|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-490 |
2.56e-94 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 295.44 E-value: 2.56e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 6 LKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVE--TNLKFNYFP----------- 71
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEpDSGEVSipKGLRIGYLPqeppldddltv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 72 ----------------------AKITEPQDSVrMVLMKITGR-DYSDFWEVERELDQI----GLAEEILEQTYASLSPGQ 124
Cdd:COG0488 79 ldtvldgdaelraleaeleeleAKLAEPDEDL-ERLAELQEEfEALGGWEAEARAEEIlsglGFPEEDLDRPVSELSGGW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 125 QTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYLKQKQG-YIVVSHDRYFLNQVIDHVISIDRAQISSFKGNYETW 203
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGtVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 204 AAERANADEREISLNATMKKDIKKLeqatrqkQEWSRateRKKAGApdkgfvgHKAAKVMSKalniRDRAEK-KLTDKKQ 282
Cdd:COG0488 238 LEQRAERLEQEAAAYAKQQKKIAKE-------EEFIR---RFRAKA-------RKAKQAQSR----IKALEKlEREEPPR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 283 LLKNIEIQdelqLNYQPYLGPQnnaLLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNELIA 362
Cdd:COG0488 297 RDKTVEIR----FPPPERLGKK---VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDS 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 363 kGNLKIRENLRISYLPQDFDQLQG------TLEQFAaeKEVEVQDLLAMLRKLGFERTMFDYRIEQMSMGQKRKVALARS 436
Cdd:COG0488 370 -GTVKLGETVKIGYFDQHQEELDPdktvldELRDGA--PGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKL 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 488922799 437 LCEEANLYIWDEPLNYLDVITREQIQNLVLKFKPTLLVVEHDREFVQKIATQTV 490
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRIL 500
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-487 |
3.91e-44 |
|
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: 163.18 E-value: 3.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNQiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQN-QVEYEGKV--ETNLKFNYFP-------- 71
Cdd:TIGR03719 4 IYTMNRVSKVVPPK-KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvDKDFNGEArpQPGIKVGYLPqepqldpt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 72 -------------------------AKITEPQDSVRmVLMKITGR-----DYSDFWEVERELDQiglAEEIL-----EQT 116
Cdd:TIGR03719 83 ktvrenveegvaeikdaldrfneisAKYAEPDADFD-KLAAEQAElqeiiDAADAWDLDSQLEI---AMDALrcppwDAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 117 YASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYLKQKQGYIV-VSHDRYFLNQVIDHVISIDRAQISS 195
Cdd:TIGR03719 159 VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVaVTHDRYFLDNVAGWILELDRGRGIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 196 FKGNYETWaaeranadereislnatmkkdikkLEQ-ATRQKQEWSRATERKKAGAPDKGFV--GHKAAKVMSKAlniRDR 272
Cdd:TIGR03719 239 WEGNYSSW------------------------LEQkQKRLEQEEKEESARQKTLKRELEWVrqSPKGRQAKSKA---RLA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 273 AEKKLTDKKQLLKNIEiqDELQLNYQPYLGpqnNALLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIK 352
Cdd:TIGR03719 292 RYEELLSQEFQKRNET--AEIYIPPGPRLG---DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 353 AMLGQnELIAKGNLKIRENLRISYLPQDFDQLQGTleqfaaeKEV--EVQDLLAMLRKLGFERTMFDY------------ 418
Cdd:TIGR03719 367 MITGQ-EQPDSGTIEIGETVKLAYVDQSRDALDPN-------KTVweEISGGLDIIKLGKREIPSRAYvgrfnfkgsdqq 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 419 -RIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKPTLLVVEHDREFVQKIAT 487
Cdd:TIGR03719 439 kKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIAT 508
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-493 |
1.32e-43 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 161.21 E-value: 1.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 18 KPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKV--ETNLKFnyfpAKITEPQ---DSVRMVLMKITGr 91
Cdd:PRK15064 14 KPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEpSAGNVslDPNERL----GKLRQDQfafEEFTVLDTVIMG- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 92 dYSDFWEVERELDQI-GLAE-----------------------------EIL-------EQTYASLS---PGQQTKALLA 131
Cdd:PRK15064 89 -HTELWEVKQERDRIyALPEmseedgmkvadlevkfaemdgytaearagELLlgvgipeEQHYGLMSevaPGWKLRVLLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 132 -AMFADQNSFqLIDEPTNHLDAAGRDLLAKYLKQKQG-YIVVSHDRYFLNQVIDHVISIDRAQISSFKGNYETWAAERAN 209
Cdd:PRK15064 168 qALFSNPDIL-LLDEPTNNLDINTIRWLEDVLNERNStMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAATQ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 210 ADEREISLNATMKKDIKKLEQ--------ATRQKQEWSRATERKKAGAPDKgfvghKAAKVMSKAlnIRDRAEKKLtdkk 281
Cdd:PRK15064 247 ARERLLADNAKKKAQIAELQSfvsrfsanASKAKQATSRAKQIDKIKLEEV-----KPSSRQNPF--IRFEQDKKL---- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 282 qllknieiqdelqlnyqpylgpQNNALlEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNELI 361
Cdd:PRK15064 316 ----------------------HRNAL-EVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 362 AkGNLKIRENLRISYLPQD----FDQ---LQGTLEQFAAEKEVEvQDLLAMLRKLGFERTMFDYRIEQMSMGQKRKVALA 434
Cdd:PRK15064 373 S-GTVKWSENANIGYYAQDhaydFENdltLFDWMSQWRQEGDDE-QAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFG 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 488922799 435 RSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKPTLLVVEHDREFVQKIATQTVNLK 493
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEIT 509
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-190 |
3.29e-41 |
|
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: 144.51 E-value: 3.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQ-VEYEGKVET--NLKFNYFPakitepqds 80
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGElEPDEGIVTWgsTVKIGYFE--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 81 vrmvlmkitgrdysdfwevereldqiglaeeileQtyasLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAK 160
Cdd:cd03221 70 ----------------------------------Q----LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|.
gi 488922799 161 YLKQKQG-YIVVSHDRYFLNQVIDHVISIDR 190
Cdd:cd03221 112 ALKEYPGtVILVSHDRYFLDQVATKIIELED 142
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-487 |
4.06e-40 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 153.18 E-value: 4.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 1 MGIIQLKNVSFSYDNQikPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEY-EGKV--ETNLK----------- 66
Cdd:PRK11147 1 MSLISIHGAWLSFSDA--PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLdDGRIiyEQDLIvarlqqdpprn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 67 -----FNYFPAKI------------------TEPQDSVRMVLMKITGR-DYSDFWEVERE----LDQIGL-AEEILeqty 117
Cdd:PRK11147 79 vegtvYDFVAEGIeeqaeylkryhdishlveTDPSEKNLNELAKLQEQlDHHNLWQLENRinevLAQLGLdPDAAL---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 118 ASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYLKQKQGYIV-VSHDRYFLNQVIDHVISIDRAQISSF 196
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIfISHDRSFIRNMATRIVDLDRGKLVSY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 197 KGNYETWAAERANADEREISLNATMKKdikKLEQatrqKQEWSRAterkkagapdkgfvGHKAAKVMSKAlniRDRAEKK 276
Cdd:PRK11147 235 PGNYDQYLLEKEEALRVEELQNAEFDR---KLAQ----EEVWIRQ--------------GIKARRTRNEG---RVRALKA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 277 LTDKKQLLKNIEIQDELQLNYQPYLGpqnNALLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLG 356
Cdd:PRK11147 291 LRRERSERREVMGTAKMQVEEASRSG---KIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 357 QNELIAkGNLKIRENLRISYlpqdFDQ------LQGTLEQFAAE--KEVEV----QDLLAMLRKLGF--ERTMFDYRieQ 422
Cdd:PRK11147 368 QLQADS-GRIHCGTKLEVAY----FDQhraeldPEKTVMDNLAEgkQEVMVngrpRHVLGYLQDFLFhpKRAMTPVK--A 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488922799 423 MSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKPTLLVVEHDREFVQKIAT 487
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVT 505
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
309-494 |
3.43e-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: 136.42 E-value: 3.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 309 LEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNELIaKGNLKIRENLRISYLPQdfdqlqgtl 388
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPD-EGIVTWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 389 eqfaaekevevqdllamlrklgfertmfdyrieqMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKF 468
Cdd:cd03221 71 ----------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEY 116
|
170 180
....*....|....*....|....*.
gi 488922799 469 KPTLLVVEHDREFVQKIATQTVNLKK 494
Cdd:cd03221 117 PGTVILVSHDRYFLDQVATKIIELED 142
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-487 |
2.78e-33 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 132.55 E-value: 2.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNQiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQN-QVEYEGKV--ETNLKFNYFPakiTEPQ- 78
Cdd:PRK11819 6 IYTMNRVSKVVPPK-KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvDKEFEGEArpAPGIKVGYLP---QEPQl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 79 ---DSVRMV-------------------------------LMKITGR-----DYSDFWEVERELDQiglAEEIL-----E 114
Cdd:PRK11819 82 dpeKTVRENveegvaevkaaldrfneiyaayaepdadfdaLAAEQGElqeiiDAADAWDLDSQLEI---AMDALrcppwD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 115 QTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYLKQKQGYIV-VSHDRYFLNQVIDHVISIDRAQI 193
Cdd:PRK11819 159 AKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVaVTHDRYFLDNVAGWILELDRGRG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 194 SSFKGNYETWaaeranadereislnatmkkdikkLEQ-ATRQKQEWSRATERKKAGAPDKGFV--GHKAAKVMSKAlniR 270
Cdd:PRK11819 239 IPWEGNYSSW------------------------LEQkAKRLAQEEKQEAARQKALKRELEWVrqSPKARQAKSKA---R 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 271 DRAEKKLTDKKQLLKNieiqDELQLNYQPylGPQ-NNALLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKST 349
Cdd:PRK11819 292 LARYEELLSEEYQKRN----ETNEIFIPP--GPRlGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKST 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 350 LIKAMLGQnELIAKGNLKIRENLRISYLPQDFDQLQGtleqfaaEKEV--EVQDLLAMLrKLGfERTM--------FDY- 418
Cdd:PRK11819 366 LFKMITGQ-EQPDSGTIKIGETVKLAYVDQSRDALDP-------NKTVweEISGGLDII-KVG-NREIpsrayvgrFNFk 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488922799 419 ------RIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKPTLLVVEHDREFVQKIAT 487
Cdd:PRK11819 436 ggdqqkKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIAT 510
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-205 |
4.46e-33 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 131.73 E-value: 4.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVE--TNLKFNYFPAKITE--P 77
Cdd:COG0488 315 VLELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEpDSGTVKlgETVKIGYFDQHQEEldP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 78 QDSVRMVLmkitgrdySDFWEVERELDQIGLAEEIL---EQTY---ASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLD 151
Cdd:COG0488 393 DKTVLDEL--------RDGAPGGTEQEVRGYLGRFLfsgDDAFkpvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488922799 152 AAGRDLLAKYLKQKQG-YIVVSHDRYFLNQVIDHVISIDRAQISSFKGNYETWAA 205
Cdd:COG0488 465 IETLEALEEALDDFPGtVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-486 |
3.28e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 123.09 E-value: 3.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEYEGKVETNLKF---NYFPAKITEPQD 79
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLdgrDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 80 SVRMVL-------------------MKITGRDYSDFWE-VERELDQIGLaEEILEQTYASLSPGQQTKALLAAMFADQNS 139
Cdd:COG1123 84 RIGMVFqdpmtqlnpvtvgdqiaeaLENLGLSRAEARArVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 140 FQLIDEPTNHLDAAGR----DLLAKyLKQKQGY--IVVSHDRYFLNQVIDHVISIDRAQIssfkgnyetwaAERANADEr 213
Cdd:COG1123 163 LLIADEPTTALDVTTQaeilDLLRE-LQRERGTtvLLITHDLGVVAEIADRVVVMDDGRI-----------VEDGPPEE- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 214 eislnatMKKDIKKLEQATRQKQEWSRATERKKAGAPdkgfvghkaakvmskALNIRDraekkltdkkqllknieiqdeL 293
Cdd:COG1123 230 -------ILAAPQALAAVPRLGAARGRAAPAAAAAEP---------------LLEVRN---------------------L 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 294 QLNYQPYLGPQNNALleadslvlqragkllnQPLNLELKKNERMVIQGENGSGKSTLIKAMLG-----------QNELIA 362
Cdd:COG1123 267 SKRYPVRGKGGVRAV----------------DDVSLTLRRGETLGLVGESGSGKSTLARLLLGllrptsgsilfDGKDLT 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 363 KGNLKIRENLR--ISYLPQD-----------FDQLQGTLEQFAAEKEVEVQDLLA-MLRKLGFERTMFDYRIEQMSMGQK 428
Cdd:COG1123 331 KLSRRSLRELRrrVQMVFQDpysslnprmtvGDIIAEPLRLHGLLSRAERRERVAeLLERVGLPPDLADRYPHELSGGQR 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488922799 429 RKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVL----KFKPTLLVVEHDREFVQKIA 486
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlqrELGLTYLFISHDLAVVRYIA 472
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
305-494 |
4.86e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.80 E-value: 4.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 305 NNALLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNELiAKGNLKI------RENLRISYLP 378
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP-TSGTVRLfgkpprRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 379 Q--DFDqlqgtlEQFAaekeVEVQDLLAM--LRKLGF----------------ERT-MFDY---RIEQMSMGQKRKVALA 434
Cdd:COG1121 82 QraEVD------WDFP----ITVRDVVLMgrYGRRGLfrrpsradreavdealERVgLEDLadrPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488922799 435 RSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKP---TLLVVEHDREFVQKIATQTVNLKK 494
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNR 214
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-483 |
1.92e-28 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 119.12 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 17 IKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEYEGKVETnLKFNYFPAKITE--PQDSVRMVLMKITGRdyS 94
Cdd:PRK10636 13 VRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYT-FPGNWQLAWVNQetPALPQPALEYVIDGD--R 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 95 DFWEVERELDQ-----------------------------------IGLAEEILEQTYASLSPGQQTKALLAAMFADQNS 139
Cdd:PRK10636 90 EYRQLEAQLHDanerndghaiatihgkldaidawtirsraasllhgLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 140 FQLIDEPTNHLDAAGRDLLAKYLKQKQG-YIVVSHDRYFLNQVIDHVISIDRAQISSFKGNYETWAAERANADEREISLN 218
Cdd:PRK10636 170 LLLLDEPTNHLDLDAVIWLEKWLKSYQGtLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQQQAMY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 219 ATMKKDIKKLE--------QATRQKQEWSRAterkkagapdkgfvghkaakvmskalnirdraekKLTDKKQLLKNIEIQ 290
Cdd:PRK10636 250 ESQQERVAHLQsyidrfraKATKAKQAQSRI----------------------------------KMLERMELIAPAHVD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 291 DELQLNYQpylGPQN--NALLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNELIaKGNLKI 368
Cdd:PRK10636 296 NPFHFSFR---APESlpNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPV-SGEIGL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 369 RENLRISYLPQDfdQLQ------GTLEQFA--AEKEVEvQDLLAMLRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEE 440
Cdd:PRK10636 372 AKGIKLGYFAQH--QLEflradeSPLQHLArlAPQELE-QKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQR 448
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 488922799 441 ANLYIWDEPLNYLDVITREQIQNLVLKFKPTLLVVEHDREFVQ 483
Cdd:PRK10636 449 PNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLR 491
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
311-492 |
1.99e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 115.16 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 311 ADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNELIAkGNLKIRENLRISYLPQDFDQ------- 383
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDS-GEVSIPKGLRIGYLPQEPPLdddltvl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 384 ---LQGTLEQFAAEKEV------------------EVQDLLA-------------MLRKLGFERTMFDYRIEQMSMGQKR 429
Cdd:COG0488 80 dtvLDGDAELRALEAELeeleaklaepdedlerlaELQEEFEalggweaearaeeILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488922799 430 KVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKPTLLVVEHDREFVQKIATQTVNL 492
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILEL 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
327-494 |
4.10e-25 |
|
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: 102.61 E-value: 4.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNELiAKGNLKI------RENLRISYLPQ--DFDQ-------------LQ 385
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP-TSGSIRVfgkpleKERKRIGYVPQrrSIDRdfpisvrdvvlmgLY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 386 GTLEQFAAEKEVEVQDLLAMLRKLGfertMFDY---RIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQ 462
Cdd:cd03235 97 GHKGLFRRLSKADKAKVDEALERVG----LSELadrQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIY 172
|
170 180 190
....*....|....*....|....*....|....*
gi 488922799 463 NLVLKFKP---TLLVVEHDREFVQKIATQTVNLKK 494
Cdd:cd03235 173 ELLRELRRegmTILVVTHDLGLVLEYFDRVLLLNR 207
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
310-486 |
6.08e-25 |
|
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: 100.40 E-value: 6.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 310 EADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNElIAKGNLKIREnlrisylpqdfdqlqgtle 389
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-PTSGEILIDG------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 390 qfaaeKEVEVQDLLAMLRKLGFertmfdyrIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKF- 468
Cdd:cd00267 61 -----KDIAKLPLEELRRRIGY--------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELa 127
|
170 180
....*....|....*....|
gi 488922799 469 --KPTLLVVEHDREFVQKIA 486
Cdd:cd00267 128 eeGRTVIIVTHDPELAELAA 147
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
325-451 |
1.38e-24 |
|
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: 99.26 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIKAMLGQ-----------NELIAKGNLKIReNLRISYLPQDfDQLQGTL----- 388
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLlsptegtilldGQDLTDDERKSL-RKEIGYVFQD-PQLFPRLtvren 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488922799 389 --------EQFAAEKEVEVQDLLAMLRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLN 451
Cdd:pfam00005 80 lrlglllkGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
309-492 |
1.44e-24 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 101.05 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 309 LEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGqneLI--AKGNLKIRENL-----------RIS 375
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALAD---LDppTSGEIYLDGKPlsampppewrrQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 376 YLPQDFDQLQGTLEQF------AAEKEVEVQDLLAMLRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEP 449
Cdd:COG4619 78 YVPQEPALWGGTVRDNlpfpfqLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488922799 450 LNYLDVITREQIQNLVLKFKP----TLLVVEHDREFVQKIATQTVNL 492
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAeegrAVLWVSHDPEQIERVADRVLTL 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
327-494 |
1.69e-24 |
|
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: 101.00 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLG-----------QNELIAKGNLKIReNLRISYLPQDFD-QLQGT------- 387
Cdd:cd03225 20 ISLTIKKGEFVLIVGPNGSGKSTLLRLLNGllgptsgevlvDGKDLTKLSLKEL-RRKVGLVFQNPDdQFFGPtveeeva 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 388 --LEQFAAEKEVEVQDLLAMLRKLGFErTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLV 465
Cdd:cd03225 99 fgLENLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELL 177
|
170 180 190
....*....|....*....|....*....|..
gi 488922799 466 LKFK---PTLLVVEHDREFVQKIATQTVNLKK 494
Cdd:cd03225 178 KKLKaegKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
325-486 |
2.13e-24 |
|
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: 101.04 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIKAMLG-----------QNELIAKGNLKIRENLR--ISYLPQD----------- 380
Cdd:cd03257 22 DDVSFSIKKGETLGLVGESGSGKSTLARAILGllkptsgsiifDGKDLLKLSRRLRKIRRkeIQMVFQDpmsslnprmti 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 381 FDQL------QGTLEQFAAEKEVevqdLLAMLRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLD 454
Cdd:cd03257 102 GEQIaeplriHGKLSKKEARKEA----VLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALD 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 488922799 455 VITREQIQNLVLK----FKPTLLVVEHDREFVQKIA 486
Cdd:cd03257 178 VSVQAQILDLLKKlqeeLGLTLLFITHDLGVVAKIA 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-215 |
4.12e-23 |
|
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: 98.01 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQN---------QVEYEGKVETNLKF------- 67
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGllkpdsgsiLIDGEDVRKEPREArrqigvl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 68 ---NYFPAKITePQDSVRMV--LMKITGRDYSDfwEVERELDQIGLaEEILEQTYASLSPGQQTKALLAAMFADQNSFQL 142
Cdd:COG4555 80 pdeRGLYDRLT-VRENIRYFaeLYGLFDEELKK--RIEELIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488922799 143 IDEPTNHLDAAGRDLLAKYLKQ--KQGYIVV--SHDRYFLNQVIDHVISIDRAQIsSFKGNYETWAAERANADEREI 215
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRAlkKEGKTVLfsSHIMQEVEALCDRVVILHKGKV-VAQGSLDELREEIGEENLEDA 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
327-494 |
6.66e-23 |
|
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: 95.16 E-value: 6.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQ-----------NELIAKGNLKIREnlRISYLPQD---FDQLQGtleqfa 392
Cdd:cd03230 19 ISLTVEKGEIYGLLGPNGAGKTTLIKIILGLlkpdsgeikvlGKDIKKEPEEVKR--RIGYLPEEpslYENLTV------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 393 aekevevqdllamlrklgfeRTMFDYrieqmSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFK--- 469
Cdd:cd03230 91 --------------------RENLKL-----SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKkeg 145
|
170 180
....*....|....*....|....*
gi 488922799 470 PTLLVVEHDREFVQKIATQTVNLKK 494
Cdd:cd03230 146 KTILLSSHILEEAERLCDRVAILNN 170
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
325-494 |
3.41e-22 |
|
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: 95.31 E-value: 3.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIKAMLG-----------QNELIAKGNLKIREnlRISYLPQDFD----------- 382
Cdd:COG4555 18 KDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGllkpdsgsiliDGEDVRKEPREARR--QIGVLPDERGlydrltvreni 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 383 QLQGTL-EQFAAEKEVEVQDLlamLRKLGFERTMfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQI 461
Cdd:COG4555 96 RYFAELyGLFDEELKKRIEEL---IELLGLEEFL-DRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLL 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 488922799 462 QNLVLKFKP---TLLVVEHDREFVQKIATQTVNLKK 494
Cdd:COG4555 172 REILRALKKegkTVLFSSHIMQEVEALCDRVVILHK 207
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-192 |
4.96e-22 |
|
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: 94.07 E-value: 4.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 5 QLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLKFNYFPAKI-TE 76
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLngllgptSGEVLVDGKDLTKLSLKELRRKVgLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 77 PQDSVRMVLMKIT-----------GRDYSDFWE-VERELDQIGLaEEILEQTYASLSPGQQTKALLAAMFADQNSFQLID 144
Cdd:cd03225 81 FQNPDDQFFGPTVeeevafglenlGLPEEEIEErVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488922799 145 EPTNHLDAAGRDLLAKYLK--QKQGY--IVVSHDRYFLNQVIDHVISIDRAQ 192
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKklKAEGKtiIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
307-465 |
9.04e-22 |
|
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: 93.31 E-value: 9.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 307 ALLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLG-----------QNELIAKGNLKIREnlRIS 375
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGllppsagevlwNGEPIRDAREDYRR--RLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 376 YLPQD---FDQLqgTLE---QFAAE---KEVEVQDLLAMLRKLGFERTMfDYRIEQMSMGQKRKVALARSLCEEANLYIW 446
Cdd:COG4133 79 YLGHAdglKPEL--TVRenlRFWAAlygLRADREAIDEALEAVGLAGLA-DLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170
....*....|....*....
gi 488922799 447 DEPLNYLDVITREQIQNLV 465
Cdd:COG4133 156 DEPFTALDAAGVALLAELI 174
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-190 |
1.81e-21 |
|
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: 92.60 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 5 QLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVE--------TNLKFNYFPAKIT 75
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKpTSGSIRvfgkplekERKRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 76 EPQD---SVR-MVLMKITGR-------DYSDFWEVERELDQIGLaEEILEQTYASLSPGQQTKALLAAMFADQNSFQLID 144
Cdd:cd03235 79 IDRDfpiSVRdVVLMGLYGHkglfrrlSKADKAKVDEALERVGL-SELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488922799 145 EPTNHLDAAGR----DLLAKYLKQKQGYIVVSHDryfLNQV---IDHVISIDR 190
Cdd:cd03235 158 EPFAGVDPKTQediyELLRELRREGMTILVVTHD---LGLVleyFDRVLLLNR 207
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-191 |
2.24e-21 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 92.16 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLKFNYFpAKIT- 75
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILagllppsAGEVLWNGEPIRDAREDYR-RRLAy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 76 -EPQDSVRMVLmkiTGRDYSDFW-----------EVERELDQIGLAEeILEQTYASLSPGQQTKALLAAMFADQNSFQLI 143
Cdd:COG4133 80 lGHADGLKPEL---TVRENLRFWaalyglradreAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488922799 144 DEPTNHLDAAGRDLLAKYLKQ--KQGYIVV--SHDRYFLNQviDHVISIDRA 191
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAhlARGGAVLltTHQPLELAA--ARVLDLGDF 205
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
308-478 |
2.84e-21 |
|
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: 92.80 E-value: 2.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 308 LLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNELiAKG----------NLKIREnL--RIS 375
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKP-SSGevlldgrdlaSLSRRE-LarRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 376 YLPQDFDQL----------------QGTLEQFAAEKEVEVQDLLAMLRKLGF-ERtmfdyRIEQMSMGQKRKVALARSLC 438
Cdd:COG1120 79 YVPQEPPAPfgltvrelvalgryphLGLFGRPSAEDREAVEEALERTGLEHLaDR-----PVDELSGGERQRVLIARALA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488922799 439 EEANLYIWDEPLNYLD----VITREQIQNLVLKFKPTLLVVEHD 478
Cdd:COG1120 154 QEPPLLLLDEPTSHLDlahqLEVLELLRRLARERGRTVVMVLHD 197
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-192 |
3.22e-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: 90.00 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 5 QLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVEtnlkfnyfpakitepqdsvrm 83
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEIL--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 84 vlmkITGRDYSDfWEVERELDQIGlaeeILEQtyasLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYLK 163
Cdd:cd00267 58 ----IDGKDIAK-LPLEELRRRIG----YVPQ----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
|
170 180 190
....*....|....*....|....*....|...
gi 488922799 164 Q--KQG--YIVVSHDRYFLNQVIDHVISIDRAQ 192
Cdd:cd00267 125 ElaEEGrtVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-186 |
1.21e-20 |
|
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: 91.26 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNqiKPVFDQVALEIDA-SWkLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLKFN------ 68
Cdd:COG1120 1 MLEAENLSVGYGG--RPVLDDVSLSLPPgEV-TALLGPNGSGKSTLLRALagllkpsSGEVLLDGRDLASLSRRelarri 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 69 -YFPAKITEPQD-SVR-MVLMkitGR-DYSDFWE---------VERELDQIGLaEEILEQTYASLSPGQQTKALLAAMFA 135
Cdd:COG1120 78 aYVPQEPPAPFGlTVReLVAL---GRyPHLGLFGrpsaedreaVEEALERTGL-EHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 136 DQNSFQLIDEPTNHLDAAGR----DLLAKyLKQKQGY--IVVSHDryfLNQVI---DHVI 186
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQlevlELLRR-LARERGRtvVMVLHD---LNLAAryaDRLV 209
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-482 |
1.21e-20 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 95.31 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 35 GLIGRNGRGKTTLMK---------------ILQNQVEYEGKVETNLK--FNYFPAKITEPQDSVRMVLMK-------ITG 90
Cdd:PLN03073 207 GLVGRNGTGKTTFLRymamhaidgipkncqILHVEQEVVGDDTTALQcvLNTDIERTQLLEEEAQLVAQQrelefetETG 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 91 RDYSD-------------FWEVERELDQIGL--AEEILEQTYASLS--PGQQTK-------------ALLAAMFAdQNSF 140
Cdd:PLN03073 287 KGKGAnkdgvdkdavsqrLEEIYKRLELIDAytAEARAASILAGLSftPEMQVKatktfsggwrmriALARALFI-EPDL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 141 QLIDEPTNHLDAAGRDLLAKYL-KQKQGYIVVSHDRYFLNQVIDHVISIDRAQISSFKGNYETWAAERanaDEReislna 219
Cdd:PLN03073 366 LLLDEPTNHLDLHAVLWLETYLlKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFERTR---EEQ------ 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 220 tMKKDIKKLEQATRQKQEWSRATERKKAGApdkgfvgHKAAKVMSkalniRDRAEKKLTDKKQLLKNIEIQDELQlnyQP 299
Cdd:PLN03073 437 -LKNQQKAFESNERSRSHMQAFIDKFRYNA-------KRASLVQS-----RIKALDRLGHVDAVVNDPDYKFEFP---TP 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 300 YLGPQNNALLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNELIAkGNLKIRENLRISYLPQ 379
Cdd:PLN03073 501 DDRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSS-GTVFRSAKVRMAVFSQ 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 380 ---DFDQLQGT--LEQFAAEKEVEVQDLLAMLRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLD 454
Cdd:PLN03073 580 hhvDGLDLSSNplLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
490 500
....*....|....*....|....*....
gi 488922799 455 VITREQ-IQNLVLkFKPTLLVVEHDREFV 482
Cdd:PLN03073 660 LDAVEAlIQGLVL-FQGGVLMVSHDEHLI 687
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-478 |
8.80e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 92.56 E-value: 8.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 34 LGLIGRNGRGKTTLMKILQNQV-----EYEGKVE----------TNLkFNYFpAKITE--------PQ----------DS 80
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELipnlgDYEEEPSwdevlkrfrgTEL-QNYF-KKLYNgeikvvhkPQyvdlipkvfkGK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 81 VRMVLMKITGRDYSDfwEVereLDQIGLaEEILEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAK 160
Cdd:PRK13409 180 VRELLKKVDERGKLD--EV---VERLGL-ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVAR 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 161 YLK---QKQGYIVVSHDRYFLNQVID--HVISIDRAQ---ISSFKGNyetwaaeranaderEISLNATMKkdikkleqat 232
Cdd:PRK13409 254 LIRelaEGKYVLVVEHDLAVLDYLADnvHIAYGEPGAygvVSKPKGV--------------RVGINEYLK---------- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 233 rqkqewsraterkkagapdkGFVGHKAAKVMSKALNIRDRAEKKLTDKKQLLKNIEIQDELqlnyqpylgpqNNALLEAD 312
Cdd:PRK13409 310 --------------------GYLPEENMRIRPEPIEFEERPPRDESERETLVEYPDLTKKL-----------GDFSLEVE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 313 slvlqrAGkllnqplnlELKKNERMVIQGENGSGKSTLIKaMLGQNELIAKGnlKIRENLRISYLPQdfdqlqgtleQFA 392
Cdd:PRK13409 359 ------GG---------EIYEGEVIGIVGPNGIGKTTFAK-LLAGVLKPDEG--EVDPELKISYKPQ----------YIK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 393 AEKEVEVQDLLAM--------------LRKLGFERtMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVitr 458
Cdd:PRK13409 411 PDYDGTVEDLLRSitddlgssyykseiIKPLQLER-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--- 486
|
490 500
....*....|....*....|....*..
gi 488922799 459 EQ-------IQNLVLKFKPTLLVVEHD 478
Cdd:PRK13409 487 EQrlavakaIRRIAEEREATALVVDHD 513
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
325-494 |
1.41e-19 |
|
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: 91.50 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIKAMLG--------------QNELIAKGNLKIRENlRISYLPQDF--------- 381
Cdd:COG1123 23 DGVSLTIAPGETVALVGESGSGKSTLALALMGllphggrisgevllDGRDLLELSEALRGR-RIGMVFQDPmtqlnpvtv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 382 -DQLQGTLEQFAAEKEVEVQDLLAMLRKLGFERtMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQ 460
Cdd:COG1123 102 gDQIAEALENLGLSRAEARARVLELLEAVGLER-RLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAE 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 488922799 461 I----QNLVLKFKPTLLVVEHDREFVQKIATQTVNLKK 494
Cdd:COG1123 181 IldllRELQRERGTTVLLITHDLGVVAEIADRVVVMDD 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
325-490 |
1.44e-19 |
|
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: 87.39 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIKAMLG-----------QNELIAKGNLK-IREnlRISYLPQD-FDQLQGT---- 387
Cdd:COG1122 18 DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGllkptsgevlvDGKDITKKNLReLRR--KVGLVFQNpDDQLFAPtvee 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 388 -----LEQFA-AEKEVE--VQDLLAMLRKLGFErtmfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITRE 459
Cdd:COG1122 96 dvafgPENLGlPREEIRerVEEALELVGLEHLA----DRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRR 171
|
170 180 190
....*....|....*....|....*....|....
gi 488922799 460 QIQNLVLKFKP---TLLVVEHDREFVQKIATQTV 490
Cdd:COG1122 172 ELLELLKRLNKegkTVIIVTHDLDLVAELADRVI 205
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
329-492 |
1.87e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 91.55 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 329 LELKKNERMVIQGENGSGKSTLIKaMLGQNELIAKGNLKIRENLRISYLPQDFDQ-LQGTLEQFAAEKEVEVQDLL---- 403
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMK-ILNGEVLLDDGRIIYEQDLIVARLQQDPPRnVEGTVYDFVAEGIEEQAEYLkryh 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 404 AMLRKLGF---ERTM-----------------FDYRIEQ---------------MSMGQKRKVALARSLCEEANLYIWDE 448
Cdd:PRK11147 103 DISHLVETdpsEKNLnelaklqeqldhhnlwqLENRINEvlaqlgldpdaalssLSGGWLRKAALGRALVSNPDVLLLDE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488922799 449 PLNYLDVITREQIQNLVLKFKPTLLVVEHDREFVQKIATQTVNL 492
Cdd:PRK11147 183 PTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDL 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
309-487 |
2.76e-19 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 86.66 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 309 LEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQ-----------NELIAKGNLKIREnlRISYL 377
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLlrptsgevrvlGEDVARDPAEVRR--RIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 378 PQDF---DQLQG--TLEQFA-------AEKEVEVQDLLAMLRKLGFERTmfdyRIEQMSMGQKRKVALARSLCEEANLYI 445
Cdd:COG1131 79 PQEPalyPDLTVreNLRFFArlyglprKEARERIDELLELFGLTDAADR----KVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488922799 446 WDEPLNYLDVITREQIQNLVLKFKP---TLLVVEHDREFVQKIAT 487
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCD 199
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-478 |
3.04e-19 |
|
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: 90.61 E-value: 3.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 34 LGLIGRNGRGKTTLMKILQNQV-----EYEGKVETN--LK-------FNYFpAKITE--------PQ----------DSV 81
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELkpnlgDYDEEPSWDevLKrfrgtelQDYF-KKLANgeikvahkPQyvdlipkvfkGTV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 82 RMVLMKITGRDYSDfwEVERELDqiglAEEILEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLD-----AAGRd 156
Cdd:COG1245 181 RELLEKVDERGKLD--ELAEKLG----LENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrlNVAR- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 157 LLAKYLKQKQGYIVVSHDRYFLNQVID--HVISIDRAQ---ISSFKGNyetwaaeranaderEISLNATMKkdikkleqa 231
Cdd:COG1245 254 LIRELAEEGKYVLVVEHDLAILDYLADyvHILYGEPGVygvVSKPKSV--------------RVGINQYLD--------- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 232 trqkqewsraterkkagapdkGFVghkaakvmsKALNIRDRAE------KKLTDKKQLLKNIEIqDELQLNYqpylgpqN 305
Cdd:COG1245 311 ---------------------GYL---------PEENVRIRDEpiefevHAPRREKEEETLVEY-PDLTKSY-------G 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 306 NALLEADslvlqrAGkllnqplnlELKKNERMVIQGENGSGKSTLIKaMLGQNELIAKGnlKIRENLRISYLPQ----DF 381
Cdd:COG1245 353 GFSLEVE------GG---------EIREGEVLGIVGPNGIGKTTFAK-ILAGVLKPDEG--EVDEDLKISYKPQyispDY 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 382 DqlqGTLEQFAAEK----------EVEVqdllamLRKLGFERtMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLN 451
Cdd:COG1245 415 D---GTVEEFLRSAntddfgssyyKTEI------IKPLGLEK-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
490 500 510
....*....|....*....|....*....|....
gi 488922799 452 YLDVitrEQ-------IQNLVLKFKPTLLVVEHD 478
Cdd:COG1245 485 HLDV---EQrlavakaIRRFAENRGKTAMVVDHD 515
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-193 |
8.02e-19 |
|
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: 84.95 E-value: 8.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 2 GIIQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGkveTNLKfNYFPAKI 74
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLaglykptSGSVLLDG---TDIR-QLDPADL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 75 TE-----PQDSvrmVLMKITGRD-------YSDFWEVERELDQIGLAE-----------EILEQTYaSLSPGQQTKALLA 131
Cdd:cd03245 77 RRnigyvPQDV---TLFYGTLRDnitlgapLADDERILRAAELAGVTDfvnkhpngldlQIGERGR-GLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488922799 132 AMFADQNSFQLIDEPTNHLDAAGRDLLAKYLKQKQG---YIVVSHdRYFLNQVIDHVISIDRAQI 193
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdktLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
325-477 |
1.34e-18 |
|
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: 83.20 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNElIAKGNLKI---------RENLR--ISYLPQDFDQLQGTLEqfaa 393
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD-PTSGEILIdgvdlrdldLESLRknIAYVPQDPFLFSGTIR---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 394 ekevevQDLLamlrklgfertmfdyrieqmSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKP--T 471
Cdd:cd03228 94 ------ENIL--------------------SGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkT 147
|
....*.
gi 488922799 472 LLVVEH 477
Cdd:cd03228 148 VIVIAH 153
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
301-494 |
2.85e-18 |
|
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: 87.51 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 301 LGPQNNALLEADSLVLQRA-GKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNELIAkGNLKI---------RE 370
Cdd:COG4988 329 LPAAGPPSIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYS-GSILIngvdlsdldPA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 371 NLR--ISYLPQD---FdqlQGTLEQ---FAAEK--EVEVQDLLAMLRKLGFERTM---FDYRI-EQ---MSMGQKRKVAL 433
Cdd:COG4988 408 SWRrqIAWVPQNpylF---AGTIREnlrLGRPDasDEELEAALEAAGLDEFVAALpdgLDTPLgEGgrgLSGGQAQRLAL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488922799 434 ARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKP--TLLVVEHDREFVqKIATQTVNLKK 494
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALL-AQADRILVLDD 546
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
327-494 |
2.87e-18 |
|
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: 87.97 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNELiAKGNLKI---------RENLR--ISYLPQDFDQLQGTLEQ---FA 392
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP-TSGRILIdgidlrqidPASLRrqIGVVLQDVFLFSGTIREnitLG 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 393 AEkEVEVQDLLAMLRKLG---FERTM---FDYRIEQM----SMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQ 462
Cdd:COG2274 573 DP-DATDEEIIEAARLAGlhdFIEALpmgYDTVVGEGgsnlSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL 651
|
170 180 190
....*....|....*....|....*....|....
gi 488922799 463 NLVLKFKP--TLLVVEHDREFVqKIATQTVNLKK 494
Cdd:COG2274 652 ENLRRLLKgrTVIIIAHRLSTI-RLADRIIVLDK 684
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
330-478 |
3.09e-18 |
|
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: 84.00 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 330 ELKKNERMVIQGENGSGKSTLIKAMLGqnELIAKGNLKIRENLRISYLPQ----DFdqlQGTLEQFAAEKeveVQDLLA- 404
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAG--VLKPDEGDIEIELDTVSYKPQyikaDY---EGTVRDLLSSI---TKDFYTh 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 405 ------MLRKLGFERTMfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVitrEQ-------IQNLVLKFKPT 471
Cdd:cd03237 93 pyfkteIAKPLQIEQIL-DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV---EQrlmaskvIRRFAENNEKT 168
|
....*..
gi 488922799 472 LLVVEHD 478
Cdd:cd03237 169 AFVVEHD 175
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-193 |
4.25e-18 |
|
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: 81.71 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 5 QLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILqnqveyegkvetnlkfnyfpAKITEPQD-SVrm 83
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTL--------------------AGLLKPSSgEI-- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 84 vlmKITGRDYSDFWEVERE---------LDQIGLAEeILEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAG 154
Cdd:cd03214 57 ---LLDGKDLASLSPKELArkiayvpqaLELLGLAH-LADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488922799 155 R----DLLAKyLKQKQGY--IVVSHDryfLNQVI---DHVISIDRAQI 193
Cdd:cd03214 133 QiellELLRR-LARERGKtvVMVLHD---LNLAAryaDRVILLKDGRI 176
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
310-478 |
6.84e-18 |
|
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: 81.33 E-value: 6.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 310 EADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNELiAKG----------NLKIRE-NLRISYLP 378
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKP-SSGeilldgkdlaSLSPKElARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 379 QdfdqlqgtleqfaAEKEVEVQDLLamlrklgfertmfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITR 458
Cdd:cd03214 80 Q-------------ALELLGLAHLA-------------DRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180
....*....|....*....|....
gi 488922799 459 ----EQIQNLVLKFKPTLLVVEHD 478
Cdd:cd03214 134 iellELLRRLARERGKTVVMVLHD 157
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
308-490 |
7.74e-18 |
|
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: 82.93 E-value: 7.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 308 LLEADSLVLQRAGKLLNQP----LNLELKKNERMVIQGENGSGKSTLIKAMLGQNElIAKGNLKI----------RENLR 373
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPvlkdVSLEVAPGESFGLVGESGSGKSTLLRALAGLER-PWSGEVTFdgrpvtrrrrKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 374 -ISYLPQD----FDQLQgTLEQFAAE-------KEVEvQDLLAMLRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEA 441
Cdd:COG1124 80 rVQMVFQDpyasLHPRH-TVDRILAEplrihglPDRE-ERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488922799 442 NLYIWDEPLNYLDVITREQIQNLVLKFKP----TLLVVEHDREFVQKIATQTV 490
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREerglTYLFVSHDLAVVAHLCDRVA 210
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-189 |
1.03e-17 |
|
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: 82.46 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 27 EIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVETNL-KFNYFPAKITEPQD-SVRMVLMKITGRDYSD-FWEVERe 102
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKpDEGDIEIELdTVSYKPQYIKADYEgTVRDLLSSITKDFYTHpYFKTEI- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 103 LDQIGLaEEILEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYLKQ-----KQGYIVVSHDRYF 177
Cdd:cd03237 100 AKPLQI-EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRfaennEKTAFVVEHDIIM 178
|
170
....*....|..
gi 488922799 178 LNQVIDHVISID 189
Cdd:cd03237 179 IDYLADRLIVFE 190
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-208 |
1.42e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 85.33 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEY-EGKVE--TNLKFNYFpakitePQDS 80
Cdd:PRK15064 320 LEVENLTKGFDN--GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPdSGTVKwsENANIGYY------AQDH 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 81 VRMVLMKITGRDYSDFWEVERELDQI--GL-------AEEILEQTyASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLD 151
Cdd:PRK15064 392 AYDFENDLTLFDWMSQWRQEGDDEQAvrGTlgrllfsQDDIKKSV-KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488922799 152 AAGRDLLAKYLKQKQG-YIVVSHDRYFLNQVIDHVISIDRAQISSFKGNYETWAAERA 208
Cdd:PRK15064 471 MESIESLNMALEKYEGtLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQG 528
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-193 |
2.98e-17 |
|
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: 84.89 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 2 GIIQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVE---TNLKfNYFPAKITE- 76
Cdd:COG2274 472 GDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEpTSGRILidgIDLR-QIDPASLRRq 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 77 ----PQDSvrmVLMK------IT-GRDYSDFWEVERELDQIGLAEEILE-----QTY-----ASLSPGQQTKALLAAMFA 135
Cdd:COG2274 551 igvvLQDV---FLFSgtirenITlGDPDATDEEIIEAARLAGLHDFIEAlpmgyDTVvgeggSNLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488922799 136 DQNSFQLIDEPTNHLDAAGRDLLAKYLKQ-KQGY--IVVSHDRYFLNQViDHVISIDRAQI 193
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRlLKGRtvIIIAHRLSTIRLA-DRIIVLDKGRI 687
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
325-478 |
5.39e-17 |
|
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: 79.82 E-value: 5.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNElIAKGNLKI------RENLRISYLPQDF---------------DQ 383
Cdd:cd03293 21 EDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLER-PTSGEVLVdgepvtGPGPDRGYVFQQDallpwltvldnvalgLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 384 LQGTLeqfAAEKEVEVQDLLAMLRKLGFErtmfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQN 463
Cdd:cd03293 100 LQGVP---KAEARERAEELLELVGLSGFE----NAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQE 172
|
170
....*....|....*....
gi 488922799 464 LVL----KFKPTLLVVEHD 478
Cdd:cd03293 173 ELLdiwrETGKTVLLVTHD 191
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
309-493 |
1.13e-16 |
|
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: 77.61 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 309 LEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNElIAKGNlkirenlrISYLPQDFDQLQGTL 388
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE-PDSGS--------ILIDGEDLTDLEDEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 389 EQFAAEKEVEVQDLLamlrkLGFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITR----EQIQNL 464
Cdd:cd03229 72 PPLRRRIGMVFQDFA-----LFPHLTVLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRrevrALLKSL 146
|
170 180
....*....|....*....|....*....
gi 488922799 465 VLKFKPTLLVVEHDREFVQKIATQTVNLK 493
Cdd:cd03229 147 QAQLGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-193 |
1.27e-16 |
|
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: 78.45 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 5 QLKNVSFSYDNQIKpVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQN-QVEYEGKVETNLKfnyfPAKITEPQDSVRM 83
Cdd:cd03226 1 RIENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGlIKESSGSILLNGK----PIKAKERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 84 VLMKItgrDYSDFWE-VEREL--------DQIGLAEEIL---------EQTYASLSPGQQTKALLAAMFADQNSFQLIDE 145
Cdd:cd03226 76 VMQDV---DYQLFTDsVREELllglkeldAGNEQAETVLkdldlyalkERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488922799 146 PTNHLDAAGRDLLAKYLK--QKQGY--IVVSHDRYFLNQVIDHVISIDRAQI 193
Cdd:cd03226 153 PTSGLDYKNMERVGELIRelAAQGKavIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
327-493 |
2.28e-16 |
|
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: 77.68 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNE------LIAKGNLKIRENLR-ISYLPQD----------FDQLQGTLE 389
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKessgsiLLNGKPIKAKERRKsIGYVMQDvdyqlftdsvREELLLGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 390 QFAAEKEvEVQDLLAMLRKLGF-ERTMFDyrieqMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKF 468
Cdd:cd03226 99 ELDAGNE-QAETVLKDLDLYALkERHPLS-----LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIREL 172
|
170 180
....*....|....*....|....*...
gi 488922799 469 ---KPTLLVVEHDREFVQKIATQTVNLK 493
Cdd:cd03226 173 aaqGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
327-486 |
2.51e-16 |
|
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: 78.31 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNE---------------LIAKGNLKIRenLRISYLPQD---------FD 382
Cdd:cd03261 19 VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRpdsgevlidgedisgLSEAELYRLR--RRMGMLFQSgalfdsltvFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 383 QLQGTLEQFAAEKEVEVQDLLAMlrKLGFE--RTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQ 460
Cdd:cd03261 97 NVAFPLREHTRLSEEEIREIVLE--KLEAVglRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGV 174
|
170 180 190
....*....|....*....|....*....|
gi 488922799 461 IQNLVLKFKPTL----LVVEHDREFVQKIA 486
Cdd:cd03261 175 IDDLIRSLKKELgltsIMVTHDLDTAFAIA 204
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-193 |
2.99e-16 |
|
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: 76.28 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVetnlkfnyfpakitepqdsvr 82
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKpDSGEI--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 83 mvlmKITGRDYSDFWEVERE-----LDQIGL-----AEEILEqtyasLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDA 152
Cdd:cd03230 58 ----KVLGKDIKKEPEEVKRrigylPEEPSLyenltVRENLK-----LSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488922799 153 AGRDLLAKYLKQ--KQGYIVV--SHDRYFLNQVIDHVISIDRAQI 193
Cdd:cd03230 129 ESRREFWELLRElkKEGKTILlsSHILEEAERLCDRVAILNNGRI 173
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-208 |
3.54e-16 |
|
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: 80.97 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEY-EGKVE---TNLKfNYFPAKITE--- 76
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPqSGSITlggVDLR-DLDEDDLRRria 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 77 --PQD------SVR-MVLMkitGRDYSDFWEVERELDQIGLAEEI----------LEQTYASLSPGQQTKALLAAMFADQ 137
Cdd:COG4987 413 vvPQRphlfdtTLReNLRL---ARPDATDEELWAALERVGLGDWLaalpdgldtwLGEGGRRLSGGERRRLALARALLRD 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488922799 138 NSFQLIDEPTNHLDAA-GRDLLAKYLKQKQGY--IVVSHDRYFLNQViDHVISIDRAQISSfKGNYETWAAERA 208
Cdd:COG4987 490 APILLLDEPTEGLDAAtEQALLADLLEALAGRtvLLITHRLAGLERM-DRILVLEDGRIVE-QGTHEELLAQNG 561
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
306-480 |
3.88e-16 |
|
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: 77.82 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 306 NALLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNELIAKGNLKI------RENL-----RI 374
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLfgerrgGEDVwelrkRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 375 SY----LPQDFDQLQ--------------GTLEQFAAEKEVEVQDLLAMLRklgfertMFDY---RIEQMSMGQKRKVAL 433
Cdd:COG1119 81 GLvspaLQLRFPRDEtvldvvlsgffdsiGLYREPTDEQRERARELLELLG-------LAHLadrPFGTLSQGEQRRVLI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488922799 434 ARSLCEEANLYIWDEPLNYLDVITREQ----IQNLVLKFKPTLLVVEHDRE 480
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELllalLDKLAAEGAPTLVLVTHHVE 204
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
326-490 |
4.31e-16 |
|
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: 77.17 E-value: 4.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 326 PLNLELKKNERMVIQGENGSGKSTLIKAMLG-----QNELIAKG----NLKIRENlRISYLPQD---FDQLqgTLEQ--- 390
Cdd:cd03259 18 DLSLTVEPGEFLALLGPSGCGKTTLLRLIAGlerpdSGEILIDGrdvtGVPPERR-NIGMVFQDyalFPHL--TVAEnia 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 391 FA--------AEKEVEVQDLLAMLRKLGFErtmfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQ 462
Cdd:cd03259 95 FGlklrgvpkAEIRARVRELLELVGLEGLL----NRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELR 170
|
170 180 190
....*....|....*....|....*....|..
gi 488922799 463 NLVLK----FKPTLLVVEHDREFVQKIATQTV 490
Cdd:cd03259 171 EELKElqreLGITTIYVTHDQEEALALADRIA 202
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
325-480 |
1.14e-15 |
|
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: 79.42 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIKAMLG----QNELIAKGNLKIR----ENLR--ISYLPQD---FDqlqGTLEQ- 390
Cdd:COG4987 352 DGLSLTLPPGERVAIVGPSGSGKSTLLALLLRfldpQSGSITLGGVDLRdldeDDLRrrIAVVPQRphlFD---TTLREn 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 391 --FAAEkEVEVQDLLAMLRKLG---FERTM---FDYRI----EQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITR 458
Cdd:COG4987 429 lrLARP-DATDEELWAALERVGlgdWLAALpdgLDTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATE 507
|
170 180
....*....|....*....|....
gi 488922799 459 EQIQNLVLKFKP--TLLVVEHDRE 480
Cdd:COG4987 508 QALLADLLEALAgrTVLLITHRLA 531
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-189 |
1.23e-15 |
|
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: 74.73 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVE------TNLKFNYFPAKITE 76
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDpTSGEILidgvdlRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 77 -PQDSvrmVLMKITgrdysdfwevereldqigLAEEIleqtyasLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGR 155
Cdd:cd03228 81 vPQDP---FLFSGT------------------IRENI-------LSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170 180 190
....*....|....*....|....*....|....*..
gi 488922799 156 DLLAKYLKQKQGY---IVVSHdRYFLNQVIDHVISID 189
Cdd:cd03228 133 ALILEALRALAKGktvIVIAH-RLSTIRDADRIIVLD 168
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
21-186 |
1.25e-15 |
|
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: 79.44 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 21 FDQVALEIDASW-----KLGLIGRNGRGKTTLMKILQNQVE-YEGKVETNLKFNYFPAKITEPQD-SVRMVLMKITGRDY 93
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKpDEGEVDEDLKISYKPQYISPDYDgTVEEFLRSANTDDF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 94 SDFWEVERELDQIGLaEEILEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYLK-----QKQGY 168
Cdd:COG1245 431 GSSYYKTEIIKPLGL-EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRrfaenRGKTA 509
|
170
....*....|....*...
gi 488922799 169 IVVSHDRYFLNQVIDHVI 186
Cdd:COG1245 510 MVVDHDIYLIDYISDRLM 527
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
328-493 |
1.63e-15 |
|
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: 75.60 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 328 NLELKKNERMVIQGENGSGKSTLIKaMLG------------QNELIAKGNLKIRENLR---ISYLPQDFdQLqgtLEQFA 392
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLN-ILGgldrptsgevrvDGTDISKLSEKELAAFRrrhIGFVFQSF-NL---LPDLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 393 AEKEVEV-------------QDLLAMLRKLGFERTMfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITRE 459
Cdd:cd03255 99 ALENVELplllagvpkkerrERAEELLERVGLGDRL-NHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGK 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 488922799 460 QIQNLVLK----FKPTLLVVEHDREFVqKIATQTVNLK 493
Cdd:cd03255 178 EVMELLRElnkeAGTTIVVVTHDPELA-EYADRIIELR 214
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-186 |
4.37e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.93 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 34 LGLIGRNGRGKTTLMKILQNQVE-YEGKVETNLKFNYFPAKITEPQD-SVRMVLMKITGRDYSDFWEVEReLDQIGLaEE 111
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKpDEGEVDPELKISYKPQYIKPDYDgTVEDLLRSITDDLGSSYYKSEI-IKPLQL-ER 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 112 ILEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYLK-----QKQGYIVVSHDRYFLNQVIDHVI 186
Cdd:PRK13409 446 LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRriaeeREATALVVDHDIYMIDYISDRLM 525
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
308-455 |
9.29e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.91 E-value: 9.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 308 LLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLG-----------QNELIA-------------- 362
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGlarpdagevlwQGEPIRrqrdeyhqdllylg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 363 -----KGNLKIRENLRISYlpqdfdQLQGTLEQFAaekeveVQDLLAMLRKLGFErtmfDYRIEQMSMGQKRKVALARSL 437
Cdd:PRK13538 81 hqpgiKTELTALENLRFYQ------RLHGPGDDEA------LWEALAQVGLAGFE----DVPVRQLSAGQQRRVALARLW 144
|
170
....*....|....*...
gi 488922799 438 CEEANLYIWDEPLNYLDV 455
Cdd:PRK13538 145 LTRAPLWILDEPFTAIDK 162
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-235 |
3.57e-14 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 74.82 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNQIkpVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVE--TNLKFNYFPAKITE--- 76
Cdd:PRK10636 312 LLKMEKVSAGYGDRI--ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELApVSGEIGlaKGIKLGYFAQHQLEflr 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 77 PQDSVRMVLMKITGRdysdfwEVEREL-DQIG----LAEEILEQTyASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLD 151
Cdd:PRK10636 390 ADESPLQHLARLAPQ------ELEQKLrDYLGgfgfQGDKVTEET-RRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 152 AAGRDLLAKYLKQKQG-YIVVSHDRYFLNQVIDHVISIDRAQISSFKG---NYETWAAE------RANADEREISLN-AT 220
Cdd:PRK10636 463 LDMRQALTEALIDFEGaLVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGdleDYQQWLSDvqkqenQTDEAPKENNANsAQ 542
|
250
....*....|....*
gi 488922799 221 MKKDIKKLEQATRQK 235
Cdd:PRK10636 543 ARKDQKRREAELRTQ 557
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-485 |
4.50e-14 |
|
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: 74.45 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEYE---GKVETNL----KFNYF--PAKI 74
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptsGRIIYHValceKCGYVerPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 75 TEP------------------QDSVRMVLMK----ITGRDYSDFWE------VERELDQIG--------LAEEILEQTYA 118
Cdd:TIGR03269 79 GEPcpvcggtlepeevdfwnlSDKLRRRIRKriaiMLQRTFALYGDdtvldnVLEALEEIGyegkeavgRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 119 S---------LSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYLKQ-----KQGYIVVSHDRYFLNQVIDH 184
Cdd:TIGR03269 159 ShrithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavkasGISMVLTSHWPEVIEDLSDK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 185 VISIDRAQISSfKGNYETWAA---ERANADEREisLNATMKKDIKKLEQATrqkqewsraterKKAGAPDKGFVghkaak 261
Cdd:TIGR03269 239 AIWLENGEIKE-EGTPDEVVAvfmEGVSEVEKE--CEVEVGEPIIKVRNVS------------KRYISVDRGVV------ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 262 vmsKALNirdraekkltdkkqllknieiqdelqlnyqpylgpqnnalleadslvlqragkllnqPLNLELKKNERMVIQG 341
Cdd:TIGR03269 298 ---KAVD---------------------------------------------------------NVSLEVKEGEIFGIVG 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 342 ENGSGKSTLIKAMLGQNElIAKGNLKIR------------ENLR------ISYLPQDFDQL--QGTLEQFAAEKEVEVQD 401
Cdd:TIGR03269 318 TSGAGKTTLSKIIAGVLE-PTSGEVNVRvgdewvdmtkpgPDGRgrakryIGILHQEYDLYphRTVLDNLTEAIGLELPD 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 402 LLAM------LRKLGFE----RTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLK---- 467
Cdd:TIGR03269 397 ELARmkavitLKMVGFDeekaEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKaree 476
|
570
....*....|....*...
gi 488922799 468 FKPTLLVVEHDREFVQKI 485
Cdd:TIGR03269 477 MEQTFIIVSHDMDFVLDV 494
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
328-493 |
5.42e-14 |
|
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: 71.45 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 328 NLELKKNERMVIQGENGSGKSTLIKAMLGQNElIAKGNLKI---------RENLR-----ISYLPQDFD----------- 382
Cdd:cd03256 21 SLSINPGEFVALIGPSGAGKSTLLRCLNGLVE-PTSGSVLIdgtdinklkGKALRqlrrqIGMIFQQFNlierlsvlenv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 383 ---------QLQGTLEQFaaeKEVEVQDLLAMLRKLGFErTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYL 453
Cdd:cd03256 100 lsgrlgrrsTWRSLFGLF---PKEEKQRALAALERVGLL-DKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488922799 454 DVITREQIQNLVLK----FKPTLLVVEHDREFVQKIATQTVNLK 493
Cdd:cd03256 176 DPASSRQVMDLLKRinreEGITVIVSLHQVDLAREYADRIVGLK 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
308-492 |
6.98e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.65 E-value: 6.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 308 LLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLG----QNELIAKGNLKIR------------EN 371
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGfvpyQHGSITLDGKPVEgpgaergvvfqnEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 372 LrisyLP-QD-FDQLQGTLEQFAAEKEVEVQDLLAMLRKLGFERtmFDYR-IEQMSMGQKRKVALARSLCEEANLYIWDE 448
Cdd:PRK11248 81 L----LPwRNvQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEG--AEKRyIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488922799 449 PLNYLDVITREQIQNLVLKF-----KPTLLVVeHDREFVQKIATQTVNL 492
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLwqetgKQVLLIT-HDIEEAVFMATELVLL 202
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-202 |
7.28e-14 |
|
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: 74.02 E-value: 7.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVE------TNLKFNYFPAKIT- 75
Cdd:COG4988 337 IELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPpYSGSILingvdlSDLDPASWRRQIAw 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 76 ---EP---QDSVRMVLMkITGRDYSDfWEVERELDQIGLAEEI--LEQTYAS--------LSPGQ-QTKALlAAMFADQN 138
Cdd:COG4988 416 vpqNPylfAGTIRENLR-LGRPDASD-EELEAALEAAGLDEFVaaLPDGLDTplgeggrgLSGGQaQRLAL-ARALLRDA 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488922799 139 SFQLIDEPTNHLDAAG-RDLLAKYLKQKQGY--IVVSHDRYFLNQViDHVISIDRAQISSFkGNYET 202
Cdd:COG4988 493 PLLLLDEPTAHLDAETeAEILQALRRLAKGRtvILITHRLALLAQA-DRILVLDDGRIVEQ-GTHEE 557
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-193 |
8.26e-14 |
|
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: 70.32 E-value: 8.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLK--FNYFPAKI 74
Cdd:cd03268 1 LKTNDLTKTYGK--KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIlglikpdSGEITFDGKSYQKNIeaLRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 75 TEP--------QDSVRmVLMKITGRDYSdfwEVERELDQIGLAEEILEQTyASLSPGQQTKALLAAMFADQNSFQLIDEP 146
Cdd:cd03268 79 EAPgfypnltaRENLR-LLARLLGIRKK---RIDEVLDVVGLKDSAKKKV-KGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488922799 147 TNHLDAAG----RDLLAKYLKQKQGYIVVSHDRYFLNQVIDHVISIDRAQI 193
Cdd:cd03268 154 TNGLDPDGikelRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-148 |
1.93e-13 |
|
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: 67.67 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 21 FDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLKFNYFPAKI------------TEPQDSV 81
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIagllsptEGTILLDGQDLTDDERKSLRKEIgyvfqdpqlfprLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 82 RMVL-MKITGRDYSD--FWEVERELDQIGLAEEILEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTN 148
Cdd:pfam00005 81 RLGLlLKGLSKREKDarAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
309-463 |
5.31e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.03 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 309 LEADSL-VLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQneLIAKGNLKI-------------RENLri 374
Cdd:PRK11174 350 IEAEDLeILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF--LPYQGSLKIngielreldpeswRKHL-- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 375 SYLPQDFDQLQGTLE------QFAAEKEvEVQDLLAMLRKLGFERTM---FDYRI-EQM---SMGQKRKVALARSLCEEA 441
Cdd:PRK11174 426 SWVGQNPQLPHGTLRdnvllgNPDASDE-QLQQALENAWVSEFLPLLpqgLDTPIgDQAaglSVGQAQRLALARALLQPC 504
|
170 180
....*....|....*....|..
gi 488922799 442 NLYIWDEPLNYLDVITREQIQN 463
Cdd:PRK11174 505 QLLLLDEPTASLDAHSEQLVMQ 526
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
314-494 |
5.70e-13 |
|
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: 68.09 E-value: 5.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 314 LVLQRAGKLLNQPLNLELKKN-ERMVIQGENGSGKSTLIKAMLGQnELIAKGNLKI--------RENL-------RISYL 377
Cdd:cd03297 2 LCVDIEKRLPDFTLKIDFDLNeEVTGIFGASGAGKSTLLRCIAGL-EKPDGGTIVLngtvlfdsRKKInlppqqrKIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 378 PQD---FDQLQ-------GTLEQFAAEKEVEVQDLLAMLrklGFERTMFDYrIEQMSMGQKRKVALARSLCEEANLYIWD 447
Cdd:cd03297 81 FQQyalFPHLNvrenlafGLKRKRNREDRISVDELLDLL---GLDHLLNRY-PAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488922799 448 EPLNYLDVITREQIQNLVLK----FKPTLLVVEHDREFVQKIATQTVNLKK 494
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQikknLNIPVIFVTHDLSEAEYLADRIVVMED 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
305-477 |
6.26e-13 |
|
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: 67.49 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 305 NNALLEADSLVLQRAGKLLNqpLNLELKKNERMVIQGENGSGKSTLIKAMLGQNELIaKGNLKIreNLRISYLPQdfdQ- 383
Cdd:cd03250 4 EDASFTWDSGEQETSFTLKD--INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKL-SGSVSV--PGSIAYVSQ---Ep 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 384 --LQGTL-------EQFAAEKEVEVQDLLAMLRKLgferTMFDYRIEQM--------SMGQKRKVALARSLCEEANLYIW 446
Cdd:cd03250 76 wiQNGTIrenilfgKPFDEERYEKVIKACALEPDL----EILPDGDLTEigekginlSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190
....*....|....*....|....*....|....*
gi 488922799 447 DEPLNYLDVITREQI-QNLV---LKFKPTLLVVEH 477
Cdd:cd03250 152 DDPLSAVDAHVGRHIfENCIlglLLNNKTRILVTH 186
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
309-455 |
6.86e-13 |
|
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: 67.38 E-value: 6.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 309 LEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLG------------------------QNELIA-- 362
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGllrpdsgevrwngtplaeqrdephENILYLgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 363 ----KGNLKIRENLRisYLPQDFDQLQGTLEqfaaekevevqDLLAMLRKLGFERTMFdyriEQMSMGQKRKVALARSLC 438
Cdd:TIGR01189 81 lpglKPELSALENLH--FWAAIHGGAQRTIE-----------DALAAVGLTGFEDLPA----AQLSAGQQRRLALARLWL 143
|
170
....*....|....*..
gi 488922799 439 EEANLYIWDEPLNYLDV 455
Cdd:TIGR01189 144 SRRPLWILDEPTTALDK 160
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
309-486 |
7.26e-13 |
|
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: 68.23 E-value: 7.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 309 LEADSLVLQRAG-KLLNQpLNLELKKNERMVIQGENGSGKSTLIKAMLGQ--------------------NELIAKG--- 364
Cdd:cd03219 1 LEVRGLTKRFGGlVALDD-VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFlrptsgsvlfdgeditglppHEIARLGigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 365 ---------NLKIRENLRISYLpqdFDQLQGTLEQFAAEKEVEVQDL-LAMLRKLGFERTMfDYRIEQMSMGQKRKVALA 434
Cdd:cd03219 80 tfqiprlfpELTVLENVMVAAQ---ARTGSGLLLARARREEREARERaEELLERVGLADLA-DRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488922799 435 RSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKP---TLLVVEHDREFVQKIA 486
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRErgiTVLLVEHDMDVVMSLA 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
304-488 |
7.26e-13 |
|
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: 68.08 E-value: 7.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 304 QNNALLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQ-----------NELIAKGNLKIRENL 372
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLlrpdsgeilvdGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 373 R--ISYLPQD---FDQLqgTLEQ---FA-------AEKEVE--VQDLLAMLRKLGFErtmfDYRIEQMSMGQKRKVALAR 435
Cdd:COG1127 81 RrrIGMLFQGgalFDSL--TVFEnvaFPlrehtdlSEAEIRelVLEKLELVGLPGAA----DKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488922799 436 SLCEEANLYIWDEPLNYLDVITREQIQNLVL----KFKPTLLVVEHDREFVQKIATQ 488
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRelrdELGLTSVVVTHDLDSAFAIADR 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
325-480 |
7.90e-13 |
|
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: 70.39 E-value: 7.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNEL----IAKGNLKIRENL------RISYLPQDFDQLQGTL------ 388
Cdd:TIGR02857 339 RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPtegsIAVNGVPLADADadswrdQIAWVPQHPFLFAGTIaenirl 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 389 -EQFAAEKEVE-------VQDLLAMLRkLGFErTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQ 460
Cdd:TIGR02857 419 aRPDASDAEIRealeragLDEFVAALP-QGLD-TPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAE 496
|
170 180
....*....|....*....|..
gi 488922799 461 IQNLVLKFKP--TLLVVEHDRE 480
Cdd:TIGR02857 497 VLEALRALAQgrTVLLVTHRLA 518
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
307-480 |
9.12e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 68.35 E-value: 9.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 307 ALLEADSLVLQRAGKLLNQP----LNLELKKNERMVIQGENGSGKSTLIKAMLG-----QNELIAKGN------------ 365
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPalqdVSLTIESGEFVVALGASGCGKTTLLNLIAGflapsSGEITLDGVpvtgpgadrgvv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 366 ---------LKIRENLRISYlpqdfdQLQGtleQFAAEKEVEVQDLLAMLRKLGFERtmfdYRIEQMSMGQKRKVALARS 436
Cdd:COG4525 82 fqkdallpwLNVLDNVAFGL------RLRG---VPKAERRARAEELLALVGLADFAR----RRIWQLSGGMRQRVGIARA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488922799 437 LCEEANLYIWDEPLNYLDVITREQIQNLVLKF-----KPTLLVVeHDRE 480
Cdd:COG4525 149 LAADPRFLLMDEPFGALDALTREQMQELLLDVwqrtgKGVFLIT-HSVE 196
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
309-465 |
9.47e-13 |
|
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: 67.13 E-value: 9.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 309 LEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLG------------------QNELIA-------- 362
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGlspplagrvllnggpldfQRDSIArgllylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 363 ----KGNLKIRENLRISYLPQDFDQlqgtleqfaaekeveVQDLLAMLRKLGFErtmfDYRIEQMSMGQKRKVALARSLC 438
Cdd:cd03231 81 apgiKTTLSVLENLRFWHADHSDEQ---------------VEEALARVGLNGFE----DRPVAQLSAGQQRRVALARLLL 141
|
170 180
....*....|....*....|....*..
gi 488922799 439 EEANLYIWDEPLNYLDVITREQIQNLV 465
Cdd:cd03231 142 SGRPLWILDEPTTALDKAGVARFAEAM 168
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-186 |
9.95e-13 |
|
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: 66.44 E-value: 9.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQ-------NQVEYEGKVETNLKFNyfpakITE 76
Cdd:cd03229 1 LELKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAgleepdsGSILIDGEDLTDLEDE-----LPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 77 PQDSVRMVLmkitgRDYSDFWEVEReLDQIGLAeeileqtyasLSPGQQTKALLA-AMFADQNSFqLIDEPTNHLDAAGR 155
Cdd:cd03229 74 LRRRIGMVF-----QDFALFPHLTV-LENIALG----------LSGGQQQRVALArALAMDPDVL-LLDEPTSALDPITR 136
|
170 180 190
....*....|....*....|....*....|....*.
gi 488922799 156 D---LLAKYLKQKQGY--IVVSHDRYFLNQVIDHVI 186
Cdd:cd03229 137 RevrALLKSLQAQLGItvVLVTHDLDEAARLADRVV 172
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-193 |
1.04e-12 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 67.78 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVETN-LKFNYFPAKITE----- 76
Cdd:COG1131 1 IEVRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRpTSGEVRVLgEDVARDPAEVRRrigyv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 77 PQDSVrmVLMKITGRDYSDFW-------------EVERELDQIGLaEEILEQTYASLSPGQQTKALLAAMFADQNSFQLI 143
Cdd:COG1131 79 PQEPA--LYPDLTVRENLRFFarlyglprkeareRIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488922799 144 DEPTNHLDAAGRDLLAKYLKQ--KQGYIVV--SHDRYFLNQVIDHVISIDRAQI 193
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRElaAEGKTVLlsTHYLEEAERLCDRVAIIDKGRI 209
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
327-493 |
1.29e-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: 66.89 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNElIAKGNLKIRENlRISYLP----------QD---------FDQLQGT 387
Cdd:cd03301 19 LNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEE-PTSGRIYIGGR-DVTDLPpkdrdiamvfQNyalyphmtvYDNIAFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 388 LEQFAAEKEVEVQDLLAMLRKLGFErTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLD----VITREQIQN 463
Cdd:cd03301 97 LKLRKVPKDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKR 175
|
170 180 190
....*....|....*....|....*....|
gi 488922799 464 LVLKFKPTLLVVEHDREFVQKIATQTVNLK 493
Cdd:cd03301 176 LQQRLGTTTIYVTHDQVEAMTMADRIAVMN 205
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
341-493 |
1.32e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.99 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 341 GENGSGKSTLIKAMLGQNELiAKGNLKI---------RENLrISYLPQDfdqlqgtlEQFAAEKEVEVQDLLAMLR--KL 409
Cdd:PRK15056 40 GVNGSGKSTLFKALMGFVRL-ASGKISIlgqptrqalQKNL-VAYVPQS--------EEVDWSFPVLVEDVVMMGRygHM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 410 GFERT-----------------MFDYR---IEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFK 469
Cdd:PRK15056 110 GWLRRakkrdrqivtaalarvdMVEFRhrqIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELR 189
|
170 180
....*....|....*....|....*..
gi 488922799 470 P---TLLVVEHDREFVQKIATQTVNLK 493
Cdd:PRK15056 190 DegkTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
327-492 |
1.37e-12 |
|
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: 66.75 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGqNELIAKGNLKIRE---------NLRISYLPQD---FDQLqgTLEQFAAE 394
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAG-FETPQSGRVLINGvdvtaappaDRPVSMLFQEnnlFAHL--TVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 395 --------KEVEVQDLLAMLRKLGFERtmFDYRI-EQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLV 465
Cdd:cd03298 94 glspglklTAEDRQAIEVALARVGLAG--LEKRLpGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|.
gi 488922799 466 LKF----KPTLLVVEHDREFVQKIATQTVNL 492
Cdd:cd03298 172 LDLhaetKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
327-470 |
1.42e-12 |
|
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: 66.76 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKaMLGQNELIAKGNLKIREN----------LRISYLPQD---------------F 381
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLK-MLTGELRPTSGTAYINGYsirtdrkaarQSLGYCPQFdalfdeltvrehlrfY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 382 DQLQGtLEQFAAEKEVEvqdllAMLRKLGFERTMfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQI 461
Cdd:cd03263 100 ARLKG-LPKSEIKEEVE-----LLLRVLGLTDKA-NKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAI 172
|
....*....
gi 488922799 462 QNLVLKFKP 470
Cdd:cd03263 173 WDLILEVRK 181
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
309-465 |
2.06e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.05 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 309 LEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLG------------------------------QN 358
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGllppaagtikldggdiddpdvaeachylghRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 359 ELiaKGNLKIRENLRisyLPQDFdqlQGTLEQFAAE--KEVEVQDLLAmlRKLGFertmfdyrieqMSMGQKRKVALARS 436
Cdd:PRK13539 83 AM--KPALTVAENLE---FWAAF---LGGEELDIAAalEAVGLAPLAH--LPFGY-----------LSAGQKRRVALARL 141
|
170 180
....*....|....*....|....*....
gi 488922799 437 LCEEANLYIWDEPLNYLDVITREQIQNLV 465
Cdd:PRK13539 142 LVSNRPIWILDEPTAALDAAAVALFAELI 170
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
327-482 |
2.29e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 65.72 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNELIAkGNLKIRENLRISYLPQ---DFDQL---------------QGTL 388
Cdd:NF040873 11 VDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTS-GTVRRAGGARVAYVPQrseVPDSLpltvrdlvamgrwarRGLW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 389 EQFAAEKEVEVQDLLAMLRKLGFERTmfdyRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKF 468
Cdd:NF040873 90 RRLTRDDRAAVDDALERVGLADLAGR----QLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEE 165
|
170
....*....|....*..
gi 488922799 469 ---KPTLLVVEHDREFV 482
Cdd:NF040873 166 harGATVVVVTHDLELV 182
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-175 |
3.06e-12 |
|
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: 68.85 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKV--------ETNLKFNY----- 69
Cdd:TIGR02857 322 LEFSGVSVAYPGR-RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDpTEGSIavngvplaDADADSWRdqiaw 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 70 -------FPAKITEpqdSVRMvlmkitGRDYSDFWEVERELDQIGLAEEI--LEQTYAS--------LSPGQQTKALLAA 132
Cdd:TIGR02857 401 vpqhpflFAGTIAE---NIRL------ARPDASDAEIREALERAGLDEFVaaLPQGLDTpigeggagLSGGQAQRLALAR 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488922799 133 MFADQNSFQLIDEPTNHLDAAG----RDLLAKyLKQKQGYIVVSHDR 175
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETeaevLEALRA-LAQGRTVLLVTHRL 517
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
327-494 |
3.20e-12 |
|
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: 65.76 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLG-----QNELIAKGN-LKIRENLRISYLPQD---------------FDQLQ 385
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGiilpdSGEVLFDGKpLDIAARNRIGYLPEErglypkmkvidqlvyLAQLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 386 GTLEQFAAEkevevqDLLAMLRKLGFErtmfDY---RIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQ 462
Cdd:cd03269 99 GLKKEEARR------RIDEWLERLELS----EYankRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLK 168
|
170 180 190
....*....|....*....|....*....|....*
gi 488922799 463 NLVLKFK---PTLLVVEHDREFVQKIATQTVNLKK 494
Cdd:cd03269 169 DVIRELAragKTVILSTHQMELVEELCDRVLLLNK 203
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
330-478 |
4.47e-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: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 330 ELKKNERMVIQGENGSGKSTLIKAMLGQneLIAKGNLKIRENLRISYLPQDFDqlqgtleqfaaekevevqdllamlrkl 409
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQ--LIPNGDNDEWDGITPVYKPQYID--------------------------- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488922799 410 gfertmfdyrieqMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITR----EQIQNLVLKFKPTLLVVEHD 478
Cdd:cd03222 72 -------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRlnaaRAIRRLSEEGKKTALVVEHD 131
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
325-477 |
5.30e-12 |
|
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: 64.26 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIKAMLGqneliakgnlkirenlrisylpqDFDQLQGTLeQFAaekEVEVQDLLA 404
Cdd:cd03247 19 KNLSLELKQGEKIALLGRSGSGKSTLLQLLTG-----------------------DLKPQQGEI-TLD---GVPVSDLEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 405 MLRKLG---------FERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKF--KPTLL 473
Cdd:cd03247 72 ALSSLIsvlnqrpylFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVlkDKTLI 151
|
....
gi 488922799 474 VVEH 477
Cdd:cd03247 152 WITH 155
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-193 |
6.63e-12 |
|
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: 65.22 E-value: 6.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNQIKPVF--DQVALEIDASWKLGLIGRNGRGKTTLMKILQN-------QVEYEGKVETNLKFNYFPAK 73
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKalDDVSFSIKKGETLGLVGESGSGKSTLARAILGllkptsgSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 74 ITE----PQDSVRMV--LMKI------------TGRDYSDFWEVERE-LDQIGLAEEILEQTYASLSPGQQTKALLAAMF 134
Cdd:cd03257 81 RKEiqmvFQDPMSSLnpRMTIgeqiaeplrihgKLSKKEARKEAVLLlLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488922799 135 ADQNSFQLIDEPTNHLDAAGR----DLLAKyLKQKQG--YIVVSHDRYFLNQVIDHVISIDRAQI 193
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQaqilDLLKK-LQEELGltLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
325-461 |
6.64e-12 |
|
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: 66.03 E-value: 6.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIKAMLGqnELIAKGNlKIRENLRISYLPQDFDQLQGTL----------EQFAAE 394
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILG--ELEPSEG-KIKHSGRISFSSQFSWIMPGTIkeniifgvsyDEYRYK 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488922799 395 KEVEV----QDLLAMLRKlgfERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQI 461
Cdd:cd03291 131 SVVKAcqleEDITKFPEK---DNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-193 |
1.15e-11 |
|
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: 66.85 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNQIKPVF---DQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLKfnyfPA 72
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVravDDVSLTLRRGETLGLVGESGSGKSTLARLLlgllrptSGSILFDGKDLTKLS----RR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 73 KITEPQDSVRMV----------LMKI--------------TGRDYSDfwEVERELDQIGLAEEILEQTYASLSPGQQTKA 128
Cdd:COG1123 336 SLRELRRRVQMVfqdpysslnpRMTVgdiiaeplrlhgllSRAERRE--RVAELLERVGLPPDLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488922799 129 LLAAMFADQNSFQLIDEPTNHLDAAGR----DLLAKyLKQKQG--YIVVSHDRYFLNQVIDHVISIDRAQI 193
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQaqilNLLRD-LQRELGltYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-174 |
1.28e-11 |
|
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: 64.12 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQ------------NQVEYEGKVETNLKF---- 67
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrlndlipgapdeGEVLLDGKDIYDLDVdvle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 68 ------------NYFPAKItepQDSVRMVLmKITGRDYSDFWE--VERELDQIGLAEEILEQTYA-SLSPGQQTKALLAA 132
Cdd:cd03260 79 lrrrvgmvfqkpNPFPGSI---YDNVAYGL-RLHGIKLKEELDerVEEALRKAALWDEVKDRLHAlGLSGGQQQRLCLAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488922799 133 MFADQNSFQLIDEPTNHLDAAGR----DLLAKyLKQKQGYIVVSHD 174
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTakieELIAE-LKKEYTIVIVTHN 199
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-192 |
1.34e-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: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 20 VFDQVALEIDASWKLGLIGRNGRGKTTLMKILQN-QVEYEGKVETNLKFNYFPAKITEP-------QDSVRMVLmkiTGR 91
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGlSPPLAGRVLLNGGPLDFQRDSIARgllylghAPGIKTTL---SVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 92 DYSDFW-------EVERELDQIGLA--EEIleqTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYL 162
Cdd:cd03231 92 ENLRFWhadhsdeQVEEALARVGLNgfEDR---PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
170 180 190
....*....|....*....|....*....|..
gi 488922799 163 KQ--KQGYIVVSHDRYFLNQVIDHVISIDRAQ 192
Cdd:cd03231 169 AGhcARGGMVVLTTHQDLGLSEAGARELDLGF 200
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
327-480 |
2.03e-11 |
|
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: 63.89 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLG-----QNELIAKG----NLKiRENLRISYLPQD---------FDQLQGTL 388
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGfikpdSGKILLNGkditNLP-PEKRDISYVPQNyalfphmtvYKNIAYGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 389 EQFAAEKEVEVQDLLAMLRKLGFERtMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLK- 467
Cdd:cd03299 97 KKRKVDKKEIERKVLEIAEMLGIDH-LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKi 175
|
170
....*....|....*.
gi 488922799 468 ---FKPTLLVVEHDRE 480
Cdd:cd03299 176 rkeFGVTVLHVTHDFE 191
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
327-486 |
2.19e-11 |
|
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: 64.69 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLG--QNELIAKGNL----------------KIRENlRISYLPQD-------- 380
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGllPPPGITSGEIlfdgedllklsekelrKIRGR-EIQMIFQDpmtslnpv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 381 ---FDQLQGTLEQF------AAEKEVevqdlLAMLRKLGF---ERTMFDYRiEQMSMGQKRKVALARSLCEEANLYIWDE 448
Cdd:COG0444 103 mtvGDQIAEPLRIHgglskaEARERA-----IELLERVGLpdpERRLDRYP-HELSGGMRQRVMIARALALEPKLLIADE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488922799 449 PLNYLDVITREQIQNLVL----KFKPTLLVVEHD----REFVQKIA 486
Cdd:COG0444 177 PTTALDVTIQAQILNLLKdlqrELGLAILFITHDlgvvAEIADRVA 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-173 |
2.35e-11 |
|
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: 62.23 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMK-ILQNQVEYEGKVetnlkfnyfpakitepqdsvr 82
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARlILGLLRPTSGRV--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 83 mvlmKITGRDYSDfWEVERELDQIG-LAEEI--LEQTYAS--LSPGQQTKALLA-AMFADQnSFQLIDEPTNHLDAAGRD 156
Cdd:cd03246 60 ----RLDGADISQ-WDPNELGDHVGyLPQDDelFSGSIAEniLSGGQRQRLGLArALYGNP-RILVLDEPNSHLDVEGER 133
|
170 180
....*....|....*....|.
gi 488922799 157 LLAKYLK--QKQGY--IVVSH 173
Cdd:cd03246 134 ALNQAIAalKAAGAtrIVIAH 154
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-183 |
2.90e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.90 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQikPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEYEGKVETNLKFNYFPAKITEPQDSV-- 81
Cdd:PRK14258 8 IKVNNLSFYYDTQ--KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLnr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 82 --RMVLM--------------------KITGrdysdfWEVERELDQI--------GLAEEILEQTYAS---LSPGQQTKA 128
Cdd:PRK14258 86 lrRQVSMvhpkpnlfpmsvydnvaygvKIVG------WRPKLEIDDIvesalkdaDLWDEIKHKIHKSaldLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 129 LLAAMFADQNSFQLIDEPTNHLDAAGRD-----LLAKYLKQKQGYIVVSHDRYFLNQVID 183
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMkveslIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
327-477 |
3.89e-11 |
|
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: 62.61 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNE------LIakGNLKIRE----NLR--ISYLPQDFDQLQGTLEQFAAE 394
Cdd:cd03245 23 VSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKptsgsvLL--DGTDIRQldpaDLRrnIGYVPQDVTLFYGTLRDNITL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 395 KEVEVQD--LLAMLRKLGFERTM------FDYRI----EQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQ-I 461
Cdd:cd03245 101 GAPLADDerILRAAELAGVTDFVnkhpngLDLQIgergRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERlK 180
|
170
....*....|....*..
gi 488922799 462 QNLVLKFKP-TLLVVEH 477
Cdd:cd03245 181 ERLRQLLGDkTLIIITH 197
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-193 |
3.93e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 63.50 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEYEGKVetnLKFNYFPAKITEPQDSVR 82
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGT---ITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 83 MVLMKI----------TGRDYSDFW----EVERE---------LDQIGLaEEILEQTYASLSPGQQTKALLAAMFADQNS 139
Cdd:PRK13635 82 QVGMVFqnpdnqfvgaTVQDDVAFGleniGVPREemvervdqaLRQVGM-EDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488922799 140 FQLIDEPTNHLDAAGR-DLLA--KYLKQKQGYIVVS--HDryfLNQVI--DHVISIDRAQI 193
Cdd:PRK13635 161 IIILDEATSMLDPRGRrEVLEtvRQLKEQKGITVLSitHD---LDEAAqaDRVIVMNKGEI 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-207 |
4.54e-11 |
|
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: 64.96 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVETNlkfnyfpakitepqDSV 81
Cdd:TIGR03719 322 VIEAENLTKAFGD--KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQpDSGTIEIG--------------ETV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 82 RMVLMKiTGRDYSD-----FWEVERELDQIGLAE-EILEQTYAS---------------LSPGQQTKALLAAMFADQNSF 140
Cdd:TIGR03719 386 KLAYVD-QSRDALDpnktvWEEISGGLDIIKLGKrEIPSRAYVGrfnfkgsdqqkkvgqLSGGERNRVHLAKTLKSGGNV 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488922799 141 QLIDEPTNHLDAAGRDLLAKYLKQKQG-YIVVSHDRYFLNQVIDHVISID-RAQISSFKGNYETWAAER 207
Cdd:TIGR03719 465 LLLDEPTNDLDVETLRALEEALLNFAGcAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEYEEDK 533
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
325-480 |
4.80e-11 |
|
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: 62.64 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIKaMLGQNELIAKGNLKIrENLRISYLPQDFDQLQGTLEQFA------------ 392
Cdd:cd03300 17 DGVSLDIKEGEFFTLLGPSGCGKTTLLR-LIAGFETPTSGEILL-DGKDITNLPPHKRPVNTVFQNYAlfphltvfenia 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 393 ----------AEKEVEVQDLLAMLRKLGFERTMfdyrIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQ 462
Cdd:cd03300 95 fglrlkklpkAEIKERVAEALDLVQLEGYANRK----PSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQ 170
|
170 180
....*....|....*....|..
gi 488922799 463 ----NLVLKFKPTLLVVEHDRE 480
Cdd:cd03300 171 lelkRLQKELGITFVFVTHDQE 192
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-174 |
6.84e-11 |
|
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: 64.30 E-value: 6.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLKFNYFPAKIT- 75
Cdd:TIGR02868 335 LELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLaglldplQGEVTLDGVPVSSLDQDEVRRRVSv 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 76 EPQD------SVRMVLMkiTGR-DYSDfWEVERELDQIGLAEEI----------LEQTYASLSPGQQTKALLAAMFADQN 138
Cdd:TIGR02868 414 CAQDahlfdtTVRENLR--LARpDATD-EELWAALERVGLADWLralpdgldtvLGEGGARLSGGERQRLALARALLADA 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 488922799 139 SFQLIDEPTNHLDA-AGRDLLAKYLKQKQGY--IVVSHD 174
Cdd:TIGR02868 491 PILLLDEPTEHLDAeTADELLEDLLAALSGRtvVLITHH 529
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
309-490 |
7.95e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 62.08 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 309 LEADSLVLQRAGKLLNqpLNLELKKNERMVIQGENGSGKSTLIkamlgqnELIA------KGNLKIR-ENLR-------- 373
Cdd:COG3840 2 LRLDDLTYRYGDFPLR--FDLTIAAGERVAILGPSGAGKSTLL-------NLIAgflppdSGRILWNgQDLTalppaerp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 374 ISYLPQD---FDQLqgTLEQ------------FAAEKevevQDLLAMLRKLGFErTMFDYRIEQMSMGQKRKVALARSLC 438
Cdd:COG3840 73 VSMLFQEnnlFPHL--TVAQniglglrpglklTAEQR----AQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488922799 439 EEANLYIWDEPLNYLDVITREQIQNLV----LKFKPTLLVVEHDREFVQKIATQTV 490
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVdelcRERGLTVLMVTHDPEDAARIADRVL 201
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
327-478 |
8.29e-11 |
|
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: 64.30 E-value: 8.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGqneLIA--KGNLKI--------RENL---RISYLPQD---FDQlqgTLEQ 390
Cdd:TIGR02868 354 VSLDLPPGERVAILGPSGSGKSTLLATLAG---LLDplQGEVTLdgvpvsslDQDEvrrRVSVCAQDahlFDT---TVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 391 --FAAEKEVEVQDLLAMLRKLGFERTM------FDYRIEQM----SMGQKRKVALARSLCEEANLYIWDEPLNYLDVITR 458
Cdd:TIGR02868 428 nlRLARPDATDEELWAALERVGLADWLralpdgLDTVLGEGgarlSGGERQRLALARALLADAPILLLDEPTEHLDAETA 507
|
170 180
....*....|....*....|..
gi 488922799 459 EQIQNLVLKFKP--TLLVVEHD 478
Cdd:TIGR02868 508 DELLEDLLAALSgrTVVLITHH 529
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
327-488 |
8.60e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 62.03 E-value: 8.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAM-----LGQNELIAKG------NLKIREnLRIS--------YLpqdFDQLQGt 387
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeITSGDLIVDGlkvndpKVDERL-IRQEagmvfqqfYL---FPHLTA- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 388 LEQFA--------AEKEVEVQDLLAMLRKLGFERTMFDYRIEqMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITRE 459
Cdd:PRK09493 95 LENVMfgplrvrgASKEEAEKQARELLAKVGLAERAHHYPSE-LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRH 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 488922799 460 QiqnlVLKFKP-------TLLVVEHDREFVQKIATQ 488
Cdd:PRK09493 174 E----VLKVMQdlaeegmTMVIVTHEIGFAEKVASR 205
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
327-482 |
8.95e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.05 E-value: 8.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGqneLIA--KGNLKIRENLRISYLPQDFD---QLQGTLEQFAAEKE-VEVQ 400
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLG---LVApdEGVIKRNGKLRIGYVPQKLYldtTLPLTVNRFLRLRPgTKKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 401 DLLAMLRKLGFERtMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKPTL----LVVE 476
Cdd:PRK09544 100 DILPALKRVQAGH-LIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcavLMVS 178
|
....*.
gi 488922799 477 HDREFV 482
Cdd:PRK09544 179 HDLHLV 184
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
327-494 |
1.11e-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: 61.08 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGqneLIAKGNLKIRenlrisYLPQDFDQLQGTLEQFA-------------A 393
Cdd:cd03268 19 ISLHVKKGEIYGFLGPNGAGKTTTMKIILG---LIKPDSGEIT------FDGKSYQKNIEALRRIGalieapgfypnltA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 394 EKEVEVQDLLAMLRKLGFERTMF--------DYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLV 465
Cdd:cd03268 90 RENLRLLARLLGIRKKRIDEVLDvvglkdsaKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELI 169
|
170 180 190
....*....|....*....|....*....|..
gi 488922799 466 LKFKP---TLLVVEHDREFVQKIATQTVNLKK 494
Cdd:cd03268 170 LSLRDqgiTVLISSHLLSEIQKVADRIGIINK 201
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-193 |
1.13e-10 |
|
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: 61.01 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLM-------KILQNQVEYEGKVETNLK---------- 66
Cdd:cd03262 1 IEIKNLHKSFGD--FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLrcinlleEPDSGTIIIDGLKLTDDKkninelrqkv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 67 ------FNYFPAK-----ITEPqdsvrmvLMKITGRDYSDFWEVERE-LDQIGLAEEIleQTY-ASLSPGQQTKALLAAM 133
Cdd:cd03262 79 gmvfqqFNLFPHLtvlenITLA-------PIKVKGMSKAEAEERALElLEKVGLADKA--DAYpAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488922799 134 FADQNSFQLIDEPTNHLDA--AGR--DLLAKYLKQKQGYIVVSHDRYFLNQVIDHVISIDRAQI 193
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPelVGEvlDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
327-494 |
1.18e-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: 61.55 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKaMLgqNELIAKGNLKIREN-----------LR--ISYLPQDFD----------- 382
Cdd:cd03295 20 LNLEIAKGEFLVLIGPSGSGKTTTMK-MI--NRLIEPTSGEIFIDgedireqdpveLRrkIGYVIQQIGlfphmtveeni 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 383 ----QLQGTLEqfaAEKEVEVQDLLAMLrklGFERTMFDYRI-EQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVIT 457
Cdd:cd03295 97 alvpKLLKWPK---EKIRERADELLALV---GLDPAEFADRYpHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPIT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488922799 458 REQIQNLVLKFK----PTLLVVEHDREFVQKIATQTVNLKK 494
Cdd:cd03295 171 RDQLQEEFKRLQqelgKTIVFVTHDIDEAFRLADRIAIMKN 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
317-477 |
1.29e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 63.69 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 317 QRAGKLLNQpLNLELKKNERMVIQGENGSGKSTLI----KAMLGQNELIAKGNLKIRE----NLR--ISYLPQDFDQLQG 386
Cdd:PRK11160 350 DQPQPVLKG-LSLQIKAGEKVALLGRTGCGKSTLLqlltRAWDPQQGEILLNGQPIADyseaALRqaISVVSQRVHLFSA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 387 TLE---QFAAEKEVEVQdLLAMLRKLGFErtmfdYRIE--------------QMSMGQKRKVALARSLCEEANLYIWDEP 449
Cdd:PRK11160 429 TLRdnlLLAAPNASDEA-LIEVLQQVGLE-----KLLEddkglnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEP 502
|
170 180 190
....*....|....*....|....*....|.
gi 488922799 450 LNYLDVITREQIQNLVLKF---KpTLLVVEH 477
Cdd:PRK11160 503 TEGLDAETERQILELLAEHaqnK-TVLMITH 532
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
327-467 |
1.53e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.84 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNELIAKGNLKIRENlrISYLPQDFDQLQGTLEQ-------FAAEKEVEV 399
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGS--VAYVPQVSWIFNATVREnilfgsdFESERYWRA 713
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488922799 400 QDLLAMLRKL----GFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLK 467
Cdd:PLN03232 714 IDVTALQHDLdllpGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK 785
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
282-494 |
2.01e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 62.90 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 282 QLLKNIEIQDELQLNyQPYLGPQNNALLEADSLVLQRA-GKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGqneL 360
Cdd:COG4178 337 GFEEALEAADALPEA-ASRIETSEDGALALEDLTLRTPdGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG---L 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 361 --IAKGNLKIRENLRISYLPQDFDQLQGTL-EQFA---AEKEVEVQDLLAMLRKLGFERtmFDYRIEQ-------MSMGQ 427
Cdd:COG4178 413 wpYGSGRIARPAGARVLFLPQRPYLPLGTLrEALLypaTAEAFSDAELREALEAVGLGH--LAERLDEeadwdqvLSLGE 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488922799 428 KRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKP--TLLVVEHdREFVQKIATQTVNLKK 494
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPgtTVISVGH-RSTLAAFHDRVLELTG 558
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-193 |
2.16e-10 |
|
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: 60.58 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQIKPVF--DQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLK-------- 66
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILggldrptSGEVRVDGTDISKLSekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 67 ----------FN---YFPAKitepqDSVRMVLMkITGRDYSDFWEVERE-LDQIGLaEEILEQTYASLSPGQQTKALLAA 132
Cdd:cd03255 81 rrhigfvfqsFNllpDLTAL-----ENVELPLL-LAGVPKKERRERAEElLERVGL-GDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488922799 133 MFADQNSFQLIDEPTNHLDAAGR----DLLAKyLKQKQGY--IVVSHDRYFLNQViDHVISIDRAQI 193
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGkevmELLRE-LNKEAGTtiVVVTHDPELAEYA-DRIIELRDGKI 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-193 |
2.59e-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: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMK-ILQNQVEYEGKVetnlKFNYFPakITEPQDSVR 82
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQlLTGDLKPQQGEI----TLDGVP--VSDLEKALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 83 MVLMKITGRDYSdfwevereldqigLAEEILEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGR----DLL 158
Cdd:cd03247 75 SLISVLNQRPYL-------------FDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITErqllSLI 141
|
170 180 190
....*....|....*....|....*....|....*
gi 488922799 159 AKYLKQKQgYIVVSHDRYFLNQViDHVISIDRAQI 193
Cdd:cd03247 142 FEVLKDKT-LIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
327-461 |
3.10e-10 |
|
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: 63.01 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNEliaKGNLKIRENLRISYLPQDFDQLQGTLEQ---FAAE--------- 394
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELE---PSEGKIKHSGRISFSPQTSWIMPGTIKDniiFGLSydeyrytsv 521
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488922799 395 -KEVEVQDLLAMLRKLgfERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQI 461
Cdd:TIGR01271 522 iKACQLEEDIALFPEK--DKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-190 |
3.59e-10 |
|
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: 59.54 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 36 LIGRNGRGKTTLMKILqnQVEYEGKVETNLKFNYFPAKITEPQD---SVRMVLMKITGRDYsdfwEVERELDQIGLA--- 109
Cdd:cd03240 27 IVGQNGAGKTTIIEAL--KYALTGELPPNSKGGAHDPKLIREGEvraQVKLAFENANGKKY----TITRSLAILENVifc 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 110 --EEI---LEQTYASLSPGQQTKALLA-----AMFADQN-SFQLIDEPTNHLDAAGR-----DLLAKYLKQKQG-YIVVS 172
Cdd:cd03240 101 hqGESnwpLLDMRGRCSGGEKVLASLIirlalAETFGSNcGILALDEPTTNLDEENIeeslaEIIEERKSQKNFqLIVIT 180
|
170
....*....|....*...
gi 488922799 173 HDRYFLnQVIDHVISIDR 190
Cdd:cd03240 181 HDEELV-DAADHIYRVEK 197
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
327-494 |
3.68e-10 |
|
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: 59.73 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQnELIAKGNLKIR----ENLRISYLP----------QDFDQL--QGTLEQ 390
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKE-ELPTSGTIRVNgqdvSDLRGRAIPylrrkigvvfQDFRLLpdRNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 391 FAAEKEV----------EVQDLLAMLRKLGFERTMfdyrIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQ 460
Cdd:cd03292 99 VAFALEVtgvppreirkRVPAALELVGLSHKHRAL----PAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 488922799 461 IQNLVLKFK---PTLLVVEHDREFVQKIATQTVNLKK 494
Cdd:cd03292 175 IMNLLKKINkagTTVVVATHAKELVDTTRHRVIALER 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
327-486 |
3.75e-10 |
|
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: 59.69 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKaMLG------QNELIAKGNLKIRENL----RISYLPQDF---DQLQGT--LEQF 391
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIK-MLTtllkptSGRATVAGHDVVREPRevrrRIGIVFQDLsvdDELTGWenLYIH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 392 A-------AEKEVEVQDLLAMLRKLGFErtmfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQ---- 460
Cdd:cd03265 98 ArlygvpgAERRERIDELLDFVGLLEAA----DRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHvwey 173
|
170 180
....*....|....*....|....*.
gi 488922799 461 IQNLVLKFKPTLLVVEHDREFVQKIA 486
Cdd:cd03265 174 IEKLKEEFGMTILLTTHYMEEAEQLC 199
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-174 |
4.56e-10 |
|
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: 59.41 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDN--QIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEY-EGKVEtnlkfnYFPAKITEPQDS 80
Cdd:cd03293 1 LEVRNVSKTYGGggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPtSGEVL------VDGEPVTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 81 VRMVL------------------MKITGRDYSDFWE-VERELDQIGLAEeiLEQTY-ASLSPGQQTKALLAAMFADQNSF 140
Cdd:cd03293 75 RGYVFqqdallpwltvldnvalgLELQGVPKAEARErAEELLELVGLSG--FENAYpHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 488922799 141 QLIDEPTNHLDAAGR-----DLLAKYLKQKQGYIVVSHD 174
Cdd:cd03293 153 LLLDEPFSALDALTReqlqeELLDIWRETGKTVLLVTHD 191
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-193 |
4.57e-10 |
|
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: 59.34 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQIkPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLKFNYFP---AK 73
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIykeelptSGTIRVNGQDVSDLRGRAIPylrRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 74 I-TEPQDSvRMVL-----------MKITGRDYSDFWE-VERELDQIGLAEEilEQTYAS-LSPGQQTKALLAAMFADQNS 139
Cdd:cd03292 80 IgVVFQDF-RLLPdrnvyenvafaLEVTGVPPREIRKrVPAALELVGLSHK--HRALPAeLSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488922799 140 FQLIDEPTNHLDAAGRDLLAKYLKQ--KQGYIVV--SHDRYFLNQVIDHVISIDRAQI 193
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKinKAGTTVVvaTHAKELVDTTRHRVIALERGKL 214
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
327-478 |
4.60e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 61.20 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKaMLGQNELIAKGNLKIRENlRISYLPQDFDQLQGTLEQFAAEKEVEVQDLLAML 406
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLR-MIAGLEDITSGDLFIGEK-RMNDVPPAERGVGMVFQSYALYPHLSVAENMSFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 407 RKL-GFERTMFDYRIEQ-----------------MSMGQKRKVALARSLCEEANLYIWDEPLNYLD----VITREQIQNL 464
Cdd:PRK11000 100 LKLaGAKKEEINQRVNQvaevlqlahlldrkpkaLSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQMRIEISRL 179
|
170
....*....|....
gi 488922799 465 VLKFKPTLLVVEHD 478
Cdd:PRK11000 180 HKRLGRTMIYVTHD 193
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
327-477 |
4.82e-10 |
|
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: 59.43 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNELiAKGNLKI---------RENLR--ISYLPQDFDQLQGTL------- 388
Cdd:cd03244 23 ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL-SSGSILIdgvdiskigLHDLRsrISIIPQDPVLFSGTIrsnldpf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 389 EQFAAEKEVEVQDLLAMLRKLGFERTMFDYRIE----QMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNL 464
Cdd:cd03244 102 GEYSDEELWQALERVGLKEFVESLPGGLDTVVEeggeNLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKT 181
|
170
....*....|....*
gi 488922799 465 V-LKFK-PTLLVVEH 477
Cdd:cd03244 182 IrEAFKdCTVLTIAH 196
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-155 |
5.07e-10 |
|
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: 59.13 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQIkpVFDQVALEIDASWkLGLIGRNGRGKTTLMKILQNQVE-YEGKVETN-LKFNYFPAKITE----- 76
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPpSSGTIRIDgQDVLKQPQKLRRrigyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 77 PQDSvrMVLMKITGRDYSDF--W-----------EVERELDQIGLAEEiLEQTYASLSPGQ-QTKALLAAMFADQnSFQL 142
Cdd:cd03264 78 PQEF--GVYPNFTVREFLDYiaWlkgipskevkaRVDEVLELVNLGDR-AKKKIGSLSGGMrRRVGIAQALVGDP-SILI 153
|
170
....*....|...
gi 488922799 143 IDEPTNHLDAAGR 155
Cdd:cd03264 154 VDEPTAGLDPEER 166
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-193 |
6.14e-10 |
|
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: 59.27 E-value: 6.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQIK-------------------PVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEY 57
Cdd:cd03267 1 IEVSNLSKSYRVYSKepgligslkslfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILsgllqptSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 58 EGKVETNLKfNYFPAKIT-------------EPQDSVRMvLMKITGRDYSDFWEVERELDQIGLAEEILEQTYASLSPGQ 124
Cdd:cd03267 81 AGLVPWKRR-KKFLRRIGvvfgqktqlwwdlPVIDSFYL-LAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488922799 125 QTKALLAAMFADQNSFQLIDEPTNHLDA----AGRDLLAKYLKQKQGYIVV-SHDRYFLNQVIDHVISIDRAQI 193
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVvaqeNIRNFLKEYNRERGTTVLLtSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
309-494 |
6.85e-10 |
|
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: 57.93 E-value: 6.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 309 LEADSLVLQR-AGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMlgqNEL--IAKGNLKIRENLRISYLPQDFDQLQ 385
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL---AGLwpWGSGRIGMPEGEDLLFLPQRPYLPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 386 GTLEQfaaekevevQDLLAMLRKLgfertmfdyrieqmSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLV 465
Cdd:cd03223 78 GTLRE---------QLIYPWDDVL--------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
170 180
....*....|....*....|....*....
gi 488922799 466 LKFKPTLLVVEHdREFVQKIATQTVNLKK 494
Cdd:cd03223 135 KELGITVISVGH-RPSLWKFHDRVLDLDG 162
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
315-478 |
7.35e-10 |
|
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: 59.58 E-value: 7.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 315 VLQRAGKLL-NQPLNLELKKNERMVIQGENGSGKSTLIKAMlgqNELI------------------AKGNLKIRENlRIS 375
Cdd:cd03294 30 ILKKTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCI---NRLIeptsgkvlidgqdiaamsRKELRELRRK-KIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 376 YLPQDFD---------------QLQGTLEQFAAEKEVEVQDLLAMLrklGFErtmfDYRIEQMSMGQKRKVALARSLCEE 440
Cdd:cd03294 106 MVFQSFAllphrtvlenvafglEVQGVPRAEREERAAEALELVGLE---GWE----HKYPDELSGGMQQRVGLARALAVD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488922799 441 ANLYIWDEPLNYLDVITREQIQNLVL----KFKPTLLVVEHD 478
Cdd:cd03294 179 PDILLMDEAFSALDPLIRREMQDELLrlqaELQKTIVFITHD 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
327-480 |
7.49e-10 |
|
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: 58.00 E-value: 7.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGqNELIAKGNLKI---------RENLR--ISYLPQDFDQLQGTLeqfaaek 395
Cdd:cd03246 21 VSFSIEPGESLAIIGPSGSGKSTLARLILG-LLRPTSGRVRLdgadisqwdPNELGdhVGYLPQDDELFSGSI------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 396 eveVQDLLamlrklgfertmfdyrieqmSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFK---PTL 472
Cdd:cd03246 93 ---AENIL--------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaagATR 149
|
....*...
gi 488922799 473 LVVEHDRE 480
Cdd:cd03246 150 IVIAHRPE 157
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
327-494 |
7.62e-10 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 58.91 E-value: 7.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQnELIAKG-------NL-KIREN----LR--ISYLPQDFdQL-------- 384
Cdd:COG2884 21 VSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE-ERPTSGqvlvngqDLsRLKRReipyLRrrIGVVFQDF-RLlpdrtvye 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 385 --------QGTleqfaAEKEVEvQDLLAMLRKLGFERTMfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVI 456
Cdd:COG2884 99 nvalplrvTGK-----SRKEIR-RRVREVLDLVGLSDKA-KALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488922799 457 TREQIQNLVLKFK---PTLLVVEHDREFVQKIATQTVNLKK 494
Cdd:COG2884 172 TSWEIMELLEEINrrgTTVLIATHDLELVDRMPKRVLELED 212
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
307-454 |
8.51e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.71 E-value: 8.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 307 ALLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLG-------QNELIAKGNLKIRENLRISYL-- 377
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGllhvesgQIQIDGKTATRGDRSRFMAYLgh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 378 ----PQDFDQLQgTLEQFAAEKEVEVQDL----LAMLRKLGFERTMfdyrIEQMSMGQKRKVALARSLCEEANLYIWDEP 449
Cdd:PRK13543 90 lpglKADLSTLE-NLHFLCGLHGRRAKQMpgsaLAIVGLAGYEDTL----VRQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
....*
gi 488922799 450 LNYLD 454
Cdd:PRK13543 165 YANLD 169
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
325-478 |
9.20e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 60.09 E-value: 9.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIKAMLGQnELIAKGNLKIRENL---------RISYLPQDFD------------- 382
Cdd:COG3839 20 KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGL-EDPTSGEILIGGRDvtdlppkdrNIAMVFQSYAlyphmtvyeniaf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 383 --QLQGTLeqfAAEKEVEVQDLLAMLRklgfertmfdyrIE--------QMSMGQKRKVALARSLCEEANLYIWDEPLNY 452
Cdd:COG3839 99 plKLRKVP---KAEIDRRVREAAELLG------------LEdlldrkpkQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190
....*....|....*....|....*....|
gi 488922799 453 LD----VITREQIQNLVLKFKPTLLVVEHD 478
Cdd:COG3839 164 LDaklrVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
327-482 |
9.28e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 9.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQ-NELIAKGNLKIRENlrisylpqDFDQLQGTLEQFAAEKEV-EVQDLLA 404
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlKGTPVAGCVDVPDN--------QFGREASLIDAIGRKGDFkDAVELLN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 405 MLrKLGfERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLD----VITREQIQNLVLKFKPTLLVVEHDRE 480
Cdd:COG2401 121 AV-GLS-DAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtaKRVARNLQKLARRAGITLVVATHHYD 198
|
..
gi 488922799 481 FV 482
Cdd:COG2401 199 VI 200
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
327-477 |
1.02e-09 |
|
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: 58.78 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNElIAKGNLKI---------RENLR--ISYLPQDFDQLQGTL------- 388
Cdd:cd03254 22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYD-PQKGQILIdgidirdisRKSLRsmIGVVLQDTFLFSGTImenirlg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 389 -------EQFAAEKEVEVQDLLAMLRKlGFErTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQI 461
Cdd:cd03254 101 rpnatdeEVIEAAKEAGAHDFIMKLPN-GYD-TVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLI 178
|
170
....*....|....*...
gi 488922799 462 QNLVLKFKP--TLLVVEH 477
Cdd:cd03254 179 QEALEKLMKgrTSIIIAH 196
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-180 |
1.04e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.01 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLKfnyfPAKITE 76
Cdd:PRK13548 3 LEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsgelspdSGEVRLNGRPLADWS----PAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 77 -----PQDS-----------VRMvlmkitGRdySDFWEVERELDQigLAEEILEQT---------YASLSPGQQTKALLA 131
Cdd:PRK13548 77 rravlPQHSslsfpftveevVAM------GR--APHGLSRAEDDA--LVAAALAQVdlahlagrdYPQLSGGEQQRVQLA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 132 ---AMFADQNSFQ---LIDEPTNHLDAAGRDL---LAKYLKQKQGY--IVVSHDryfLNQ 180
Cdd:PRK13548 147 rvlAQLWEPDGPPrwlLLDEPTSALDLAHQHHvlrLARQLAHERGLavIVVLHD---LNL 203
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-151 |
1.44e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 59.86 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 1 MGIIQLKNVSFSYDNQikPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQN-------QVEYEGKVETNLKFNYFPAK 73
Cdd:PRK09536 1 MPMIDVSDLSVEFGDT--TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGtltptagTVLVAGDDVEALSARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 74 I-TEPQD-------SVRMV--------LMKITGRDYSDFWEVERELDQIGLAEeILEQTYASLSPGQQTKALLAAMFADQ 137
Cdd:PRK09536 79 VaSVPQDtslsfefDVRQVvemgrtphRSRFDTWTETDRAAVERAMERTGVAQ-FADRPVTSLSGGERQRVLLARALAQA 157
|
170
....*....|....
gi 488922799 138 NSFQLIDEPTNHLD 151
Cdd:PRK09536 158 TPVLLLDEPTASLD 171
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
328-490 |
1.50e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.05 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 328 NLELKKNERMVIQGENGSGKSTLIKamlgqneLIA------KGNLKIR-ENLR--------ISYLPQD---FDQLqgTLE 389
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLN-------LIAgfltpaSGSLTLNgQDHTttppsrrpVSMLFQEnnlFSHL--TVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 390 Q-----------FAAEKEVEVQDllaMLRKLGFErTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITR 458
Cdd:PRK10771 90 QniglglnpglkLNAAQREKLHA---IARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 488922799 459 EQIQNLVLKF----KPTLLVVEHDREFVQKIATQTV 490
Cdd:PRK10771 166 QEMLTLVSQVcqerQLTLLMVSHSLEDAARIAPRSL 201
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
303-480 |
1.56e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.46 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 303 PQNNA------LLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKaMLGQNELIAKGNLkIRENLRISY 376
Cdd:PRK11607 8 PQAKTrkaltpLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLR-MLAGFEQPTAGQI-MLDGVDLSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 377 LP----------QDFDQL-QGTLEQ---FA--------AEKEVEVQDLLAMLRKLGFERTmfdyRIEQMSMGQKRKVALA 434
Cdd:PRK11607 86 VPpyqrpinmmfQSYALFpHMTVEQniaFGlkqdklpkAEIASRVNEMLGLVHMQEFAKR----KPHQLSGGQRQRVALA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488922799 435 RSLCEEANLYIWDEPLNYLDVITREQIQNLVL----KFKPTLLVVEHDRE 480
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVdileRVGVTCVMVTHDQE 211
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
327-494 |
1.58e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 59.02 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMlgqNELI--AKGNLKIREnLRISYLPQD-----FDQLQGTLEQF-------- 391
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNI---NALLkpTTGTVTVDD-ITITHKTKDkyirpVRKRIGMVFQFpesqlfed 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 392 AAEKEVEV-------------QDLLAMLRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITR 458
Cdd:PRK13646 102 TVEREIIFgpknfkmnldevkNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488922799 459 EQIQNLVLKFK----PTLLVVEHDREFVQKIATQTVNLKK 494
Cdd:PRK13646 182 RQVMRLLKSLQtdenKTIILVSHDMNEVARYADEVIVMKE 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-175 |
1.88e-09 |
|
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: 57.53 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQikPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLkfnyfPAKite 76
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIaglerpdSGEILIDGRDVTGV-----PPE--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 77 pQDSVRMVLmkitgRDYSDF-----WE-------------------VERELDQIGLaeEILEQTYAS-LSPGQQTKALLA 131
Cdd:cd03259 71 -RRNIGMVF-----QDYALFphltvAEniafglklrgvpkaeirarVRELLELVGL--EGLLNRYPHeLSGGQQQRVALA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488922799 132 AMFADQNSFQLIDEPTNHLDAAGRDLLAKYLK---QKQGY--IVVSHDR 175
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKelqRELGIttIYVTHDQ 191
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-193 |
2.26e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 58.10 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNL-------KFN 68
Cdd:PRK11231 2 TLRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFarlltpqSGTVFLGDKPISMLssrqlarRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 69 YFPAKITEPQD-SVRMVLMkiTGRD-YSDFW---------EVERELDQIGLaEEILEQTYASLSPGQQTKALLAAMFADQ 137
Cdd:PRK11231 80 LLPQHHLTPEGiTVRELVA--YGRSpWLSLWgrlsaednaRVNQAMEQTRI-NHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488922799 138 NSFQLIDEPTNHLDAAGRDLLAKYLKQ--KQG--YIVVSHDryfLNQV---IDHVISIDRAQI 193
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRElnTQGktVVTVLHD---LNQAsryCDHLVVLANGHV 216
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-171 |
2.38e-09 |
|
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: 56.98 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 19 PVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQN-QVEYEGKVETNlkfnyfPAKITEPQDSVRMVL--------MK-- 87
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGlLRPDSGEVRWN------GTPLAEQRDEPHENIlylghlpgLKpe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 88 ITGRDYSDFW---------EVERELDQIGLAEeiLEQT-YASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDL 157
Cdd:TIGR01189 88 LSALENLHFWaaihggaqrTIEDALAAVGLTG--FEDLpAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170
....*....|....*.
gi 488922799 158 LAKYLKQ--KQGYIVV 171
Cdd:TIGR01189 166 LAGLLRAhlARGGIVL 181
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-194 |
2.83e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.41 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNQikPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILqNQVE--------------YEGKVETNL--- 65
Cdd:PRK09493 1 MIEFKNVSKHFGPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEeitsgdlivdglkvNDPKVDERLirq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 66 -------KFNYFPaKITePQDSVRMVLMKITGRDYSDFWEVEREL-DQIGLAEEIleQTYAS-LSPGQQTKALLAAMFAD 136
Cdd:PRK09493 78 eagmvfqQFYLFP-HLT-ALENVMFGPLRVRGASKEEAEKQARELlAKVGLAERA--HHYPSeLSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488922799 137 QNSFQLIDEPTNHLDAAGRDLLAKYLKQ--KQG--YIVVSHDRYFLNQVIDHVISIDRAQIS 194
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDlaEEGmtMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
339-478 |
3.26e-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: 57.76 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 339 IQGENGSGKSTLIKAMLGQneliAKGNL--------------------------KIRE-NLRISYLPQDFDQL----QGT 387
Cdd:cd03236 31 LVGPNGIGKSTALKILAGK----LKPNLgkfddppdwdeildefrgselqnyftKLLEgDVKVIVKPQYVDLIpkavKGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 388 LEQFAAEK-EVEVQDLLamLRKLGFERTMfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLV- 465
Cdd:cd03236 107 VGELLKKKdERGKLDEL--VDQLELRHVL-DRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIr 183
|
170
....*....|....*
gi 488922799 466 --LKFKPTLLVVEHD 478
Cdd:cd03236 184 elAEDDNYVLVVEHD 198
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
325-469 |
3.29e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.88 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNELIAkGNLKIRE-----------NLRISYLPQD------------- 380
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTS-GELLIDDhplhfgdysyrSQRIRMIFQDpstslnprqrisq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 381 -FD---QLQGTLEQFAAEKEVevqdlLAMLRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVI 456
Cdd:PRK15112 109 iLDfplRLNTDLEPEQREKQI-----IETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170
....*....|...
gi 488922799 457 TREQIQNLVLKFK 469
Cdd:PRK15112 184 MRSQLINLMLELQ 196
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-185 |
4.52e-09 |
|
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: 58.66 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVS---FSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVETNLKFNYfpAKITEPQ 78
Cdd:TIGR03269 279 IIKVRNVSkryISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEpTSGEVNVRVGDEW--VDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 79 DSVRMVLMKITG---RDYSDFWE---VERELDQIGL------------------------AEEILEQTYASLSPGQQTKA 128
Cdd:TIGR03269 357 PDGRGRAKRYIGilhQEYDLYPHrtvLDNLTEAIGLelpdelarmkavitlkmvgfdeekAEEILDKYPDELSEGERHRV 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488922799 129 LLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYL-----KQKQGYIVVSHDRYFLNQVIDHV 185
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkareEMEQTFIIVSHDMDFVLDVCDRA 498
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
22-193 |
5.95e-09 |
|
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: 56.68 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 22 DQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLKfnyfPAKITE---------PQ------- 78
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsgflrptSGSVLFDGEDITGLP----PHEIARlgigrtfqiPRlfpeltv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 79 -DSVRMVLMKITGRDYSDFWEVERELDQIGLAEEILEQ---------TYASLSPGQQtKAL-LAAMFADQNSFQLIDEPT 147
Cdd:cd03219 93 lENVMVAAQARTGSGLLLARARREEREARERAEELLERvgladladrPAGELSYGQQ-RRLeIARALATDPKLLLLDEPA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488922799 148 NHLDAAGRDLLAKYLKQ--KQGY--IVVSHDRYFLNQVIDHVISIDRAQI 193
Cdd:cd03219 172 AGLNPEETEELAELIRElrERGItvLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
321-486 |
6.34e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.59 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 321 KLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMlgqNELIAKGNLKIRENLRISYLPQD-------------------- 380
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL---NRLIEIYDSKIKVDGKVLYFGKDifqidaiklrkevgmvfqqp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 381 --------FDQLQGTLEQFAAEKEVEVQDLLA-MLRKLGFERTMFDY---RIEQMSMGQKRKVALARSLCEEANLYIWDE 448
Cdd:PRK14246 100 npfphlsiYDNIAYPLKSHGIKEKREIKKIVEeCLRKVGLWKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488922799 449 PLNYLDVITREQIQNLV--LKFKPTLLVVEHDREFVQKIA 486
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLIteLKNEIAIVIVSHNPQQVARVA 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
326-448 |
7.58e-09 |
|
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: 57.89 E-value: 7.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 326 PLNLELKKNERMVIQGENGSGKSTLIKAMLG-----------QNELIAKGNlkiRENLR--IS------YLpqdFDQLQG 386
Cdd:COG4615 350 PIDLTIRRGELVFIVGGNGSGKSTLAKLLTGlyrpesgeillDGQPVTADN---REAYRqlFSavfsdfHL---FDRLLG 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488922799 387 TLEQFAAEKeveVQDLLAML---RKLGFERTMFDYRieQMSMGQKRKVALARSLCEEANLYIWDE 448
Cdd:COG4615 424 LDGEADPAR---ARELLERLeldHKVSVEDGRFSTT--DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
327-467 |
7.64e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 7.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNELIAKGNLKIREnlRISYLPQDFDQLQGTLEQ-------FAAEKEVEV 399
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRG--TVAYVPQVSWIFNATVRDnilfgspFDPERYERA 713
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488922799 400 QDLLAMLRKL----GFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLK 467
Cdd:PLN03130 714 IDVTALQHDLdllpGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIK 785
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
328-486 |
7.74e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 7.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 328 NLELKKNERMVIQGENGSGKSTLIKAMlgQNELIA-KGNLKIRENlRISYLpqDFDQLQGTLEQ---------------- 390
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARAL--AGELPLlSGERQSQFS-HITRL--SFEQLQKLVSDewqrnntdmlspgedd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 391 ---FAAE---KEVEVQDLLAMLRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNL 464
Cdd:PRK10938 98 tgrTTAEiiqDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAEL 177
|
170 180
....*....|....*....|....*....
gi 488922799 465 V--LKFKPTLLVVEHDR-----EFVQKIA 486
Cdd:PRK10938 178 LasLHQSGITLVLVLNRfdeipDFVQFAG 206
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-159 |
8.42e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.65 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 18 KPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKvetNLKFNYFPAKIT--EPQDSVRMVLmki 88
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIagllppaAGTIKLDGG---DIDDPDVAEACHylGHRNAMKPAL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 89 TGRDYSDFW---------EVERELDQIGLAEeILEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLA 159
Cdd:PRK13539 89 TVAENLEFWaaflggeelDIAAALEAVGLAP-LAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFA 167
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
327-494 |
8.73e-09 |
|
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: 56.00 E-value: 8.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKaMLGQNELIAKGNLKI--------------------RENLRISYLpqdfdqLQG 386
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLR-LLAGIYPPDSGTVTVrgrvssllglgggfnpeltgRENIYLNGR------LLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 387 TLEQFAAEKEVEVQDllamLRKLG-FertmFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQ----I 461
Cdd:cd03220 114 LSRKEIDEKIDEIIE----FSELGdF----IDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKcqrrL 185
|
170 180 190
....*....|....*....|....*....|...
gi 488922799 462 QNLVLKFKpTLLVVEHDREFVQKIATQTVNLKK 494
Cdd:cd03220 186 RELLKQGK-TVILVSHDPSSIKRLCDRALVLEK 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
321-461 |
1.01e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.25 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 321 KLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNElIAKGnlKIRENLRISYLPQDFDQLQGTLEQ----FAAEKE 396
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFE-ISEG--RVWAERSIAYVPQQAWIMNATVRGnilfFDEEDA 749
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488922799 397 VEVQD------LLAMLRKL--GFERTMFDYRIeQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQI 461
Cdd:PTZ00243 750 ARLADavrvsqLEADLAQLggGLETEIGEKGV-NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV 821
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-188 |
1.01e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.33 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 5 QLKNVSFSYDNQIkpVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-QNQVEYEGKVETN-------------LKFNYF 70
Cdd:PRK10575 13 ALRNVSFRVPGRT--LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLgRHQPPSEGEILLDaqpleswsskafaRKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 71 PAKITEPQDSVRMVLMKI--------TGR-DYSDFWEVERELDQIGLaEEILEQTYASLSPGQQTKALLAAMFADQNSFQ 141
Cdd:PRK10575 91 PQQLPAAEGMTVRELVAIgrypwhgaLGRfGAADREKVEEAISLVGL-KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488922799 142 LIDEPTNHLDAAGR-DLLA--KYLKQKQGY--IVVSHDRYFLNQVIDHVISI 188
Cdd:PRK10575 170 LLDEPTSALDIAHQvDVLAlvHRLSQERGLtvIAVLHDINMAARYCDYLVAL 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
33-245 |
1.03e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 33 KLGLIGRNGRGKTTLMKILQNQVEYE-GKVE--TNLKFNYFPA--KITEPQDSVRMVL------MKITGRD-----Y-SD 95
Cdd:PRK11147 347 KIALIGPNGCGKTTLLKLMLGQLQADsGRIHcgTKLEVAYFDQhrAELDPEKTVMDNLaegkqeVMVNGRPrhvlgYlQD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 96 F-WEVERELDQIglaeeileqtyASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYLKQKQG-YIVVSH 173
Cdd:PRK11147 427 FlFHPKRAMTPV-----------KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGtVLLVSH 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488922799 174 DRYFL-NQVIDHVISIDRAQISSFKGNYETWAAERANAdereISLNATMKkdiKKLEQATRQKQEWSRATERK 245
Cdd:PRK11147 496 DRQFVdNTVTECWIFEGNGKIGRYVGGYHDARQQQAQY----LALKQPAV---KKKEEAAAPKAETVKRSSKK 561
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
327-462 |
1.04e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 57.48 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNElIAKGNLKI---------RENLR--ISYLPQDFDQLQGTLEQ---FA 392
Cdd:COG1132 359 ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD-PTSGRILIdgvdirdltLESLRrqIGVVPQDTFLFSGTIREnirYG 437
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488922799 393 AEK--EVEVQDLLAMLRKLGFERTM---FDYRIEQ----MSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQ 462
Cdd:COG1132 438 RPDatDEEVEEAAKAAQAHEFIEALpdgYDTVVGErgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQ 516
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-190 |
1.13e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.89 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVETN--LKFNYFPAKI----T 75
Cdd:PRK09544 4 LVSLENVSVSFGQ--RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVApDEGVIKRNgkLRIGYVPQKLyldtT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 76 EPQDSVRMVLMKiTGRDYSDFWEVERELDqiglAEEILEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGR 155
Cdd:PRK09544 82 LPLTVNRFLRLR-PGTKKEDILPALKRVQ----AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488922799 156 DLLAKYLKQKQ-----GYIVVSHDRYFLNQVIDHVISIDR 190
Cdd:PRK09544 157 VALYDLIDQLRreldcAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-151 |
1.23e-08 |
|
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: 55.31 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 2 GIIQLKNVSFSYDNQiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLKFNYFPAKI 74
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLmrfydpqKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 75 -TEPQDSV---RMVLMKIT-GRDYSDFWEVERELDQIGLAEEI--LEQTY--------ASLSPGQ-QTKALLAAMFADQN 138
Cdd:cd03254 80 gVVLQDTFlfsGTIMENIRlGRPNATDEEVIEAAKEAGAHDFImkLPNGYdtvlgengGNLSQGErQLLAIARAMLRDPK 159
|
170
....*....|...
gi 488922799 139 SFqLIDEPTNHLD 151
Cdd:cd03254 160 IL-ILDEATSNID 171
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
328-464 |
1.27e-08 |
|
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: 53.97 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 328 NLELKKNERMVIQGENGSGKSTLIKAMLGqneliakgnlkirenlrisYLPQDfdqlQGTLeqFAAEKEVEVQDLLAMLR 407
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSG-------------------LYKPD----SGEI--LVDGKEVSFASPRDARR 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 488922799 408 kLGFErtmfdyRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLdviTREQIQNL 464
Cdd:cd03216 75 -AGIA------MVYQLSVGERQMVEIARALARNARLLILDEPTAAL---TPAEVERL 121
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
318-461 |
1.41e-08 |
|
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: 54.48 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 318 RAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQ-NELIAKGNLKI------RENLR--ISYLPQDfDQLQGTL 388
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrTGLGVSGEVLIngrpldKRSFRkiIGYVPQD-DILHPTL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488922799 389 E-----QFAAEkevevqdllamLRKLgfertmfdyrieqmSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQI 461
Cdd:cd03213 98 TvretlMFAAK-----------LRGL--------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
327-490 |
1.54e-08 |
|
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: 54.84 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMlgqNEL--IAKGNLKIrENLRISYLPQDFDQLQ---GTLEQ----FA----- 392
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCI---NLLeePDSGTIII-DGLKLTDDKKNINELRqkvGMVFQqfnlFPhltvl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 393 ---AEKEVEVQDL---------LAMLRKLGFERTMfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLD------ 454
Cdd:cd03262 95 eniTLAPIKVKGMskaeaeeraLELLEKVGLADKA-DAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpelvge 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 488922799 455 VItrEQIQNLVlKFKPTLLVVEHDREFVQKIATQTV 490
Cdd:cd03262 174 VL--DVMKDLA-EEGMTMVVVTHEMGFAREVADRVI 206
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
393-479 |
1.56e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 56.27 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 393 AEKEVEVQDLLAMLRKLGFErtmfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDV----ITREQIQNLVLKF 468
Cdd:PRK11432 111 EERKQRVKEALELVDLAGFE----DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAnlrrSMREKIRELQQQF 186
|
90
....*....|.
gi 488922799 469 KPTLLVVEHDR 479
Cdd:PRK11432 187 NITSLYVTHDQ 197
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
327-486 |
1.69e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 55.82 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLG-----------QNELIAKGNLK---IRENLRISYLPQDFDQLQGTLEQFA 392
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGllkptsgkiiiDGVDITDKKVKlsdIRKKVGLVFQYPEYQLFEETIEKDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 393 A---------EKEVEVQDLLAM-LRKLGFErTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITRE--- 459
Cdd:PRK13637 106 AfgpinlglsEEEIENRVKRAMnIVGLDYE-DYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDeil 184
|
170 180
....*....|....*....|....*...
gi 488922799 460 -QIQNLVLKFKPTLLVVEHDREFVQKIA 486
Cdd:PRK13637 185 nKIKELHKEYNMTIILVSHSMEDVAKLA 212
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
326-448 |
1.75e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.90 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 326 PLNLELKKNERMVIQGENGSGKSTLikAML---------GQ----NELIAKGNlkiRENLR--ISYLPQD---FDQLQGT 387
Cdd:PRK10522 341 PINLTIKRGELLFLIGGNGSGKSTL--AMLltglyqpqsGEilldGKPVTAEQ---PEDYRklFSAVFTDfhlFDQLLGP 415
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488922799 388 lEQFAAEKEVeVQDLLA---MLRKLGFErtmfDYRIE--QMSMGQKRKVALARSLCEEANLYIWDE 448
Cdd:PRK10522 416 -EGKPANPAL-VEKWLErlkMAHKLELE----DGRISnlKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
12-151 |
1.89e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.96 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 12 SYDNQIKPVFDQVALEIdASWKLGLI-GRNGRGKTTLMKILQNQ-VEYEGKVETNLKFNYFPAKITepqdsvrmvLMKIT 89
Cdd:COG2401 37 ELRVVERYVLRDLNLEI-EPGEIVLIvGASGSGKSTLLRLLAGAlKGTPVAGCVDVPDNQFGREAS---------LIDAI 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488922799 90 GRDySDFWEVERELDQIGLAEEIL-EQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLD 151
Cdd:COG2401 107 GRK-GDFKDAVELLNAVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-193 |
1.91e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.46 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 1 MGIIQLKNVSFSY-------DNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLK 66
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLvglespsQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 67 --------------FNYFPAKItEPQDSVRMVLMKITgRDYSDFWEVERE------LDQIGLAEEILEQTYASLSPGQQT 126
Cdd:PRK10419 81 raqrkafrrdiqmvFQDSISAV-NPRKTVREIIREPL-RHLLSLDKAERLarasemLRAVDLDDSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488922799 127 KALLAAMFADQNSFQLIDEPTNHLD----AAGRDLLAKyLKQKQG--YIVVSHDRYFLNQVIDHVISIDRAQI 193
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKK-LQQQFGtaCLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
341-494 |
1.94e-08 |
|
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: 54.51 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 341 GENGSGKSTLIKAMLG-----------QNELIAKGNLKIREnlRISYLPQDFdqlqGTLEQFAAEKEVEVQDLL------ 403
Cdd:cd03264 32 GPNGAGKTTLMRILATltppssgtiriDGQDVLKQPQKLRR--RIGYLPQEF----GVYPNFTVREFLDYIAWLkgipsk 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 404 -------AMLRKLGfertMFDY---RIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKPTLL 473
Cdd:cd03264 106 evkarvdEVLELVN----LGDRakkKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRI 181
|
170 180
....*....|....*....|...
gi 488922799 474 VV--EHDREFVQKIATQTVNLKK 494
Cdd:cd03264 182 VIlsTHIVEDVESLCNQVAVLNK 204
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
404-492 |
2.16e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.79 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 404 AMLRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKPTLLVVEHDREFVQ 483
Cdd:PLN03073 326 SILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLN 405
|
....*....
gi 488922799 484 KIATQTVNL 492
Cdd:PLN03073 406 TVVTDILHL 414
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-193 |
2.24e-08 |
|
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: 54.21 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNL---KFNYFPak 73
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMIlgiilpdSGEVLFDGKPLDIAarnRIGYLP-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 74 itE-----PQDSVRMVLMKIT---------GRDYSDFWeVEReLDQIGLAEEILEQtyasLSPGQQTKALLAAMFADQNS 139
Cdd:cd03269 77 --EerglyPKMKVIDQLVYLAqlkglkkeeARRRIDEW-LER-LELSEYANKRVEE----LSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488922799 140 FQLIDEPTNHLDAAGRDLLAKYLKQKQG----YIVVSHDRYFLNQVIDHVISIDRAQI 193
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARagktVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
327-493 |
2.33e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.13 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNeLIAKGNLKI------RENLR-----ISYLPQD-FDQLQ--------- 385
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY-LPQRGRVKVmgrevnAENEKwvrskVGLVFQDpDDQVFsstvwddva 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 386 -GTLEQFAAEKEVE--VQDLLAMLRklgfertMFDYRIE---QMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITRE 459
Cdd:PRK13647 103 fGPVNMGLDKDEVErrVEEALKAVR-------MWDFRDKppyHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 488922799 460 QIQNLVLKFK---PTLLVVEHDREFVQKIATQTVNLK 493
Cdd:PRK13647 176 TLMEILDRLHnqgKTVIVATHDVDLAAEWADQVIVLK 212
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
305-488 |
2.34e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.82 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 305 NNALLEADSLVLQ-RAGKLLNQPL---NLELKKNERMVIQGENGSGKSTLIKAMLG-----QNELIAKGN---------- 365
Cdd:PRK11629 2 NKILLQCDNLCKRyQEGSVQTDVLhnvSFSIGEGEMMAIVGSSGSGKSTLLHLLGGldtptSGDVIFNGQpmsklssaak 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 366 LKIReNLRISYLPQ------DFDQLQGTLEQF--AAEKEVEVQD-LLAMLRKLGFERTMfDYRIEQMSMGQKRKVALARS 436
Cdd:PRK11629 82 AELR-NQKLGFIYQfhhllpDFTALENVAMPLliGKKKPAEINSrALEMLAAVGLEHRA-NHRPSELSGGERQRVAIARA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488922799 437 LCEEANLYIWDEPLNYLDVITREQIQNLVLKFK----PTLLVVEHDREFVQKIATQ 488
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNrlqgTAFLVVTHDLQLAKRMSRQ 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-193 |
2.91e-08 |
|
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: 54.43 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGK---------------- 60
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIvgllrpdSGEVLIDGEdisglseaelyrlrrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 61 ---------------VETNLKF------NYFPAKITEpqdsvrMVLMKitgrdysdfwevereLDQIGLAEEilEQTY-A 118
Cdd:cd03261 79 mgmlfqsgalfdsltVFENVAFplrehtRLSEEEIRE------IVLEK---------------LEAVGLRGA--EDLYpA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 119 SLSPGQQTKALLA-AMFADQnsfQLI--DEPTNHLD--AAGR-DLLAKYLKQKQG--YIVVSHDRYFLNQVIDHVISIDR 190
Cdd:cd03261 136 ELSGGMKKRVALArALALDP---ELLlyDEPTAGLDpiASGViDDLIRSLKKELGltSIMVTHDLDTAFAIADRIAVLYD 212
|
...
gi 488922799 191 AQI 193
Cdd:cd03261 213 GKI 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
325-480 |
3.02e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.40 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIK-------------AMLGQNelIAKGNLKIRENLR---ISYLPQDFdQLQGTL 388
Cdd:PRK10584 27 TGVELVVKRGETIALIGESGSGKSTLLAilaglddgssgevSLVGQP--LHQMDEEARAKLRakhVGFVFQSF-MLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 389 EqfaAEKEVEVQDLL-------------AMLRKLGFERTMfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDV 455
Cdd:PRK10584 104 N---ALENVELPALLrgessrqsrngakALLEQLGLGKRL-DHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180
....*....|....*....|....*....
gi 488922799 456 ITREQIQNLVL----KFKPTLLVVEHDRE 480
Cdd:PRK10584 180 QTGDKIADLLFslnrEHGTTLILVTHDLQ 208
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
309-490 |
3.14e-08 |
|
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: 54.11 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 309 LEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNELIAK----GNLKIR-----------ENLR 373
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdeGEVLLDgkdiydldvdvLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 374 --------------------ISYLPQdfdqLQGTLEQFAAEKEVEVqdllaMLRKLG-FERTMFDYRIEQMSMGQKRKVA 432
Cdd:cd03260 81 rrvgmvfqkpnpfpgsiydnVAYGLR----LHGIKLKEELDERVEE-----ALRKAAlWDEVKDRLHALGLSGGQQQRLC 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 433 LARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFK--PTLLVVEHDREFVQKIATQTV 490
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKkeYTIVIVTHNMQQAARVADRTA 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
327-488 |
3.76e-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: 54.12 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAM-------------LGQN-ELIAKGNL-KIREnlRISYLPQDFDQLQG--TLE 389
Cdd:cd03258 24 VSLSVPKGEIFGIIGRSGAGKSTLIRCInglerptsgsvlvDGTDlTLLSGKELrKARR--RIGMIFQHFNLLSSrtVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 390 QFA----------AEKEVEVQDLLAMLrklGFERTMFDYrIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITRE 459
Cdd:cd03258 102 NVAlpleiagvpkAEIEERVLELLELV---GLEDKADAY-PAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQ 177
|
170 180 190
....*....|....*....|....*....|...
gi 488922799 460 QIQNLVL----KFKPTLLVVEHDREFVQKIATQ 488
Cdd:cd03258 178 SILALLRdinrELGLTIVLITHEMEVVKRICDR 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
423-478 |
4.17e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 54.30 E-value: 4.17e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 423 MSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLV----LKFKPTLLVVEHD 478
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIeslwQQHGFTVLLVTHD 193
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-193 |
4.18e-08 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 53.69 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSY--------------------DNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVE 56
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLagiyppdSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 57 YEGKVETNLKFNYFpakiTEPQ----DSVRMVLMkITGRDYSDFWEVERELdqIGLAE--EILEQTYASLSPGQqtKALL 130
Cdd:cd03220 81 VRGRVSSLLGLGGG----FNPEltgrENIYLNGR-LLGLSRKEIDEKIDEI--IEFSElgDFIDLPVKTYSSGM--KARL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488922799 131 AamFADQNSFQ----LIDEPTNHLDAAGR----DLLAKYLKQKQGYIVVSHDRYFLNQVIDHVISIDRAQI 193
Cdd:cd03220 152 A--FAIATALEpdilLIDEVLAVGDAAFQekcqRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-193 |
5.04e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 55.22 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 2 GIIQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLM------------KILQNQVEYEGKVETNLKfny 69
Cdd:PRK11160 337 VSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLqlltrawdpqqgEILLNGQPIADYSEAALR--- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 70 fpAKITE-PQ------DSVR--MVLMKITGRDySDFWEVereLDQIGLaEEILEQTYA----------SLSPGQQTKALL 130
Cdd:PRK11160 414 --QAISVvSQrvhlfsATLRdnLLLAAPNASD-EALIEV---LQQVGL-EKLLEDDKGlnawlgeggrQLSGGEQRRLGI 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488922799 131 AAMFADQNSFQLIDEPTNHLDAAGR----DLLAKYLKQKQgYIVVSHDRYFLNQvIDHVISIDRAQI 193
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETErqilELLAEHAQNKT-VLMITHRLTGLEQ-FDRICVMDNGQI 551
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-200 |
5.17e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNqiKPV-FDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVETNLKfnyfpakitepqds 80
Cdd:PLN03073 508 IISFSDASFGYPG--GPLlFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQpSSGTVFRSAK-------------- 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 81 VRMVLMK---ITGRDYSDF--------------WEVERELDQIGLAEEILEQTYASLSPGQQTKALLAAMFADQNSFQLI 143
Cdd:PLN03073 572 VRMAVFSqhhVDGLDLSSNpllymmrcfpgvpeQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLL 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488922799 144 DEPTNHLDAAGRDLLAKYLKQKQGYI-VVSHDRYFLNQVIDHVISIDRAQISSFKGNY 200
Cdd:PLN03073 652 DEPSNHLDLDAVEALIQGLVLFQGGVlMVSHDEHLISGSVDELWVVSEGKVTPFHGTF 709
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
327-469 |
5.29e-08 |
|
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: 53.70 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLG-----------QNELIAKGNLKIRENLRISYLPQD---FDQLqgTLEQfa 392
Cdd:cd03218 19 VSLSVKQGEIVGLLGPNGAGKTTTFYMIVGlvkpdsgkillDGQDITKLPMHKRARLGIGYLPQEasiFRKL--TVEE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 393 aekevevqDLLAMLRKLGFERTMFDYRIEQM-----------------SMGQKRKVALARSLCEEANLYIWDEPLNYLDV 455
Cdd:cd03218 95 --------NILAVLEIRGLSKKEREEKLEELleefhithlrkskasslSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170
....*....|....
gi 488922799 456 ITREQIQNLVLKFK 469
Cdd:cd03218 167 IAVQDIQKIIKILK 180
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
303-478 |
6.80e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.64 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 303 PQNNALLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKaMLGQNELIAKGNLKIRENL---------- 372
Cdd:PRK10575 6 NHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPPSEGEILLDAQPleswsskafa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 373 -RISYLPQDFDQLQ----------------GTLEQFAAEKEVEVQDLLAMLRKLGFERTMFDyrieQMSMGQKRKVALAR 435
Cdd:PRK10575 85 rKVAYLPQQLPAAEgmtvrelvaigrypwhGALGRFGAADREKVEEAISLVGLKPLAHRLVD----SLSGGERQRAWIAM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488922799 436 SLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKP----TLLVVEHD 478
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQerglTVIAVLHD 207
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
338-485 |
7.01e-08 |
|
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: 52.99 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 338 VIQGENGSGKSTLIKAML----GQNELIAKGNLK----IRENLRISYLPQDFDQLQGtlEQFAAEKEVEVQDLLAMLRKL 409
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyaltGELPPNSKGGAHdpklIREGEVRAQVKLAFENANG--KKYTITRSLAILENVIFCHQG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 410 GFERTMFDYRiEQMSMGQKRKV------ALARSLCEEANLYIWDEPLNYLD---------VITREQIQNLVlkfkPTLLV 474
Cdd:cd03240 104 ESNWPLLDMR-GRCSGGEKVLAsliirlALAETFGSNCGILALDEPTTNLDeenieeslaEIIEERKSQKN----FQLIV 178
|
170
....*....|.
gi 488922799 475 VEHDREFVQKI 485
Cdd:cd03240 179 ITHDEELVDAA 189
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-195 |
7.20e-08 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 53.12 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYD--NQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLK------- 66
Cdd:COG1136 4 LLELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggldrptSGEVLIDGQDISSLSerelarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 67 -----------FNYFP---AKitepqDSVRMVLMkITGRDYSdfwevERE------LDQIGLAeEILEQTYASLSPGQQT 126
Cdd:COG1136 84 rrrhigfvfqfFNLLPeltAL-----ENVALPLL-LAGVSRK-----ERRerarelLERVGLG-DRLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488922799 127 KALLA-AMFADQnsfQLI--DEPTNHLD-AAGRDLLA--KYLKQKQGY--IVVSHDRYFLNQViDHVISIDRAQISS 195
Cdd:COG1136 152 RVAIArALVNRP---KLIlaDEPTGNLDsKTGEEVLEllRELNRELGTtiVMVTHDPELAARA-DRVIRLRDGRIVS 224
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
18-193 |
9.50e-08 |
|
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: 53.28 E-value: 9.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 18 KPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLKFNYFPAKI--------TEPQDSVR 82
Cdd:TIGR03873 14 RLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLagalrpdAGTVDLAGVDLHGLSRRARARRValveqdsdTAVPLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 83 MVLMkiTGR-DYSDFWEVERELDqIGLAEEIL---------EQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDA 152
Cdd:TIGR03873 94 DVVA--LGRiPHRSLWAGDSPHD-AAVVDRALartelshlaDRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488922799 153 AGRDLLAKYLKQKQG----YIVVSHDRYFLNQVIDHVISIDRAQI 193
Cdd:TIGR03873 171 RAQLETLALVRELAAtgvtVVAALHDLNLAASYCDHVVVLDGGRV 215
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-204 |
1.04e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.09 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 11 FSYdnQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKvetnlKFNYFPAKITEPQDSVRM 83
Cdd:PRK13638 9 FRY--QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLsgllrpqKGAVLWQGK-----PLDYSKRGLLALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 84 VLMKITGRD-YSDF-WEVERELDQIGLAEEIL-----------------EQTYASLSPGQQTKALLAAMFADQNSFQLID 144
Cdd:PRK13638 82 VFQDPEQQIfYTDIdSDIAFSLRNLGVPEAEItrrvdealtlvdaqhfrHQPIQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488922799 145 EPTNHLDAAGRD----LLAKYLKQKQGYIVVSHDRYFLNQVIDHVISIDRAQISSFKGNYETWA 204
Cdd:PRK13638 162 EPTAGLDPAGRTqmiaIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-174 |
1.19e-07 |
|
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: 52.69 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYdNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVetnlkfnYFPAKITEPQDSVR 82
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEpTSGEI-------FIDGEDIREQDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 83 M------------------------VLMKITGrdysdfWEVER------ELDQ-IGLAEEILEQTYAS-LSPGQQTKALL 130
Cdd:cd03295 73 LrrkigyviqqiglfphmtveeniaLVPKLLK------WPKEKireradELLAlVGLDPAEFADRYPHeLSGGQQQRVGV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488922799 131 A-AMFADQNSFqLIDEPTNHLDAAGRDLLA---KYLKQKQG--YIVVSHD 174
Cdd:cd03295 147 ArALAADPPLL-LMDEPFGALDPITRDQLQeefKRLQQELGktIVFVTHD 195
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-193 |
1.29e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.10 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYdnQIKPVFDQVAL-EIDASWKLG----LIGRNGRGKTTLMK----ILQ---------NQVEYEGKVETNL 65
Cdd:PRK13634 3 ITFQKVEHRY--QYKTPFERRALyDVNVSIPSGsyvaIIGHTGSGKSTLLQhlngLLQptsgtvtigERVITAGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 66 K---------FNyFPakitEPQDSVRMVLMKIT------GRDYSDFWEVERE-LDQIGLAEEILEQTYASLSPGQQTKAL 129
Cdd:PRK13634 81 KplrkkvgivFQ-FP----EHQLFEETVEKDICfgpmnfGVSEEDAKQKAREmIELVGLPEELLARSPFELSGGQMRRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488922799 130 LAAMFADQNSFQLIDEPTNHLDAAGR----DLLAKYLKQKQGYIV-VSHDRYFLNQVIDHVISIDRAQI 193
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRkemmEMFYKLHKEKGLTTVlVTHSMEDAARYADQIVVMHKGTV 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
327-486 |
1.32e-07 |
|
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: 52.44 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLG--------------------QNELIAKG------------NLKIRENLRI 374
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGllpprsgsirfdgrditglpPHERARAGigyvpegrrifpELTVEENLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 375 SYLPQDFDQLQGTLEQfaaekevevqdLLAMLRKLgfeRTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLD 454
Cdd:cd03224 99 GAYARRRAKRKARLER-----------VYELFPRL---KERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLA 164
|
170 180 190
....*....|....*....|....*....|....*
gi 488922799 455 VITREQIQNLVLKFKP---TLLVVEHDREFVQKIA 486
Cdd:cd03224 165 PKIVEEIFEAIRELRDegvTILLVEQNARFALEIA 199
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
313-486 |
1.41e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 52.77 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 313 SLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQnELIAKGNlkirenlrISYLPQDFDQLQGTlEQFA 392
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-ESPSQGN--------VSWRGEPLAKLNRA-QRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 393 AEKEVEV--QD---------------------------------LLAMLRKLGFERTMFDYRIEQMSMGQKRKVALARSL 437
Cdd:PRK10419 87 FRRDIQMvfQDsisavnprktvreiireplrhllsldkaerlarASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARAL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488922799 438 CEEANLYIWDEPLNYLDVITREQIQNLVLK----FKPTLLVVEHDREFVQKIA 486
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDLVLQAGVIRLLKKlqqqFGTACLFITHDLRLVERFC 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-215 |
1.44e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 52.74 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 18 KPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVETNLKFNYFPAKI-----TEPQDSVRMVLMKITGR 91
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDGKVLYFGKDIfqidaIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 92 DYSDFWE--------------------VERELDQIGLAEEI---LEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTN 148
Cdd:PRK14246 103 PHLSIYDniayplkshgikekreikkiVEECLRKVGLWKEVydrLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 149 HLDAAGRDLLAKY---LKQKQGYIVVSHDRYFLNQVIDHVISIDRAQISSFKGNYETWAAERANADEREI 215
Cdd:PRK14246 183 MIDIVNSQAIEKLiteLKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-190 |
1.47e-07 |
|
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: 52.11 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 2 GIIQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVE------TNLKFNYFPAKI 74
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVElSSGSILidgvdiSKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 75 TE-PQDSvrmVLMKITGRD-------YSDfWEVERELDQIGLAEEILEQTY----------ASLSPGQQ-----TKALLA 131
Cdd:cd03244 81 SIiPQDP---VLFSGTIRSnldpfgeYSD-EELWQALERVGLKEFVESLPGgldtvveeggENLSVGQRqllclARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488922799 132 amfadQNSFQLIDEPTNHLDAAGRDLLAKYLKQK---QGYIVVSHdRyflnqvIDHVISIDR 190
Cdd:cd03244 157 -----KSKILVLDEATASVDPETDALIQKTIREAfkdCTVLTIAH-R------LDTIIDSDR 206
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
327-494 |
1.60e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 52.32 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKaMLGQNELIAKGNLKIRENL----------RISYLPQD----FDQ--------- 383
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEMPRSGTLNIAGNHfdfsktpsdkAIRELRRNvgmvFQQynlwphltv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 384 ----------LQGTLEQFAAEKEVEvqdLLAMLRKLGFErtmfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYL 453
Cdd:PRK11124 100 qqnlieapcrVLGLSKDQALARAEK---LLERLRLKPYA----DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488922799 454 DVITREQIQNLVLKFKP---TLLVVEHDREFVQKIATQTVNLKK 494
Cdd:PRK11124 173 DPEITAQIVSIIRELAEtgiTQVIVTHEVEVARKTASRVVYMEN 216
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
327-477 |
1.97e-07 |
|
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: 51.64 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNElIAKGNLKIR---------ENLR--ISYLPQDFDQLQGT----LEQF 391
Cdd:cd03369 27 VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLE-AEEGKIEIDgidistiplEDLRssLTIIPQDPTLFSGTirsnLDPF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 392 AAEKEVEVQDLLamlrklgfertmfdyRI----EQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLK 467
Cdd:cd03369 106 DEYSDEEIYGAL---------------RVseggLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIRE 170
|
170
....*....|..
gi 488922799 468 F--KPTLLVVEH 477
Cdd:cd03369 171 EftNSTILTIAH 182
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-51 |
2.14e-07 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 53.24 E-value: 2.14e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488922799 2 GIIQLKNVSFSYDNQiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL 51
Cdd:COG1132 338 GEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLL 386
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-164 |
2.32e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.44 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 1 MGIiQLKNVSFSYDN----QIKPVFDqVALEI-DASWKlGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLKFN 68
Cdd:PRK13649 1 MGI-NLQNVSYTYQAgtpfEGRALFD-VNLTIeDGSYT-AFIGHTGSGKSTIMQLLnglhvptQGSVRVDDTLITSTSKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 69 --------------YFPakitEPQDSVRMVLMKIT------GRDYSDFWEVERE-LDQIGLAEEILEQTYASLSPGQQTK 127
Cdd:PRK13649 78 kdikqirkkvglvfQFP----ESQLFEETVLKDVAfgpqnfGVSQEEAEALAREkLALVGISESLFEKNPFELSGGQMRR 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 488922799 128 ALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYLKQ 164
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKK 190
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
303-480 |
2.54e-07 |
|
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: 51.67 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 303 PQNNALLEADSLVLQ---RAGKL--LnQPLNLELKKNERMVIQGENGSGKSTLIK-------------AMLGQNelIAKG 364
Cdd:COG4181 3 SSSAPIIELRGLTKTvgtGAGELtiL-KGISLEVEAGESVAIVGASGSGKSTLLGllagldrptsgtvRLAGQD--LFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 365 NLKIRENLR---ISYLPQDFdQLQGT---LE------QFAAEKEVEvQDLLAMLRKLGF-ERtmFDYRIEQMSMGQKRKV 431
Cdd:COG4181 80 DEDARARLRarhVGFVFQSF-QLLPTltaLEnvmlplELAGRRDAR-ARARALLERVGLgHR--LDHYPAQLSGGEQQRV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488922799 432 ALARSLCEEANLYIWDEPLNYLDVITREQIQNLVL----KFKPTLLVVEHDRE 480
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLFelnrERGTTLVLVTHDPA 208
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
327-454 |
2.58e-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: 53.41 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNELIaKGNLKIRENlrISYLPQDF----DQLQGT------LEQFAAEKE 396
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKV-EGHVHMKGS--VAYVPQQAwiqnDSLRENilfgkaLNEKYYQQV 733
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488922799 397 VEVQDLLAMLRKL-GFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLD 454
Cdd:TIGR00957 734 LEACALLPDLEILpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-193 |
3.13e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.72 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNQIKPVFDQVALEID-ASWKlGLIGRNGRGKTTLMKILQNQVEYEGKVETnlKFNYFPAKITEP---- 77
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPrGSWT-ALIGHNGSGKSTISKLINGLLLPDDNPNS--KITVDGITLTAKtvwd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 78 -QDSVRMVLMK--------ITGRDYSDFWE------------VERELDQIGLAEEILEQTyASLSPGQQTKALLAAMFAD 136
Cdd:PRK13640 82 iREKVGIVFQNpdnqfvgaTVGDDVAFGLEnravprpemikiVRDVLADVGMLDYIDSEP-ANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488922799 137 QNSFQLIDEPTNHLDAAGRDL---LAKYLKQKQGYIVVS--HDRYFLNQViDHVISIDRAQI 193
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQilkLIRKLKKKNNLTVISitHDIDEANMA-DQVLVLDDGKL 221
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
392-486 |
3.33e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 52.27 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 392 AAEKEVEVqdlLAMLRKLGFeRTMFDYRIEQM-SMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVL---- 466
Cdd:PRK11308 127 AAERREKA---LAMMAKVGL-RPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMdlqq 202
|
90 100
....*....|....*....|
gi 488922799 467 KFKPTLLVVEHDREFVQKIA 486
Cdd:PRK11308 203 ELGLSYVFISHDLSVVEHIA 222
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-195 |
3.40e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.66 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 1 MGIIQLKNVSFSYD-NQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEYE-GKV--------ETN------ 64
Cdd:PRK13650 2 SNIIEVKNLTFKYKeDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGQIiidgdlltEENvwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 65 ---LKF----NYFPAKITEpqDSVRMVLMKiTGRDYSDFWE-VERELDQIGLaEEILEQTYASLSPGQQTKALLAAMFAD 136
Cdd:PRK13650 82 kigMVFqnpdNQFVGATVE--DDVAFGLEN-KGIPHEEMKErVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488922799 137 QNSFQLIDEPTNHLDAAGRDLLAKYLKQ-KQGY----IVVSHDryfLNQVI--DHVISIDRAQISS 195
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGiRDDYqmtvISITHD---LDEVAlsDRVLVMKNGQVES 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
341-494 |
4.05e-07 |
|
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: 50.83 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 341 GENGSGKSTLIKAMLG-----------------QNELIAKGNLKI-------------RENLRIsylpqdFDQLQGtLEQ 390
Cdd:cd03266 38 GPNGAGKTTTLRMLAGllepdagfatvdgfdvvKEPAEARRRLGFvsdstglydrltaRENLEY------FAGLYG-LKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 391 FAAEKEVEVqdllaMLRKLGFERTMfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKP 470
Cdd:cd03266 111 DELTARLEE-----LADRLGMEELL-DRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRA 184
|
170 180
....*....|....*....|....*..
gi 488922799 471 ---TLLVVEHDREFVQKIATQTVNLKK 494
Cdd:cd03266 185 lgkCILFSTHIMQEVERLCDRVVVLHR 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
321-490 |
4.32e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 52.01 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 321 KLLNQpLNLELKKNERMVIQGENGSGKSTLIKAMLG---QNE--LIAKGN----LKIRENlRISYLPQD---------FD 382
Cdd:PRK10851 16 QVLND-ISLDIPSGQMVALLGPSGSGKTTLLRIIAGlehQTSghIRFHGTdvsrLHARDR-KVGFVFQHyalfrhmtvFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 383 QLQGTLEQF-------AAEKEVEVQDLLAMLrKLGFERTMFDyriEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDV 455
Cdd:PRK10851 94 NIAFGLTVLprrerpnAAAIKAKVTQLLEMV-QLAHLADRYP---AQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 488922799 456 ITREQ----IQNLVLKFKPTLLVVEHDREFVQKIATQTV 490
Cdd:PRK10851 170 QVRKElrrwLRQLHEELKFTSVFVTHDQEEAMEVADRVV 208
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
328-490 |
4.49e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.55 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 328 NLELKKNERMVIQGENGSGKSTLIKamLGQNELIAK------GNLKIRENLR-------------ISYLPQDFDQLQGTL 388
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQ--LTNGLIISEtgqtivGDYAIPANLKkikevkrlrkeigLVFQFPEYQLFQETI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 389 EQ--------FAAEKEVEVQDLLAMLRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQ 460
Cdd:PRK13645 109 EKdiafgpvnLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEED 188
|
170 180 190
....*....|....*....|....*....|....
gi 488922799 461 IQNLVLK----FKPTLLVVEHDREFVQKIATQTV 490
Cdd:PRK13645 189 FINLFERlnkeYKKRIIMVTHNMDQVLRIADEVI 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
333-478 |
5.20e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.91 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 333 KNERMVIQGENGSGKSTLIKAMLG-----------QNELIAKGNLK-IRENLRISYLPQDfDQLQGTLEQ----FAAEKE 396
Cdd:PRK13648 34 KGQWTSIVGHNGSGKSTIAKLMIGiekvksgeifyNNQAITDDNFEkLRKHIGIVFQNPD-NQFVGSIVKydvaFGLENH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 397 -VEVQDLLAMLRKLGFERTMFDYRIEQ---MSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKP-- 470
Cdd:PRK13648 113 aVPYDEMHRRVSEALKQVDMLERADYEpnaLSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSeh 192
|
170
....*....|
gi 488922799 471 --TLLVVEHD 478
Cdd:PRK13648 193 niTIISITHD 202
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-202 |
5.23e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.42 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSY---DNQIKpVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL---------------QNQVEYEGKVETN 64
Cdd:PRK10535 4 LLELKDIRRSYpsgEEQVE-VLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptsgtyrvagQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 65 LKFNYFP---------AKITEPQD-SVRMVlmkitgrdYSDFWEVERE------LDQIGLAEEILEQTyASLSPGQQTKA 128
Cdd:PRK10535 83 LRREHFGfifqryhllSHLTAAQNvEVPAV--------YAGLERKQRLlraqelLQRLGLEDRVEYQP-SQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488922799 129 LLAAMFADQNSFQLIDEPTNHLDA-AGRDLLAkYLKQ--KQGY--IVVSHDRYFLNQViDHVISIDRAQISSFKGNYET 202
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDShSGEEVMA-ILHQlrDRGHtvIIVTHDPQVAAQA-ERVIEIRDGEIVRNPPAQEK 230
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
325-483 |
5.45e-07 |
|
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: 49.63 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIkamlgqNELIAKgnlkirenlrisylpQDFDQLQGTLEQFAAEKEVEVqDLLA 404
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLV------NEGLYA---------------SGKARLISFLPKFSRNKLIFI-DQLQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 405 MLRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEA--NLYIWDEPLNYLDVITREQIQNLV---LKFKPTLLVVEHDR 479
Cdd:cd03238 70 FLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIkglIDLGNTVILIEHNL 149
|
....
gi 488922799 480 EFVQ 483
Cdd:cd03238 150 DVLS 153
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-191 |
6.41e-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: 49.35 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQikPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEY-EGKVetnlKFNYFPAKITEPQDS-- 80
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPdSGEI----LVDGKEVSFASPRDArr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 81 --VRMVLmkitgrdysdfwevereldQIGLAEeileqtyaslspgQQTKALLAAMFADQNsFQLIDEPTNHLDAAGRDLL 158
Cdd:cd03216 75 agIAMVY-------------------QLSVGE-------------RQMVEIARALARNAR-LLILDEPTAALTPAEVERL 121
|
170 180 190
....*....|....*....|....*....|....*...
gi 488922799 159 AKYLKQ--KQG--YIVVSHDryflnqvIDHVISI-DRA 191
Cdd:cd03216 122 FKVIRRlrAQGvaVIFISHR-------LDEVFEIaDRV 152
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
307-478 |
7.06e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 50.54 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 307 ALLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGqnELIAKGNlKIR---ENLRiSYLPQDFDQ 383
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG--ELSPDSG-EVRlngRPLA-DWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 384 LQGTLEQ-------FAAEkEV-------------EVQDLL-AMLRKLGF----ERtmfDYRieQMSMGQKRKVALARSLC 438
Cdd:PRK13548 77 RRAVLPQhsslsfpFTVE-EVvamgraphglsraEDDALVaAALAQVDLahlaGR---DYP--QLSGGEQQRVQLARVLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488922799 439 ------EEANLYIWDEPLNYLDVitREQIQ------NLVLKFKPTLLVVEHD 478
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDL--AHQHHvlrlarQLAHERGLAVIVVLHD 200
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-193 |
7.26e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 50.76 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNQiKPVFDQVALEIDASWKLGLIGRNGRGKTTLM------------KIL------------------- 51
Cdd:PRK13644 1 MIRLENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLAlhlngllrpqkgKVLvsgidtgdfsklqgirklv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 52 ----QN-QVEYEGK-VETNLKFNyfPAKITEPQDSVRMvlmkitgrdysdfwEVERELDQIGLaEEILEQTYASLSPGQQ 125
Cdd:PRK13644 80 givfQNpETQFVGRtVEEDLAFG--PENLCLPPIEIRK--------------RVDRALAEIGL-EKYRHRSPKTLSGGQG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488922799 126 TKALLAAMFADQNSFQLIDEPTNHLDA-AGRDLL--AKYLKQKQGYIV-VSHDRYFLnQVIDHVISIDRAQI 193
Cdd:PRK13644 143 QCVALAGILTMEPECLIFDEVTSMLDPdSGIAVLerIKKLHEKGKTIVyITHNLEEL-HDADRIIVMDRGKI 213
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-196 |
8.07e-07 |
|
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: 49.72 E-value: 8.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 2 GIIQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEY-EGKVE------TNLKFNYFPAKI 74
Cdd:cd03369 5 GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAeEGKIEidgidiSTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 75 T-EPQDSvrmVLMKITGR-------DYSDfweverelDQIGLAEEILEQTyASLSPGQQTKALLAAMFADQNSFQLIDEP 146
Cdd:cd03369 85 TiIPQDP---TLFSGTIRsnldpfdEYSD--------EEIYGALRVSEGG-LNLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488922799 147 TNHLDAAGRDLLAKYLK---QKQGYIVVSHDryfLNQVIDH--VISIDRAQISSF 196
Cdd:cd03369 153 TASIDYATDALIQKTIReefTNSTILTIAHR---LRTIIDYdkILVMDAGEVKEY 204
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-193 |
8.61e-07 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 49.99 E-value: 8.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNQiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMK-------ILQNQVEYEGKVETNLK--------- 66
Cdd:TIGR02315 1 MLEVENLSKVYPNG-KQALKNINLNINPGEFVAIIGPSGAGKSTLLRcinrlvePSSGSILLEGTDITKLRgkklrklrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 67 -----FNYFpaKITEPQDSVRMVLMkitGR-DYSDFW--------EVERE-----LDQIGLAEEILeQTYASLSPGQQTK 127
Cdd:TIGR02315 80 rigmiFQHY--NLIERLTVLENVLH---GRlGYKPTWrsllgrfsEEDKEralsaLERVGLADKAY-QRADQLSGGQQQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488922799 128 ALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYLK---QKQGYIVVS--HDRYFLNQVIDHVISIDRAQI 193
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKrinKEDGITVIInlHQVDLAKKYADRIVGLKAGEI 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-174 |
8.70e-07 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 50.09 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 1 MGIIQLKNVSFSY--DNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKvetnlkfnyfp 71
Cdd:COG1116 5 APALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIaglekptSGEVLVDGK----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 72 aKITEPQDSVRMV-----LM-------------KITGRDYSDFWE-VERELDQIGLAEeiLEQTY-ASLSPGQQTKALLA 131
Cdd:COG1116 74 -PVTGPGPDRGVVfqepaLLpwltvldnvalglELRGVPKAERRErARELLELVGLAG--FEDAYpHQLSGGMRQRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488922799 132 AMFADQNSFQLIDEPTNHLDAAGR----DLLAKYLKQKQGYIV-VSHD 174
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRerlqDELLRLWQETGKTVLfVTHD 198
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
309-478 |
8.88e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 50.40 E-value: 8.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 309 LEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQN-----ELIAKGN----LKIRENLR-ISYLP 378
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLtpqsgTVFLGDKpismLSSRQLARrLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 379 QdfdqlqgtleQFAAEKEVEVQDLLAMLR--------KLG----------FERT----MFDYRIEQMSMGQKRKVALARS 436
Cdd:PRK11231 83 Q----------HHLTPEGITVRELVAYGRspwlslwgRLSaednarvnqaMEQTrinhLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488922799 437 LCEEANLYIWDEPLNYLDVITREQIQNLVLKFK---PTLLVVEHD 478
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRELNtqgKTVVTVLHD 197
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
302-477 |
8.97e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 50.57 E-value: 8.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 302 GPQNNALLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNELIAkGNLKI----------REN 371
Cdd:PRK13537 1 GPMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDA-GSISLcgepvpsrarHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 372 LRISYLPQdFDQL------QGTLEQF-------AAEKEVEVQDLLAMLRklgFERTMfDYRIEQMSMGQKRKVALARSLC 438
Cdd:PRK13537 80 QRVGVVPQ-FDNLdpdftvRENLLVFgryfglsAAAARALVPPLLEFAK---LENKA-DAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488922799 439 EEANLYIWDEPLNYLDVITR----EQIQNLVLKFKpTLLVVEH 477
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARhlmwERLRSLLARGK-TILLTTH 196
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
103-201 |
9.03e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 50.62 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 103 LDQIGLAEEILEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGR----DLLAKYLKQKQGYIVVSHDRYFL 178
Cdd:PRK13631 160 LNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEhemmQLILDAKANNKTVFVITHTMEHV 239
|
90 100
....*....|....*....|...
gi 488922799 179 NQVIDHVISIDRAQISSFKGNYE 201
Cdd:PRK13631 240 LEVADEVIVMDKGKILKTGTPYE 262
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
327-477 |
9.20e-07 |
|
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: 49.92 E-value: 9.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAML-------GQnelIAKGNLKIRE----NLR--ISYLPQD------------- 380
Cdd:cd03253 20 VSFTIPAGKKVAIVGPSGSGKSTILRLLFrfydvssGS---ILIDGQDIREvtldSLRraIGVVPQDtvlfndtigynir 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 381 FDQLQGTLEQ-FAAEKEVEVQDLLAMLRKlGFErTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITRE 459
Cdd:cd03253 97 YGRPDATDEEvIEAAKAAQIHDKIMRFPD-GYD-TIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTER 174
|
170 180
....*....|....*....|.
gi 488922799 460 QIQ---NLVLKFKpTLLVVEH 477
Cdd:cd03253 175 EIQaalRDVSKGR-TTIVIAH 194
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
327-482 |
9.44e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 50.23 E-value: 9.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLG-----QNELI---------AKGNLKIRENLRISYLPQDFDQLQGTLEQ-- 390
Cdd:PRK13636 25 ININIKKGEVTAILGGNGAGKSTLFQNLNGilkpsSGRILfdgkpidysRKGLMKLRESVGMVFQDPDNQLFSASVYQdv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 391 -FAA------EKEVEvQDLLAMLRKLGFERtMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQN 463
Cdd:PRK13636 105 sFGAvnlklpEDEVR-KRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMK 182
|
170 180
....*....|....*....|...
gi 488922799 464 LVLKFKP----TLLVVEHDREFV 482
Cdd:PRK13636 183 LLVEMQKelglTIIIATHDIDIV 205
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
327-486 |
1.05e-06 |
|
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: 49.64 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLG-----QNELIAKGNL----KIRENLRISYLPQDFDQLQGTL---EQFAAE 394
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGllqptSGEVRVAGLVpwkrRKKFLRRIGVVFGQKTQLWWDLpviDSFYLL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 395 KEV---------EVQDLLAMLRKLGferTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLV 465
Cdd:cd03267 120 AAIydlpparfkKRLDELSELLDLE---ELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFL 196
|
170 180
....*....|....*....|....*
gi 488922799 466 LKF----KPTLLVVEHDREFVQKIA 486
Cdd:cd03267 197 KEYnrerGTTVLLTSHYMKDIEALA 221
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-160 |
1.05e-06 |
|
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: 49.91 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 2 GIIQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVETN-LKFNYFPAKITEPQD 79
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDiFDGKIVIDgIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 80 SVRM---VLMKITGRDYSD---------FWEVeRELDQI--------GLAEEILEQTYASLSPGQQTKALLAAMFADQNS 139
Cdd:cd03288 98 SIILqdpILFSGSIRFNLDpeckctddrLWEA-LEIAQLknmvkslpGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180
....*....|....*....|.
gi 488922799 140 FQLIDEPTNHLDAAGRDLLAK 160
Cdd:cd03288 177 ILIMDEATASIDMATENILQK 197
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-193 |
1.09e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 50.49 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQN-------QVEYEGK---VETNLKFNYFPa 72
Cdd:COG4152 1 MLELKGLTKRFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGilapdsgEVLWDGEpldPEDRRRIGYLP- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 73 kitE-----PQDSVRMVLM---------KITGRDYSDFWevereLDQIGLAEeileqtYA-----SLSPGQQTKALLAAM 133
Cdd:COG4152 78 ---EerglyPKMKVGEQLVylarlkglsKAEAKRRADEW-----LERLGLGD------RAnkkveELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488922799 134 FADQNSFQLIDEPTNHLDAAGRDLLAKYLKQ--KQGYIVV--SHDryfLNQV---IDHVISIDRAQI 193
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRElaAKGTTVIfsSHQ---MELVeelCDRIVIINKGRK 207
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
328-486 |
1.17e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 50.48 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 328 NLELKKNERMVIQGENGSGKSTLIKAMLGqneLIakgnlKIRENlRISYLPQDFdqLQGTLEQF-AAEKEVEV--QDLLA 404
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIG---LV-----KATDG-EVAWLGKDL--LGMKDDEWrAVRSDIQMifQDPLA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 405 ----------------------------------MLRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPL 450
Cdd:PRK15079 110 slnprmtigeiiaeplrtyhpklsrqevkdrvkaMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488922799 451 NYLDVITREQIQNLVLKFKP----TLLVVEHDREFVQKIA 486
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQRemglSLIFIAHDLAVVKHIS 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-204 |
1.27e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.01 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 2 GIIQLKNVSFSYDNQIKPVF---DQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEYEG--------KVETNLKfnyf 70
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFEFkalNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETgqtivgdyAIPANLK---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 71 paKITEPQDSVRMVLMKITGRDYSDFWE-VERE----------------------LDQIGLAEEILEQTYASLSPGQQTK 127
Cdd:PRK13645 81 --KIKEVKRLRKEIGLVFQFPEYQLFQEtIEKDiafgpvnlgenkqeaykkvpelLKLVQLPEDYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 128 ALLAAMFADQNSFQLIDEPTNHLDAAG-RDLLAKYLK----QKQGYIVVSHDRYFLNQVIDHVISIDRAQISSFKGNYET 202
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGeEDFINLFERlnkeYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
..
gi 488922799 203 WA 204
Cdd:PRK13645 239 FS 240
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
327-486 |
1.37e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 49.69 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLG-----QNELIAKGN---------LKIRENLRISYLPQDfDQL-QGTLEQF 391
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGilkptSGEVLIKGEpikydkkslLEVRKTVGIVFQNPD-DQLfAPTVEED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 392 AA---------EKEVE--VQDLLAMLRKLGFERTMfdyrIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQ 460
Cdd:PRK13639 100 VAfgplnlglsKEEVEkrVKEALKAVGMEGFENKP----PHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180
....*....|....*....|....*....
gi 488922799 461 IQNLVLKFKP---TLLVVEHDREFVQKIA 486
Cdd:PRK13639 176 IMKLLYDLNKegiTIIISTHDVDLVPVYA 204
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-193 |
1.40e-06 |
|
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: 49.39 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 2 GIIQLKNVSFSYDNQI-KPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQN-------QVEYEGKVETNLKFNYFPAK 73
Cdd:cd03248 10 GIVKFQNVTFAYPTRPdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENfyqpqggQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 74 IT----EPQDSVRMVLMKIT-GRDYSDFWEVERELDQIGLAEEI--LEQTY--------ASLSPGQQTKALLAAMFADQN 138
Cdd:cd03248 90 VSlvgqEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFIseLASGYdtevgekgSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488922799 139 SFQLIDEPTNHLDAAGRDLLAKYLK---QKQGYIVVSHdRYFLNQVIDHVISIDRAQI 193
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYdwpERRTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
327-482 |
1.71e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 48.87 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNELI--------------AKGNLKIRENLRISYLPQDFDQLQGTLEQ-- 390
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLegkvhwsnknesepSFEATRSRNRYSVAYAAQKPWLLNATVEEni 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 391 -----FAAEKEVEVQDLLAMLRKLGF----ERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDV-ITREQ 460
Cdd:cd03290 100 tfgspFNKQRYKAVTDACSLQPDIDLlpfgDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSDHL 179
|
170 180
....*....|....*....|....*.
gi 488922799 461 IQNLVLKF----KPTLLVVEHDREFV 482
Cdd:cd03290 180 MQEGILKFlqddKRTLVLVTHKLQYL 205
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-193 |
1.75e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 50.49 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 2 GIIQLKNVSFSYDNQI-KPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQN-------QVEYEGKVETNLKFNYFPAK 73
Cdd:TIGR00958 477 GLIEFQDVSFSYPNRPdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNlyqptggQVLLDGVPLVQYDHHYLHRQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 74 I----TEPQDSVRMVLMKIT-GRDYSDFWEVERELDQIGLAEEI--LEQTYAS--------LSPGQQTKALLAAMFADQN 138
Cdd:TIGR00958 557 ValvgQEPVLFSGSVRENIAyGLTDTPDEEIMAAAKAANAHDFImeFPNGYDTevgekgsqLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488922799 139 SFQLIDEPTNHLDAAGRDLLAKYLKQKQGYIVVSHDRYFLNQVIDHVISIDRAQI 193
Cdd:TIGR00958 637 RVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-164 |
1.94e-06 |
|
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: 50.68 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 2 GIIQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEYEGKVETN-------------LKFN 68
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDgvswnsvtlqtwrKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 69 YFPAKITEPQDSVRMVLMKITGRDYSDFWEVERELDQIGLAEE-------ILEQTYASLSPGQQTKALLAAMFADQNSFQ 141
Cdd:TIGR01271 1296 VIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQfpdkldfVLVDGGYVLSNGHKQLMCLARSILSKAKIL 1375
|
170 180
....*....|....*....|...
gi 488922799 142 LIDEPTNHLDAAGRDLLAKYLKQ 164
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
317-454 |
2.22e-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: 48.81 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 317 QRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLG--QNELIAKGNLKIRENLR--------ISYLPQDFDQLQG 386
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrvEGGGTTSGQILFNGQPRkpdqfqkcVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 387 -TLEQF--------------AAEKEVEVQDLLamLRKLGFERtMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLN 451
Cdd:cd03234 96 lTVRETltytailrlprkssDAIRKKRVEDVL--LRDLALTR-IGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
...
gi 488922799 452 YLD 454
Cdd:cd03234 173 GLD 175
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
327-477 |
2.33e-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: 50.33 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNElIAKGNLKIR---------ENLR--ISYLPQDFDQLQGTL----EQF 391
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINE-SAEGEIIIDglniakiglHDLRfkITIIPQDPVLFSGSLrmnlDPF 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 392 AAEKEVEVQDLLAMLRKLGFERTM---FDYRI----EQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNL 464
Cdd:TIGR00957 1384 SQYSDEEVWWALELAHLKTFVSALpdkLDHECaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQST 1463
|
170
....*....|....*
gi 488922799 465 V-LKFKP-TLLVVEH 477
Cdd:TIGR00957 1464 IrTQFEDcTVLTIAH 1478
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
332-494 |
2.37e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 49.46 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 332 KKNERMVIQGENGSGKSTLIKAMlgqNELI--AKGNLKIR----------ENLRISYLP---QDFDQLQGTLE---QF-- 391
Cdd:PRK13631 50 EKNKIYFIIGNSGSGKSTLVTHF---NGLIksKYGTIQVGdiyigdkknnHELITNPYSkkiKNFKELRRRVSmvfQFpe 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 392 ------AAEKEV------------EVQDLLAM-LRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNY 452
Cdd:PRK13631 127 yqlfkdTIEKDImfgpvalgvkksEAKKLAKFyLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAG 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488922799 453 LDVITREQIQNLVLKFKP---TLLVVEHDREFVQKIATQTVNLKK 494
Cdd:PRK13631 207 LDPKGEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADEVIVMDK 251
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-193 |
2.51e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 48.91 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 6 LKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQN-QVEYEGKVETNlkfnyfPAKITEPQDSVRMV 84
Cdd:PRK11247 15 LNAVSKRYGE--RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGlETPSAGELLAG------TAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 85 -----------LMKITGRDYSDFW--EVERELDQIGLAEEILEQTyASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLD 151
Cdd:PRK11247 87 fqdarllpwkkVIDNVGLGLKGQWrdAALQALAAVGLADRANEWP-AALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488922799 152 AAGR----DLLAKyLKQKQGYIV--VSHDRYFLNQVIDHVISIDRAQI 193
Cdd:PRK11247 166 ALTRiemqDLIES-LWQQHGFTVllVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-193 |
2.66e-06 |
|
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: 48.35 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNQIK--PVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLKfnyfPAK 73
Cdd:cd03258 1 MIELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInglerptSGSVLVDGTDLTLLS----GKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 74 ITEPQDSVRMVL------------------MKITGRDYSDFWE-VERELDQIGLAEEilEQTY-ASLSPGQQTKALLAAM 133
Cdd:cd03258 77 LRKARRRIGMIFqhfnllssrtvfenvalpLEIAGVPKAEIEErVLELLELVGLEDK--ADAYpAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488922799 134 FADQNSFQLIDEPTNHLDAAGRD----LLAKyLKQKQG--YIVVSHDRYFLNQVIDHVISIDRAQI 193
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQsilaLLRD-INRELGltIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
36-193 |
3.08e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 48.83 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 36 LIGRNGRGKTTLMKILQN--------------QVEYEGKVETNLKFNYFPAKITEPQD-SVRMVLMK--------ITGRD 92
Cdd:PRK10253 38 IIGPNGCGKSTLLRTLSRlmtpahghvwldgeHIQHYASKEVARRIGLLAQNATTPGDiTVQELVARgryphqplFTRWR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 93 YSDFWEVERELDQIGLAEeILEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGR-DLLA--KYLKQKQGYI 169
Cdd:PRK10253 118 KEDEEAVTKAMQATGITH-LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQiDLLEllSELNREKGYT 196
|
170 180
....*....|....*....|....*....
gi 488922799 170 V--VSHDryfLNQVI---DHVISIDRAQI 193
Cdd:PRK10253 197 LaaVLHD---LNQACryaSHLIALREGKI 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-216 |
3.40e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 48.37 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 1 MGIIQLKNVSFSYDNQikPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEY--EGKVETNLKFN---YFPAKIT 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQV--EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypEARVSGEVYLDgqdIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 76 EPQDSVRMV---------------------LMKITGRDYSDFWEVERELDQIGLAEEI---LEQTYASLSPGQQTKALLA 131
Cdd:PRK14247 79 ELRRRVQMVfqipnpipnlsifenvalglkLNRLVKSKKELQERVRWALEKAQLWDEVkdrLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 132 AMFADQNSFQLIDEPTNHLD---AAGRDLLAKYLKQKQGYIVVSHDRYFLNQVIDHVISIDRAQISSFKGNYETWAAERA 208
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDpenTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
....*...
gi 488922799 209 NADEREIS 216
Cdd:PRK14247 239 ELTEKYVT 246
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
36-164 |
3.93e-06 |
|
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: 47.64 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 36 LIGRNGRGKTTLMKILQNQVEYEGKVETNLKFNYFPAKITE----------PQDSVRMVLMkiTGRDYSDFweverELDQ 105
Cdd:cd03233 38 VLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKEFAekypgeiiyvSEEDVHFPTL--TVRETLDF-----ALRC 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488922799 106 IGlaeeilEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYLKQ 164
Cdd:cd03233 111 KG------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRT 163
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
307-480 |
3.96e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 47.97 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 307 ALLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLG-----------QNELIAKGNLKIRENLRIS 375
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGivprdagniiiDDEDISLLPLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 376 YLPQD---------FDQLQGTLEQfaaekeveVQDLLAMLRKLGFERTMFDYRIEQM--------SMGQKRKVALARSLC 438
Cdd:PRK10895 82 YLPQEasifrrlsvYDNLMAVLQI--------RDDLSAEQREDRANELMEEFHIEHLrdsmgqslSGGERRRVEIARALA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488922799 439 EEANLYIWDEPLNYLDVITREQIQNLVLKFKPT---LLVVEHD-RE 480
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSglgVLITDHNvRE 199
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
271-477 |
4.13e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 48.67 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 271 DRAEKKLTDKKQLLKNIEIQDELQLNY-QPYLGPQNNALLEADSLVLQRAGKLLNQPLNLELKKNERMVIQGENGSGKST 349
Cdd:PRK13536 3 TRAVAEEAPRRLELSPIERKHQGISEAkASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 350 LIKAMLGqneLIAKGNLKI---------RENL---RISYLPQdFDQLQgtlEQFAAEKEV------------EVQDLLAM 405
Cdd:PRK13536 83 IARMILG---MTSPDAGKItvlgvpvpaRARLaraRIGVVPQ-FDNLD---LEFTVRENLlvfgryfgmstrEIEAVIPS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488922799 406 LrkLGFER--TMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITR----EQIQNLVLKFKpTLLVVEH 477
Cdd:PRK13536 156 L--LEFARleSKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARhliwERLRSLLARGK-TILLTTH 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
327-494 |
4.71e-06 |
|
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: 47.72 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLG-----------QNELIAKGNLKIREnlrISYLPQD---------FDQLQG 386
Cdd:cd03296 21 VSLDIPSGELVALLGPSGSGKTTLLRLIAGlerpdsgtilfGGEDATDVPVQERN---VGFVFQHyalfrhmtvFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 387 TLE-------QFAAEKEVEVQDLLAMLRKLGFErtmfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITRE 459
Cdd:cd03296 98 GLRvkprserPPEAEIRAKVHELLKLVQLDWLA----DRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRK 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 488922799 460 QIQNLVLKFKP----TLLVVEHDREFVQKIATQTVNLKK 494
Cdd:cd03296 174 ELRRWLRRLHDelhvTTVFVTHDQEEALEVADRVVVMNK 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
327-478 |
5.38e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 48.26 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKST---LIKAMLGQNE------------LIAKGNLKIRENLRISYLPQDFDQLQGTLEQ- 390
Cdd:PRK13640 26 ISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDnpnskitvdgitLTAKTVWDIREKVGIVFQNPDNQFVGATVGDd 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 391 --FAAE-KEVEVQDLLAMLRKLGFERTMFDYRIEQ---MSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNL 464
Cdd:PRK13640 106 vaFGLEnRAVPRPEMIKIVRDVLADVGMLDYIDSEpanLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKL 185
|
170
....*....|....*...
gi 488922799 465 VLKFKP----TLLVVEHD 478
Cdd:PRK13640 186 IRKLKKknnlTVISITHD 203
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-193 |
5.68e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 48.06 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLKFNYFPAKI-- 74
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILtgllkpqSGEIKIDGITISKENLKEIRKKIgi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 75 -----------TEPQDSVRMVL--MKITGRDYSDFweVERELDQIGLaEEILEQTYASLSPGQQTKALLAAMFADQNSFQ 141
Cdd:PRK13632 88 ifqnpdnqfigATVEDDIAFGLenKKVPPKKMKDI--IDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488922799 142 LIDEPTNHLDAAGRDLLAKYLK--QKQGY---IVVSHDryfLNQVI--DHVISIDRAQI 193
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVdlRKTRKktlISITHD---MDEAIlaDKVIVFSEGKL 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
327-492 |
6.66e-06 |
|
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: 46.75 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQ-NELIAKGNLKIrENLRISYLPQDFDQLQGTLEQFAAEKEVEVQDLLAM 405
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpKYEVTEGEILF-KGEDITDLPPEERARLGIFLAFQYPPEIPGVKNADF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 406 LRKLGfertmfdyriEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKP---TLLVVEHDREFV 482
Cdd:cd03217 98 LRYVN----------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITHYQRLL 167
|
170
....*....|
gi 488922799 483 QKIATQTVNL 492
Cdd:cd03217 168 DYIKPDRVHV 177
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
327-482 |
6.82e-06 |
|
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: 47.81 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLG-----QNELIAKG-NLKIRENL-----RISYLPQDFD-QLQGTLEQ---- 390
Cdd:TIGR04520 21 VSLSIEKGEFVAIIGHNGSGKSTLAKLLNGlllptSGKVTVDGlDTLDEENLweirkKVGMVFQNPDnQFVGATVEddva 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 391 FAAE------KEVE--VQDLLAMLRklgfertMFDYRIE---QMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITR- 458
Cdd:TIGR04520 101 FGLEnlgvprEEMRkrVDEALKLVG-------MEDFRDRephLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRk 173
|
170 180
....*....|....*....|....*..
gi 488922799 459 ---EQIQNLVLKFKPTLLVVEHDREFV 482
Cdd:TIGR04520 174 evlETIRKLNKEEGITVISITHDMEEA 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
328-449 |
7.00e-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: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 328 NLELKKNERMVIQGENGSGKSTLIKAMLGQ--------------------NELIAKG------------NLKIRENLRIS 375
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVyqpdsgeilldgepvrfrspRDAQAAGiaiihqelnlvpNLSVAENIFLG 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488922799 376 YLPQDFdqlqGTLEQFAAEKEVEvqdllAMLRKLGFE---RTmfdyRIEQMSMGQKRKVALARSLCEEANLYIWDEP 449
Cdd:COG1129 104 REPRRG----GLIDWRAMRRRAR-----ELLARLGLDidpDT----PVGDLSVAQQQLVEIARALSRDARVLILDEP 167
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
327-477 |
7.07e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 47.77 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMlgqNELI--AKGNL--------------KIRENLRISYLPQDfDQLQGTLEQ 390
Cdd:PRK13633 29 VNLEVKKGEFLVILGRNGSGKSTIAKHM---NALLipSEGKVyvdgldtsdeenlwDIRNKAGMVFQNPD-NQIVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 391 ----FAAE------KEV--EVQDllaMLRKLGfertMFDYRIEQ---MSMGQKRKVALARSLCEEANLYIWDEPLNYLDV 455
Cdd:PRK13633 105 edvaFGPEnlgippEEIreRVDE---SLKKVG----MYEYRRHAphlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180
....*....|....*....|....*.
gi 488922799 456 ITREQ----IQNLVLKFKPTLLVVEH 477
Cdd:PRK13633 178 SGRREvvntIKELNKKYGITIILITH 203
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
327-480 |
7.97e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 48.02 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNELIAkGNLKIrENLRISYLPQDFDQLQGTLEQFA-------------- 392
Cdd:PRK09452 33 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDS-GRIML-DGQDITHVPAENRHVNTVFQSYAlfphmtvfenvafg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 393 --------AEKEVEVQDLLAMLRKLGFErtmfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQN- 463
Cdd:PRK09452 111 lrmqktpaAEITPRVMEALRMVQLEEFA----QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNe 186
|
170 180
....*....|....*....|
gi 488922799 464 ---LVLKFKPTLLVVEHDRE 480
Cdd:PRK09452 187 lkaLQRKLGITFVFVTHDQE 206
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-51 |
8.43e-06 |
|
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: 46.84 E-value: 8.43e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 488922799 4 IQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL 51
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI 48
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-193 |
8.57e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 47.05 E-value: 8.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 1 MGIIQLKNVSFSYDNQIkpVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL---------------------------QN 53
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirvgditidtarslsqqKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 54 QV----EYEGKVETNlkFNYFPAK------ITEPqdsvrmVLMKITGRDYSDfwEVEREL-DQIGLAEEilEQTYAS-LS 121
Cdd:PRK11264 79 LIrqlrQHVGFVFQN--FNLFPHRtvleniIEGP------VIVKGEPKEEAT--ARARELlAKVGLAGK--ETSYPRrLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488922799 122 PGQQTKALLAAMFADQNSFQLIDEPTNHLDAagrDLLAKYL-------KQKQGYIVVSHDRYFLNQVIDHVISIDRAQI 193
Cdd:PRK11264 147 GGQQQRVAIARALAMRPEVILFDEPTSALDP---ELVGEVLntirqlaQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
325-477 |
1.01e-05 |
|
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: 46.76 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIKAML-------GQNELiakGNLKIRE-NLR-----ISYLPQDFDQLQGTL--- 388
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLErfydptsGEILL---DGVDIRDlNLRwlrsqIGLVSQEPVLFDGTIaen 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 389 -----------EQFAAEKEVEVQDLLAMLRKlGFErTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVIT 457
Cdd:cd03249 97 irygkpdatdeEVEEAAKKANIHDFIMSLPD-GYD-TLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180
....*....|....*....|..
gi 488922799 458 REQIQNLVLKFKP--TLLVVEH 477
Cdd:cd03249 175 EKLVQEALDRAMKgrTTIVIAH 196
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-183 |
1.04e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 2 GIIQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEYE-GKVE-----------TNLK--F 67
Cdd:PLN03232 1233 GSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEkGRIMiddcdvakfglTDLRrvL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 68 NYFPAKITEPQDSVRMVLMKITGRDYSDFWE-VER-------ELDQIGLAEEILEQTyASLSPGQQTKALLAAMFADQNS 139
Cdd:PLN03232 1313 SIIPQSPVLFSGTVRFNIDPFSEHNDADLWEaLERahikdviDRNPFGLDAEVSEGG-ENFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488922799 140 FQLIDEPTNHLDAAGRDLLAKYLKQK---QGYIVVSHDryfLNQVID 183
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLIQRTIREEfksCTMLVIAHR---LNTIID 1435
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-173 |
1.36e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 46.69 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEYEGKVETNLKFNYFPAKITEPQ-DSV 81
Cdd:PRK14239 5 ILQVSDLSVYYNK--KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRtDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 82 R------MVL-----------------MKITG-RDYSDFWE-VERELDQIGLAEEILEQTYAS---LSPGQQTKALLAAM 133
Cdd:PRK14239 83 DlrkeigMVFqqpnpfpmsiyenvvygLRLKGiKDKQVLDEaVEKSLKGASIWDEVKDRLHDSalgLSGGQQQRVCIARV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488922799 134 FADQNSFQLIDEPTNHLD--AAGR--DLLAKyLKQKQGYIVVSH 173
Cdd:PRK14239 163 LATSPKIILLDEPTSALDpiSAGKieETLLG-LKDDYTMLLVTR 205
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
311-486 |
1.93e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 46.95 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 311 ADSLVLQRAGKLLN-QPLNLELKKNERMVIQGENGSGKST-------LIKAMLGQNEL----IAK-GNLKIRENLR--IS 375
Cdd:PRK10070 30 SKEQILEKTGLSLGvKDASLAIEEGEIFVIMGLSGSGKSTmvrllnrLIEPTRGQVLIdgvdIAKiSDAELREVRRkkIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 376 YLPQDF---------DQLQGTLEQFAAEKEVEVQDLLAMLRKLGFERTMFDYRiEQMSMGQKRKVALARSLCEEANLYIW 446
Cdd:PRK10070 110 MVFQSFalmphmtvlDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488922799 447 DEPLNYLDVITREQIQNLVLKFKP----TLLVVEHDREFVQKIA 486
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLQAkhqrTIVFISHDLDEAMRIG 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-193 |
1.93e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 45.84 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSY--------------------DNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQV 55
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIagileptSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 56 EYEGKV----ETNLKFNyfpakitePQDSVR------MVLMKITGRdysdfwEVERELDQI----GLaEEILEQ---TYa 118
Cdd:COG1134 84 EVNGRVsallELGAGFH--------PELTGReniylnGRLLGLSRK------EIDEKFDEIvefaEL-GDFIDQpvkTY- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 119 slSPGQQTKalLA---AMFADqnsFQ--LIDEPTnhldAAG--------RDLLAKYLKQKQGYIVVSHDRYFLNQVIDHV 185
Cdd:COG1134 148 --SSGMRAR--LAfavATAVD---PDilLVDEVL----AVGdaafqkkcLARIRELRESGRTVIFVSHSMGAVRRLCDRA 216
|
....*...
gi 488922799 186 ISIDRAQI 193
Cdd:COG1134 217 IWLEKGRL 224
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-185 |
2.14e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 46.21 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 34 LGLIGRNGRGKTTLMKILQNQV-------EYEGKVETNLKF-------NYFpAKITE--------PQ----------DSV 81
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLkpnlgkfDDPPDWDEILDEfrgselqNYF-TKLLEgdvkvivkPQyvdlipkavkGKV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 82 RMVLMKITGRDYSDfwEVereLDQIGLaEEILEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGR----DL 157
Cdd:cd03236 108 GELLKKKDERGKLD--EL---VDQLEL-RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRlnaaRL 181
|
170 180
....*....|....*....|....*...
gi 488922799 158 LAKYLKQKQGYIVVSHDRYFLNQVIDHV 185
Cdd:cd03236 182 IRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
327-486 |
2.23e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 46.33 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIK-----------AMLGQNELIAKGNLK-IRENLRISYLPQDFDQLQGTLEQFAA- 393
Cdd:PRK13652 23 INFIAPRNSRIAVIGPNGAGKSTLFRhfngilkptsgSVLIRGEPITKENIReVRKFVGLVFQNPDDQIFSPTVEQDIAf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 394 -------EKEVEVQDLLAMLRKLGFERtMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQ----IQ 462
Cdd:PRK13652 103 gpinlglDEETVAHRVSSALHMLGLEE-LRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKElidfLN 181
|
170 180
....*....|....*....|....
gi 488922799 463 NLVLKFKPTLLVVEHDREFVQKIA 486
Cdd:PRK13652 182 DLPETYGMTVIFSTHQLDLVPEMA 205
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
327-494 |
2.25e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.01 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAML----GQNELIAKG----NLKIRENL----RISYLPQD--------FDQLQG 386
Cdd:PRK15134 305 ISFTLRPGETLGLVGESGSGKSTTGLALLrlinSQGEIWFDGqplhNLNRRQLLpvrhRIQVVFQDpnsslnprLNVLQI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 387 TLEQF--------AAEKEVEVqdlLAMLRKLGFE-RTMFDYRIEqMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVIT 457
Cdd:PRK15134 385 IEEGLrvhqptlsAAQREQQV---IAVMEEVGLDpETRHRYPAE-FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTV 460
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488922799 458 REQIQNLVLKFKPT----LLVVEHDREFVQKIATQTVNLKK 494
Cdd:PRK15134 461 QAQILALLKSLQQKhqlaYLFISHDLHVVRALCHQVIVLRQ 501
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
327-486 |
2.45e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 45.98 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIK---AML----GQNELIAK------GNLKIRENLRISYLPQDFDQLQ-------- 385
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQhfnALLkpssGTITIAGYhitpetGNKNLKKLRKKVSLVFQFPEAQlfentvlk 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 386 ----GTLEQFAAEKEVEVQdLLAMLRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQI 461
Cdd:PRK13641 106 dvefGPKNFGFSEDEAKEK-ALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEM 184
|
170 180
....*....|....*....|....*...
gi 488922799 462 QNLVLKFKP---TLLVVEHDREFVQKIA 486
Cdd:PRK13641 185 MQLFKDYQKaghTVILVTHNMDDVAEYA 212
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
318-457 |
2.68e-05 |
|
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: 44.95 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 318 RAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLGQNEliakGNLKIRENLRISYLP--QDFDQLQGTLEQFAAE- 394
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE----GNVSVEGDIHYNGIPykEFAEKYPGEIIYVSEEd 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488922799 395 ---KEVEVQDLL---------AMLRKLgfertmfdyrieqmSMGQKRKVALARSLCEEANLYIWDEPLNYLDVIT 457
Cdd:cd03233 93 vhfPTLTVRETLdfalrckgnEFVRGI--------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
309-488 |
3.00e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.46 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 309 LEADSLVLQRAGKLLNQpLNLELKKNERMVIQGENGSGKSTLIKAMLG---------QNELIAKGNLKIRENLR---ISY 376
Cdd:PRK10418 5 IELRNIALQAAQPLVHG-VSLTLQRGRVLALVGGSGSGKSLTCAAALGilpagvrqtAGRVLLDGKPVAPCALRgrkIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 377 LPQD----FDQLQgTLEQFAAE------KEVEVQDLLAMLRKLGFE---RTMFDYRIEqMS--MGQKRKVALArsLCEEA 441
Cdd:PRK10418 84 IMQNprsaFNPLH-TMHTHAREtclalgKPADDATLTAALEAVGLEnaaRVLKLYPFE-MSggMLQRMMIALA--LLCEA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488922799 442 NLYIWDEPLNYLDVITREQI----QNLVLKFKPTLLVVEHDREFVQKIATQ 488
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARIldllESIVQKRALGMLLVTHDMGVVARLADD 210
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
321-461 |
3.12e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.94 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 321 KLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLG-----------------------QNELIAKG-------NLKIRE 370
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGllnpekgeilferqsikkdlctyQKQLCFVGhrsginpYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 371 NLRIsylpqDFDQLQGTLEQfaaekevevqDLLAMLRKLGFertMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPL 450
Cdd:PRK13540 94 NCLY-----DIHFSPGAVGI----------TELCRLFSLEH---LIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170
....*....|.
gi 488922799 451 NYLDVITREQI 461
Cdd:PRK13540 156 VALDELSLLTI 166
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
299-464 |
3.26e-05 |
|
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: 46.22 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 299 PYLGPQNNALLEADSLV---------LQRAGKLLN--QPLNLELKKNERMVIQGENGSGKSTLIKAMLGqneLIAKGNlk 367
Cdd:COG4172 266 RPVPPDAPPLLEARDLKvwfpikrglFRRTVGHVKavDGVSLTLRRGETLGLVGESGSGKSTLGLALLR---LIPSEG-- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 368 irenlRISYLPQDFDQLQG-------------------------TLEQFAAE---------KEVEVQDL-LAMLRKLGFE 412
Cdd:COG4172 341 -----EIRFDGQDLDGLSRralrplrrrmqvvfqdpfgslsprmTVGQIIAEglrvhgpglSAAERRARvAEALEEVGLD 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488922799 413 RTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNL 464
Cdd:COG4172 416 PAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDL 467
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
321-480 |
3.37e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 321 KLLNQpLNLELKKNERMVIQGENGSGKSTLIKAMLG------QNELIAKGNLK--------IRENlrISYLPQDFDQ--- 383
Cdd:PRK10938 274 PILHN-LSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgySNDLTLFGRRRgsgetiwdIKKH--IGYVSSSLHLdyr 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 384 ---------LQGTLEQFAAEKEV-EVQDLLAM--LRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLN 451
Cdd:PRK10938 351 vstsvrnviLSGFFDSIGIYQAVsDRQQKLAQqwLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQ 430
|
170 180 190
....*....|....*....|....*....|....*..
gi 488922799 452 YLDVITREqiqnLVLKF--------KPTLLVVEHDRE 480
Cdd:PRK10938 431 GLDPLNRQ----LVRRFvdvlisegETQLLFVSHHAE 463
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-185 |
3.49e-05 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 44.83 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL---------QNQVEYEGKVETNLkfnyfpaki 74
Cdd:cd03217 1 LEIKDLHVSVGG--KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghpkyevtEGEILFKGEDITDL--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 75 tEPQDSVRMVLM-------KITGRDYSDFWeveRELDqiglaeeileqtyASLSPGQQTKALLAAMFADQNSFQLIDEPT 147
Cdd:cd03217 70 -PPEERARLGIFlafqyppEIPGVKNADFL---RYVN-------------EGFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488922799 148 NHLDAAGRDLLAK----YLKQKQGYIVVSHDRYFLNQVI-DHV 185
Cdd:cd03217 133 SGLDIDALRLVAEvinkLREEGKSVLIITHYQRLLDYIKpDRV 175
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
312-494 |
3.71e-05 |
|
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: 45.15 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 312 DSLVLQRagkllnqpLNLELKKNERMVIQGENGSGKSTLIKAM-----LGQNELIAKG---NLKIRENLR-----ISYLP 378
Cdd:cd03248 26 DTLVLQD--------VSFTLHPGEVTALVGPSGSGKSTVVALLenfyqPQGGQVLLDGkpiSQYEHKYLHskvslVGQEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 379 QDF-----DQLQGTLEQFAAEKEVEVQDL-----LAMLRKLGFErTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDE 448
Cdd:cd03248 98 VLFarslqDNIAYGLQSCSFECVKEAAQKahahsFISELASGYD-TEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488922799 449 PLNYLDVITREQIQNLVLKF--KPTLLVVEHDREFVQKiATQTVNLKK 494
Cdd:cd03248 177 ATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVER-ADQILVLDG 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
327-480 |
3.74e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 45.37 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLG-----------QNELIAKGNLK-IRENLRISYLPQDfDQLQG-TLEQ--- 390
Cdd:PRK13632 28 VSFEINEGEYVAILGHNGSGKSTISKILTGllkpqsgeikiDGITISKENLKeIRKKIGIIFQNPD-NQFIGaTVEDdia 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 391 FAAE-KEVEVQDLLAMLRKLGFERTMFDY---RIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVL 466
Cdd:PRK13632 107 FGLEnKKVPPKKMKDIIDDLAKKVGMEDYldkEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMV 186
|
170
....*....|....*...
gi 488922799 467 KF----KPTLLVVEHDRE 480
Cdd:PRK13632 187 DLrktrKKTLISITHDMD 204
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-151 |
3.84e-05 |
|
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: 45.25 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLK---------- 66
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLnglveptSGSVLIDGTDINKLKgkalrqlrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 67 ----FNYFPakITEPQDSVRMVLMkitGR-DYSDFW--------EVERE-----LDQIGLAEEILEQTyASLSPGQQTKA 128
Cdd:cd03256 80 igmiFQQFN--LIERLSVLENVLS---GRlGRRSTWrslfglfpKEEKQralaaLERVGLLDKAYQRA-DQLSGGQQQRV 153
|
170 180
....*....|....*....|...
gi 488922799 129 LLAAMFADQNSFQLIDEPTNHLD 151
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLD 176
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
327-488 |
4.06e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 46.26 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAM-------------LGQNelIAKGNLKIRENLRISYLPQDFdQLQGTLEQFAA 393
Cdd:PRK10535 27 ISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptsgtyrvAGQD--VATLDADALAQLRREHFGFIF-QRYHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 394 EKEVEVQDLLA-------------MLRKLGF-ERTmfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITRE 459
Cdd:PRK10535 104 AQNVEVPAVYAglerkqrllraqeLLQRLGLeDRV--EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE 181
|
170 180 190
....*....|....*....|....*....|..
gi 488922799 460 QIQNLVLKFKP---TLLVVEHDrefvQKIATQ 488
Cdd:PRK10535 182 EVMAILHQLRDrghTVIIVTHD----PQVAAQ 209
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
327-493 |
4.16e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 45.03 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNELiaKGNLKIREnlRISYLPQD-------------------------- 380
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL--ESEVRVEG--RVEFFNQNiyerrvnlnrlrrqvsmvhpkpnlfp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 381 ---FDQLQGTLEQFAAEKEVEVQDLLAMLRKLGFERTMFDYRIEQ----MSMGQKRKVALARSLCEEANLYIWDEPLNYL 453
Cdd:PRK14258 102 msvYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488922799 454 DVITREQ----IQNLVLKFKPTLLVVEHDREFVQKIATQTVNLK 493
Cdd:PRK14258 182 DPIASMKveslIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFK 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-174 |
4.21e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 45.16 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNQIkpVFDQVALEIDASWKLGLIGRNGRGKTTLMKI------LQNQVEYEGKVETNLKFNYFP-AKIT 75
Cdd:PRK14243 10 VLRTENLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFRVEGKVTFHGKNLYAPdVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 76 EPQDSVRMVLMK-----------------ITGRDySDFWE-VERELDQIGLAEEI---LEQTYASLSPGQQTKALLAAMF 134
Cdd:PRK14243 88 EVRRRIGMVFQKpnpfpksiydniaygarINGYK-GDMDElVERSLRQAALWDEVkdkLKQSGLSLSGGQQQRLCIARAI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488922799 135 ADQNSFQLIDEPTNHLDAAGR---DLLAKYLKQKQGYIVVSHD 174
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTlriEELMHELKEQYTIIIVTHN 209
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-174 |
4.89e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 45.08 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQIKPVF---DQVALEIDASWKLGLIGRNGRGKTTLMKILQN-QVEYEGKVETNLKFNYFPAKITEPQD 79
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELkalDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAlLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 80 SVRMVLMKITGR--------------------DYSDFWE--------------VERE---------LDQIGLAEEILEQT 116
Cdd:PRK13651 83 VLEKLVIQKTRFkkikkikeirrrvgvvfqfaEYQLFEQtiekdiifgpvsmgVSKEeakkraakyIELVGLDESYLQRS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488922799 117 YASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGR----DLLAKYLKQKQGYIVVSHD 174
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVkeilEIFDNLNKQGKTIILVTHD 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
327-486 |
5.27e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 45.00 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIK-----------AMLGQNELI---AKGNLKIREnlRISYLPQDFDQ--------- 383
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMnlsgllrpqkgAVLWQGKPLdysKRGLLALRQ--QVATVFQDPEQqifytdids 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 384 -LQGTLEQFA-AEKEV--EVQDLLAMLRKLGFERTmfdyRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITRE 459
Cdd:PRK13638 98 dIAFSLRNLGvPEAEItrRVDEALTLVDAQHFRHQ----PIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190
....*....|....*....|....*....|
gi 488922799 460 QIQNLVLKFKPT---LLVVEHDREFVQKIA 486
Cdd:PRK13638 174 QMIAIIRRIVAQgnhVIISSHDIDLIYEIS 203
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-193 |
5.34e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 45.21 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQI---KPVFDQVALEIDASWKLGLIGRNGRGKTTLM-------KILQNQVEYEGKVET------NLK- 66
Cdd:PRK13641 3 IKFENVDYIYSPGTpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMqhfnallKPSSGTITIAGYHITpetgnkNLKk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 67 --------FNYFPAKITEpqdsvRMVLMKIT-GRDYSDFWEVERE------LDQIGLAEEILEQTYASLSPGQQTKALLA 131
Cdd:PRK13641 83 lrkkvslvFQFPEAQLFE-----NTVLKDVEfGPKNFGFSEDEAKekalkwLKKVGLSEDLISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488922799 132 AMFADQNSFQLIDEPTNHLDAAGRDLLAKYLK--QKQGY--IVVSHDRYFLNQVIDHVISIDRAQI 193
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKdyQKAGHtvILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-189 |
6.17e-05 |
|
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: 43.30 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILqnqveyegkvetNLKFNYFPAKITEPQDSVrm 83
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL------------AGLWPWGSGRIGMPEGED-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 84 vLMKITGRDYsdfwevereLDQIGLAEEILEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYLK 163
Cdd:cd03223 66 -LLFLPQRPY---------LPLGTLREQLIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK 135
|
170 180
....*....|....*....|....*..
gi 488922799 164 QKQ-GYIVVSHdRYFLNQVIDHVISID 189
Cdd:cd03223 136 ELGiTVISVGH-RPSLWKFHDRVLDLD 161
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-186 |
6.17e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.71 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 27 EIDASWKLGLIGRNGRGKTTLMKILQNQVEYEGKvetnlkfnyfpakitepqdsvrmvlmkitgrdysdfwevERELDQI 106
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD---------------------------------------NDEWDGI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 107 GLAeeiLEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYLKQ-----KQGYIVVSHDRYFLNQV 181
Cdd:cd03222 62 TPV---YKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRlseegKKTALVVEHDLAVLDYL 138
|
....*
gi 488922799 182 IDHVI 186
Cdd:cd03222 139 SDRIH 143
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
306-478 |
6.58e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 44.70 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 306 NALLEADSLVLQRAGKLLNQPLN---LELKKNERMVIQGENGSGKSTLIKAMLGQNE------------LIAKGNLKIRE 370
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEefegkvkidgelLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 371 NLRISYLPQDFDQLQGTLEQ---FAAEKE-VEVQDLLAMLRKLGFERTMFDYRIEQ---MSMGQKRKVALARSLCEEANL 443
Cdd:PRK13642 82 KIGMVFQNPDNQFVGATVEDdvaFGMENQgIPREEMIKRVDEALLAVNMLDFKTREparLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 488922799 444 YIWDEPLNYLDVITREQIQNLVL----KFKPTLLVVEHD 478
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHeikeKYQLTVLSITHD 200
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-164 |
8.72e-05 |
|
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: 44.46 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 2 GIIQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEYEGKVETN-------------LKFN 68
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDgvswnsvplqkwrKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 69 YFPAKITEPQDSVRMVLMKITGRDYSDFWEVERE------LDQI-GLAEEILEQTYASLSPGQQTKALLAAMFADQNSFQ 141
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEvglksvIEQFpGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180
....*....|....*....|...
gi 488922799 142 LIDEPTNHLDAAGRDLLAKYLKQ 164
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQ 183
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
315-477 |
9.00e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 45.39 E-value: 9.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 315 VLQRAGKLLNQPLNLELKKNERMVIQGENGSGKSTLIKAMLG----QNELIAKGNLKIRENL-----RISYLPQD----- 380
Cdd:TIGR01257 937 IFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGllppTSGTVLVGGKDIETNLdavrqSLGMCPQHnilfh 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 381 ----------FDQLQGTlEQFAAEKEVEvqdllAMLRKLGFERTMfDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPL 450
Cdd:TIGR01257 1017 hltvaehilfYAQLKGR-SWEEAQLEME-----AMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180
....*....|....*....|....*....
gi 488922799 451 NYLDVITREQIQNLVLKFKP--TLLVVEH 477
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKYRSgrTIIMSTH 1118
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
325-455 |
1.02e-04 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 44.06 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIKAMLGqnELIAKGNLKIREN------------LRiSYLPQDFDQLQG------ 386
Cdd:COG4138 13 GPISAQVNAGELIHLIGPNGAGKSTLLARMAG--LLPGQGEILLNGRplsdwsaaelarHR-AYLSQQQSPPFAmpvfqy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 387 -TLEQFAAEKEVEVQDLLAML-RKLGFErtmfDY---RIEQMSMGQKRKVALARSLCE-------EANLYIWDEPLNYLD 454
Cdd:COG4138 90 lALHQPAGASSEAVEQLLAQLaEALGLE----DKlsrPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD 165
|
.
gi 488922799 455 V 455
Cdd:COG4138 166 V 166
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-58 |
1.06e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.11 E-value: 1.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 488922799 2 GIIQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVEYE 58
Cdd:PLN03130 1236 GSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE 1292
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-193 |
1.06e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 44.27 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQI---KPVFDQVALEIDASWKLGLIGRNGRGKTTLM------------KILQNQVEYEGKvETNLK-- 66
Cdd:PRK13637 3 IKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIqhlngllkptsgKIIIDGVDITDK-KVKLSdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 67 -------FNY-----F-----------PAKITEPQDSVRMVL---MKITGRDYsdfwevereldqiglaEEILEQTYASL 120
Cdd:PRK13637 82 rkkvglvFQYpeyqlFeetiekdiafgPINLGLSEEEIENRVkraMNIVGLDY----------------EDYKDKSPFEL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488922799 121 SPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRD-LLAKYLKQKQGY----IVVSHDRYFLNQVIDHVISIDRAQI 193
Cdd:PRK13637 146 SGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDeILNKIKELHKEYnmtiILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-193 |
1.24e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 43.92 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDN----QIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQ-VEYEGKV---------ETNL--- 65
Cdd:PRK13633 4 MIKCKNVSYKYESneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALlIPSEGKVyvdgldtsdEENLwdi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 66 ----------KFNYFPAKITE------------PQDSVRMvlmkitgrdysdfwEVERELDQIGLAEeilEQTYAS--LS 121
Cdd:PRK13633 84 rnkagmvfqnPDNQIVATIVEedvafgpenlgiPPEEIRE--------------RVDESLKKVGMYE---YRRHAPhlLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488922799 122 PGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYLKQ--KQGYIVVSHDRYFLNQVI--DHVISIDRAQI 193
Cdd:PRK13633 147 GGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVeaDRIIVMDSGKV 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
324-494 |
1.28e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 43.85 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 324 NQPLN---LELKKNERMVIQGENGSGKSTLIKAMLG----------QNELIakGNLKIRENLRISYLPQDFDQLQGTLEQ 390
Cdd:PRK09984 17 HQALHavdLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagsHIELL--GRTVQREGRLARDIRKSRANTGYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 391 FAAEKEVEVQD--LLAMLRKLGFERTMFDY------------------------RIEQMSMGQKRKVALARSLCEEANLY 444
Cdd:PRK09984 95 FNLVNRLSVLEnvLIGALGSTPFWRTCFSWftreqkqralqaltrvgmvhfahqRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488922799 445 IWDEPLNYLDV----ITREQIQNLVLKFKPTLLVVEHDREFVQKIATQTVNLKK 494
Cdd:PRK09984 175 LADEPIASLDPesarIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQ 228
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-207 |
1.40e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 44.32 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 2 GIIQLKNVSFSYDNQiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLKFNYFPAKI 74
Cdd:PRK10790 339 GRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLmgyypltEGEIRLDGRPLSSLSHSVLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 75 TE-PQDSVRM---VLMKIT-GRDYSD--FWEVereLDQIGLAE-----------EILEQTyASLSPGQQTKALLAAMFAD 136
Cdd:PRK10790 418 AMvQQDPVVLadtFLANVTlGRDISEeqVWQA---LETVQLAElarslpdglytPLGEQG-NNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488922799 137 QNSFQLIDEPTNHLDAAGRDLLAKYL---KQKQGYIVVSHDryfLNQVI--DHVISIDRAQISSfKGNYETWAAER 207
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQAIQQALaavREHTTLVVIAHR---LSTIVeaDTILVLHRGQAVE-QGTHQQLLAAQ 565
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
262-477 |
1.85e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.20 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 262 VMSKALNIRDRAEKKLTDKKQLLKNIEIQDE---LQLNYQPYLGPQNNALLEADSLVLQRAGKL--LNQPLNLELKKNER 336
Cdd:PLN03232 1185 LLSGVLRQASKAENSLNSVERVGNYIDLPSEataIIENNRPVSGWPSRGSIKFEDVHLRYRPGLppVLHGLSFFVSPSEK 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 337 MVIQGENGSGKSTLIKAMLGQNELiAKGNLKIRE---------NLR--ISYLPQDFDQLQGT----LEQFAAEKEVEVQD 401
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLNALFRIVEL-EKGRIMIDDcdvakfgltDLRrvLSIIPQSPVLFSGTvrfnIDPFSEHNDADLWE 1343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 402 LL--AMLRKLgFERTMF--DYRI----EQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVL-KFKP-T 471
Cdd:PLN03232 1344 ALerAHIKDV-IDRNPFglDAEVseggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIReEFKScT 1422
|
....*.
gi 488922799 472 LLVVEH 477
Cdd:PLN03232 1423 MLVIAH 1428
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-201 |
1.88e-04 |
|
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: 44.17 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQVE-YEGKVETNLKFNYFPAKITEPQDSVR 82
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDkVEGHVHMKGSVAYVPQQAWIQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 83 MVLM---KITGRDYSDFWEV-----ERELDQIGLAEEILEQTyASLSPGQQTKALLA-AMFADQNSFqLIDEPTNHLDA- 152
Cdd:TIGR00957 717 ENILfgkALNEKYYQQVLEAcallpDLEILPSGDRTEIGEKG-VNLSGGQKQRVSLArAVYSNADIY-LFDDPLSAVDAh 794
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488922799 153 AGRDLLAK------YLKQKQgYIVVSHDRYFLNQViDHVISIDRAQISSFkGNYE 201
Cdd:TIGR00957 795 VGKHIFEHvigpegVLKNKT-RILVTHGISYLPQV-DVIIVMSGGKISEM-GSYQ 846
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-52 |
2.01e-04 |
|
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: 42.86 E-value: 2.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 488922799 4 IQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQ 52
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQ 49
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
327-477 |
2.31e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 43.18 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQ----------NELIAKGNLKIRE--NLR--------------------- 373
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlqptegkvtvGDIVVSSTSKQKEikPVRkkvgvvfqfpesqlfeetvlk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 374 -ISYLPQDFDQLQGTLEQFAAEKevevqdllamLRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNY 452
Cdd:PRK13643 105 dVAFGPQNFGIPKEKAEKIAAEK----------LEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180
....*....|....*....|....*...
gi 488922799 453 LDVITREQIQNL---VLKFKPTLLVVEH 477
Cdd:PRK13643 175 LDPKARIEMMQLfesIHQSGQTVVLVTH 202
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-195 |
2.35e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 43.18 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNQiKPVFDQVALEIDASWKLG----LIGRNGRGKTTLMKILQNQVEyegKVETNLKFNYFPAKITEPQ 78
Cdd:PRK13643 1 MIKFEKVNYTYQPN-SPFASRALFDIDLEVKKGsytaLIGHTGSGKSTLLQHLNGLLQ---PTEGKVTVGDIVVSSTSKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 79 DSVRMVLMKI----------------------------TGRDYSDFWEVEReLDQIGLAEEILEQTYASLSPGQQTKALL 130
Cdd:PRK13643 77 KEIKPVRKKVgvvfqfpesqlfeetvlkdvafgpqnfgIPKEKAEKIAAEK-LEMVGLADEFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488922799 131 AAMFADQNSFQLIDEPTNHLDAAGRDLLAKYLKQ----KQGYIVVSHDRYFLNQVIDHVISIDRAQISS 195
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESihqsGQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
327-494 |
2.63e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 42.65 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIK-----------AMLGQNELI-----AKGNLKIREN-------LRISYLPQDFD- 382
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRcinflekpsegSIVVNGQTInlvrdKDGQLKVADKnqlrllrTRLTMVFQHFNl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 383 ---------------QLQGTLEQFAAEKEVEvqdllaMLRKLGF-ERTMFDYRIEqMSMGQKRKVALARSLCEEANLYIW 446
Cdd:PRK10619 104 wshmtvlenvmeapiQVLGLSKQEARERAVK------YLAKVGIdERAQGKYPVH-LSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488922799 447 DEPLNYLDVITREQIQNLVLKFK---PTLLVVEHDREFVQKIATQTVNLKK 494
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQ 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
327-354 |
2.70e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 42.38 E-value: 2.70e-04
10 20
....*....|....*....|....*...
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAM 354
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLI 72
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
325-494 |
2.90e-04 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 43.56 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIK--------------------------------AMLGQNELIAKGNlkIRENl 372
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAAllqnlyqptggqvlldgvplvqydhhylhrqvALVGQEPVLFSGS--VREN- 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 373 rISYLPQDFDQLQGTleqfAAEKEVEVQDLLAMLRKlGFErTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNY 452
Cdd:TIGR00958 575 -IAYGLTDTPDEEIM----AAAKAANAHDFIMEFPN-GYD-TEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488922799 453 LDVITREQIQNLVLKFKPTLLVVEHDREFVQKiATQTVNLKK 494
Cdd:TIGR00958 648 LDAECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKK 688
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-52 |
3.29e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 43.41 E-value: 3.29e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 488922799 2 GIIQLKNVSFSYDNQIKPVFDqVALEIDASWKLGLIGRNGRGKTTLMKILQ 52
Cdd:PRK13657 333 GAVEFDDVSFSYDNSRQGVED-VSFEAKPGQTVAIVGPTGAGKSTLINLLQ 382
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
100-193 |
3.71e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 42.26 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 100 ERELDQIGLAEEILEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDA--AGRDL--LAKYLKQKQGYIVVSHDR 175
Cdd:PRK10619 133 VKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPelVGEVLriMQQLAEEGKTMVVVTHEM 212
|
90
....*....|....*...
gi 488922799 176 YFLNQVIDHVISIDRAQI 193
Cdd:PRK10619 213 GFARHVSSHVIFLHQGKI 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-192 |
3.77e-04 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 42.04 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVS--FSYDNQ--IK-PVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYE-GKVETNLkfny 69
Cdd:COG4778 4 LLEVENLSktFTLHLQggKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygnylpdSGSILVRhDGGWVDL---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 70 fpAKItEPQDSVRM-------------VLMKITGRD------YSDFWEVERELDQiglAEEILE-----QTYASLSP--- 122
Cdd:COG4778 80 --AQA-SPREILALrrrtigyvsqflrVIPRVSALDvvaeplLERGVDREEARAR---ARELLArlnlpERLWDLPPatf 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488922799 123 --GQQTKALLAAMFADQNSFQLIDEPTNHLDAAGR----DLLAKYLKQKQGYIVVSHDRYFLNQVIDHVISIDRAQ 192
Cdd:COG4778 154 sgGEQQRVNIARGFIADPPLLLLDEPTASLDAANRavvvELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
325-478 |
3.80e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.52 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 325 QPLNLELKKNERMVIQGENGSGKSTLIKaMLGQNELIAKGNLKI------------------------------REN--- 371
Cdd:PRK11650 21 KGIDLDVADGEFIVLVGPSGCGKSTLLR-MVAGLERITSGEIWIggrvvnelepadrdiamvfqnyalyphmsvRENmay 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 372 -LRISYLPQdfdqlqgtleqfaAEKEVEVQDLLAMLrKLGferTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPL 450
Cdd:PRK11650 100 gLKIRGMPK-------------AEIEERVAEAARIL-ELE---PLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
|
170 180 190
....*....|....*....|....*....|..
gi 488922799 451 NYLD----VITREQIQNLVLKFKPTLLVVEHD 478
Cdd:PRK11650 163 SNLDaklrVQMRLEIQRLHRRLKTTSLYVTHD 194
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
36-263 |
4.13e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.23 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 36 LIGRNGRGKTTLMKILQNQVEY-EGKVETNLKFNYFPAKITEPQDSVRMVLMKITGRDYSDFWEV------ERELDQI-- 106
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLLSQFEIsEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAvrvsqlEADLAQLgg 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 107 GLAEEILEQTyASLSPGQQTKALLA-AMFADQNsFQLIDEPTNHLDA-AG----RDLLAKYLKQKQgYIVVSHDRYFLNQ 180
Cdd:PTZ00243 771 GLETEIGEKG-VNLSGGQKARVSLArAVYANRD-VYLLDDPLSALDAhVGervvEECFLGALAGKT-RVLATHQVHVVPR 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 181 ViDHVISIDRAQIsSFKGNYETW----------AAERANADEREISLNAT-MKKDIKKLEQATRQKQEwsrATERKKAGA 249
Cdd:PTZ00243 848 A-DYVVALGDGRV-EFSGSSADFmrtslyatlaAELKENKDSKEGDADAEvAEVDAAPGGAVDHEPPV---AKQEGNAEG 922
|
250
....*....|....
gi 488922799 250 PDKGFVGHKAAKVM 263
Cdd:PTZ00243 923 GDGAALDAAAGRLM 936
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-51 |
5.29e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 42.70 E-value: 5.29e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488922799 2 GIIQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKIL 51
Cdd:PRK11176 340 GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLL 389
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
341-494 |
5.64e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 341 GENGSGKSTLIKamLGQNELIAK-GNLKIRENLRISYLPQD------------------FDQLQGTLEQFAAEKEVEVQD 401
Cdd:PRK10636 34 GKNGCGKSTLLA--LLKNEISADgGSYTFPGNWQLAWVNQEtpalpqpaleyvidgdreYRQLEAQLHDANERNDGHAIA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 402 LL-----------------AMLRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNL 464
Cdd:PRK10636 112 TIhgkldaidawtirsraaSLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKW 191
|
170 180 190
....*....|....*....|....*....|
gi 488922799 465 VLKFKPTLLVVEHDREFVQKIATQTVNLKK 494
Cdd:PRK10636 192 LKSYQGTLILISHDRDFLDPIVDKIIHIEQ 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-161 |
5.96e-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: 42.50 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVS-FSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQNQveYEGKVETNLKFNYFPAKITEPQDSV 81
Cdd:TIGR02633 257 ILEARNLTcWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGA--YPGKFEGNVFINGKPVDIRNPAQAI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 82 RM---------------------------VLMKITGRDYSDfweVERELDQIGLAEEILEQTYAS-------LSPGQQTK 127
Cdd:TIGR02633 335 RAgiamvpedrkrhgivpilgvgknitlsVLKSFCFKMRID---AAAELQIIGSAIQRLKVKTASpflpigrLSGGNQQK 411
|
170 180 190
....*....|....*....|....*....|....
gi 488922799 128 ALLAAMFADQNSFQLIDEPTNhldaaGRDLLAKY 161
Cdd:TIGR02633 412 AVLAKMLLTNPRVLILDEPTR-----GVDVGAKY 440
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
309-469 |
6.14e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 41.63 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 309 LEADSLVLQRAGKL-LNQpLNLELKKNERMVIQGENGSGKSTLIKAMLGqneLIA--------KG---NLKIREnlRISY 376
Cdd:COG4152 2 LELKGLTKRFGDKTaVDD-VSFTVPKGEIFGLLGPNGAGKTTTIRIILG---ILApdsgevlwDGeplDPEDRR--RIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 377 LPQD---------------FDQLQGtLEQFAAEKEvevqdLLAMLRKLGFErtmfDYR---IEQMSMGQKRKVALARSLC 438
Cdd:COG4152 76 LPEErglypkmkvgeqlvyLARLKG-LSKAEAKRR-----ADEWLERLGLG----DRAnkkVEELSKGNQQKVQLIAALL 145
|
170 180 190
....*....|....*....|....*....|.
gi 488922799 439 EEANLYIWDEPLNYLDVITREQIQNLVLKFK 469
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELA 176
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
22-193 |
6.25e-04 |
|
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: 41.56 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 22 DQVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLKfnyfPAKITE-------------PQDSV 81
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLItgfyrptSGRILFDGRDITGLP----PHRIARlgiartfqnprlfPELTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 82 RM-VLMKITGRDYSDFW------------------EVERELDQIGLAEEILEQTyASLSPGQQtKAL-LAAMFADQNSFQ 141
Cdd:COG0411 97 LEnVLVAAHARLGRGLLaallrlprarreereareRAEELLERVGLADRADEPA-GNLSYGQQ-RRLeIARALATEPKLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488922799 142 LIDEPTNHLDAAGRDLLA---KYLKQKQGY--IVVSHDRYFLNQVIDHVISIDRAQI 193
Cdd:COG0411 175 LLDEPAAGLNPEETEELAeliRRLRDERGItiLLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
412-494 |
6.37e-04 |
|
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: 42.10 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 412 ERTMFDYRI----EQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQN----LVLKFKPTLLVVEHDREFVQ 483
Cdd:TIGR03269 154 EMVQLSHRIthiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaleeAVKASGISMVLTSHWPEVIE 233
|
90
....*....|.
gi 488922799 484 KIATQTVNLKK 494
Cdd:TIGR03269 234 DLSDKAIWLEN 244
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
333-411 |
8.45e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.05 E-value: 8.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488922799 333 KNERMVIQGENGSGKSTLIKAMLGQNELIAKGNLKIRENLRISYLPQDFDQLQGTLEQFAAEKEVEVQDLLAMLRKLGF 411
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKP 79
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
422-486 |
9.51e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 41.76 E-value: 9.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488922799 422 QMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKPTL----LVVEHDREFVQKIA 486
Cdd:PRK10261 463 EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFgiayLFISHDMAVVERIS 531
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
341-469 |
1.18e-03 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 40.40 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 341 GENGSGKST-------LIKAMLGQnelIAKGNLKI-------RENLRISYLPQD---F------DQLQGTLEQF---AAE 394
Cdd:COG1137 36 GPNGAGKTTtfymivgLVKPDSGR---IFLDGEDIthlpmhkRARLGIGYLPQEasiFrkltveDNILAVLELRklsKKE 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488922799 395 KEVEVQDLLAMLRKLGFERTMFDyrieQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFK 469
Cdd:COG1137 113 REERLEELLEEFGITHLRKSKAY----SLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLK 183
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
186-247 |
1.20e-03 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 37.94 E-value: 1.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 186 ISIDRAQISSFKGNYETWAAERANADEREISLNATMKKDIKKLEQ--------ATRQKQewsrATERKKA 247
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEfidrfrakASKAKQ----AQSRIKA 66
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-196 |
1.21e-03 |
|
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: 41.85 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 2 GIIQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTT----LMKILQN---QVEYEGKVETNLKFNYFPAKI 74
Cdd:TIGR00957 1283 GRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINESaegEIIIDGLNIAKIGLHDLRFKI 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 75 T-EPQD------SVRMVLMKITGRDYSDFWeVERELDQI---------GLAEEILEQTyASLSPGQQTKALLAAMFADQN 138
Cdd:TIGR00957 1363 TiIPQDpvlfsgSLRMNLDPFSQYSDEEVW-WALELAHLktfvsalpdKLDHECAEGG-ENLSVGQRQLVCLARALLRKT 1440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 139 SFQLIDEPTNHLDAAGRDLLAKYLKQKQGYIVVSHDRYFLNQVIDH--VISIDRAQISSF 196
Cdd:TIGR00957 1441 KILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYtrVIVLDKGEVAEF 1500
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-173 |
1.23e-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: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNqiKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKI------LQNQVEYEGKVE---TNL-------- 65
Cdd:COG1117 11 KIEVRNLNVYYGD--KQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndLIPGARVEGEILldgEDIydpdvdvv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 66 -----------KFNYFPAKItepQDSVRMVLmKITG-RDYSDFWE-VERELDQIGLAEEI---LEQTYASLSPGQQTKAL 129
Cdd:COG1117 89 elrrrvgmvfqKPNPFPKSI---YDNVAYGL-RLHGiKSKSELDEiVEESLRKAALWDEVkdrLKKSALGLSGGQQQRLC 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488922799 130 LAAMFADQNSFQLIDEPTNHLD--AAGR--DLLAKyLKQKQGYIVVSH 173
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDpiSTAKieELILE-LKKDYTIVIVTH 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
423-489 |
1.51e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 40.14 E-value: 1.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488922799 423 MSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQN--LVLKFKPTLLVVEHDREFVQKIATQT 489
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEEtlLGLKDDYTMLLVTRSMQQASRISDRT 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-147 |
2.20e-03 |
|
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: 39.72 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSY-DNQIkpVFDqVALEIDASWKLGLIGRNGRGKTTLMKIL-------QNQVEYEGKVETNLKfnyfPAKIT 75
Cdd:cd03224 1 LEVENLNAGYgKSQI--LFG-VSLTVPEGEIVALLGRNGAGKTTLLKTImgllpprSGSIRFDGRDITGLP----PHERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 76 E------PQD-------SVR-MVLMKITGRDYSDF-WEVERELDQIGLAEEILEQTYASLSPGQQ-----TKALLAamfa 135
Cdd:cd03224 74 RagigyvPEGrrifpelTVEeNLLLGAYARRRAKRkARLERVYELFPRLKERRKQLAGTLSGGEQqmlaiARALMS---- 149
|
170
....*....|..
gi 488922799 136 dQNSFQLIDEPT 147
Cdd:cd03224 150 -RPKLLLLDEPS 160
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
327-356 |
2.76e-03 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 39.28 E-value: 2.76e-03
10 20 30
....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLG 356
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMG 48
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
330-454 |
3.13e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 40.03 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 330 ELKKNERMVIQGENGSGKSTLIKAMLGQNELIAKGNLKIREN----------LRISYLPQDfDQLQGTLE-----QFAA- 393
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNgmpidakemrAISAYVQQD-DLFIPTLTvrehlMFQAh 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488922799 394 ----------EKEVEVQDLLAM--LRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLD 454
Cdd:TIGR00955 126 lrmprrvtkkEKRERVDEVLQAlgLRKCANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
99-174 |
3.18e-03 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 39.63 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 99 VERELDQIGLAEEilEQTY-ASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYLKQKQ-----GYIVVS 172
Cdd:TIGR03265 115 VAELLDLVGLPGS--ERKYpGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQrrlgvTTIMVT 192
|
..
gi 488922799 173 HD 174
Cdd:TIGR03265 193 HD 194
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
374-494 |
3.31e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 39.34 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 374 ISYLPQDFDQLQGTLEQFAAEKevevqdllamLRKLGFERTMFDYRIEQMSMGQKRKVALARSLCEEANLYIWDEPLNYL 453
Cdd:PRK13649 107 VAFGPQNFGVSQEEAEALAREK----------LALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 488922799 454 DVITREQIQNLVLKFKP---TLLVVEHDREFVQKIATQTVNLKK 494
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQsgmTIVLVTHLMDDVANYADFVYVLEK 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-52 |
3.52e-03 |
|
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: 39.06 E-value: 3.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQIK-PVFDQVALEIDASWKLGLIGRNGRGKTTLMKILQ 52
Cdd:cd03249 1 IEFKNVSFRYPSRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLE 50
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-193 |
5.11e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 38.96 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 3 IIQLKNVSFSYDNQIKPVFDQVALEIDASWKLGLIGRNGRGKTTLMKILqnqVEYEGKVETNLKFNYFPA---KITEPQD 79
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLM---IGIEKVKSGEIFYNNQAItddNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 80 SVRMVLMK--------ITGRD-----------YSDFWE-VERELDQIGLAEEILEQTYaSLSPGQQTKALLAAMFADQNS 139
Cdd:PRK13648 84 HIGIVFQNpdnqfvgsIVKYDvafglenhavpYDEMHRrVSEALKQVDMLERADYEPN-ALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488922799 140 FQLIDEPTNHLDAAGR-DL--LAKYLKQKQGYIVVS--HDryfLNQVI--DHVISIDRAQI 193
Cdd:PRK13648 163 VIILDEATSMLDPDARqNLldLVRKVKSEHNITIISitHD---LSEAMeaDHVIVMNKGTV 220
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
36-152 |
5.80e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.44 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 36 LIGRNGRGKTTLMKILQNQvEYEGKVETNLKFNYFPAK---------------ITEPQDSVRMVLMkitgrdYSDFWEVE 100
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAGR-KTGGYIEGDIRISGFPKKqetfarisgyceqndIHSPQVTVRESLI------YSAFLRLP 983
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488922799 101 REL---DQIGLAEEILEQT--------------YASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDA 152
Cdd:PLN03140 984 KEVskeEKMMFVDEVMELVeldnlkdaivglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
327-356 |
5.99e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.47 E-value: 5.99e-03
10 20 30
....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLG 356
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
422-486 |
6.03e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 39.30 E-value: 6.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488922799 422 QMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQNLVLKFKP----TLLVVEHDREFVQKIA 486
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNLSIVRKLA 224
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
100-193 |
6.78e-03 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 38.24 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 100 ERELDQIGLAEEilEQTY-ASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAagrDLLAKYLKQKQG-------YIVV 171
Cdd:COG4598 136 EALLAKVGLADK--RDAYpAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP---ELVGEVLKVMRDlaeegrtMLVV 210
|
90 100
....*....|....*....|..
gi 488922799 172 SHDRYFLNQVIDHVISIDRAQI 193
Cdd:COG4598 211 THEMGFARDVSSHVVFLHQGRI 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
103-174 |
8.51e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 37.84 E-value: 8.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488922799 103 LDQIGLAEEiLEQTYASLSPGQQTKALLAAMFADQNSFQLIDEPTNHLDAAGRDLLAKYL-----KQKQGYIVVSHD 174
Cdd:PRK10584 131 LEQLGLGKR-LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnrEHGTTLILVTHD 206
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-198 |
8.81e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 38.80 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 4 IQLKNVSFSYDNQ---IKPVfdqvALEIDASWKLGLIGRNGRGKTTLMKILqnqveyegkveTNLkfnYFPAKIT----- 75
Cdd:PRK10522 323 LELRNVTFAYQDNgfsVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLL-----------TGL---YQPQSGEilldg 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 76 EPQDSVRMV-LMKITGRDYSDFWEVERELDQIG------LAEEILEQ--------------TYASLSPGQQTK-ALLAAM 133
Cdd:PRK10522 385 KPVTAEQPEdYRKLFSAVFTDFHLFDQLLGPEGkpanpaLVEKWLERlkmahkleledgriSNLKLSKGQKKRlALLLAL 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488922799 134 fADQNSFQLIDEPtnhldAAGRD---------LLAKYLKQKQGYIV-VSH-DRYFLNQviDHVISIDRAQISSFKG 198
Cdd:PRK10522 465 -AEERDILLLDEW-----AADQDphfrrefyqVLLPLLQEMGKTIFaISHdDHYFIHA--DRLLEMRNGQLSELTG 532
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
366-469 |
8.88e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 38.45 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 366 LKIRENLRISYLPQdFDQLQGTLEQfAAEKEvEVQDLLamlrklgferTMF-------DYRIEQMSMGQKRKVALARSLC 438
Cdd:PRK10762 345 MSVKENMSLTALRY-FSRAGGSLKH-ADEQQ-AVSDFI----------RLFniktpsmEQAIGLLSGGNQQKVAIARGLM 411
|
90 100 110
....*....|....*....|....*....|.
gi 488922799 439 EEANLYIWDEPLNYLDVITREQIQNLVLKFK 469
Cdd:PRK10762 412 TRPKVLILDEPTRGVDVGAKKEIYQLINQFK 442
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
327-477 |
9.60e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 38.95 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 327 LNLELKKNERMVIQGENGSGKSTLIKAMLGQNEL-----------IAK-GNLKIRENLRIsyLPQDFDQLQGT----LEQ 390
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELergrilidgcdISKfGLMDLRKVLGI--IPQAPVLFSGTvrfnLDP 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488922799 391 FAAEKEVEVQDLL--AMLR------KLGFERTMFDYRiEQMSMGQKRKVALARSLCEEANLYIWDEPLNYLDVITREQIQ 462
Cdd:PLN03130 1336 FNEHNDADLWESLerAHLKdvirrnSLGLDAEVSEAG-ENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQ 1414
|
170
....*....|....*..
gi 488922799 463 NLVL-KFKP-TLLVVEH 477
Cdd:PLN03130 1415 KTIReEFKScTMLIIAH 1431
|
|
| |
