTKILLAILFT 133
Cdd:PRK10895 79 gigylpqeasifrrlsvydNLMAVLQIRDDLSAEQREDRAN-ELMEEFHIEHLRDSM----GQSLSGGERRRVEIARALA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493786691 134 KEDGFLLIDEPTNHLD----MNGRKILSEYLKSKKGFLLISHD-RNFLDGC 179
Cdd:PRK10895 154 ANPKFILLDEPFAGVDpisvIDIKRIIEHLRDSGLGVLITDHNvRETLAVC 204
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-194 |
2.53e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 49.28 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 1 MSaIKIQNLTFSYYG---YVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL--LNQETYQGKISKDVEFIKFPPNIS 75
Cdd:PRK13637 1 MS-IKIENLTHIYMEgtpFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLngLLKPTSGKIIIDGVDITDKKVKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 76 DTSK-LGI-------DLYKELI-------------SDDE-EWKLFRELNLLNVDenlvYREFK-----TLSKGEQTKILL 128
Cdd:PRK13637 80 DIRKkVGLvfqypeyQLFEETIekdiafgpinlglSEEEiENRVKRAMNIVGLD----YEDYKdkspfELSGGQKRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493786691 129 AILFTKEDGFLLIDEPTNHLDMNGR-KILSEYLKSKKGF----LLISHDRNFLDGCINHVISINRNSIDVQ 194
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRdEILNKIKELHKEYnmtiILVSHSMEDVAKLADRIIVMNKGKCELQ 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-163 |
2.67e-06 |
|
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: 48.26 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKST----LFKLLlnqETYQGKISKD-VEFIKFPPNI---- 74
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV---ELSSGSILIDgVDISKIGLHDlrsr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 75 -----------SDTSKLGIDLYKELiSDDEEWKLFRELNLLNVDENL-------VYREFKTLSKGEQTKILLAILFTKED 136
Cdd:cd03244 80 isiipqdpvlfSGTIRSNLDPFGEY-SDEELWQALERVGLKEFVESLpggldtvVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180
....*....|....*....|....*..
gi 493786691 137 GFLLIDEPTNHLDMNGRKILSEYLKSK 163
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREA 185
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
310-352 |
2.72e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 49.31 E-value: 2.72e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 493786691 310 ISVSELSAHY----GERQILSNLSFEIEQGDIVAISGRNGSGKSTLI 352
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLI 48
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
307-479 |
3.07e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 48.17 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 307 NPLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA----SNLK-------IS 375
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEgediSTLKpeiyrqqVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 376 YIPQdTSNLSGS-------LNEYIHSQDVDETLCKTILRKLDFARELFEMDMIDYSDGQKKKVLIALSLSKPAHLFIWDE 448
Cdd:PRK10247 85 YCAQ-TPTLFGDtvydnliFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190
....*....|....*....|....*....|....*
gi 493786691 449 PLNYIDVISRIQIEEII----KEAKPTLIFVEHDK 479
Cdd:PRK10247 164 ITSALDESNKHNVNEIIhryvREQNIAVLWVTHDK 198
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-164 |
3.19e-06 |
|
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: 48.13 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGYVKPI--FENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQ-ETYQGKISKD-VEFIKFPpnISDTSK 79
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLlEPDAGFATVDgFDVVKEP--AEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 80 LGI-----DLYKELiSDDEEWKLFRELNLLNVDE---------------NLVYREFKTLSKGEQTKILLAILFTKEDGFL 139
Cdd:cd03266 80 LGFvsdstGLYDRL-TARENLEYFAGLYGLKGDEltarleeladrlgmeELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180
....*....|....*....|....*
gi 493786691 140 LIDEPTNHLDMNGRKILSEYLKSKK 164
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLR 183
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-357 |
3.34e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 48.54 E-value: 3.34e-06
10 20 30
....*....|....*....|....*....|....*..
gi 493786691 321 ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLG 357
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAG 54
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
320-490 |
3.67e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.74 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 320 GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLginheytGEIKLASNL------KISYIPQDTSNLSGSLNEYI- 392
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAML-------GELPPRSDAsvvirgTVAYVPQVSWIFNATVRDNIl 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 393 ---------HSQDVDETlckTILRKLDF--ARELFEMDM--IDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDV-ISR 458
Cdd:PLN03130 701 fgspfdperYERAIDVT---ALQHDLDLlpGGDLTEIGErgVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGR 777
|
170 180 190
....*....|....*....|....*....|....
gi 493786691 459 IQIEEIIKEA--KPTLIFVEHDKRFVEDIaNKII 490
Cdd:PLN03130 778 QVFDKCIKDElrGKTRVLVTNQLHFLSQV-DRII 810
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
306-490 |
3.98e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 48.69 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 306 KNPL-----ISVSELSAHYGERQ-----ILSNLSFEIEQGDIVAISGRNGSGKSTL------------------------ 351
Cdd:PRK13631 13 PNPLsddiiLRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLvthfnglikskygtiqvgdiyigd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 352 -IKILLGINHEYTGEIKLASNLK--ISYIPQ--------DTSN---LSGSLNEYIHSQDVDEtLCKTILRKLDFARELFE 417
Cdd:PRK13631 93 kKNNHELITNPYSKKIKNFKELRrrVSMVFQfpeyqlfkDTIEkdiMFGPVALGVKKSEAKK-LAKFYLNKMGLDDSYLE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493786691 418 MDMIDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKP---TLIFVEHDKRFVEDIANKII 490
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADEVI 247
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
310-477 |
4.02e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.30 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKI---LLGINHE--YTGEIKLASnlKISYIPQ----- 379
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEarVEGEVRLFG--RNIYSPDvdpie 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 380 ---------------------DTSNLSGSLNEYIHSQDVDETLCKTILRKLDFARELFEMdMIDY----SDGQKKKVLIA 434
Cdd:PRK14267 83 vrrevgmvfqypnpfphltiyDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDR-LNDYpsnlSGGQRQRLVIA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493786691 435 LSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKP--TLIFVEH 477
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-172 |
4.16e-06 |
|
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: 47.95 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFsYYGYVKpIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL--LNQETYQGKISKDVEF----IK-------- 69
Cdd:cd03260 1 IELRDLNV-YYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrLNDLIPGAPDEGEVLLdgkdIYdldvdvle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 70 --------------FPPNISDTSKLGIDLY----KELISDDEEWKLfRELNLL-NVDENLVYREfktLSKGEQTKILLA- 129
Cdd:cd03260 79 lrrrvgmvfqkpnpFPGSIYDNVAYGLRLHgiklKEELDERVEEAL-RKAALWdEVKDRLHALG---LSGGQQQRLCLAr 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493786691 130 ILFTKEDgFLLIDEPTNHLD-MNGRKI--LSEYLKSKKGFLLISHD 172
Cdd:cd03260 155 ALANEPE-VLLLDEPTSALDpISTAKIeeLIAELKKEYTIVIVTHN 199
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-161 |
4.83e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 48.26 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 1 MSAIKIQNLTFSYYGYVKpIFENVSFSFDTNWKTGLIGRNGIGKSTLFK------------LLLNQETYQGKISKDV-EF 67
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRhfngilkptsgsVLIRGEPITKENIREVrKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 68 IK----------FPPNISDTSKLG---IDLYKELIsddeEWKLFRELNLLNVdENLVYREFKTLSKGEQTKILLAILFTK 134
Cdd:PRK13652 80 VGlvfqnpddqiFSPTVEQDIAFGpinLGLDEETV----AHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180
....*....|....*....|....*..
gi 493786691 135 EDGFLLIDEPTNHLDMNGRKILSEYLK 161
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLN 181
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
321-449 |
5.50e-06 |
|
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: 47.65 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 321 ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEY---TGEIKLA-SNLK-------ISYIPQDTSNLSG-SL 388
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNgQPRKpdqfqkcVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493786691 389 NEYIH---------------SQDVDETlckTILRKLDFAReLFEMDMIDYSDGQKKKVLIALSLSKPAHLFIWDEP 449
Cdd:cd03234 99 RETLTytailrlprkssdaiRKKRVED---VLLRDLALTR-IGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
306-478 |
5.57e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 48.40 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 306 KNPLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLAsNLKISYIPQDTSNLS 385
Cdd:PRK09452 11 LSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-GQDITHVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 386 GSLNEY---------------IHSQDVDETLCKTilRKLDFARELFEMDMID-----YSDGQKKKVLIALSL-SKPAHLF 444
Cdd:PRK09452 90 TVFQSYalfphmtvfenvafgLRMQKTPAAEITP--RVMEALRMVQLEEFAQrkphqLSGGQQQRVAIARAVvNKPKVLL 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 493786691 445 IwDEPLNYIDVISRIQIEEIIKEAKPTL----IFVEHD 478
Cdd:PRK09452 168 L-DESLSALDYKLRKQMQNELKALQRKLgitfVFVTHD 204
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
325-369 |
5.59e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 47.62 E-value: 5.59e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 493786691 325 LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINhEYTGEIKLA 369
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFA 55
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
322-357 |
6.05e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.90 E-value: 6.05e-06
10 20 30
....*....|....*....|....*....|....*.
gi 493786691 322 RQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLG 357
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG 49
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
308-467 |
6.21e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 48.48 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAhygeRQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL------------ASNLKIS 375
Cdd:COG1129 255 VVLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLdgkpvrirsprdAIRAGIA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 376 YIPQD------------TSNLS-GSLNEYIHSQDVDE----TLCKTILRKLDF--------ARELfemdmidySDGQKKK 430
Cdd:COG1129 331 YVPEDrkgeglvldlsiRENITlASLDRLSRGGLLDRrrerALAEEYIKRLRIktpspeqpVGNL--------SGGNQQK 402
|
170 180 190
....*....|....*....|....*....|....*..
gi 493786691 431 VLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKE 467
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRE 439
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-228 |
6.36e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.08 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGyvKPIFE-----NVSFSFDTNWKTGLIGRNGIGKSTLFKL---LLNQETYQGKISKdvefIKFPPNIS 75
Cdd:PRK13645 7 IILDNVSYTYAK--KTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngLIISETGQTIVGD----YAIPANLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 76 DTSKLGiDLYKE--LISDDEEWKLFRE---------------------------LNLLNVDENLVYREFKTLSKGEQTKI 126
Cdd:PRK13645 81 KIKEVK-RLRKEigLVFQFPEYQLFQEtiekdiafgpvnlgenkqeaykkvpelLKLVQLPEDYVKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 127 LLAILFTKEDGFLLIDEPTNHLDMNGRK-ILSEYLK----SKKGFLLISHDRNFLDGCINHVISINRNSIdVQSGNFTSW 201
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEdFINLFERlnkeYKKRIIMVTHNMDQVLRIADEVIVMHEGKV-ISIGSPFEI 238
|
250 260
....*....|....*....|....*..
gi 493786691 202 YENKLMKDKFEISKnEKLRKDIKRLKE 228
Cdd:PRK13645 239 FSNQELLTKIEIDP-PKLYQLMYKLKN 264
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
309-487 |
6.43e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.84 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL--------------ASNLKI 374
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdgenipamsrsrlyTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 375 SYIPQDTS---------NLSGSLNEyiHSQDVDETLCKTILRKLDF-----ARELFEMDMidySDGQKKKVLIALSLSKP 440
Cdd:PRK11831 87 SMLFQSGAlftdmnvfdNVAYPLRE--HTQLPAPLLHSTVMMKLEAvglrgAAKLMPSEL---SGGMARRAALARAIALE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493786691 441 AHLFIWDEPLNYIDVISRIQIEEIIKEAKPTL----IFVEHDKRFVEDIAN 487
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSALgvtcVVVSHDVPEVLSIAD 212
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
321-467 |
6.46e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.86 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 321 ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLasnlkisyipqDTSNLS----GSLNEYIH--S 394
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL-----------DGHDLRdytlASLRNQVAlvS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 395 QDV---DETLCKTIL--RKLDFARELFE--------MDMID----------------YSDGQKKKVLIALSLSKPAHLFI 445
Cdd:PRK11176 424 QNVhlfNDTIANNIAyaRTEQYSREQIEeaarmayaMDFINkmdngldtvigengvlLSGGQRQRIAIARALLRDSPILI 503
|
170 180
....*....|....*....|..
gi 493786691 446 WDEPLNYIDVISRIQIEEIIKE 467
Cdd:PRK11176 504 LDEATSALDTESERAIQAALDE 525
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
310-448 |
8.12e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.43 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYGERQI-LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIPQDTSNLSGSL 388
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493786691 389 NEYIH---------SQDVDETLCKTILRKLDFARELFEMD----MIDYSDGQKKKVLIALSLSKPAHLFIWDE 448
Cdd:PRK10522 403 FTDFHlfdqllgpeGKPANPALVEKWLERLKMAHKLELEDgrisNLKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
309-464 |
9.00e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 47.31 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLG--------------INHEYTGEIKLASNLKI 374
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagshielLGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 375 S-----YIPQDTsNLSGSLN--EYIHSQDVDET-LCKTILR------KLDFARELFEMDMIDY--------SDGQKKKVL 432
Cdd:PRK09984 84 SrantgYIFQQF-NLVNRLSvlENVLIGALGSTpFWRTCFSwftreqKQRALQALTRVGMVHFahqrvstlSGGQQQRVA 162
|
170 180 190
....*....|....*....|....*....|...
gi 493786691 433 IALSLSKPAHLFIWDEPLNYIDVIS-RIQIEEI 464
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESaRIVMDTL 195
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-171 |
9.04e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 47.52 E-value: 9.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 1 MSAIKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLnqetyqGKISKDVEFIKF----PPNISD 76
Cdd:PRK13536 39 TVAIDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIL------GMTSPDAGKITVlgvpVPARAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 77 TSKLGIDLYKELISDDEEWklfrelnllNVDENL-VY--------REFKT---------------------LSKGEQTKI 126
Cdd:PRK13536 111 LARARIGVVPQFDNLDLEF---------TVRENLlVFgryfgmstREIEAvipsllefarleskadarvsdLSGGMKRRL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493786691 127 LLAILFTKEDGFLLIDEPTNHLDMNGRKILSEYLKS----KKGFLLISH 171
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLDPHARHLIWERLRSllarGKTILLTTH 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-52 |
9.79e-06 |
|
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: 46.84 E-value: 9.79e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 493786691 4 IKIQNLTFSYYGYvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLL 52
Cdd:cd03253 1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF 48
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-148 |
1.27e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 14 YGYVKPIfENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLN---QETYQGKISKDVEFIKFpPNISDTSKLGID-LYKEL- 88
Cdd:PRK13549 15 FGGVKAL-DNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvypHGTYEGEIIFEGEELQA-SNIRDTERAGIAiIHQELa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 89 ---------------------ISDDEEW-----KLFRELNlLNVDenlVYREFKTLSKGEQTKILLAILFTKEDGFLLID 142
Cdd:PRK13549 93 lvkelsvleniflgneitpggIMDYDAMylraqKLLAQLK-LDIN---PATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
....*.
gi 493786691 143 EPTNHL 148
Cdd:PRK13549 169 EPTASL 174
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-196 |
1.28e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.10 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 2 SAIKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKL----LLNQETYQGKIS--------------K 63
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLinglLLPDDNPNSKITvdgitltaktvwdiR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 64 DVEFIKF--PPN------ISDTSKLGidLYKELISDDEEWKLFRELnLLNVD-ENLVYREFKTLSKGEQTKILLAILFTK 134
Cdd:PRK13640 84 EKVGIVFqnPDNqfvgatVGDDVAFG--LENRAVPRPEMIKIVRDV-LADVGmLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493786691 135 EDGFLLIDEPTNHLDMNGR-KILS--EYLKSKKGFLLIS--HDRNFLDGCiNHVISINRNSIDVQSG 196
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKeQILKliRKLKKKNNLTVISitHDIDEANMA-DQVLVLDDGKLLAQGS 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
325-469 |
1.44e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 325 LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIPQDtsnlsGSLN--EYIhSQD------ 396
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD-----GLANgiVYI-SEDrkrdgl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 397 -----VDETLCKTILRKL-----------------DFAReLFE-----MDMI--DYSDGQKKKVLIALSLSKPAHLFIWD 447
Cdd:PRK10762 342 vlgmsVKENMSLTALRYFsraggslkhadeqqavsDFIR-LFNiktpsMEQAigLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180
....*....|....*....|..
gi 493786691 448 EPLNYIDVISRIQIEEIIKEAK 469
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFK 442
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
8-149 |
1.46e-05 |
|
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: 45.62 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 8 NLTFS----YYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQETYqGKISKDVEFIKFPpnisdtskLGID 83
Cdd:cd03213 8 NLTVTvkssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTG-LGVSGEVLINGRP--------LDKR 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493786691 84 LYKELIS----DDEewkLFRELNllnVDENLVYR-EFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLD 149
Cdd:cd03213 79 SFRKIIGyvpqDDI---LHPTLT---VRETLMFAaKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-188 |
1.65e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 46.26 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 20 IFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQ-ETYQGKISKDVEF-IKFPP---NISDTSKLGIDLYKELISDDEE 94
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLvAPDEGVIKRNGKLrIGYVPqklYLDTTLPLTVNRFLRLRPGTKK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 95 WKLFRELNLLNVdENLVYREFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGRKILSEYLKSKK-----GFLLI 169
Cdd:PRK09544 99 EDILPALKRVQA-GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRreldcAVLMV 177
|
170
....*....|....*....
gi 493786691 170 SHDRNFLDGCINHVISINR 188
Cdd:PRK09544 178 SHDLHLVMAKTDEVLCLNH 196
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
306-490 |
2.03e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 46.62 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 306 KNPLISVSELSAHYGERQ-------------ILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIK-LASN 371
Cdd:PRK15079 5 KKVLLEVADLKVHFDIKDgkqwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 372 L-------------KISYIPQDTSnlsGSLN------EYI-----------HSQDVDETLcKTILRKLDFARELFEMDMI 421
Cdd:PRK15079 85 LlgmkddewravrsDIQMIFQDPL---ASLNprmtigEIIaeplrtyhpklSRQEVKDRV-KAMMLKVGLLPNLINRYPH 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493786691 422 DYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQI----EEIIKEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVvnllQQLQREMGLSLIFIAHDLAVVKHISDRVL 233
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
327-461 |
2.38e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 45.94 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 327 NLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLAS-----------NLKISYIPQDTSN------------ 383
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrSQRIRMIFQDPSTslnprqrisqil 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 384 -----LSGSLNEYIHSQDVDETLCKTILRKlDFARELFEMdmidYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISR 458
Cdd:PRK15112 111 dfplrLNTDLEPEQREKQIIETLRQVGLLP-DHASYYPHM----LAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
...
gi 493786691 459 IQI 461
Cdd:PRK15112 186 SQL 188
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
325-455 |
2.61e-05 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 45.60 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 325 LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGInHEYTGEIKLA----SNLKI-------SYIPQDTSNLSG------- 386
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNgrplSDWSAaelarhrAYLSQQQSPPFAmpvfqyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 387 SLneYIHSQDVDETLCKTI---LRKLDFARELfeMDMIDY-SDGQKKKVLIA---L----SLSKPAHLFIWDEPLNYIDV 455
Cdd:COG4138 91 AL--HQPAGASSEAVEQLLaqlAEALGLEDKL--SRPLTQlSGGEWQRVRLAavlLqvwpTINPEGQLLLLDEPMNSLDV 166
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-176 |
2.72e-05 |
|
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: 44.29 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 33 KTGLIGRNGIGKSTLFKLLLNQETYQGKISKdvefikfppnisdtsklgidlykeLISDDEewklFRELNLLNVDENLVY 112
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPGGGVI------------------------YIDGED----ILEEVLDQLLLIIVG 55
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493786691 113 REFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGRKILSEYLKSKKGFLLISHDRNFL 176
Cdd:smart00382 56 GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTV 119
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-150 |
2.79e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 45.93 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 6 IQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL------------LNQETYQGKISKDV--EFIKFP 71
Cdd:PRK10575 14 LRNVSFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLgrhqppsegeilLDAQPLESWSSKAFarKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 72 PNISDTSKLGIdlyKELISDDE-EWK----LFRELNLLNVDEN--------LVYREFKTLSKGEQTKILLAILFTKEDGF 138
Cdd:PRK10575 92 QQLPAAEGMTV---RELVAIGRyPWHgalgRFGAADREKVEEAislvglkpLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170
....*....|..
gi 493786691 139 LLIDEPTNHLDM 150
Cdd:PRK10575 169 LLLDEPTSALDI 180
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-172 |
2.80e-05 |
|
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: 45.37 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGyVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKlLLNQ--ETYQGKISKDVEFIKFPPNISDTSKLG 81
Cdd:cd03295 1 IEFENVTKRYGG-GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMK-MINRliEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 82 -----------------IDLYKELISDDEEWKLFRELNLLNV----DENLVYREFKTLSKGEQTKILLAILFTKEDGFLL 140
Cdd:cd03295 79 yviqqiglfphmtveenIALVPKLLKWPKEKIRERADELLALvgldPAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 493786691 141 IDEPTNHLDMNGRKILSEYLK-----SKKGFLLISHD 172
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKrlqqeLGKTIVFVTHD 195
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
308-368 |
3.09e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 45.37 E-value: 3.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493786691 308 PLISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL 368
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILL 64
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
309-480 |
3.12e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.16 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGERQ----ILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL---------------- 368
Cdd:PRK10584 6 IVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhqmdeearakl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 369 -ASNLKISY-----IP--------QDTSNLSGSLNEYIHSQdvdetlCKTILRKLDFARELFEMDMiDYSDGQKKKVLIA 434
Cdd:PRK10584 86 rAKHVGFVFqsfmlIPtlnalenvELPALLRGESSRQSRNG------AKALLEQLGLGKRLDHLPA-QLSGGEQQRVALA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493786691 435 LSLS-KPAHLFIwDEPLNYIDVISRIQIEEII----KEAKPTLIFVEHDKR 480
Cdd:PRK10584 159 RAFNgRPDVLFA-DEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDLQ 208
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
308-490 |
3.97e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.73 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHY--------GERQI--LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLKISYI 377
Cdd:PRK11308 4 PLLQAIDLKKHYpvkrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 378 PQDTSNLS-----------GSLN--EYIHSQDVDETLCKTILRKLDFARELFEM---------------DMidYSDGQKK 429
Cdd:PRK11308 84 PEAQKLLRqkiqivfqnpyGSLNprKKVGQILEEPLLINTSLSAAERREKALAMmakvglrpehydrypHM--FSGGQRQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493786691 430 KVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEII----KEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMmdlqQELGLSYVFISHDLSVVEHIADEVM 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-172 |
3.98e-05 |
|
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: 44.77 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSY--YGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQETYQ-GKISKDVEFIKFPPNisdtsKL 80
Cdd:cd03293 1 LEVRNVSKTYggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTsGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 81 GIdlykelisddeewkLFRELNLL---NVDENLVY-REFKTLSKGEQTKILLAILftKE---DGF--------------- 138
Cdd:cd03293 76 GY--------------VFQQDALLpwlTVLDNVALgLELQGVPKAEARERAEELL--ELvglSGFenayphqlsggmrqr 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493786691 139 -------------LLIDEPTNHLDMNGRKILSEYL-----KSKKGFLLISHD 172
Cdd:cd03293 140 valaralavdpdvLLLDEPFSALDALTREQLQEELldiwrETGKTVLLVTHD 191
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-162 |
4.22e-05 |
|
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: 44.41 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 20 IFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL------------LNQET---YQGKISKDVEFIKFPPNISDTSKLGIDL 84
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILaglspplagrvlLNGGPldfQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 85 --YKELISDDEEWKLFRELNLLNVDEnlvyREFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGRKILSEYLKS 162
Cdd:cd03231 95 rfWHADHSDEQVEEALARVGLNGFED----RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG 170
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-200 |
4.40e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 45.99 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLT-FSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQETYQGKISKD-VEFIKFPP-----NIS- 75
Cdd:PRK11174 350 IEAEDLEiLSPDG--KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINgIELRELDPeswrkHLSw 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 76 ---------DTSKLGIDLYKELISDDEEWKLfreLNLLNVDEnLVYREFK-----------TLSKGEQTKILLAILFTKE 135
Cdd:PRK11174 428 vgqnpqlphGTLRDNVLLGNPDASDEQLQQA---LENAWVSE-FLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQP 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493786691 136 DGFLLIDEPTNHLDMNGRKILSEYLKS---KKGFLLISHDRNFLDGCinHVISINRNSIDVQSGNFTS 200
Cdd:PRK11174 504 CQLLLLDEPTASLDAHSEQLVMQALNAasrRQTTLMVTHQLEDLAQW--DQIWVMQDGQIVQQGDYAE 569
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
328-479 |
4.79e-05 |
|
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: 45.90 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 328 LSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIPQDTSNLSGSLNEYIHSQDVDETLCKTILR 407
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLS 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 408 KLDFARELFEMD-------------MIDYSD----GQKKKVLIA-LSLSKPAHLfIWDEPLNYIDVISRIQIEEIIKEAK 469
Cdd:TIGR00954 551 DKDLEQILDNVQlthilereggwsaVQDWMDvlsgGEKQRIAMArLFYHKPQFA-ILDECTSAVSVDVEGYMYRLCREFG 629
|
170
....*....|
gi 493786691 470 PTLIFVEHDK 479
Cdd:TIGR00954 630 ITLFSVSHRK 639
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-51 |
4.83e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 44.69 E-value: 4.83e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493786691 1 MS-AIKIQNLTFSYYGYVKP--------------------IFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL 51
Cdd:COG1134 1 MSsMIEVENVSKSYRLYHEPsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLI 72
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-179 |
4.83e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 3 AIKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLN-QETYQGKIS-KDVEFIKF---------- 70
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRiVELEKGRIMiDDCDVAKFgltdlrrvls 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 71 -----PPNISDTSKLGIDLYKELiSDDEEWKLFRELNLLNVDEN-------LVYREFKTLSKGEQTKILLAILFTKEDGF 138
Cdd:PLN03232 1314 iipqsPVLFSGTVRFNIDPFSEH-NDADLWEALERAHIKDVIDRnpfgldaEVSEGGENFSVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493786691 139 LLIDEPTNHLDMNG----RKILSEYLKSKKgFLLISHDRNFLDGC 179
Cdd:PLN03232 1393 LVLDEATASVDVRTdsliQRTIREEFKSCT-MLVIAHRLNTIIDC 1436
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
309-481 |
5.10e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIPQDT------- 381
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQfafeeft 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 382 -----------------------SNLSGSLNEYIHSQDVD-----------ETLCKTILRKLDFARELFEMDMIDYSDGQ 427
Cdd:PRK15064 81 vldtvimghtelwevkqerdriyALPEMSEEDGMKVADLEvkfaemdgytaEARAGELLLGVGIPEEQHYGLMSEVAPGW 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493786691 428 KKKVLIALSL-SKPAHLFIwDEPLNYIDvISRIQ-IEEIIKEAKPTLIFVEHDKRF 481
Cdd:PRK15064 161 KLRVLLAQALfSNPDILLL-DEPTNNLD-INTIRwLEDVLNERNSTMIIISHDRHF 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-151 |
6.58e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 45.22 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 1 MSAIKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKL---LLNQETyqGKISKDVEFIKfppNIS-- 75
Cdd:PRK09536 1 MPMIDVSDLSVEFGD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAingTLTPTA--GTVLVAGDDVE---ALSar 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 76 -----------DTSkLGIDLYKELI---------------SDDEEWKLFRELNLLNVDEnLVYREFKTLSKGEQTKILLA 129
Cdd:PRK09536 74 aasrrvasvpqDTS-LSFEFDVRQVvemgrtphrsrfdtwTETDRAAVERAMERTGVAQ-FADRPVTSLSGGERQRVLLA 151
|
170 180
....*....|....*....|..
gi 493786691 130 ILFTKEDGFLLIDEPTNHLDMN 151
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDIN 173
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
322-478 |
6.65e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 44.78 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 322 RQILSNLSFEIEQGDIVAISGRNGSGKSTLIKIlLGINHEYT-GEIKL-----------ASNLKISYIPQDTSNLSG-SL 388
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKM-LGRHQPPSeGEILLdaqpleswsskAFARKVAYLPQQLPAAEGmTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 389 NEYI-------HS----------QDVDETLCKTILRKldFARELFEmdmiDYSDGQKKKVLIALSLSKPAHLFIWDEPLN 451
Cdd:PRK10575 103 RELVaigrypwHGalgrfgaadrEKVEEAISLVGLKP--LAHRLVD----SLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190
....*....|....*....|....*....|.
gi 493786691 452 YIDVISRIQ----IEEIIKEAKPTLIFVEHD 478
Cdd:PRK10575 177 ALDIAHQVDvlalVHRLSQERGLTVIAVLHD 207
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
310-352 |
7.39e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 44.79 E-value: 7.39e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 493786691 310 ISVSELSAHY--GERQI--LSNLSFEIEQGDIVAISGRNGSGKSTLI 352
Cdd:PRK11153 2 IELKNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLI 48
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
321-490 |
8.76e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 44.23 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 321 ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGI-----NHEYTGEIKLASNLKISYIPQDTSNLSGSLNEYIHSQ 395
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetGQTIVGDYAIPANLKKIKEVKRLRKEIGLVFQFPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 396 DVDETLCKTI---------------------LRKLDFARELFEMDMIDYSDGQKKKVLIALSLSKPAHLFIWDEPL---- 450
Cdd:PRK13645 103 LFQETIEKDIafgpvnlgenkqeaykkvpelLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTggld 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493786691 451 -----NYIDVISRIQieeiiKEAKPTLIFVEHDKRFVEDIANKII 490
Cdd:PRK13645 183 pkgeeDFINLFERLN-----KEYKKRIIMVTHNMDQVLRIADEVI 222
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
337-491 |
9.26e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.36 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 337 IVAISGRNGSGKSTlikILLGINHEYTGEiKLASNLKISYIPQDTSNLSGSLNEYIHSQDVDETLCKtILRKLDFAR--- 413
Cdd:cd03240 24 LTLIVGQNGAGKTT---IIEALKYALTGE-LPPNSKGGAHDPKLIREGEVRAQVKLAFENANGKKYT-ITRSLAILEnvi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 414 -----ELFE--MDMIDY-SDGQkkKVLIALSL--------SKPAHLFIWDEPLNYIDVISR-IQIEEIIKEAK----PTL 472
Cdd:cd03240 99 fchqgESNWplLDMRGRcSGGE--KVLASLIIrlalaetfGSNCGILALDEPTTNLDEENIeESLAEIIEERKsqknFQL 176
|
170
....*....|....*....
gi 493786691 473 IFVEHDKRFVeDIANKIIQ 491
Cdd:cd03240 177 IVITHDEELV-DAADHIYR 194
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-51 |
9.83e-05 |
|
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: 43.76 E-value: 9.83e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 493786691 4 IKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL 51
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI 48
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
35-177 |
1.10e-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: 42.94 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 35 GLIGRNGIGKSTLFKLLLNQETyqgkiskdvefikfpPNisdtsklgidlykeliSDDEEWKLFRelnllnvdenLVYR- 113
Cdd:cd03222 29 GIVGPNGTGKTTAVKILAGQLI---------------PN----------------GDNDEWDGIT----------PVYKp 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493786691 114 EFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGR-------KILSEylKSKKGFLLISHDRNFLD 177
Cdd:cd03222 68 QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRlnaaraiRRLSE--EGKKTALVVEHDLAVLD 136
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-64 |
1.15e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 44.62 E-value: 1.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493786691 4 IKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLN-QETYQGKISKD 64
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRfYDIDEGEILLD 403
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
321-492 |
1.20e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.92 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 321 ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKlasnlkisYIPQDTSNLSGSlnEYIHSQDVDET 400
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIE--------WIFKDEKNKKKT--KEKEKVLEKLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 401 LCKTILRKLDFAREL-------------------FEMDMI------------------------------------DYSD 425
Cdd:PRK13651 89 IQKTRFKKIKKIKEIrrrvgvvfqfaeyqlfeqtIEKDIIfgpvsmgvskeeakkraakyielvgldesylqrspfELSG 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 426 GQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIK---EAKPTLIFVEHDKRFVEDIANKIIQF 492
Cdd:PRK13651 169 GQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDnlnKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
308-380 |
1.20e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 44.63 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAH-YGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLA------------SNLKI 374
Cdd:COG3845 256 VVLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDgeditglsprerRRLGV 335
|
....*.
gi 493786691 375 SYIPQD 380
Cdd:COG3845 336 AYIPED 341
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-51 |
1.44e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 43.47 E-value: 1.44e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 493786691 4 IKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL 51
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLL 53
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-207 |
1.58e-04 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 44.33 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGYV-KPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNqeTYQ---GKISKDVEFIK---------- 69
Cdd:TIGR00958 479 IEFQDVSFSYPNRPdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQN--LYQptgGQVLLDGVPLVqydhhylhrq 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 70 ----------FPPNISDTSKLGIDLY---------KELISDDEEWKLFRELNlLNVDENLVYrefktLSKGEQTKILLAI 130
Cdd:TIGR00958 557 valvgqepvlFSGSVRENIAYGLTDTpdeeimaaaKAANAHDFIMEFPNGYD-TEVGEKGSQ-----LSGGQKQRIAIAR 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493786691 131 LFTKEDGFLLIDEPTNHLDMNGRKILSEYLKSK-KGFLLISHDRNFLDGCiNHVISINRNSIdVQSGNFTSWYENKLM 207
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQLLQESRSRAsRTVLLIAHRLSTVERA-DQILVLKKGSV-VEMGTHKQLMEDQGC 706
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
23-177 |
1.81e-04 |
|
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: 42.31 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 23 NVSFSFDTNWKTGLIGRNGIGKSTLFklllnQETyqGKISKDVEFIKFPPNISDTSKLGIDLYKELIsddeewklfreln 102
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLV-----NEG--LYASGKARLISFLPKFSRNKLIFIDQLQFLI------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 103 llnvDENLVY----REFKTLSKGEQTKILLA-ILFTKEDGFL-LIDEPTNHLDMNGRKILSEYLKS----KKGFLLISHD 172
Cdd:cd03238 73 ----DVGLGYltlgQKLSTLSGGELQRVKLAsELFSEPPGTLfILDEPSTGLHQQDINQLLEVIKGlidlGNTVILIEHN 148
|
....*
gi 493786691 173 RNFLD 177
Cdd:cd03238 149 LDVLS 153
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
320-355 |
1.85e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 44.18 E-value: 1.85e-04
10 20 30
....*....|....*....|....*....|....*.
gi 493786691 320 GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKIL 355
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL 381
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
321-489 |
1.85e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.08 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 321 ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL---------ASNLK-----ISYIPQDTsnlsg 386
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFngqridtlsPGKLQalrrdIQFIFQDP----- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 387 slneyIHSQDVDETLCKTILRKL--------DFARE----LFEMDMI----------DYSDGQKKKVLIALSLSKPAHLF 444
Cdd:PRK10261 411 -----YASLDPRQTVGDSIMEPLrvhgllpgKAAAArvawLLERVGLlpehawryphEFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493786691 445 IWDEPLNYIDVISRIQIEEII----KEAKPTLIFVEHDKRFVEDIANKI 489
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLldlqRDFGIAYLFISHDMAVVERISHRV 534
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-172 |
1.94e-04 |
|
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: 42.88 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSY--YGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLN-QETYQGKI------------------S 62
Cdd:cd03257 2 LEVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGlLKPTSGSIifdgkdllklsrrlrkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 63 KDVEFI------KFPPN------ISDTSKLGIDLYKELISDDEEWKLFRELNLlnvDENLVYREFKTLSKGEQTKILLAI 130
Cdd:cd03257 82 KEIQMVfqdpmsSLNPRmtigeqIAEPLRIHGKLSKKEARKEAVLLLLVGVGL---PEEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493786691 131 LFTKEDGFLLIDEPTNHLDM-NGRKILSEYLKSKK----GFLLISHD 172
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVsVQAQILDLLKKLQEelglTLLFITHD 205
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
18-172 |
1.94e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.96 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 18 KPIFENVSFSFDTNWKTGLIGRNGIGKSTLFK---LLLNQETYQGKISKDVEfikfPPNISDTSKLgidlykELISddee 94
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaigLALGGAQSATRRRSGVK----AGCIVAAVSA------ELIF---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 95 wklfrelnllnvdenlvyrEFKTLSKGEQTKILLAILF----TKEDGFLLIDEPTNHLDMNGRKILSEYLK--SKKG--F 166
Cdd:cd03227 74 -------------------TRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILehLVKGaqV 134
|
....*.
gi 493786691 167 LLISHD 172
Cdd:cd03227 135 IVITHL 140
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
9-158 |
2.10e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.13 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 9 LTFSYYG-YVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQ-ETYQGKI--------SKDVEFIkFPPNISDTS 78
Cdd:TIGR01271 429 LFFSNFSlYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGElEPSEGKIkhsgrisfSPQTSWI-MPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 79 KLGIDlYKEL--ISDDEEWKLFRELNLLNVDENLVYREFK-TLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGRKI 155
Cdd:TIGR01271 508 IFGLS-YDEYryTSVIKACQLEEDIALFPEKDKTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
...
gi 493786691 156 LSE 158
Cdd:TIGR01271 587 IFE 589
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
325-490 |
2.12e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.73 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 325 LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIpqdTSNLSGSLN--EYIHSQDVDETLC 402
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAI---SSGLNGQLTgiENIELKGLMMGLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 403 KTILRK-----LDFAR--ELFEMDMIDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYID-VISRIQIEEI--IKEAKPTL 472
Cdd:PRK13545 117 KEKIKEiipeiIEFADigKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDqTFTKKCLDKMneFKEQGKTI 196
|
170
....*....|....*...
gi 493786691 473 IFVEHDKRFVEDIANKII 490
Cdd:PRK13545 197 FFISHSLSQVKSFCTKAL 214
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-174 |
2.22e-04 |
|
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: 43.66 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 14 YGYVKPIfENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLN---QETYQGKISKDVEFIKfPPNISDTSKLGI-------D 83
Cdd:TIGR02633 11 FGGVKAL-DGIDLEVRPGECVGLCGENGAGKSTLMKILSGvypHGTWDGEIYWSGSPLK-ASNIRDTERAGIviihqelT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 84 LYKEL-----------------ISDDEEW-----KLFRELNLlnvDENLVYREFKTLSKGEQTKILLAILFTKEDGFLLI 141
Cdd:TIGR02633 89 LVPELsvaeniflgneitlpggRMAYNAMylrakNLLRELQL---DADNVTRPVGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 493786691 142 DEPTNHLDMNGRKILSEYLKSKK----GFLLISHDRN 174
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDLKahgvACVYISHKLN 202
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-51 |
2.36e-04 |
|
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: 42.52 E-value: 2.36e-04
10 20 30
....*....|....*....|....*....|....*
gi 493786691 17 VKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL 51
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLL 68
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
310-492 |
2.38e-04 |
|
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: 41.92 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELSAHYgerqiLSNLSFEIEQGDIVAISGRNGSGKSTLIKILLginhEYTGEIKLASNLKiSYIPQDTSNLsGSLn 389
Cdd:cd03238 1 LTVSGANVHN-----LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLISFLP-KFSRNKLIFI-DQL- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 390 eyihsqdvdETLCKTILRKLDFARELFEMdmidySDGQKKKVLIALSLSKPAH--LFIWDEPLNYIDVISRIQIEEIIKE 467
Cdd:cd03238 69 ---------QFLIDVGLGYLTLGQKLSTL-----SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKG 134
|
170 180
....*....|....*....|....*...
gi 493786691 468 ---AKPTLIFVEHDKRFVEDiANKIIQF 492
Cdd:cd03238 135 lidLGNTVILIEHNLDVLSS-ADWIIDF 161
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
325-489 |
2.43e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.88 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 325 LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKLASNLKISYIpqdTSNLSGSLN--EYIHSQdvdeTLC 402
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAI---SAGLSGQLTgiENIEFK----MLC 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 403 KTILRK---------LDFAR--ELFEMDMIDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYID-VISRIQIEEI--IKEA 468
Cdd:PRK13546 113 MGFKRKeikamtpkiIEFSElgEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDqTFAQKCLDKIyeFKEQ 192
|
170 180
....*....|....*....|.
gi 493786691 469 KPTLIFVEHDKRFVEDIANKI 489
Cdd:PRK13546 193 NKTIFFVSHNLGQVRQFCTKI 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
324-477 |
2.59e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 324 ILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL---------ASNLK--ISYIPQDTSNLSGSLNEYI 392
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIddcdvakfgLTDLRrvLSIIPQSPVLFSGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 393 H--SQDVDETLCKTILR---KLDFARELFEMDMI------DYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQI 461
Cdd:PLN03232 1331 DpfSEHNDADLWEALERahiKDVIDRNPFGLDAEvseggeNFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI 1410
|
170
....*....|....*...
gi 493786691 462 EEIIKEA--KPTLIFVEH 477
Cdd:PLN03232 1411 QRTIREEfkSCTMLVIAH 1428
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
320-449 |
2.78e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 43.50 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 320 GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINH---EYTGEIKL------ASNLKI--SYIPQDTSNLsGSL 388
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLngmpidAKEMRAisAYVQQDDLFI-PTL 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493786691 389 NEYIH------------------SQDVDETLCKTILRKLDFARELFEMDMIDYSDGQKKKVLIALSLSKPAHLFIWDEP 449
Cdd:TIGR00955 115 TVREHlmfqahlrmprrvtkkekRERVDEVLQALGLRKCANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
324-467 |
3.01e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.57 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 324 ILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEI-------------KLASNLKIsyIPQDTSNLSGS--- 387
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIlidgcdiskfglmDLRKVLGI--IPQAPVLFSGTvrf 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 388 -LNEYIHSQDVD--ETL----CKTILRK--LDFARELFEMDMiDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISR 458
Cdd:PLN03130 1332 nLDPFNEHNDADlwESLerahLKDVIRRnsLGLDAEVSEAGE-NFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTD 1410
|
....*....
gi 493786691 459 IQIEEIIKE 467
Cdd:PLN03130 1411 ALIQKTIRE 1419
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-162 |
3.15e-04 |
|
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: 41.96 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 19 PIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL------------LNQE---TYQGKISKDVEFIKFPPNISD--TSKLG 81
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILagllrpdsgevrWNGTplaEQRDEPHENILYLGHLPGLKPelSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 82 IDLYKElISDDEEWKLFRELNLLNVDeNLVYREFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLDMNGRKILSEYLK 161
Cdd:TIGR01189 94 LHFWAA-IHGGAQRTIEDALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLR 171
|
.
gi 493786691 162 S 162
Cdd:TIGR01189 172 A 172
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
322-486 |
3.19e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 42.38 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 322 RQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHeyTGEIKLASNLKISYIPQDTSNLSGSLNEYI--------- 392
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILP--AGVRQTAGRVLLDGKPVAPCALRGRKIATImqnprsafn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 393 -------HSQdvdETLC--------KTILRKL------DFAREL----FEMdmidySDGQKKKVLIALSLSKPAHLFIWD 447
Cdd:PRK10418 94 plhtmhtHAR---ETCLalgkpaddATLTAALeavgleNAARVLklypFEM-----SGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493786691 448 EPLNYIDVISRIQI----EEIIKEAKPTLIFVEHD----KRFVEDIA 486
Cdd:PRK10418 166 EPTTDLDVVAQARIldllESIVQKRALGMLLVTHDmgvvARLADDVA 212
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-145 |
3.80e-04 |
|
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: 41.89 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 1 MSAIKIQNLTfSYYGYVkPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQ-ETYQGKIS-KDVEFIKFPPNisDTS 78
Cdd:COG0410 1 MPMLEVENLH-AGYGGI-HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLlPPRSGSIRfDGEDITGLPPH--RIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 79 KLGIdlykelisddEEWKLFRElnlLNVDENL-------------------VY------REFK-----TLSKGEQTkiLL 128
Cdd:COG0410 77 RLGIgy------vpEGRRIFPS---LTVEENLllgayarrdraevradlerVYelfprlKERRrqragTLSGGEQQ--ML 145
|
170 180
....*....|....*....|
gi 493786691 129 AI---LFTKEDgFLLIDEPT 145
Cdd:COG0410 146 AIgraLMSRPK-LLLLDEPS 164
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-171 |
3.86e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 43.46 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQETYQGKiSKDVEFIKFPPNISDTSK-LG- 81
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG-DATVAGKSILTNISDVHQnMGy 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 82 ---IDLYKELISDDEEWKLFRELNLLNVDE----------NL---VY--REFKTLSKGEQTKILLAILFTKEDGFLLIDE 143
Cdd:TIGR01257 2017 cpqFDAIDDLLTGREHLYLYARLRGVPAEEiekvanwsiqSLglsLYadRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190
....*....|....*....|....*....|..
gi 493786691 144 PTNHLDMNGRKIL----SEYLKSKKGFLLISH 171
Cdd:TIGR01257 2097 PTTGMDPQARRMLwntiVSIIREGRAVVLTSH 2128
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-51 |
4.10e-04 |
|
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: 41.78 E-value: 4.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 493786691 4 IKIQNLTFSYyGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL 51
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCL 47
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
210-454 |
4.39e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 210 KFEISKNE---KLRKDIKRLKEAARQSKIWSDKIENtkngvkvsgiKPDKGRIGHQ-SAKMMKKSKNLEHRQNKAIEEKQ 285
Cdd:TIGR00956 694 KGAKQKGEilvFRRGSLKRAKKAGETSASNKNDIEA----------GEVLGSTDLTdESDDVNDEKDMEKESGEDIFHWR 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 286 SLLKDIEIKEslllhplhhhknplisvselsahyGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGinHEYTGE 365
Cdd:TIGR00956 764 NLTYEVKIKK------------------------EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGV 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 366 IKLASNLkISYIPQDTS--NLSGslneYIHSQDV--DETLCKTILR---------------KLDFARELFE-MDMIDYSD 425
Cdd:TIGR00956 818 ITGGDRL-VNGRPLDSSfqRSIG----YVQQQDLhlPTSTVRESLRfsaylrqpksvskseKMEYVEEVIKlLEMESYAD 892
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 493786691 426 G------------QKKKVLIALSL-SKPAHLFIWDEPLNYID 454
Cdd:TIGR00956 893 AvvgvpgeglnveQRKRLTIGVELvAKPKLLLFLDEPTSGLD 934
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-191 |
4.67e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 42.05 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQETYQ-GKISKDVEFIKfPPNISDTSK-LG 81
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKsGEIFYNNQAIT-DDNFEKLRKhIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 82 I--------------------DLYKELISDDEewkLFRELNLLNVDENLVYR---EFKTLSKGEQTKILLAILFTKEDGF 138
Cdd:PRK13648 87 IvfqnpdnqfvgsivkydvafGLENHAVPYDE---MHRRVSEALKQVDMLERadyEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 139 LLIDEPTNHLDMNGRKILSE---YLKSKKGFLLIS--HDrnfLDGCI--NHVISINRNSI 191
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDlvrKVKSEHNITIISitHD---LSEAMeaDHVIVMNKGTV 220
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
337-379 |
5.00e-04 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 40.55 E-value: 5.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 493786691 337 IVAISGRNGSGKSTLIKIL---LGINHEYTGEI------KLASnlKISYIPQ 379
Cdd:cd02020 1 IIAIDGPAGSGKSTVAKLLakkLGLPYLDTGGIrteevgKLAS--EVAAIPE 50
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
325-366 |
5.05e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.68 E-value: 5.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 493786691 325 LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEI 366
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSI 61
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
23-172 |
5.55e-04 |
|
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: 41.65 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 23 NVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQET-YQGKIS-KDVEFIKFPPNisDTSKLGI-------DLYKEL----- 88
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRpTSGSVLfDGEDITGLPPH--EIARLGIgrtfqipRLFPELtvlen 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 89 ------------ISDDEEWKLFRE--------LNLLNVDEnLVYREFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHL 148
Cdd:cd03219 96 vmvaaqartgsgLLLARARREEREareraeelLERVGLAD-LADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180
....*....|....*....|....*...
gi 493786691 149 DMNGRKILSEYLKS----KKGFLLISHD 172
Cdd:cd03219 175 NPEETEELAELIRElrerGITVLLVEHD 202
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
321-448 |
5.87e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 321 ERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYtgeiKLASNLKISY--IPQD--------TSNLSGSLNE 390
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGF----HIGVEGVITYdgITPEeikkhyrgDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 391 YIHSQDVDETL-----CKTI------LRKLDFARELFEMDMIDY------------------SDGQKKKVLIALSLSKPA 441
Cdd:TIGR00956 149 HFPHLTVGETLdfaarCKTPqnrpdgVSREEYAKHIADVYMATYglshtrntkvgndfvrgvSGGERKRVSIAEASLGGA 228
|
....*..
gi 493786691 442 HLFIWDE 448
Cdd:TIGR00956 229 KIQCWDN 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
308-490 |
6.42e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.38 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHY-----------GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLG-INHEytGEI--------- 366
Cdd:PRK15134 274 PLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRlINSQ--GEIwfdgqplhn 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 367 -----KLASNLKISYIPQD-TSNLSGSLNEY--------IHSQDVD----ETLCKTILRKLDFARELFEMDMIDYSDGQK 428
Cdd:PRK15134 352 lnrrqLLPVRHRIQVVFQDpNSSLNPRLNVLqiieeglrVHQPTLSaaqrEQQVIAVMEEVGLDPETRHRYPAEFSGGQR 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493786691 429 KKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKPT----LIFVEHDKRFVEDIANKII 490
Cdd:PRK15134 432 QRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhqlaYLFISHDLHVVRALCHQVI 497
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
310-368 |
7.89e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 42.01 E-value: 7.89e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 310 ISVSELS-AHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL 368
Cdd:PRK10790 341 IDIDNVSfAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL 400
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
115-171 |
8.20e-04 |
|
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: 41.10 E-value: 8.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493786691 115 FKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLD----MNGRKILSEYLKSKKGFLLISH 171
Cdd:cd03234 141 VKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDsftaLNLVSTLSQLARRNRIVILTIH 201
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-53 |
8.57e-04 |
|
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: 40.92 E-value: 8.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 493786691 4 IKIQNLTFSYYGYV-KPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLN 53
Cdd:cd03248 12 VKFQNVTFAYPTRPdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLEN 62
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
311-375 |
9.87e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.79 E-value: 9.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493786691 311 SVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLG--INHEYTGEIkLASNLKIS 375
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTI-LANNRKPT 135
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
308-366 |
1.01e-03 |
|
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: 41.59 E-value: 1.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 308 PLISVSELSAHY-----------GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGInHEYTGEI 366
Cdd:COG4172 274 PLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEI 342
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
324-477 |
1.03e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.07 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 324 ILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL------ASNLK-----ISYIPQDTSNLSGSLneyi 392
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVngreigAYGLRelrrqFSMIPQDPVLFDGTV---- 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 393 hSQDVD---ETLCKTILRKLDFA----RELFEMDMID---------YSDGQKKKVLIALSLSKPAHLFI-WDEPLNYIDV 455
Cdd:PTZ00243 1401 -RQNVDpflEASSAEVWAALELVglreRVASESEGIDsrvleggsnYSVGQRQLMCMARALLKKGSGFIlMDEATANIDP 1479
|
170 180
....*....|....*....|....
gi 493786691 456 ISRIQIEEIIKEA--KPTLIFVEH 477
Cdd:PTZ00243 1480 ALDRQIQATVMSAfsAYTVITIAH 1503
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-67 |
1.06e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 40.79 E-value: 1.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493786691 2 SAIKIQNLTFsYYGyVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL--LNQETYQGKISKDVEF 67
Cdd:COG1117 10 PKIEVRNLNV-YYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPGARVEGEILL 75
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-51 |
1.44e-03 |
|
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: 40.16 E-value: 1.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 493786691 4 IKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL 51
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLI 48
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
309-357 |
1.57e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.16 E-value: 1.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 493786691 309 LISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLG 357
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG 49
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
334-482 |
1.59e-03 |
|
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: 38.89 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 334 QGDIVAISGRNGSGKSTLIKILLginheytgeiklasnlkisyipqdtsNLSGSLNEYIHSQDVDETLCKTILRKLDfar 413
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALA--------------------------RELGPPGGGVIYIDGEDILEEVLDQLLL--- 51
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493786691 414 ELFEMDMIDYSDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKEAKPTLIFVEHDKRFV 482
Cdd:smart00382 52 IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-62 |
1.67e-03 |
|
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: 39.76 E-value: 1.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493786691 4 IKIQNLTFSY---YGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQ-ETYQGKIS 62
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGElEKLSGSVS 63
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
327-355 |
1.80e-03 |
|
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: 40.32 E-value: 1.80e-03
10 20
....*....|....*....|....*....
gi 493786691 327 NLSFEIEQGDIVAISGRNGSGKSTLIKIL 355
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCI 70
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
424-489 |
2.62e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.79 E-value: 2.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 424 SDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEII----KEAKPTLIFVEHDKRFVEDIANKI 489
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLtrlnQNNNTTILLISHDLQMLSQWADKI 229
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
310-357 |
2.82e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.49 E-value: 2.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 493786691 310 ISVSELSAHYGERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLG 357
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG 49
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
309-489 |
2.88e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 39.79 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 309 LISVSELSAHY-GERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL----ASNLKISYIPQDTSN 383
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrgepITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 384 LSGSLNEYIHSQDVDETLC----------KTILRKLDFARELFEMDMI------DYSDGQKKKVLIALSLSKPAHLFIWD 447
Cdd:PRK13652 83 VFQNPDDQIFSPTVEQDIAfgpinlgldeETVAHRVSSALHMLGLEELrdrvphHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493786691 448 EPLNYIDVISRIQ----IEEIIKEAKPTLIFVEHDKRFVEDIANKI 489
Cdd:PRK13652 163 EPTAGLDPQGVKElidfLNDLPETYGMTVIFSTHQLDLVPEMADYI 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-467 |
3.60e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 39.77 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTfSYYGYVKPIfENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLN-QETYQGKIS-KDVEFIKFPPNISdtSKLG 81
Cdd:PRK09700 6 ISMAGIG-KSFGPVHAL-KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGiHEPTKGTITiNNINYNKLDHKLA--AQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 82 ID-LYKELISDDEewklfrelnlLNVDENLV----------------YREFKtlskgEQTKILLAILFTKEDgfllidep 144
Cdd:PRK09700 82 IGiIYQELSVIDE----------LTVLENLYigrhltkkvcgvniidWREMR-----VRAAMMLLRVGLKVD-------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 145 tnhldmngrkilseyLKSKKGFLLISHdRNFLDgcINHVISINRNSIDVQSGnfTSWYENKLMKDKFEISKneKLRKDIK 224
Cdd:PRK09700 139 ---------------LDEKVANLSISH-KQMLE--IAKTLMLDAKVIIMDEP--TSSLTNKEVDYLFLIMN--QLRKEGT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 225 -------RLKEAARqskiWSDKIENTKNGVKV-SGIKPDkgrIGHQSAKMMKKSKNLEHRQNKAIEEKQSLLKDieikes 296
Cdd:PRK09700 197 aivyishKLAEIRR----ICDRYTVMKDGSSVcSGMVSD---VSNDDIVRLMVGRELQNRFNAMKENVSNLAHE------ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 297 lllhplhhhknPLISVSELSAHygERQILSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEIKL-------- 368
Cdd:PRK09700 264 -----------TVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLngkdispr 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 369 ----ASNLKISYIPQDT------SNLSGSLNEYIHSQDVDETL--------CKTILRKLDFARELF-------EMDMIDY 423
Cdd:PRK09700 331 spldAVKKGMAYITESRrdngffPNFSIAQNMAISRSLKDGGYkgamglfhEVDEQRTAENQRELLalkchsvNQNITEL 410
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 493786691 424 SDGQKKKVLIALSLSKPAHLFIWDEPLNYIDVISRIQIEEIIKE 467
Cdd:PRK09700 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQ 454
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-88 |
3.76e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.11 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 3 AIKIQNLTFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLN-QETYQGKISKDVefikfppniSDTSKLG 81
Cdd:PLN03130 1237 SIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRiVELERGRILIDG---------CDISKFG 1307
|
....*...
gi 493786691 82 I-DLYKEL 88
Cdd:PLN03130 1308 LmDLRKVL 1315
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-172 |
3.84e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 39.26 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 18 KPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQ-ETYQGKISKDVEFIKFP------------------------- 71
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSKIKVDGKVLYFGkdifqidaiklrkevgmvfqqpnpf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 72 PNISDTSKLGIDLYKELISDDEEWK-----LFRELNLLNVDENLVYREFKTLSKGEQTKILLAILFTKEDGFLLIDEPTN 146
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKkiveeCLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190
....*....|....*....|....*....|
gi 493786691 147 HLDMNG----RKILSEyLKSKKGFLLISHD 172
Cdd:PRK14246 183 MIDIVNsqaiEKLITE-LKNEIAIVIVSHN 211
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
99-194 |
3.84e-03 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 39.18 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 99 RELNLLNVDENLVYREFKTLSKGEQTKILLAILFTKEDGFLLIDEPTNHLD--MNGR--KILSEYLKSKKGFLLISHDRN 174
Cdd:PRK10619 134 KYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpeLVGEvlRIMQQLAEEGKTMVVVTHEMG 213
|
90 100
....*....|....*....|
gi 493786691 175 FLDGCINHVISINRNSIDVQ 194
Cdd:PRK10619 214 FARHVSSHVIFLHQGKIEEE 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-171 |
4.01e-03 |
|
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: 38.75 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 21 FENVSFSFDTNW--------------KTGLIGRNGIGKSTLFKLLLN-QETYQGKI------SKDVEFIKFPPNI----- 74
Cdd:cd03254 5 FENVNFSYDEKKpvlkdinfsikpgeTVAIVGPTGAGKTTLINLLMRfYDPQKGQIlidgidIRDISRKSLRSMIgvvlq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 75 -----SDTSKLGIDLYKELISDDEEWKLFRELNLLNVDENL-------VYREFKTLSKGEQTKILLAILFTKEDGFLLID 142
Cdd:cd03254 85 dtflfSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLpngydtvLGENGGNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190
....*....|....*....|....*....|..
gi 493786691 143 EPTNHLDMNGRKILSEYLKS---KKGFLLISH 171
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKlmkGRTSIIIAH 196
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
325-366 |
4.50e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.33 E-value: 4.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 493786691 325 LSNLSFEIEQGDIVAISGRNGSGKSTLIKILLGINHEYTGEI 366
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI 55
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-61 |
4.75e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 39.01 E-value: 4.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493786691 4 IKIQNLTFSYYGYVKPI--FENVSFSFDTNWKTGLIGRNGIGKSTLFKL--LLNQETyQGKI 61
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCinLLERPT-SGRV 62
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-51 |
5.36e-03 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 38.48 E-value: 5.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 493786691 1 MSAIKIQNLTFSYYGyVKPIfENVSFSFDTNWKTGLIGRNGIGKSTLFKLL 51
Cdd:COG0411 2 DPLLEVRGLTKRFGG-LVAV-DDVSLEVERGEIVGLIGPNGAGKTTLFNLI 50
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-172 |
6.21e-03 |
|
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: 38.47 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGYVkpiFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLN-QETYQGKISKDVEFI-KFPP--------- 72
Cdd:cd03299 1 LKVENLSKDWKEFK---LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGfIKPDSGKILLNGKDItNLPPekrdisyvp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 73 ---------NISDTSKLGIDLYKELISDDEEwKLFRELNLLNVDEnLVYREFKTLSKGEQTKILLAILFTKEDGFLLIDE 143
Cdd:cd03299 78 qnyalfphmTVYKNIAYGLKKRKVDKKEIER-KVLEIAEMLGIDH-LLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190
....*....|....*....|....*....|....
gi 493786691 144 PTNHLDMNGRKILSEYLK-----SKKGFLLISHD 172
Cdd:cd03299 156 PFSALDVRTKEKLREELKkirkeFGVTVLHVTHD 189
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
10-61 |
6.67e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 38.93 E-value: 6.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 493786691 10 TFSYYGYVKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQ-ETYQGKI 61
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHfDVSEGDI 372
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-144 |
6.91e-03 |
|
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: 38.29 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGyvKPIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLL--LNQETyQGKISKDVEFI-KFPpnISDTSKL 80
Cdd:cd03218 1 LRAENLSKRYGK--RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIvgLVKPD-SGKILLDGQDItKLP--MHKRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 81 GI-------DLYKEL-----IS--------DDEEWK-----LFRELNLLNVDENLVYrefkTLSKGEQTKILLAILFTKE 135
Cdd:cd03218 76 GIgylpqeaSIFRKLtveenILavleirglSKKEREekleeLLEEFHITHLRKSKAS----SLSGGERRRVEIARALATN 151
|
....*....
gi 493786691 136 DGFLLIDEP 144
Cdd:cd03218 152 PKFLLLDEP 160
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-182 |
7.24e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.84 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGyvKPIFENVSFSFDT--NWKtgLIGRNGIGKSTLFKLLL--------NQETYQGK----------ISK 63
Cdd:PRK10938 261 IVLNNGVVSYND--RPILHNLSWQVNPgeHWQ--IVGPNGAGKSTLLSLITgdhpqgysNDLTLFGRrrgsgetiwdIKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 64 DVEFIkfppnisdTSKLGID--------------------LYKElISDDEEWKLFRELNLLNVDENLVYREFKTLSKGEQ 123
Cdd:PRK10938 337 HIGYV--------SSSLHLDyrvstsvrnvilsgffdsigIYQA-VSDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQ 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493786691 124 TKILLAILFTKEDGFLLIDEPTNHLDMNGRKILSEYL-----KSKKGFLLISHDRNFLDGCINH 182
Cdd:PRK10938 408 RLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVdvlisEGETQLLFVSHHAEDAPACITH 471
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-52 |
9.41e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.86 E-value: 9.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGYVK-PIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLL 52
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLM 1215
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-172 |
9.78e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 38.15 E-value: 9.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 4 IKIQNLTFSYYGYVK-PIFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQ-ETYQGKISKDVEFIKFPPNISDTSKLG 81
Cdd:PRK13642 5 LEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLfEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493786691 82 I-------DLYKELISDD-----EEWKLFRELNLLNVDENLV--------YREFKTLSKGEQTKILLAILFTKEDGFLLI 141
Cdd:PRK13642 85 MvfqnpdnQFVGATVEDDvafgmENQGIPREEMIKRVDEALLavnmldfkTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 493786691 142 DEPTNHLDMNGRKILSEYLKSKKG-----FLLISHD 172
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEkyqltVLSITHD 200
|
|
| |
