|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
82-606 |
4.47e-171 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 496.89 E-value: 4.47e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 82 IENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKhIGARKLA-------IPSHIDLLYCEQEIQVDST-SAI 153
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLK-ILAGELEpdsgevsIPKGLRIGYLPQEPPLDDDlTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 154 DTVVKSDKKRLALLEEEAKLMSEIEEGkTEAAERMKEVADELRDIGADSAEPRARRILAGLGFSKEMQEKPCTDFSGGWR 233
Cdd:COG0488 80 DTVLDGDAELRALEAELEELEAKLAEP-DEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 234 MRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKLHTYRGNYTLFK 313
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 314 KQYAQDMQVHEKNFDQQQKQLKAMKK-------EGKSAKQAEEQVKQ--QMANkakkggkknagkvnddddagapELLQR 384
Cdd:COG0488 239 EQRAERLEQEAAAYAKQQKKIAKEEEfirrfraKARKAKQAQSRIKAleKLER----------------------EEPPR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 385 RKEYsVKFQFPETTKLNPPVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKH 464
Cdd:COG0488 297 RDKT-VEIRFPPPERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 465 RTLRIGWFDQHaNEALNGEQTPVEFLC-TKFNIDYQEARKQLGTTGLAAHAHTVKIKDLSGGQKSRVALCNLALGGPDII 543
Cdd:COG0488 376 ETVKIGYFDQH-QEELDPDKTVLDELRdGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 544 ILDEPTNNLDIESIDALAEAIRDFNGGVVMVTHDERLVVRTDCNLWVVENQGIDEIDGDFEDY 606
Cdd:COG0488 455 LLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDY 517
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
79-608 |
3.82e-149 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 447.77 E-value: 3.82e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 79 DIKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARKL-AIPSHIDLLYCEQEIQVDSTSAIDTVV 157
Cdd:PLN03073 177 DIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIdGIPKNCQILHVEQEVVGDDTTALQCVL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 158 KSDKKRLALLEEEAKLMSEIEEGKTEAA------------------ERMKEVADELRDIGADSAEPRARRILAGLGFSKE 219
Cdd:PLN03073 257 NTDIERTQLLEEEAQLVAQQRELEFETEtgkgkgankdgvdkdavsQRLEEIYKRLELIDAYTAEARAASILAGLSFTPE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 220 MQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDN 299
Cdd:PLN03073 337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHG 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 300 QKLHTYRGNYTLFKKQYAQDMQVHEKNFDQQQKQLKAMK----KEGKSAKQAEeqvKQQMANKAKKGGKKNAGKVNDDDd 375
Cdd:PLN03073 417 QKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQafidKFRYNAKRAS---LVQSRIKALDRLGHVDAVVNDPD- 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 376 agapellqrrkeysVKFQFPE-TTKLNPPVLGLHDVNFGY-GKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGK 453
Cdd:PLN03073 493 --------------YKFEFPTpDDRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 454 IDPNDGELRKHRTLRIGWFDQHANEALNGEQTPVEFLCTKF-NIDYQEARKQLGTTGLAAHAHTVKIKDLSGGQKSRVAL 532
Cdd:PLN03073 559 LQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFpGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAF 638
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 533 CNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGGVVMVTHDERLVVRTDCNLWVVENQGIDEIDGDFEDYKK 608
Cdd:PLN03073 639 AKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKK 714
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
92-613 |
1.86e-96 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 308.64 E-value: 1.86e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 92 KLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHI------GARKLAIPSHIDLLYCEQEIQVDSTSAIDTVVKSDKKrLA 165
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLkneisaDGGSYTFPGNWQLAWVNQETPALPQPALEYVIDGDRE-YR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 166 LLEEEAKLMSEIEEGKTEAAermkeVADELRDIGADSAEPRARRILAGLGFSKEMQEKPCTDFSGGWRMRISLARALFLE 245
Cdd:PRK10636 93 QLEAQLHDANERNDGHAIAT-----IHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 246 PTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKLHTYRGNYTLFKKQYAQDMQVHEK 325
Cdd:PRK10636 168 SDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQQQA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 326 NFDQQQKQLKAM-------KKEGKSAKQAEEQVK--QQMANKakkggkknagkvnddddagAPELLQRRKEYSvkFQFPE 396
Cdd:PRK10636 248 MYESQQERVAHLqsyidrfRAKATKAKQAQSRIKmlERMELI-------------------APAHVDNPFHFS--FRAPE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 397 TtkLNPPVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKHRTLRIGWFDQHA 476
Cdd:PRK10636 307 S--LPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 477 NEALNGEQTPVEFLCTKFNIDY-QEARKQLGTTGLAAHAHTVKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIE 555
Cdd:PRK10636 385 LEFLRADESPLQHLARLAPQELeQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 17559834 556 SIDALAEAIRDFNGGVVMVTHDERLVVRTDCNLWVVENQGIDEIDGDFEDYKKEVLDA 613
Cdd:PRK10636 465 MRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDV 522
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
92-606 |
4.93e-72 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 241.33 E-value: 4.93e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 92 KLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIG------ARKLAIPSHIDLLYCEQ-EIQVDSTSAIDTV-------- 156
Cdd:PRK15064 14 KPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGgdlepsAGNVSLDPNERLGKLRQdQFAFEEFTVLDTVimghtelw 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 157 -VKSDKKRLALLEEeaklMSEiEEGkteaaerMKeVAD---ELRDIGADSAEPRARRILAGLGFSKEMQEKPCTDFSGGW 232
Cdd:PRK15064 94 eVKQERDRIYALPE----MSE-EDG-------MK-VADlevKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 233 RMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKLHTYRGNYTLF 312
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 313 KKQYAQdmqvheknfdQQQKQLK--AMKKE--------------GKS-AKQAEEQVKQqmankakkggkknagkvndddd 375
Cdd:PRK15064 241 MTAATQ----------ARERLLAdnAKKKAqiaelqsfvsrfsaNASkAKQATSRAKQ---------------------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 376 agapelLQRRKEYSVK--------FQFPETTKLNPPVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLL 447
Cdd:PRK15064 289 ------IDKIKLEEVKpssrqnpfIRFEQDKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 448 KLLIGKIDPNDGELRKHRTLRIGWFDQHANEALNGEQTPVEFLC--TKFNIDYQEARKQLGTTGLAAHAHTVKIKDLSGG 525
Cdd:PRK15064 363 RTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDLTLFDWMSqwRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 526 QKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGGVVMVTHDERLVVRTDCNLWVVENQGIDEIDGDFED 605
Cdd:PRK15064 443 EKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEE 522
|
.
gi 17559834 606 Y 606
Cdd:PRK15064 523 Y 523
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
94-605 |
2.27e-70 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 239.47 E-value: 2.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 94 LFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArklaipshiDLLYCEQEIQVDStsaiDTVV---KSDKKRlallEEE 170
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG---------EVLLDDGRIIYEQ----DLIVarlQQDPPR----NVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 171 AKLMSEIEEGKTEAAERMKEVADELRDIGADSAE----------------------PRARRILAGLGFSKemqEKPCTDF 228
Cdd:PRK11147 81 GTVYDFVAEGIEEQAEYLKRYHDISHLVETDPSEknlnelaklqeqldhhnlwqleNRINEVLAQLGLDP---DAALSSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKLHTYRGN 308
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 309 YTLFKKQYAQDMQVHE-KN--FDQQQKQLKAMKKEGKSAKQA--EEQVK--QQMANkakkggkknagkvnddddagapEL 381
Cdd:PRK11147 238 YDQYLLEKEEALRVEElQNaeFDRKLAQEEVWIRQGIKARRTrnEGRVRalKALRR----------------------ER 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 382 LQRRKEY-SVKFQFPETTKLNPPVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGE 460
Cdd:PRK11147 296 SERREVMgTAKMQVEEASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 461 LRKHRTLRIGWFDQHaNEALNGEQTPVEFLCtkfnidyqEARKQLGTTGLAAH--------------AHTvKIKDLSGGQ 526
Cdd:PRK11147 376 IHCGTKLEVAYFDQH-RAELDPEKTVMDNLA--------EGKQEVMVNGRPRHvlgylqdflfhpkrAMT-PVKALSGGE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 527 KSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGGVVMVTHDERLVVRTDCNLWVVENQG-IDEIDGDFED 605
Cdd:PRK11147 446 RNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGkIGRYVGGYHD 525
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
91-617 |
3.84e-68 |
|
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: 231.36 E-value: 3.84e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 91 GKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHI-GARK----LAIPS-HIDLLYCEQEIQVDSTSAIDTVVK---SDK 161
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMaGVDKdfngEARPQpGIKVGYLPQEPQLDPTKTVRENVEegvAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 162 KR-LALLEEEAKLMSEIEEGKTEAAERMKEVADELRDIGADSAEPR------ARRILAGlgfskemqEKPCTDFSGGWRM 234
Cdd:TIGR03719 97 KDaLDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQleiamdALRCPPW--------DADVTKLSGGERR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 235 RISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKLHTYRGNYTLFKK 314
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 315 QYAQDMQVHEKnfdQQQKQLKAMKKE------GKSAKQA---------EEQVKQQmankakkggkknagkvnddddagap 379
Cdd:TIGR03719 249 QKQKRLEQEEK---EESARQKTLKRElewvrqSPKGRQAkskarlaryEELLSQE------------------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 380 ellQRRKEYSVKFQFPETTKLNPPVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDG 459
Cdd:TIGR03719 301 ---FQKRNETAEIYIPPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 460 ELRKHRTLRIGWFDQhANEALNGEQTPVEFL-------------------CTKFNIDYQEARKqlgttglaahahtvKIK 520
Cdd:TIGR03719 378 TIEIGETVKLAYVDQ-SRDALDPNKTVWEEIsggldiiklgkreipsrayVGRFNFKGSDQQK--------------KVG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 521 DLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGGVVMVTHDERLVVRTDCNLWVVENQG-IDEI 599
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDShVEWF 522
|
570
....*....|....*...
gi 17559834 600 DGDFEDYKKEVLDALGEA 617
Cdd:TIGR03719 523 EGNFSEYEEDKKRRLGED 540
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
91-577 |
3.96e-61 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 212.67 E-value: 3.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 91 GKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHI-GARKL----AIPSH-IDLLYCEQEIQVDSTsaiDTV-------V 157
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMaGVDKEfegeARPAPgIKVGYLPQEPQLDPE---KTVrenveegV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 158 KSDKKRLALLEEEAKLMSEIEEGKTEAAERMKEVADELRDIGADSAEPR------ARRILAGlgfskemqEKPCTDFSGG 231
Cdd:PRK11819 96 AEVKAALDRFNEIYAAYAEPDADFDALAAEQGELQEIIDAADAWDLDSQleiamdALRCPPW--------DAKVTKLSGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 232 WRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKLHTYRGNYTL 311
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 312 FKKQYAQDMQVHEKnfdQQQKQLKAMKKE------GKSAKQA---------EEQVKQQmankakkggkknagkvndddda 376
Cdd:PRK11819 248 WLEQKAKRLAQEEK---QEAARQKALKRElewvrqSPKARQAkskarlaryEELLSEE---------------------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 377 gapellQRRKEYSVKFQFPETTKLNPPVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDP 456
Cdd:PRK11819 303 ------YQKRNETNEIFIPPGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 457 NDGELRKHRTLRIGWFDQHaNEALNGEQT-------------------PVEFLCTKFNIDYQEARKqlgttglaahahtv 517
Cdd:PRK11819 377 DSGTIKIGETVKLAYVDQS-RDALDPNKTvweeisggldiikvgnreiPSRAYVGRFNFKGGDQQK-------------- 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 518 KIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGGVVMVTHD 577
Cdd:PRK11819 442 KVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHD 501
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
407-595 |
3.25e-48 |
|
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: 165.31 E-value: 3.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKHRTLRIGWFDQhanealngeqtp 486
Cdd:cd03221 3 LENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 487 veflctkfnidyqearkqlgttglaahahtvkikdLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRD 566
Cdd:cd03221 71 -----------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKE 115
|
170 180
....*....|....*....|....*....
gi 17559834 567 FNGGVVMVTHDERLVVRTDCNLWVVENQG 595
Cdd:cd03221 116 YPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
80-310 |
2.55e-45 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 168.32 E-value: 2.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGarklaipshidllyceQEIQVDStsaiDTVVKS 159
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA----------------GELEPDS----GTVKLG 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 DKKRLALLeeeAKLMSEIEEGKTeaaermkeVADELRDIGADSAEPRARRILAGLGFSKEMQEKPCTDFSGGWRMRISLA 239
Cdd:COG0488 376 ETVKIGYF---DQHQEELDPDKT--------VLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALA 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559834 240 RALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKLHTYRGNYT 310
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYD 515
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
80-301 |
3.59e-45 |
|
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: 156.84 E-value: 3.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARKLAIpshidllycEQEIQVDSTSaidtvvks 159
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPD---------EGIVTWGSTV-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 dkkRLALLEEeaklmseieegkteaaermkevadelrdigadsaeprarrilaglgfskemqekpctdFSGGWRMRISLA 239
Cdd:cd03221 64 ---KIGYFEQ----------------------------------------------------------LSGGEKMRLALA 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559834 240 RALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQK 301
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
403-581 |
1.34e-34 |
|
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: 130.29 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 403 PVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKH----RTLRIGWFDQ---- 474
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgepiRDAREDYRRRlayl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 475 -HANeALNGEQTPVE---FLC--TKFNIDYQEARKQLGTTGLAAHAHtVKIKDLSGGQKSRVALCNLALGGPDIIILDEP 548
Cdd:COG4133 81 gHAD-GLKPELTVREnlrFWAalYGLRADREAIDEALEAVGLAGLAD-LPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 17559834 549 TNNLDIESIDALAEAIRDF--NGG-VVMVTHDERLV 581
Cdd:COG4133 159 FTALDAAGVALLAELIAAHlaRGGaVLLTTHQPLEL 194
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
401-577 |
1.12e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 128.67 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 401 NPPVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR------KHRTLRIGWFDQ 474
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 475 HANEALNgeqTPV---EFLCT----KFNI-------DYQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRV----ALCNla 536
Cdd:COG1121 83 RAEVDWD---FPItvrDVVLMgrygRRGLfrrpsraDREAVDEALERVGLEDLADR-PIGELSGGQQQRVllarALAQ-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17559834 537 lgGPDIIILDEPTNNLDIESIDALAEAIRDFNG---GVVMVTHD 577
Cdd:COG1121 157 --DPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHD 198
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
74-581 |
3.35e-33 |
|
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: 133.49 E-value: 3.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 74 MENSMDIKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIgARKLAIPSHIdllycEQEIQVDSTSAI 153
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAL-MGLLPHGGRI-----SGEVLLDGRDLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 154 DTVVKSDKKRLALLEEEAKL---MSEIEEGKTEAAErmkevadeLRDIGADSAEPRARRILAGLGFSKEMQEKPcTDFSG 230
Cdd:COG1123 75 ELSEALRGRRIGMVFQDPMTqlnPVTVGDQIAEALE--------NLGLSRAEARARVLELLEAVGLERRLDRYP-HQLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 231 GWRMRISLARALFLEPTLLMLDEPTNHLDLNAVI----WLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKLHTYR 306
Cdd:COG1123 146 GQRQRVAIAMALALDPDLLIADEPTTALDVTTQAeildLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 307 GNYTLFkkqyaqdmqvheknfdQQQKQLKAMKKEGKSAKQAEEqvkqqmankakkggkknagkvnddDDAGAPELLQRRk 386
Cdd:COG1123 226 PPEEIL----------------AAPQALAAVPRLGAARGRAAP------------------------AAAAAEPLLEVR- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 387 eySVKFQFPETTKlnPPVLGLHDVNFgygkdvlfkKLNFGvdmdSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR---- 462
Cdd:COG1123 265 --NLSKRYPVRGK--GGVRAVDDVSL---------TLRRG----ETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgk 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 463 -----KHRTLR-----IGWFDQHANEALNGEQTpV-----EFLCTKFNIDYQEARKQ----LGTTGLAAHAHTVKIKDLS 523
Cdd:COG1123 328 dltklSRRSLRelrrrVQMVFQDPYSSLNPRMT-VgdiiaEPLRLHGLLSRAERRERvaelLERVGLPPDLADRYPHELS 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559834 524 GGQKSRVALCN-LALGgPDIIILDEPTNNLDIeSI-----DALAEAIRDFNGGVVMVTHDERLV 581
Cdd:COG1123 407 GGQRQRVAIARaLALE-PKLLILDEPTSALDV-SVqaqilNLLRDLQRELGLTYLFISHDLAVV 468
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
407-577 |
4.45e-32 |
|
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: 123.41 E-value: 4.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR---KHRTL---RIGWFDQHANE-- 478
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgKPLEKerkRIGYVPQRRSIdr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 479 ---------ALNGEQTPVEFLCTKFNIDYQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILDEPT 549
Cdd:cd03235 82 dfpisvrdvVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADR-QIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190
....*....|....*....|....*....|.
gi 17559834 550 NNLDIESIDALAEAIRDFNG---GVVMVTHD 577
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRRegmTILVVTHD 191
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
407-581 |
2.05e-30 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 116.58 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrigwfdqhaneaLNGEQTp 486
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL-----------------IDGKDI- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 487 veflctkFNIDYQEARKQLGTtglaahahtvkIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRD 566
Cdd:cd00267 64 -------AKLPLEELRRRIGY-----------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRE 125
|
170
....*....|....*...
gi 17559834 567 FNGG---VVMVTHDERLV 581
Cdd:cd00267 126 LAEEgrtVIIVTHDPELA 143
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
407-593 |
7.03e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 116.84 E-value: 7.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR------------KHRTlRI----- 469
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkplsampppEWRR-QVayvpq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 470 --GWFDQHANEALngeqtPVEFLCTKFNIDYQEARKQLGTTGLAAHAHTVKIKDLSGGQKSRVALC-NLALGgPDIIILD 546
Cdd:COG4619 82 epALWGGTVRDNL-----PFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIrALLLQ-PDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17559834 547 EPTNNLDIESIDALAEAIRDF----NGGVVMVTHDERLVVRTDCNLWVVEN 593
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
404-577 |
2.12e-28 |
|
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: 113.99 E-value: 2.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 404 VLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR---------KHRTL--RIGWF 472
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgrdlaslSRRELarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 473 DQHanealngeqTPVEFLCTKFNI------------------DYQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCn 534
Cdd:COG1120 81 PQE---------PPAPFGLTVRELvalgryphlglfgrpsaeDREAVEEALERTGLEHLADR-PVDELSGGERQRVLIA- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17559834 535 LAL-GGPDIIILDEPTNNLDI----ESIDALAEAIRDFNGGVVMVTHD 577
Cdd:COG1120 150 RALaQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHD 197
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
407-577 |
2.29e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.54 E-value: 2.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGE-------LRKHRTL---RIGWFDQHA 476
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEvrvlgedVARDPAEvrrRIGYVPQEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 477 N--EALNGEQTpVEFLCTKFNIDYQEARKQ----LGTTGLAAHAHTvKIKDLSGGQKSRVALCnLAL-GGPDIIILDEPT 549
Cdd:COG1131 83 AlyPDLTVREN-LRFFARLYGLPRKEARERidelLELFGLTDAADR-KVGTLSGGMKQRLGLA-LALlHDPELLILDEPT 159
|
170 180 190
....*....|....*....|....*....|.
gi 17559834 550 NNLDIESIDALAEAIRDFNGG---VVMVTHD 577
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEgktVLLSTHY 190
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
407-581 |
2.35e-27 |
|
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: 109.86 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKD--VLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR-----------KHRTLRIGW-F 472
Cdd:cd03225 2 LKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvdgkdltklslKELRRKVGLvF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 473 ----DQHANEALNGEqtpVEFLCTKFNIDYQEARKQ----LGTTGLAAHAHTVkIKDLSGGQKSRVAL-CNLALGgPDII 543
Cdd:cd03225 82 qnpdDQFFGPTVEEE---VAFGLENLGLPEEEIEERveeaLELVGLEGLRDRS-PFTLSGGQKQRVAIaGVLAMD-PDIL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17559834 544 ILDEPTNNLDIESIDALAEAIRDFNG---GVVMVTHDERLV 581
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLL 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
407-583 |
3.64e-27 |
|
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: 108.29 E-value: 3.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrigwfdqhaneaLNGeqTP 486
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL-----------------LDG--KD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 487 VEflctkfNIDYQEARKQLG-------TTGLAAHAHTVkIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDI----E 555
Cdd:cd03214 63 LA------SLSPKELARKIAyvpqaleLLGLAHLADRP-FNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIahqiE 135
|
170 180
....*....|....*....|....*...
gi 17559834 556 SIDALAEAIRDFNGGVVMVTHDERLVVR 583
Cdd:cd03214 136 LLELLRRLARERGKTVVMVLHDLNLAAR 163
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
80-302 |
4.58e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.14 E-value: 4.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIgARkLAIPSHIDLLYceQEIQVDSTSAIDTvvks 159
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRAL-AD-LDPPTSGEIYL--DGKPLSAMPPPEW---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 dKKRLALLEEEAKLMSEIeegkteaaermkeVAD------ELRDIGADsaEPRARRILAGLGFSKEMQEKPCTDFSGGWR 233
Cdd:COG4619 73 -RRQVAYVPQEPALWGGT-------------VRDnlpfpfQLRERKFD--RERALELLERLGLPPDILDKPVERLSGGER 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 234 MRISLARALFLEPTLLMLDEPTNHLDLN---AVI-WLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKL 302
Cdd:COG4619 137 QRLALIRALLLQPDVLLLDEPTSALDPEntrRVEeLLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
401-605 |
2.86e-26 |
|
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: 113.31 E-value: 2.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 401 NPPVLGLHDVNFGYGKD-VLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR---------KHRTLR-- 468
Cdd:COG4988 333 GPPSIELEDVSFSYPGGrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvdlsdlDPASWRrq 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 469 IGWFDQHA---------NEALNGEQTPVEFLctkfnidyQEARKQLGTTGLAAHA----HTVkIKD----LSGGQKSRVA 531
Cdd:COG4988 413 IAWVPQNPylfagtireNLRLGRPDASDEEL--------EAALEAAGLDEFVAALpdglDTP-LGEggrgLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 532 LCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGG--VVMVTHDERLVVRTDCnLWVVENQGIDEIdGDFED 605
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALLAQADR-ILVLDDGRIVEQ-GTHEE 557
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
407-583 |
3.81e-26 |
|
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: 107.03 E-value: 3.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGY-GKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrigWFDQHANEALNGE-- 483
Cdd:COG1122 3 LENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVL--------VDGKDITKKNLRElr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 484 -------QTP------------VEFLCTKFNIDYQEARKQ----LGTTGLAAHAHTVkIKDLSGGQKSRVALCN-LALGg 539
Cdd:COG1122 75 rkvglvfQNPddqlfaptveedVAFGPENLGLPREEIRERveeaLELVGLEHLADRP-PHELSGGQKQRVAIAGvLAME- 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17559834 540 PDIIILDEPTNNLDIESIDALAEAIRDFNG---GVVMVTHDERLVVR 583
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAE 199
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
407-593 |
4.30e-26 |
|
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: 104.77 E-value: 4.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYG---KDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR---------KHRTLR--IGWF 472
Cdd:cd03228 3 FKNVSFSYPgrpKPVL-KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdlrdlDLESLRknIAYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 473 DQHAnealngeqtpveFLctkFNidyqearkqlGTtglaahahtvkIKD--LSGGQKSRVALCNLALGGPDIIILDEPTN 550
Cdd:cd03228 82 PQDP------------FL---FS----------GT-----------IREniLSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17559834 551 NLDIESIDALAEAIRDFNGG--VVMVTHDERLVVRTDCnLWVVEN 593
Cdd:cd03228 126 ALDPETEALILEALRALAKGktVIVIAHRLSTIRDADR-IIVLDD 169
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
80-319 |
8.98e-26 |
|
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: 106.48 E-value: 8.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGarKLAIPSHidllyceQEIQVDSTSAIDTVVKs 159
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLA--GLLKPDS-------GSILIDGEDVRKEPRE- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 DKKRLALLEEEaklmSEIEEGKTeaAERMKEVADELRDIGADSAEPRARRILAGLGFSKEMqEKPCTDFSGGWRMRISLA 239
Cdd:COG4555 72 ARRQIGVLPDE----RGLYDRLT--VRENIRYFAELYGLFDEELKKRIEELIELLGLEEFL-DRRVGELSTGMKKKVALA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 240 RALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWK---KTLLIVSHDQGFLDSVCTDIIHLDNQKLHtYRGNYTLFKKQY 316
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALKkegKTVLFSSHIMQEVEALCDRVVILHKGKVV-AQGSLDELREEI 223
|
...
gi 17559834 317 AQD 319
Cdd:COG4555 224 GEE 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
407-587 |
1.65e-25 |
|
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: 104.26 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDV-LFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGEL--------RKHRTLRIGWFDQHAN 477
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpikAKERRKSIGYVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 478 EALNGEQTPVEFLCTKFNID--YQEARKQLGTTGLAA----HAHtvkikDLSGGQKSRVALCNLALGGPDIIILDEPTNN 551
Cdd:cd03226 82 YQLFTDSVREELLLGLKELDagNEQAETVLKDLDLYAlkerHPL-----SLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 17559834 552 LDIESIDALAEAIRDFNG---GVVMVTHDERLVVRTdCN 587
Cdd:cd03226 157 LDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKV-CD 194
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
402-585 |
2.26e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 104.74 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 402 PPVLGLHDVNFGYGK-DVLFKKLNfGVDMD----SRIAIVGPNGVGKSTLLKLLiGKIDP----------------NDGE 460
Cdd:COG1136 2 SPLLELRNLTKSYGTgEGEVTALR-GVSLSieagEFVAIVGPSGSGKSTLLNIL-GGLDRptsgevlidgqdisslSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 461 LRKHRTLRIGWFDQHAN--EALNGEQ---TPVEFLCTKFNIDYQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCNl 535
Cdd:COG1136 80 LARLRRRHIGFVFQFFNllPELTALEnvaLPLLLAGVSRKERRERARELLERVGLGDRLDH-RPSQLSGGQQQRVAIAR- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 536 AL-GGPDIIILDEPTNNLDIES----IDALAEAIRDFNGGVVMVTHDERLVVRTD 585
Cdd:COG1136 158 ALvNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPELAARAD 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
420-550 |
2.50e-25 |
|
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: 101.96 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 420 FKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGEL-----------RKHRTLRIGWFDQHANeaLNGEQTPVE 488
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltddeRKSLRKEIGYVFQDPQ--LFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559834 489 FLC----------TKFNIDYQEARKQLGTTGLAAHAHTVKIKDLSGGQKSRVALCNLALGGPDIIILDEPTN 550
Cdd:pfam00005 79 NLRlglllkglskREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
99-256 |
9.01e-25 |
|
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: 100.41 E-value: 9.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLKHIgaRKLAIPShidllycEQEIQVDSTSAIDTVVKSDKKRLALLEEEAKLMSEie 178
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLI--AGLLSPT-------EGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 179 egkTEAAERMKEVADeLRDIGADSAEPRARRILAGLG---FSKEMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPT 255
Cdd:pfam00005 74 ---LTVRENLRLGLL-LKGLSKREKDARAEEALEKLGlgdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 17559834 256 N 256
Cdd:pfam00005 150 A 150
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
99-299 |
3.19e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 101.68 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLKHI-GarkLAIPSHIDLLYCEQEIQVDSTSAidtvvksdKKRLALLEEEAKLMSEI 177
Cdd:COG1131 20 SLTVEPGEIFGLLGPNGAGKTTTIRMLlG---LLRPTSGEVRVLGEDVARDPAEV--------RRRIGYVPQEPALYPDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 178 eegkTeaAERMKEVADELRDIGADSAEPRARRILAGLGFSkEMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNH 257
Cdd:COG1131 89 ----T--VRENLRFFARLYGLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17559834 258 LDLNAVIWLDNYLQTWK---KTLLIVSHDQGFLDSVCTDIIHLDN 299
Cdd:COG1131 162 LDPEARRELWELLRELAaegKTVLLSTHYLEEAERLCDRVAIIDK 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
80-302 |
3.75e-24 |
|
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: 99.39 E-value: 3.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHI-GARKlaiPShidllycEQEIQVDSTSAIDTVVK 158
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIlGLLK---PD-------SGEIKVLGKDIKKEPEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 159 SdKKRLALLEEEAKLMSEIeegkteaaermkevadelrdigadsaepRARRILaglgfskemqekpctDFSGGWRMRISL 238
Cdd:cd03230 71 V-KRRIGYLPEEPSLYENL----------------------------TVRENL---------------KLSGGMKQRLAL 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17559834 239 ARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWK---KTLLIVSHDQGFLDSVCTDIIHLDNQKL 302
Cdd:cd03230 107 AQALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
407-581 |
2.32e-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: 97.08 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrigwfdqhaneaLNGEQTP 486
Cdd:cd03230 3 VRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK-----------------VLGKDIK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 487 VEFLCTKFNIDY--QEARKQLGTTGLaahahtvKIKDLSGGQKSRVALCnLAL-GGPDIIILDEPTNNLDIESIDALAEA 563
Cdd:cd03230 66 KEPEEVKRRIGYlpEEPSLYENLTVR-------ENLKLSGGMKQRLALA-QALlHDPELLILDEPTSGLDPESRREFWEL 137
|
170 180
....*....|....*....|.
gi 17559834 564 IRDFN---GGVVMVTHDERLV 581
Cdd:cd03230 138 LRELKkegKTILLSSHILEEA 158
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
402-585 |
3.27e-23 |
|
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: 103.52 E-value: 3.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 402 PPVLGLHDVNFGY-GKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR-----------KHRTLRI 469
Cdd:TIGR02857 319 ASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladadaDSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 470 GWFDQHanealngeqtPVEFLCT-KFNI----------DYQEARKQLG----TTGLAAHAHTVKIKD---LSGGQKSRVA 531
Cdd:TIGR02857 399 AWVPQH----------PFLFAGTiAENIrlarpdasdaEIREALERAGldefVAALPQGLDTPIGEGgagLSGGQAQRLA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 532 LCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGG--VVMVTHDERLVVRTD 585
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHRLALAALAD 524
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
81-301 |
5.01e-23 |
|
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: 95.77 E-value: 5.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 81 KIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPShidllycEQEIQVDstsaidtvvksd 160
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAG--LLKPT-------SGEILID------------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 161 kkrlalleeeaklmseieegkteaaermkevadeLRDIGADSAEPRARRILAglgfskemqekpCTDFSGGWRMRISLAR 240
Cdd:cd00267 60 ----------------------------------GKDIAKLPLEELRRRIGY------------VPQLSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559834 241 ALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKK---TLLIVSHDQGFLDSVCTDIIHLDNQK 301
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
405-579 |
7.08e-23 |
|
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: 96.66 E-value: 7.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 405 LGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR----KHRTLRIGWFDQ-----H 475
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRwngtPLAEQRDEPHENilylgH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 476 ANeALNGEQTPVE---FLCTKFNIDYQEARKQLGTTGLAAHAHTVkIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNL 552
Cdd:TIGR01189 81 LP-GLKPELSALEnlhFWAAIHGGAQRTIEDALAAVGLTGFEDLP-AAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180 190
....*....|....*....|....*....|
gi 17559834 553 DIESIDALAEAIRDF---NGGVVMVTHDER 579
Cdd:TIGR01189 159 DKAGVALLAGLLRAHlarGGIVLLTTHQDL 188
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
421-585 |
9.52e-23 |
|
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: 96.79 E-value: 9.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 421 KKLNFGVDMDSRIAIVGPNGVGKSTLLKLlIGKIDP----------------NDGELRKHRTLRIGW-FDQHAneaLNGE 483
Cdd:cd03255 21 KGVSLSIEKGEFVAIVGPSGSGKSTLLNI-LGGLDRptsgevrvdgtdisklSEKELAAFRRRHIGFvFQSFN---LLPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 484 QTPVE------FLCTKFNIDYQE-ARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIES 556
Cdd:cd03255 97 LTALEnvelplLLAGVPKKERRErAEELLERVGLGDRLNH-YPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSET 175
|
170 180 190
....*....|....*....|....*....|...
gi 17559834 557 ----IDALAEAIRDFNGGVVMVTHDERLVVRTD 585
Cdd:cd03255 176 gkevMELLRELNKEAGTTIVVVTHDPELAEYAD 208
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
413-588 |
3.28e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.61 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 413 GYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKHRTLRIGWFDQH--ANEALN--------- 481
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRseVPDSLPltvrdlvam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 482 ---GEQTPVEFLCTKFNIDYQEARKQLGTTGLAAHAhtvkIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESID 558
Cdd:NF040873 81 grwARRGLWRRLTRDDRAAVDDALERVGLADLAGRQ----LGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180 190
....*....|....*....|....*....|...
gi 17559834 559 ALAEAIRDFNG---GVVMVTHDERLVVRTDCNL 588
Cdd:NF040873 157 RIIALLAEEHArgaTVVVVTHDLELVRRADPCV 189
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
70-354 |
4.35e-22 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 100.80 E-value: 4.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 70 QLAQMENSMDI--KIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKhigarklaipshidLLYceQEIQV 147
Cdd:PRK11147 308 QVEEASRSGKIvfEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLK--------------LML--GQLQA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 148 DSTSA-IDT---VVKSDKKRlALLEEEAKLMSEIEEGKteaaermKEVAdelrdIGAdsaepRARRILAGLG---FSKEM 220
Cdd:PRK11147 372 DSGRIhCGTkleVAYFDQHR-AELDPEKTVMDNLAEGK-------QEVM-----VNG-----RPRHVLGYLQdflFHPKR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 221 QEKPCTDFSGGWRMRISLARaLFLEPT-LLMLDEPTNHLDLNAVIWLDNYLQTWKKTLLIVSHDQGFLD-SVCTDIIHLD 298
Cdd:PRK11147 434 AMTPVKALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDnTVTECWIFEG 512
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 299 NQKLHTYRGNYtlfkkqyaQDMQvheknfdQQQKQLKAMKKEGKSAKQAEEQVKQQ 354
Cdd:PRK11147 513 NGKIGRYVGGY--------HDAR-------QQQAQYLALKQPAVKKKEEAAAPKAE 553
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
403-577 |
1.10e-21 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 94.74 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 403 PVLGLHDVNFGY-GKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGE---------------LRKHRT 466
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEilvdgqdvtalrgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 467 lRIGWFDQHANeaLNGEQTPVE-----------FLCTKFNI----DYQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRVA 531
Cdd:COG3638 81 -RIGMIFQQFN--LVPRLSVLTnvlagrlgrtsTWRSLLGLfppeDRERALEALERVGLADKAYQ-RADQLSGGQQQRVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17559834 532 LCNLALGGPDIIILDEPTNNLDIES----IDALAEAIRDFNGGVVMVTHD 577
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTarqvMDLLRRIAREDGITVVVNLHQ 206
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
393-598 |
1.14e-21 |
|
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: 99.07 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 393 QFPETTKLNP--PVLGLHDVNFGY---GKDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR----- 462
Cdd:COG4987 320 TEPAEPAPAPggPSLELEDVSFRYpgaGRPVL-DGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvd 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 463 ----KHRTLR--IGWFDQHA---------NEAL-NGEQTPveflctkfnidyQEARKQLGTTGLAAHAHTvkIKD----- 521
Cdd:COG4987 399 lrdlDEDDLRrrIAVVPQRPhlfdttlreNLRLaRPDATD------------EELWAALERVGLGDWLAA--LPDgldtw 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 522 -------LSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGG--VVMVTHDERLVVRTDcNLWVVE 592
Cdd:COG4987 465 lgeggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtVLLITHRLAGLERMD-RILVLE 543
|
....*.
gi 17559834 593 NQGIDE 598
Cdd:COG4987 544 DGRIVE 549
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
402-576 |
1.63e-21 |
|
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: 94.00 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 402 PPVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDG----------------ELRKHr 465
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvrlfgerrggedvwELRKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 466 tlrIGWFDQHANEALNGEQTPVEFLCTKFN-----------IDYQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRV---- 530
Cdd:COG1119 80 ---IGLVSPALQLRFPRDETVLDVVLSGFFdsiglyreptdEQRERARELLELLGLAHLADR-PFGTLSQGEQRRVliar 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17559834 531 ALcnlaLGGPDIIILDEPTNNLDIESIDALAEAIRDFNGG----VVMVTH 576
Cdd:COG1119 156 AL----VKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaptLVLVTH 201
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
395-616 |
1.64e-21 |
|
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: 99.14 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 395 PETTKLNPPVLG----LHDVNFGYGKDV--LFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR------ 462
Cdd:COG2274 460 EGRSKLSLPRLKgdieLENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidl 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 463 ---KHRTLR--IGWFDQHA---------NEALNGEQTPVEflctkfniDYQEARKQLGttglaAHA---------HTVkI 519
Cdd:COG2274 540 rqiDPASLRrqIGVVLQDVflfsgtireNITLGDPDATDE--------EIIEAARLAG-----LHDfiealpmgyDTV-V 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 520 KD----LSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGG--VVMVTHDERLVVRTDcNLWVVEN 593
Cdd:COG2274 606 GEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGrtVIIIAHRLSTIRLAD-RIIVLDK 684
|
250 260
....*....|....*....|...
gi 17559834 594 QGIDEiDGDFEdykkEVLDALGE 616
Cdd:COG2274 685 GRIVE-DGTHE----ELLARKGL 702
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
407-617 |
5.60e-21 |
|
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: 92.23 E-value: 5.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDmDSRI-AIVGPNGVGKSTLLKLLIGKIDPNDGEL-----------RKHRTlRIGWFDQ 474
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAK-DGEItGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedvrkepREARR-QIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 475 --HANEALNGEQTpVEFLCTKFNIDYQEARKQ----LGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILDEP 548
Cdd:COG4555 82 erGLYDRLTVREN-IRYFAELYGLFDEELKKRieelIELLGLEEFLDR-RVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 549 TNNLDIESIDALAEAIRDF---NGGVVMVTHDERLVVRTdC-------NLWVVENQGIDEID--GDFEDYKKEVLDALGE 616
Cdd:COG4555 160 TNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEAL-CdrvvilhKGKVVAQGSLDELReeIGEENLEDAFVALIGS 238
|
.
gi 17559834 617 A 617
Cdd:COG4555 239 E 239
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
80-302 |
5.66e-21 |
|
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: 92.01 E-value: 5.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDIS-AQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQVDSTSAIdtvvk 158
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG--LLKPTSGEVLVDGKDITKKNLREL----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 159 sdKKRLALL--EEEAKL-MSEIEEgkteaaermkEVADELRDIGADSAEPRAR--RILAGLGFSkEMQEKPCTDFSGGWR 233
Cdd:COG1122 74 --RRKVGLVfqNPDDQLfAPTVEE----------DVAFGPENLGLPREEIRERveEALELVGLE-HLADRPPHELSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559834 234 MRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWK---KTLLIVSHDQGFLDSVCTDIIHLDNQKL 302
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNkegKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
403-605 |
8.98e-21 |
|
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: 96.13 E-value: 8.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 403 PVLGLHDVNFGYGKDVLF--KKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPN---DGELR-----------KHRT 466
Cdd:COG1123 3 PLLEVRDLSVRYPGGDVPavDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLldgrdllelseALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 467 LRIGWFDQHANEALN----GEQtpVEFLCTKFNIDYQEARKQ----LGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALG 538
Cdd:COG1123 83 RRIGMVFQDPMTQLNpvtvGDQ--IAEALENLGLSRAEARARvlelLEAVGLERRLDR-YPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559834 539 GPDIIILDEPTNNLD----IESIDALAEAIRDFNGGVVMVTHDERLVVRTdCNLWVVENQGIDEIDGDFED 605
Cdd:COG1123 160 DPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEI-ADRVVVMDDGRIVEDGPPEE 229
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
81-305 |
9.49e-21 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 89.80 E-value: 9.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 81 KIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKhigarklaipshidllyceqeiqvdstsAIDTVVKSD 160
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLK----------------------------TLAGLLKPS 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 161 KKRLALLEEEAKLMSEIEegkteaaermkevadelrdigadsaepRARRI------LAGLGFSkEMQEKPCTDFSGGWRM 234
Cdd:cd03214 53 SGEILLDGKDLASLSPKE---------------------------LARKIayvpqaLELLGLA-HLADRPFNELSGGERQ 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 235 RISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWK----KTLLIVSHDQGFLDSVCTDIIHLDNQKLHTY 305
Cdd:cd03214 105 RVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLArergKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
80-283 |
1.58e-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: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIgARKLAiPSHIDLLYCEQEIQvdSTSAIDTVvks 159
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRAL-AGLLK-PSSGEVLLDGRDLA--SLSRRELA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 dkKRLALLEEEaklmseieegkTEAAERMKeVAD--------ELRDIGADSAE--PRARRILAGLGFSkEMQEKPCTDFS 229
Cdd:COG1120 75 --RRIAYVPQE-----------PPAPFGLT-VRElvalgrypHLGLFGRPSAEdrEAVEEALERTGLE-HLADRPVDELS 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17559834 230 GGWRMRISLARALFLEPTLLMLDEPTNHLDL-NAVIWLD---NYLQTWKKTLLIVSHD 283
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTSHLDLaHQLEVLEllrRLARERGRTVVMVLHD 197
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
78-301 |
1.71e-20 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 89.85 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 78 MDIKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGarKLAIPSHIDLLYCEQEIQVDSTSAidtvv 157
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILA--GLLPPSAGEVLWNGEPIRDAREDY----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 158 ksdKKRLALLEEEAKLMSEIeegkTeaaermkeVADELR---DI-GADSAEPRARRILAGLGFSkEMQEKPCTDFSGGWR 233
Cdd:COG4133 74 ---RRRLAYLGHADGLKPEL----T--------VRENLRfwaALyGLRADREAIDEALEAVGLA-GLADLPVRQLSAGQK 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559834 234 MRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKK---TLLIVSHDQgfLDSVCTDIIHLDNQK 301
Cdd:COG4133 138 RRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLArggAVLLTTHQP--LELAAARVLDLGDFK 206
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
418-576 |
2.11e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.48 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 418 VLFKKLNFGV---DMdsrIAIVGPNGVGKSTLLKLLIGKIDPNDGE-------LRKHRT------LRIGwfdqHANeALN 481
Cdd:PRK13538 15 ILFSGLSFTLnagEL---VQIEGPNGAGKTSLLRILAGLARPDAGEvlwqgepIRRQRDeyhqdlLYLG----HQP-GIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 482 GEQTPVE---FLCTKFN-IDYQEARKQLGTTGLAAHAHtVKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESI 557
Cdd:PRK13538 87 TELTALEnlrFYQRLHGpGDDEALWEALAQVGLAGFED-VPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV 165
|
170 180
....*....|....*....|..
gi 17559834 558 DALAEAIRDF--NGG-VVMVTH 576
Cdd:PRK13538 166 ARLEALLAQHaeQGGmVILTTH 187
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
409-595 |
3.49e-20 |
|
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: 89.98 E-value: 3.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 409 DVNFGY--GKDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGE---------------LRKHrtlrIGW 471
Cdd:cd03253 5 NVTFAYdpGRPVL-KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSilidgqdirevtldsLRRA----IGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 472 FDQHAnealngeqtpVEFLCT-KFNIDY----------QEARKqlgttglAAHAHTVKIK--------------DLSGGQ 526
Cdd:cd03253 80 VPQDT----------VLFNDTiGYNIRYgrpdatdeevIEAAK-------AAQIHDKIMRfpdgydtivgerglKLSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559834 527 KSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGG--VVMVTHdeRLVVRTDCNLWVVENQG 595
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGrtTIVIAH--RLSTIVNADKIIVLKDG 211
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
415-576 |
3.52e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.16 E-value: 3.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 415 GKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIG---------KIDPNDGELRKHRTL--RIGwfdqHANeALNGE 483
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGllppaagtiKLDGGDIDDPDVAEAchYLG----HRN-AMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 484 QTPVEflctkfNIDYQeaRKQLGTT-----------GLAAHAHtVKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNL 552
Cdd:PRK13539 88 LTVAE------NLEFW--AAFLGGEeldiaaaleavGLAPLAH-LPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*..
gi 17559834 553 DIESIDALAEAIRDF---NGGVVMVTH 576
Cdd:PRK13539 159 DAAAVALFAELIRAHlaqGGIVIAATH 185
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
409-577 |
4.40e-20 |
|
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: 89.93 E-value: 4.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 409 DVNFGYGKDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGE---------------LRKHRTlRIGWFD 473
Cdd:cd03256 7 SKTYPNGKKAL-KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSvlidgtdinklkgkaLRQLRR-QIGMIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 474 QHANeaLNGEQTPVE-FLCTKFN--------------IDYQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALG 538
Cdd:cd03256 85 QQFN--LIERLSVLEnVLSGRLGrrstwrslfglfpkEEKQRALAALERVGLLDKAYQ-RADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17559834 539 GPDIIILDEPTNNLDIES----IDALAEAIRDFNGGVVMVTHD 577
Cdd:cd03256 162 QPKLILADEPVASLDPASsrqvMDLLKRINREEGITVIVSLHQ 204
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
79-298 |
5.70e-20 |
|
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: 89.87 E-value: 5.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 79 DIKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARKLAIPSHIDLlyceqeiqvdstSAIDTVVK 158
Cdd:TIGR03873 1 GLRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDL------------AGVDLHGL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 159 SDKKR---LALLEEEAKlmseieegkTEAAERMKEVADELRD-----IGADSAEPRA--RRILAGLGFSkEMQEKPCTDF 228
Cdd:TIGR03873 69 SRRARarrVALVEQDSD---------TAVPLTVRDVVALGRIphrslWAGDSPHDAAvvDRALARTELS-HLADRDMSTL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEPTNHLDLNA---VIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLD 298
Cdd:TIGR03873 139 SGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAqleTLALVRELAATGVTVVAALHDLNLAASYCDHVVVLD 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
395-578 |
7.88e-20 |
|
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: 93.19 E-value: 7.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 395 PETTKLNPPVLGLHDVNFGY-GKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELrkhrTL------ 467
Cdd:TIGR02868 325 AGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV----TLdgvpvs 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 468 ---------RIGWFDQHA---------NEAL-NGEQTPveflctkfnidyQEARKQLGTTGLAAH-------AHTVKIKD 521
Cdd:TIGR02868 401 sldqdevrrRVSVCAQDAhlfdttvreNLRLaRPDATD------------EELWAALERVGLADWlralpdgLDTVLGEG 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559834 522 ---LSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGG--VVMVTHDE 578
Cdd:TIGR02868 469 garLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGrtVVLITHHL 530
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
90-301 |
1.23e-19 |
|
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: 87.52 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 90 QGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARKLAIpshidllycEQEIQVDSTSAIDTVVKSDKKRLALLEE 169
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPT---------SGEVLVDGKDLTKLSLKELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 170 EAK---LMSEIEEgkteaaermkEVADELRDIGADSAE--PRARRILAGLGFSkEMQEKPCTDFSGGWRMRISLARALFL 244
Cdd:cd03225 83 NPDdqfFGPTVEE----------EVAFGLENLGLPEEEieERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 245 EPTLLMLDEPTNHLDLNAVIWLDNYLQTWK---KTLLIVSHDQGFLDSVCTDIIHLDNQK 301
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKaegKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
74-303 |
1.59e-19 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 88.22 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 74 MENSMDIKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLK-------------HIGARKLAIPSHiDLLY 140
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKailgllpptsgtvRLFGKPPRRARR-RIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 141 CEQEIQVDST---SAIDTVVKSDKKRLALLeeeaKLMSEieEGKTEAAERMKEV-ADELRDigadsaepraRRIlaglgf 216
Cdd:COG1121 80 VPQRAEVDWDfpiTVRDVVLMGRYGRRGLF----RRPSR--ADREAVDEALERVgLEDLAD----------RPI------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 217 skemqekpcTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWK---KTLLIVSHDQGFLDSVCTD 293
Cdd:COG1121 138 ---------GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRregKTILVVTHDLGAVREYFDR 208
|
250
....*....|
gi 17559834 294 IIHLDNQKLH 303
Cdd:COG1121 209 VLLLNRGLVA 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
407-581 |
1.77e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.42 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVL-FKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrigWFDQHANEaLNGEQT 485
Cdd:COG2884 4 FENVSKRYPGGREaLSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVL--------VNGQDLSR-LKRREI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 486 PveFLctKFNI-----DYQ-----------------------EARKQ----LGTTGLAAHAHTvKIKDLSGGQKSRVALc 533
Cdd:COG2884 75 P--YL--RRRIgvvfqDFRllpdrtvyenvalplrvtgksrkEIRRRvrevLDLVGLSDKAKA-LPHELSGGEQQRVAI- 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17559834 534 nlA---LGGPDIIILDEPTNNLDIESIDALAEAIRDFN-GG--VVMVTHDERLV 581
Cdd:COG2884 149 --AralVNRPELLLADEPTGNLDPETSWEIMELLEEINrRGttVLIATHDLELV 200
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
414-574 |
1.88e-19 |
|
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: 86.89 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 414 YGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrTLRIGWFDQHAN----------EALNGE 483
Cdd:cd03268 10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT---FDGKSYQKNIEAlrrigalieaPGFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 484 QTPVEFL---CTKFNIDYQEARKQLGTTGLAAHAHtVKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDAL 560
Cdd:cd03268 87 LTARENLrllARLLGIRKKRIDEVLDVVGLKDSAK-KKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKEL 165
|
170
....*....|....*.
gi 17559834 561 AEAIRDFN--GGVVMV 574
Cdd:cd03268 166 RELILSLRdqGITVLI 181
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
401-577 |
1.99e-19 |
|
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: 87.73 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 401 NPPVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDG---------------ELRKHR 465
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGeilvdgqditglsekELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 466 tLRIGWFDQHAneAL--------NgeqtpVEF-LCTKFNIDYQEARKQ----LGTTGLAAHAHtvkiK---DLSGGQKSR 529
Cdd:COG1127 82 -RRIGMLFQGG--ALfdsltvfeN-----VAFpLREHTDLSEAEIRELvlekLELVGLPGAAD----KmpsELSGGMRKR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17559834 530 VALCN-LALgGPDIIILDEPTNNLDIESIDALAEAIRD----FNGGVVMVTHD 577
Cdd:COG1127 150 VALARaLAL-DPEILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHD 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
415-576 |
2.59e-19 |
|
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: 86.39 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 415 GKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKHRT----LRIGWFDQ-----HANeALNGEQT 485
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfQRDSIARGllylgHAP-GIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 486 PVE---FLCtKFNIDYQ--EArkqLGTTGLAAHAHtVKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDAL 560
Cdd:cd03231 90 VLEnlrFWH-ADHSDEQveEA---LARVGLNGFED-RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170
....*....|....*....
gi 17559834 561 AEAIRDF---NGGVVMVTH 576
Cdd:cd03231 165 AEAMAGHcarGGMVVLTTH 183
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
404-581 |
3.30e-19 |
|
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: 86.79 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 404 VLGLHDVNFGYGKDVLFKKLNFGVDMD----SRIAIVGPNGVGKSTLLKLLIGKIDPNDGE--------------LRKHR 465
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSikkgETLGLVGESGSGKSTLARAILGLLKPTSGSiifdgkdllklsrrLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 466 TLRIGWFDQHANEALN-----GEQTpVEFLCTKFNIDYQEARKqlgttgLAAHAHTVKIKD-----------LSGGQKSR 529
Cdd:cd03257 81 RKEIQMVFQDPMSSLNprmtiGEQI-AEPLRIHGKLSKKEARK------EAVLLLLVGVGLpeevlnrypheLSGGQRQR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17559834 530 VALCN-LALgGPDIIILDEPTNNLDIES----IDALAEAIRDFNGGVVMVTHDERLV 581
Cdd:cd03257 154 VAIARaLAL-NPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHDLGVV 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
80-310 |
4.16e-19 |
|
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: 91.15 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGAR------KLAIPSHIDLLYCEQeiqvdSTSAI 153
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQeqpdsgTIEIGETVKLAYVDQ-----SRDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 154 DtvvksDKKrlalleeeaKLMSEIEEGkteaaermkevADELRdIGadSAEPRARRILAGLGFSKEMQEKPCTDFSGGWR 233
Cdd:TIGR03719 398 D-----PNK---------TVWEEISGG-----------LDIIK-LG--KREIPSRAYVGRFNFKGSDQQKKVGQLSGGER 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17559834 234 MRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLD-NQKLHTYRGNYT 310
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFS 527
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
80-302 |
5.87e-19 |
|
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: 85.73 E-value: 5.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPShidllycEQEIQVDSTSAIDTvvKS 159
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILG--LIKPD-------SGEITFDGKSYQKN--IE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 DKKRLALLEEEAKL---MSEIEEGKTEAAERMKEvadelrdigadsaEPRARRILAGLGFsKEMQEKPCTDFSGGWRMRI 236
Cdd:cd03268 70 ALRRIGALIEAPGFypnLTARENLRLLARLLGIR-------------KKRIDEVLDVVGL-KDSAKKKVKGFSLGMKQRL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17559834 237 SLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKK---TLLIVSHDQGFLDSVCTDIIHLDNQKL 302
Cdd:cd03268 136 GIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDqgiTVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
407-577 |
6.22e-19 |
|
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: 86.08 E-value: 6.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLL----------------------IGKIDPNDGELRKh 464
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndlipgapdegevlldgkdIYDLDVDVLELRR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 465 rtlRIGW-FdqhanealngeQTPVEFLCTKF-NIDY--------------QEARKQLGTTGLAAHAHT-VKIKDLSGGQK 527
Cdd:cd03260 82 ---RVGMvF-----------QKPNPFPGSIYdNVAYglrlhgiklkeeldERVEEALRKAALWDEVKDrLHALGLSGGQQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17559834 528 SRVALCN-LALGgPDIIILDEPTNNLDIESIDALAEAIRDFNG--GVVMVTHD 577
Cdd:cd03260 148 QRLCLARaLANE-PEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
401-617 |
8.17e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 86.68 E-value: 8.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 401 NPPVLGLHDVNFGYGKD----VLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR------KHRTLRIG 470
Cdd:COG1116 4 AAPALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgkpvTGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 471 W-FDQHA---------NEALngeqtPVEFLCTKFNIDYQEARKQLGTTGLAAHAHtVKIKDLSGGQKSRVALCN-LALgG 539
Cdd:COG1116 84 VvFQEPAllpwltvldNVAL-----GLELRGVPKAERRERARELLELVGLAGFED-AYPHQLSGGMRQRVAIARaLAN-D 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 540 PDIIILDEPTNNLDI---ESI-DALAEAIRDFNGGVVMVTHD--------ERLVVRTDCNLWVVEnqgIDEIDG------ 601
Cdd:COG1116 157 PEVLLMDEPFGALDAltrERLqDELLRLWQETGKTVLFVTHDvdeavflaDRVVVLSARPGRIVE---EIDVDLprprdr 233
|
250 260
....*....|....*....|..
gi 17559834 602 ------DFEDYKKEVLDALGEA 617
Cdd:COG1116 234 elrtspEFAALRAEILDLLREE 255
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
407-577 |
1.33e-18 |
|
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: 85.25 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDG---------------ELRKHRTlRIGW 471
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGevlidgedisglseaELYRLRR-RMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 472 FDQHAneALNGEQTPVE----FLCTKFNIDYQE----ARKQLGTTGLAaHAHTVKIKDLSGGQKSRVALCN-LALGgPDI 542
Cdd:cd03261 82 LFQSG--ALFDSLTVFEnvafPLREHTRLSEEEireiVLEKLEAVGLR-GAEDLYPAELSGGMKKRVALARaLALD-PEL 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 17559834 543 IILDEPTNNLDIESIDALAEAIRD----FNGGVVMVTHD 577
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSlkkeLGLTSIMVTHD 196
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
82-309 |
1.56e-18 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 89.18 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 82 IENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHI--------GARKLAIPSHIDllYCEQeiqvDSTSAi 153
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLvgelepdsGTVKWSENANIG--YYAQ----DHAYD- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 154 dtvvksdkkrlalLEEEAKLMSEIEEGKTEaaermkevadelrdiGADsaEPRARRILAGLGFSKEMQEKPCTDFSGGWR 233
Cdd:PRK15064 395 -------------FENDLTLFDWMSQWRQE---------------GDD--EQAVRGTLGRLLFSQDDIKKSVKVLSGGEK 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 234 MRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKLHTYRGNY 309
Cdd:PRK15064 445 GRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTY 520
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
409-568 |
2.00e-18 |
|
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: 85.04 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 409 DVNFGYGKDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDG---------------ELRKHRTlRIGWFD 473
Cdd:TIGR02315 8 SKVYPNGKQAL-KNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGsillegtditklrgkKLRKLRR-RIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 474 QHANeaLNGEQTPVE-----FLCTKFNI----------DYQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALG 538
Cdd:TIGR02315 86 QHYN--LIERLTVLEnvlhgRLGYKPTWrsllgrfseeDKERALSALERVGLADKAYQ-RADQLSGGQQQRVAIARALAQ 162
|
170 180 190
....*....|....*....|....*....|
gi 17559834 539 GPDIIILDEPTNNLDIESIDALAEAIRDFN 568
Cdd:TIGR02315 163 QPDLILADEPIASLDPKTSKQVMDYLKRIN 192
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
412-577 |
2.07e-18 |
|
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: 84.48 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 412 FGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGE-------LRKHRTL---RIGWFDQHanEALN 481
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTayingysIRTDRKAarqSLGYCPQF--DALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 482 GEQTPVEFL-------CTKFNIDYQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDI 554
Cdd:cd03263 88 DELTVREHLrfyarlkGLPKSEIKEEVELLLRVLGLTDKANK-RARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180
....*....|....*....|....*
gi 17559834 555 ESIDALAEAIRDFNGG--VVMVTHD 577
Cdd:cd03263 167 ASRRAIWDLILEVRKGrsIILTTHS 191
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
402-585 |
3.00e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.78 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 402 PPVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKHRTLRIGWFDQHANEALN 481
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 482 GEQTPVEFLCTKFNI---DYQEARKQLGttglAAHAHTVKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESID 558
Cdd:PRK09544 82 LPLTVNRFLRLRPGTkkeDILPALKRVQ----AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180 190
....*....|....*....|....*....|..
gi 17559834 559 ALAEAI----RDFNGGVVMVTHDERLVV-RTD 585
Cdd:PRK09544 158 ALYDLIdqlrRELDCAVLMVSHDLHLVMaKTD 189
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
80-299 |
4.10e-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: 84.08 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIEN----FDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLK-------------HIGARKLAIPSHIDLLyce 142
Cdd:COG1124 2 LEVRNlsvsYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRalaglerpwsgevTFDGRPVTRRRRKAFR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 143 QEIQV---DSTSAID---TVvksdkkrLALLEEEAKLMseieeGKTEAAERMKEVadeLRDIGADSAEpRARRIlaglgf 216
Cdd:COG1124 79 RRVQMvfqDPYASLHprhTV-------DRILAEPLRIH-----GLPDREERIAEL---LEQVGLPPSF-LDRYP------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 217 skemqekpcTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLN--AVIWldNYLQTWKK----TLLIVSHDQGFLDSV 290
Cdd:COG1124 137 ---------HQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSvqAEIL--NLLKDLREerglTYLFVSHDLAVVAHL 205
|
....*....
gi 17559834 291 CTDIIHLDN 299
Cdd:COG1124 206 CDRVAVMQN 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
434-577 |
5.08e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 84.01 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 434 AIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrigwFDQHANEALNGEQ-----------TPVEF------------- 489
Cdd:COG4559 31 AIIGPNGAGKSTLLKLLTGELTPSSGEVR---------LNGRPLAAWSPWElarrravlpqhSSLAFpftveevvalgra 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 490 -LCTKFNIDYQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRV----ALCNLA---LGGPDIIILDEPTNNLDIESIDALA 561
Cdd:COG4559 102 pHGSSAAQDRQIVREALALVGLAHLAGR-SYQTLSGGEQQRVqlarVLAQLWepvDGGPRWLFLDEPTSALDLAHQHAVL 180
|
170
....*....|....*....
gi 17559834 562 EAIRDF---NGGVVMVTHD 577
Cdd:COG4559 181 RLARQLarrGGGVVAVLHD 199
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
405-576 |
5.16e-18 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 81.98 E-value: 5.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 405 LGLHDVNFGYG--KDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELrkhrtlrigwfdqhaneALNG 482
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI-----------------TLDG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 483 EQTPveflctkfniDYQEA-RKQLGTTGLAAHAHTVKIKD-----LSGGQKSRVALCNLALGGPDIIILDEPTNNLDIES 556
Cdd:cd03247 64 VPVS----------DLEKAlSSLISVLNQRPYLFDTTLRNnlgrrFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180
....*....|....*....|..
gi 17559834 557 IDALAEAIRDF--NGGVVMVTH 576
Cdd:cd03247 134 ERQLLSLIFEVlkDKTLIWITH 155
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
405-555 |
5.27e-18 |
|
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: 83.01 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 405 LGLHDVNFGYGKDVLFKKLN--FGVDMdsrIAIVGPNGVGKSTLLKLLI-------GKIDPNDGELRKHRTL---RIGWF 472
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSltLGPGM---YGLLGPNGAGKTTLMRILAtltppssGTIRIDGQDVLKQPQKlrrRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 473 DQH--------ANEALNgeqtpveFLCTKFNIDYQEARKQ----LGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGP 540
Cdd:cd03264 78 PQEfgvypnftVREFLD-------YIAWLKGIPSKEVKARvdevLELVNLGDRAKK-KIGSLSGGMRRRVGIAQALVGDP 149
|
170
....*....|....*
gi 17559834 541 DIIILDEPTNNLDIE 555
Cdd:cd03264 150 SILIVDEPTAGLDPE 164
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
407-613 |
7.52e-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: 83.31 E-value: 7.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYG-----KDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGEL-----------RKHRTLRIG 470
Cdd:COG1124 4 VRNLSVSYGqggrrVPVL-KDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtfdgrpvtrrrRKAFRRRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 471 WFDQHANEALNGEQTpVE------FLCTKFNIDYQEARKQLGTTGLAAHAHTVKIKDLSGGQKSRVALCN-LALgGPDII 543
Cdd:COG1124 83 MVFQDPYASLHPRHT-VDrilaepLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARaLIL-EPELL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 544 ILDEPTNNLDI----ESIDALAEAIRDFNGGVVMVTHDERLVVRTdC-------NLWVVENQGIDEIDGDFE-DYKKEVL 611
Cdd:COG1124 161 LLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVAHL-CdrvavmqNGRIVEELTVADLLAGPKhPYTRELL 239
|
..
gi 17559834 612 DA 613
Cdd:COG1124 240 AA 241
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
407-580 |
1.16e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 86.76 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKD--VLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGE---------------LRK------ 463
Cdd:COG1132 342 FENVSFSYPGDrpVL-KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRilidgvdirdltlesLRRqigvvp 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 464 ------HRTLR--IGWFDQHANEAlngeqtpveflctkfniDYQEARKqlgttglAAHAHTVkIKD-------------- 521
Cdd:COG1132 421 qdtflfSGTIRenIRYGRPDATDE-----------------EVEEAAK-------AAQAHEF-IEAlpdgydtvvgergv 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 522 -LSGGQKSRVAlcnLA---LGGPDIIILDEPTNNLDIESIDALAEAIRDFNGG--VVMVTHdeRL 580
Cdd:COG1132 476 nLSGGQRQRIA---IAralLKDPPILILDEATSALDTETEALIQEALERLMKGrtTIVIAH--RL 535
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
405-585 |
1.57e-17 |
|
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: 80.34 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 405 LGLHDVNFGYG--KDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrigwfdqhanealng 482
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 483 eqtpveflctkfnIDYQEARkQLGTTGLAAHAHTV---------KIKD--LSGGQKSRVALCNLALGGPDIIILDEPTNN 551
Cdd:cd03246 61 -------------LDGADIS-QWDPNELGDHVGYLpqddelfsgSIAEniLSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190
....*....|....*....|....*....|....*..
gi 17559834 552 LDIESIDALAEAIRDFNGG---VVMVTHDERLVVRTD 585
Cdd:cd03246 127 LDVEGERALNQAIAALKAAgatRIVIAHRPETLASAD 163
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
402-584 |
1.97e-17 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 81.43 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 402 PPVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGEL--------RKHRTLRIGWFD 473
Cdd:PRK13543 9 PPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgktatRGDRSRFMAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 474 QHAneALNGEQTPVE---FLCTKFNIDYQEA-RKQLGTTGLAAHAHTVkIKDLSGGQKSRVALCNLALGGPDIIILDEPT 549
Cdd:PRK13543 89 HLP--GLKADLSTLEnlhFLCGLHGRRAKQMpGSALAIVGLAGYEDTL-VRQLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17559834 550 NNLDIESIDALAEAIRDF---NGGVVMVTHDER--LVVRT 584
Cdd:PRK13543 166 ANLDLEGITLVNRMISAHlrgGGAALVTTHGAYaaPPVRT 205
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
407-577 |
2.67e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 85.77 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKHRTLRI-------------GWFD 473
Cdd:PRK11147 6 IHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVarlqqdpprnvegTVYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 474 ------QHANEALNG--------EQTPVEFLCTKF-----NIDYQ-----EARKQ--LGTTGLAAHAhtvKIKDLSGGQK 527
Cdd:PRK11147 86 fvaegiEEQAEYLKRyhdishlvETDPSEKNLNELaklqeQLDHHnlwqlENRINevLAQLGLDPDA---ALSSLSGGWL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17559834 528 SRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGGVVMVTHD 577
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHD 212
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
407-577 |
4.50e-17 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 80.26 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR----------KHRTlRIGW-FDQH 475
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILidgrdvtgvpPERR-NIGMvFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 476 AN-EALNGEQTpVEFLCTKFNIDYQEARKQ----LGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILDEPTN 550
Cdd:cd03259 82 ALfPHLTVAEN-IAFGLKLRGVPKAEIRARvrelLELVGLEGLLNR-YPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190
....*....|....*....|....*....|.
gi 17559834 551 NLDIES----IDALAEAIRDFNGGVVMVTHD 577
Cdd:cd03259 160 ALDAKLreelREELKELQRELGITTIYVTHD 190
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
393-584 |
4.92e-17 |
|
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: 80.14 E-value: 4.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 393 QFPETTKLNPP-VLGLHDVNFGygkdvlfkklnfgVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGE----------L 461
Cdd:cd03292 2 EFINVTKTYPNgTAALDGINIS-------------ISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTirvngqdvsdL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 462 RKHRT--LR--IGWFDQ------HANEALNgeqtpVEFLCTKFNIDYQEARKQ----LGTTGLAAHAHTVKiKDLSGGQK 527
Cdd:cd03292 69 RGRAIpyLRrkIGVVFQdfrllpDRNVYEN-----VAFALEVTGVPPREIRKRvpaaLELVGLSHKHRALP-AELSGGEQ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 528 SRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGG---VVMVTHDERLVVRT 584
Cdd:cd03292 143 QRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAgttVVVATHAKELVDTT 202
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
426-577 |
5.32e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 80.97 E-value: 5.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 426 GVDMDSR----IAIVGPNGVGKSTLLKLLIGKIDPNDG---------------ELRKHR-TLRigwfdQHAN-------- 477
Cdd:PRK13548 20 DVSLTLRpgevVAILGPNGAGKSTLLRALSGELSPDSGevrlngrpladwspaELARRRaVLP-----QHSSlsfpftve 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 478 -------EALNGEQTPVEFLCtkfnidyQEARKQLGTTGLAAHAHTVkikdLSGGQKSRV----ALCNLAL--GGPDIII 544
Cdd:PRK13548 95 evvamgrAPHGLSRAEDDALV-------AAALAQVDLAHLAGRDYPQ----LSGGEQQRVqlarVLAQLWEpdGPPRWLL 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 17559834 545 LDEPTNNLDIESIDALAEAIRDF----NGGVVMVTHD 577
Cdd:PRK13548 164 LDEPTSALDLAHQHHVLRLARQLaherGLAVIVVLHD 200
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
380-617 |
6.32e-17 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 84.53 E-value: 6.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 380 ELLQRRKEYSvkfqfPETTKLNPPVL-G---LHDVNFGY---GKDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIG 452
Cdd:TIGR03375 440 ELMQLPVERP-----EGTRFLHRPRLqGeieFRNVSFAYpgqETPAL-DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLG 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 453 KIDPNDG---------------ELRKHrtlrIGWFdqhanealngEQTPVEFLCT-KFNIDY----------QEARKQLG 506
Cdd:TIGR03375 514 LYQPTEGsvlldgvdirqidpaDLRRN----IGYV----------PQDPRLFYGTlRDNIALgapyaddeeiLRAAELAG 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 507 TTGLAA-HAHTVKIK------DLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGG--VVMVTHD 577
Cdd:TIGR03375 580 VTEFVRrHPDGLDMQigergrSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGktLVLVTHR 659
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 17559834 578 E---RLVVRtdcnLWVVENQGIdEIDGDfedyKKEVLDALGEA 617
Cdd:TIGR03375 660 TsllDLVDR----IIVMDNGRI-VADGP----KDQVLEALRKG 693
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
92-354 |
1.22e-16 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 83.68 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 92 KLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGAR------KLAIPSHIDLLYCEQEiQVDstsaidtVVKSDKKRLA 165
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGElapvsgEIGLAKGIKLGYFAQH-QLE-------FLRADESPLQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 166 LLEEEAKlmseieegkteaaermKEVADELRDIgadsaeprarriLAGLGFSKEMQEKPCTDFSGGWRMRISLARALFLE 245
Cdd:PRK10636 397 HLARLAP----------------QELEQKLRDY------------LGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQR 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 246 PTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKLHTYRGNYTLFkKQYAQDMQVHEK 325
Cdd:PRK10636 449 PNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY-QQWLSDVQKQEN 527
|
250 260 270
....*....|....*....|....*....|
gi 17559834 326 NFDQQQKQLKAMKKEG-KSAKQAEEQVKQQ 354
Cdd:PRK10636 528 QTDEAPKENNANSAQArKDQKRREAELRTQ 557
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
80-284 |
1.28e-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: 79.10 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGarKLAIPSHIDLLYCEQEIqvdstsaidTVVKS 159
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIA--GLERPDSGEILIDGRDV---------TGVPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 DKKRLALLEEEAKL---MSeieegkteaaermkeVAD------ELRDIGADSAEPRARRILAGLGFSKEMQEKPcTDFSG 230
Cdd:cd03259 70 ERRNIGMVFQDYALfphLT---------------VAEniafglKLRGVPKAEIRARVRELLELVGLEGLLNRYP-HELSG 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17559834 231 GWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQT----WKKTLLIVSHDQ 284
Cdd:cd03259 134 GQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKElqreLGITTIYVTHDQ 191
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
405-582 |
1.56e-16 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 79.05 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 405 LGLHDVNFGYGKDVLFKKLNFGVDMDSR----IAIVGPNGVGKSTLLKLLIGKIDPNDGELR------KHRTLRIGW-FD 473
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEegefVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvTGPGPDRGYvFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 474 QHA---------NEALngeqtPVEFLCTKFNIDYQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCN-LALgGPDII 543
Cdd:cd03293 81 QDAllpwltvldNVAL-----GLELQGVPKAEARERAEELLELVGLSGFENA-YPHQLSGGMRQRVALARaLAV-DPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17559834 544 ILDEPTNNLDI---ESI-DALAEAIRDFNGGVVMVTHD--------ERLVV 582
Cdd:cd03293 154 LLDEPFSALDAltrEQLqEELLDIWRETGKTVLLVTHDideavflaDRVVV 204
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
426-576 |
2.68e-16 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 76.70 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 426 GVDMDSR----IAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrigwfdqhaneaLNGEqtPVEFLctkfniDYQEA 501
Cdd:cd03216 18 GVSLSVRrgevHALLGENGAGKSTLMKILSGLYKPDSGEIL-----------------VDGK--EVSFA------SPRDA 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17559834 502 RKQlgttGLAAhahtvkIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDF--NG-GVVMVTH 576
Cdd:cd03216 73 RRA----GIAM------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraQGvAVIFISH 140
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
80-310 |
3.81e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 81.70 E-value: 3.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHI-GarklaipshidllyceQEiQVDSTSAI--DTV 156
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMItG----------------QE-QPDSGTIKigETV 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 157 VKS--DKKRLALlEEEAKLMSEIEEGkteaaermkevADELRdIGadSAEPRARRILAGLGFSKEMQEKPCTDFSGGWRM 234
Cdd:PRK11819 388 KLAyvDQSRDAL-DPNKTVWEEISGG-----------LDIIK-VG--NREIPSRAYVGRFNFKGGDQQKKVGVLSGGERN 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17559834 235 RISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHL-DNQKLHTYRGNYT 310
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFeGDSQVEWFEGNFQ 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
96-295 |
4.41e-16 |
|
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: 81.49 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 96 DKASLTIVYGRRYGLVGPNGMGKTTLLKHI-------------GARKLAIPSHIDLLYCEQEIQV---DSTSAIDtvvks 159
Cdd:COG1123 282 DDVSLTLRRGETLGLVGESGSGKSTLARLLlgllrptsgsilfDGKDLTKLSRRSLRELRRRVQMvfqDPYSSLN----- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 dkKRLALLEEeaklmseIEEGkteaaermkevADELRDIGADSAEPRARRILAGLGFSKEMQEKPCTDFSGGWRMRISLA 239
Cdd:COG1123 357 --PRMTVGDI-------IAEP-----------LRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 240 RALFLEPTLLMLDEPTNHLD-------LNAviwLDNYLQTWKKTLLIVSHDQGFLDSVCTDII 295
Cdd:COG1123 417 RALALEPKLLILDEPTSALDvsvqaqiLNL---LRDLQRELGLTYLFISHDLAVVRYIADRVA 476
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
423-583 |
4.98e-16 |
|
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: 77.86 E-value: 4.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 423 LNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGE----------LRKHRTLRIGW---FdQHANE----------- 478
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSvlfdgeditgLPPHEIARLGIgrtF-QIPRLfpeltvlenvm 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 479 -ALNGeQTPVEFLCTKFNIDYQEARKQ----LGTTGLAAHAHTVkIKDLSGGQKSRVALCnLAL-GGPDIIILDEPTNNL 552
Cdd:cd03219 98 vAAQA-RTGSGLLLARARREEREARERaeelLERVGLADLADRP-AGELSYGQQRRLEIA-RALaTDPKLLLLDEPAAGL 174
|
170 180 190
....*....|....*....|....*....|....
gi 17559834 553 DIESIDALAEAIRDFNG---GVVMVTHDERLVVR 583
Cdd:cd03219 175 NPEETEELAELIRELRErgiTVLLVEHDMDVVMS 208
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
407-583 |
6.43e-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: 76.07 E-value: 6.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrigwfdqhaneaLNGEQTp 486
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL-----------------IDGEDL- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 487 veflcTKFNIDYQEARKQLGTT----GLAAHAhTVK---IKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIE---S 556
Cdd:cd03229 65 -----TDLEDELPPLRRRIGMVfqdfALFPHL-TVLeniALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPItrrE 138
|
170 180
....*....|....*....|....*...
gi 17559834 557 IDALAEAIRDFNG-GVVMVTHDERLVVR 583
Cdd:cd03229 139 VRALLKSLQAQLGiTVVLVTHDLDEAAR 166
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
407-576 |
8.26e-16 |
|
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: 76.86 E-value: 8.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKD--VLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDG---------------ELRKHrtlrI 469
Cdd:cd03245 5 FRNVSFSYPNQeiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGsvlldgtdirqldpaDLRRN----I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 470 GWFDQHA---------NEAL-NGEQTPVEFLctkfnidyqEARKQLGTTGLAA-HAHTVKIK------DLSGGQKSRVAL 532
Cdd:cd03245 81 GYVPQDVtlfygtlrdNITLgAPLADDERIL---------RAAELAGVTDFVNkHPNGLDLQigergrGLSGGQRQAVAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17559834 533 CNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGG--VVMVTH 576
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITH 197
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
78-283 |
8.39e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.75 E-value: 8.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 78 MDIKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIgARKLAiPSHIDLLYCEQEIQVDSTsaidtvv 157
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCF-ARLLT-PQSGTVFLGDKPISMLSS------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 158 KSDKKRLALLE------EEAKLMSEIEEGKTEaaermkevadELRDIGADSAEPRAR--RILAGLGFSkEMQEKPCTDFS 229
Cdd:PRK11231 72 RQLARRLALLPqhhltpEGITVRELVAYGRSP----------WLSLWGRLSAEDNARvnQAMEQTRIN-HLADRRLTDLS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17559834 230 GGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNY---LQTWKKTLLIVSHD 283
Cdd:PRK11231 141 GGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLmreLNTQGKTVVTVLHD 197
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
403-577 |
8.69e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 78.13 E-value: 8.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 403 PVLGLHDVNFGY--GKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR-KHRTL----------RI 469
Cdd:PRK13635 4 EIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITvGGMVLseetvwdvrrQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 470 GWFDQHANE-------------ALNGEQTPVEFLCTKFnidyQEARKQLGTTGLAAH--AHtvkikdLSGGQKSRVALCN 534
Cdd:PRK13635 84 GMVFQNPDNqfvgatvqddvafGLENIGVPREEMVERV----DQALRQVGMEDFLNRepHR------LSGGQKQRVAIAG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17559834 535 LALGGPDIIILDEPTNNLDIESIDALAEAIRDFN--GG--VVMVTHD 577
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKeqKGitVLSITHD 200
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
80-298 |
8.93e-16 |
|
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: 76.70 E-value: 8.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIEN----FDISAQGKLL---FDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARKLAIPSHIdlLYCEQEIQVDSTSA 152
Cdd:COG4778 5 LEVENlsktFTLHLQGGKRlpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSI--LVRHDGGWVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 153 idtvvkSDKKRLALLEEEAKLMS------------EIeegkteaaermkeVADELRDIG--ADSAEPRARRILAGLGFSK 218
Cdd:COG4778 83 ------SPREILALRRRTIGYVSqflrviprvsalDV-------------VAEPLLERGvdREEARARARELLARLNLPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 219 EMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDL---NAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDII 295
Cdd:COG4778 144 RLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAanrAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVV 223
|
...
gi 17559834 296 HLD 298
Cdd:COG4778 224 DVT 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
80-302 |
9.52e-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: 76.77 E-value: 9.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQVDSTSAIDTVvks 159
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVG--LLRPDSGEVLIDGEDISGLSEAELYRL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 dKKRLALLEEEAKL---MSEIEEgkteaaermkeVADELRDIGADSAEPRARRILAGLGFS--KEMQEKPCTDFSGGWRM 234
Cdd:cd03261 76 -RRRMGMLFQSGALfdsLTVFEN-----------VAFPLREHTRLSEEEIREIVLEKLEAVglRGAEDLYPAELSGGMKK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559834 235 RISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTL----LIVSHDQGFLDSVCTDIIHLDNQKL 302
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELgltsIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
433-594 |
2.10e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.97 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIGKIDPNDGELR---------------KHRTLRIGWFDQH-----ANEALNGEQTPVEFLCT 492
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSlvgqplhqmdeearaKLRAKHVGFVFQSfmlipTLNALENVELPALLRGE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 493 KFNIDYQEARKQLGTTGLAAHAHTVKIKdLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAI----RDFN 568
Cdd:PRK10584 119 SSRQSRNGAKALLEQLGLGKRLDHLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHG 197
|
170 180
....*....|....*....|....*.
gi 17559834 569 GGVVMVTHDERLVVRTDCNLWVVENQ 594
Cdd:PRK10584 198 TTLILVTHDLQLAARCDRRLRLVNGQ 223
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
48-302 |
2.89e-15 |
|
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: 79.03 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 48 GIGSGAELGAHF-TVSQLSKTGTQLAQMENSMDIKIENFDIS-AQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHI 125
Cdd:COG4988 304 GIAAAEKIFALLdAPEPAAPAGTAPLPAAGPPSIELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 126 GarKLAIPSHIDLLYCEQEIQVDSTSAIdtvvksdKKRLALLEEEAKLMSE-IEE----GKTEA-AERMKEVADelrdig 199
Cdd:COG4988 384 L--GFLPPYSGSILINGVDLSDLDPASW-------RRQIAWVPQNPYLFAGtIREnlrlGRPDAsDEELEAALE------ 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 200 adsaeprarriLAGL-GFSKEMQEKPCTD-------FSGGWRMRISLARALFLEPTLLMLDEPTNHLDLN--AVIW--LD 267
Cdd:COG4988 449 -----------AAGLdEFVAALPDGLDTPlgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAEteAEILqaLR 517
|
250 260 270
....*....|....*....|....*....|....*
gi 17559834 268 NYLQTwkKTLLIVSHDQGFLDSvCTDIIHLDNQKL 302
Cdd:COG4988 518 RLAKG--RTVILITHRLALLAQ-ADRILVLDDGRI 549
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
80-299 |
2.96e-15 |
|
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: 74.15 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGarKLAIPSHIDLLYCEQEIQvdstsAIDTVVKS 159
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIA--GLEEPDSGSILIDGEDLT-----DLEDELPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 DKKRLALLEEEAKLMSEieegkteaaermKEVADElrdigadsaeprarrILAGLgfskemqekpctdfSGGWRMRISLA 239
Cdd:cd03229 74 LRRRIGMVFQDFALFPH------------LTVLEN---------------IALGL--------------SGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559834 240 RALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQT----WKKTLLIVSHDQGFLDSVCTDIIHLDN 299
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
409-585 |
3.58e-15 |
|
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: 74.64 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 409 DVNFGYGKDVLFKKLNFGVDMDS-RIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKHRTLrigWFDQHANEALNGEQTPV 487
Cdd:cd03297 1 MLCVDIEKRLPDFTLKIDFDLNEeVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV---LFDSRKKINLPPQQRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 488 EF----------LCTKFNIDY-----------QEARKQLGTTGLAaHAHTVKIKDLSGGQKSRVALCNLALGGPDIIILD 546
Cdd:cd03297 78 GLvfqqyalfphLNVRENLAFglkrkrnredrISVDELLDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17559834 547 EPTNNLDIES----IDALAEAIRDFNGGVVMVTHD--------ERLVVRTD 585
Cdd:cd03297 157 EPFSALDRALrlqlLPELKQIKKNLNIPVIFVTHDlseaeylaDRIVVMED 207
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
99-302 |
3.68e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 75.78 E-value: 3.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQVDSTSaiDTVVK-SDKKRLALLEEEAKLMSEI 177
Cdd:PRK10619 25 SLQANAGDVISIIGSSGSGKSTFLRCINF--LEKPSEGSIVVNGQTINLVRDK--DGQLKvADKNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 178 EE--GKTEAAERMKEVADELRDIGADSAEPRARRILAGLGFSKEMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPT 255
Cdd:PRK10619 101 FNlwSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17559834 256 NHLD---LNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKL 302
Cdd:PRK10619 181 SALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
78-261 |
3.83e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.57 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 78 MDIKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPS----HIDllyceqEIQVDSTSAi 153
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAING--TLTPTagtvLVA------GDDVEALSA- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 154 dtvvKSDKKRLALLEEEAKLMSE------IEEGKTEAAERMKevadelrdiGADSAEPRA-RRILAGLGFSKeMQEKPCT 226
Cdd:PRK09536 73 ----RAASRRVASVPQDTSLSFEfdvrqvVEMGRTPHRSRFD---------TWTETDRAAvERAMERTGVAQ-FADRPVT 138
|
170 180 190
....*....|....*....|....*....|....*
gi 17559834 227 DFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLN 261
Cdd:PRK09536 139 SLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
80-301 |
4.07e-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: 73.57 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIEN--FDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGarKLAIPShidllycEQEIQVDSTSAIDTVV 157
Cdd:cd03228 1 IEFKNvsFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLL--RLYDPT-------SGEILIDGVDLRDLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 158 KSDKKRLALLEEEAKLMSeieegkteaaermkevaDELRDigadsaeprarRILaglgfskemqekpctdfSGGWRMRIS 237
Cdd:cd03228 72 ESLRKNIAYVPQDPFLFS-----------------GTIRE-----------NIL-----------------SGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17559834 238 LARALFLEPTLLMLDEPTNHLD-LNAVIWLDNyLQTW--KKTLLIVSHDqgfLDSV--CTDIIHLDNQK 301
Cdd:cd03228 107 IARALLRDPPILILDEATSALDpETEALILEA-LRALakGKTVIVIAHR---LSTIrdADRIIVLDDGR 171
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
405-578 |
5.00e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 74.44 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 405 LGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPN---DGELrkhrtlrigWFDQHANEALN 481
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEV---------LLNGRRLTALP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 482 GE--------QTPVEF------------LCTKFNidyQEARKQ-----LGTTGLAAHAHtvkiKD---LSGGQKSRVALC 533
Cdd:COG4136 73 AEqrrigilfQDDLLFphlsvgenlafaLPPTIG---RAQRRArveqaLEEAGLAGFAD----RDpatLSGGQRARVALL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17559834 534 NLALGGPDIIILDEPTNNLDI---ESIDALA-EAIRDFNGGVVMVTHDE 578
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDAalrAQFREFVfEQIRQRGIPALLVTHDE 194
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
85-307 |
5.37e-15 |
|
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: 74.33 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 85 FDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPShidllycEQEIQVDstsAIDTVvkSDKKrl 164
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAG--LLEPD-------AGFATVD---GFDVV--KEPA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 165 alleeEAKLMSEIEEGKTEAAERM--KEVAD---ELRDIGADSAEPRARRILAGLGFsKEMQEKPCTDFSGGWRMRISLA 239
Cdd:cd03266 75 -----EARRRLGFVSDSTGLYDRLtaRENLEyfaGLYGLKGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559834 240 RALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWK---KTLLIVSHDQGFLDSVCTDIIHLDNQKLHtYRG 307
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRalgKCILFSTHIMQEVERLCDRVVVLHRGRVV-YEG 218
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
415-580 |
5.90e-15 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 77.77 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 415 GKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR---------KHRTL--RIGWFDQHAnEALNGe 483
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRldgadlkqwDRETFgkHIGYLPQDV-ELFPG- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 484 qTPVEFLCtKFNiDYQEARKQLGTTGLA-AHAHTVKIKD------------LSGGQKSRVALCNLALGGPDIIILDEPTN 550
Cdd:TIGR01842 407 -TVAENIA-RFG-ENADPEKIIEAAKLAgVHELILRLPDgydtvigpggatLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190
....*....|....*....|....*....|...
gi 17559834 551 NLDIESIDALAEAIRDFN---GGVVMVTHDERL 580
Cdd:TIGR01842 484 NLDEEGEQALANAIKALKargITVVVITHRPSL 516
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
401-595 |
6.50e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.17 E-value: 6.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 401 NPPVLGLHDVNFGYGKDVLF--KKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDG---------------ELRK 463
Cdd:PRK13648 4 KNSIIVFKNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGeifynnqaitddnfeKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 464 HrtlrIGWFDQHANEALNGE--QTPVEFLCTKFNIDYQ-------EARKQLGTTGLAAHahtvKIKDLSGGQKSRVALCN 534
Cdd:PRK13648 84 H----IGIVFQNPDNQFVGSivKYDVAFGLENHAVPYDemhrrvsEALKQVDMLERADY----EPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 535 LALGGPDIIILDEPTNNLDIESIDALAEAIR----DFNGGVVMVTHDerLVVRTDCNLWVVENQG 595
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRkvksEHNITIISITHD--LSEAMEADHVIVMNKG 218
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
409-582 |
7.69e-15 |
|
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: 74.77 E-value: 7.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 409 DVNFGY--GKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDG----------------ELRKhrtlRIG 470
Cdd:TIGR04520 5 NVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGkvtvdgldtldeenlwEIRK----KVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 471 WFDQHANEALNGeqTPVE----FLCTKFNIDY-------QEARKQLGTTGLAAHA-HTvkikdLSGGQKSRVALCN-LAL 537
Cdd:TIGR04520 81 MVFQNPDNQFVG--ATVEddvaFGLENLGVPReemrkrvDEALKLVGMEDFRDREpHL-----LSGGQKQRVAIAGvLAM 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17559834 538 gGPDIIILDEPTNNLD-------IESIDALAeaiRDFNGGVVMVTHD-------ERLVV 582
Cdd:TIGR04520 154 -RPDIIILDEATSMLDpkgrkevLETIRKLN---KEEGITVISITHDmeeavlaDRVIV 208
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
401-577 |
9.10e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 75.90 E-value: 9.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 401 NPPVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrigwfdqhaneaL 480
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIL-----------------L 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 481 NGEQ---TPVE--FLCTKF-------------NIDY---------QEARKQ----LGTTGLAAHAHTvKIKDLSGGQKSR 529
Cdd:COG3842 65 DGRDvtgLPPEkrNVGMVFqdyalfphltvaeNVAFglrmrgvpkAEIRARvaelLELVGLEGLADR-YPHQLSGGQQQR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17559834 530 VALCN-LALgGPDIIILDEPTNNLDIESIDALAEAIRD----FNGGVVMVTHD 577
Cdd:COG3842 144 VALARaLAP-EPRVLLLDEPLSALDAKLREEMREELRRlqreLGITFIYVTHD 195
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
95-259 |
9.38e-15 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 77.40 E-value: 9.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 95 FDKASLTIVYGRRYGLVGPNGMGKTTLLKHIgARklAIPSHidllycEQEIQVDSTSAIDTVVKSDKKRLALLEEEAKLM 174
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATL-AG--LLDPL------QGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 175 -SEIEE----GKTEAAErmKEVADELRDIGAdsaEPRARRILAGLgfSKEMQEKPCTdFSGGWRMRISLARALFLEPTLL 249
Cdd:TIGR02868 422 dTTVREnlrlARPDATD--EELWAALERVGL---ADWLRALPDGL--DTVLGEGGAR-LSGGERQRLALARALLADAPIL 493
|
170
....*....|
gi 17559834 250 MLDEPTNHLD 259
Cdd:TIGR02868 494 LLDEPTEHLD 503
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
96-302 |
9.84e-15 |
|
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: 73.78 E-value: 9.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 96 DKASLTIVYGRRYGLVGPNGMGKTTLLKHIGarKLAIPShidllycEQEIQVDSTSA--IDTVVKsdKKRLALLEEEAKL 173
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLA--GLYKPT-------SGSVLLDGTDIrqLDPADL--RRNIGYVPQDVTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 174 MS-----EIEEGKTEAAERMKEVADELrdIGADSAEPRARRilaglGFSKEMQEKPCtDFSGGWRMRISLARALFLEPTL 248
Cdd:cd03245 90 FYgtlrdNITLGAPLADDERILRAAEL--AGVTDFVNKHPN-----GLDLQIGERGR-GLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 249 LMLDEPTNHLDLNAVIWLDNYLQTWK--KTLLIVSHDQGFLDsVCTDIIHLDNQKL 302
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLgdKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
80-295 |
1.11e-14 |
|
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: 73.69 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKA----SLTIVYGRRYGLVGPNGMGKTTLLKHI-------------GARKLAIPSHIDLLYCE 142
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKAlddvSFSIKKGETLGLVGESGSGKSTLARAIlgllkptsgsiifDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 143 QEIQV---DSTSAIDTVVKsdkkrlalleeeaklmseIEEgkteaaermkEVADELRDIGADSAEPRARRI----LAGLG 215
Cdd:cd03257 82 KEIQMvfqDPMSSLNPRMT------------------IGE----------QIAEPLRIHGKLSKKEARKEAvlllLVGVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 216 FSKE-MQEKPcTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDL---NAVIWLDNYLQT-WKKTLLIVSHDQGFLDSV 290
Cdd:cd03257 134 LPEEvLNRYP-HELSGGQRQRVAIARALALNPKLLIADEPTSALDVsvqAQILDLLKKLQEeLGLTLLFITHDLGVVAKI 212
|
....*
gi 17559834 291 CTDII 295
Cdd:cd03257 213 ADRVA 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
421-577 |
1.14e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 73.91 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 421 KKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR-----------KHRTlRIG---------WFDQHANEAL 480
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglvpwkrrkKFLR-RIGvvfgqktqlWWDLPVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 481 NgeqtpveFLCTKFNIDYQEARKQL-GTTGLAAHAHTVKI--KDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESI 557
Cdd:cd03267 117 Y-------LLAAIYDLPPARFKKRLdELSELLDLEELLDTpvRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180
....*....|....*....|....
gi 17559834 558 DALAEAIRDFN---GGVVMVT-HD 577
Cdd:cd03267 190 ENIRNFLKEYNrerGTTVLLTsHY 213
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
399-577 |
1.17e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.59 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 399 KLNPPVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELrkhrtlrigWFDQHANE 478
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL---------LFEGEDIS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 479 ALNGE----------QTPVEFLCTKF-NI-----------DYQEARKQLGTTGLAAHAHTVKIKDLSGGQKSRVALC-NL 535
Cdd:PRK10247 73 TLKPEiyrqqvsycaQTPTLFGDTVYdNLifpwqirnqqpDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIrNL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17559834 536 ALgGPDIIILDEPTNNLDIESIDALAEAI----RDFNGGVVMVTHD 577
Cdd:PRK10247 153 QF-MPKVLLLDEITSALDESNKHNVNEIIhryvREQNIAVLWVTHD 197
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
407-580 |
1.28e-14 |
|
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: 73.73 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYG--KDV-LFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGEL----RKHRTLRIGWFDQHAnea 479
Cdd:cd03249 3 FKNVSFRYPsrPDVpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgVDIRDLNLRWLRSQI--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 480 lnG--EQTPVEFLCT-KFNIDY----------QEARKQlgttglaAHAHTVKIKD--------------LSGGQKSRVAL 532
Cdd:cd03249 80 --GlvSQEPVLFDGTiAENIRYgkpdatdeevEEAAKK-------ANIHDFIMSLpdgydtlvgergsqLSGGQKQRIAI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17559834 533 CNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGG--VVMVTHdeRL 580
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGrtTIVIAH--RL 198
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
79-302 |
1.36e-14 |
|
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: 77.18 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 79 DIKIEN--FDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIgARkLAIPSHIDLLYCEQEI-QVDSTSAidt 155
Cdd:COG2274 473 DIELENvsFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL-LG-LYEPTSGRILIDGIDLrQIDPASL--- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 156 vvksdKKRLALLEEEAKLMSE-IEE----GKTEAA-ERMKEVAdelRDIGADSAeprarrILA-GLGFSKEMQEKPcTDF 228
Cdd:COG2274 548 -----RRQIGVVLQDVFLFSGtIREnitlGDPDATdEEIIEAA---RLAGLHDF------IEAlPMGYDTVVGEGG-SNL 612
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWK--KTLLIVSHDqgfLDSV--CTDIIHLDNQKL 302
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLkgRTVIIIAHR---LSTIrlADRIIVLDKGRI 687
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
401-584 |
1.40e-14 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 73.05 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 401 NPPVLGLHDVNFGYGK-DVLFkklnfgvdmdsriaIVGPNGVGKSTLLKLLIGKIDPNDGELR---------KHRTL--- 467
Cdd:TIGR02673 12 PGGVAALHDVSLHIRKgEFLF--------------LTGPSGAGKTTLLKLLYGALTPSRGQVRiagedvnrlRGRQLpll 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 468 --RIGWFDQhaNEALNGEQTPVEFLCTKFNIDYQEAR---KQLGTT----GLAAHAHTVKIKdLSGGQKSRVALCNLALG 538
Cdd:TIGR02673 78 rrRIGVVFQ--DFRLLPDRTVYENVALPLEVRGKKEReiqRRVGAAlrqvGLEHKADAFPEQ-LSGGEQQRVAIARAIVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17559834 539 GPDIIILDEPTNNLD---IESIDALAEAIRDFNGGVVMVTHDERLVVRT 584
Cdd:TIGR02673 155 SPPLLLADEPTGNLDpdlSERILDLLKRLNKRGTTVIVATHDLSLVDRV 203
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
81-303 |
1.42e-14 |
|
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: 72.95 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 81 KIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHI---------GARKLAIPSHIDLL---YCEQEIQVD 148
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIlgllkptsgSIRVFGKPLEKERKrigYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 149 STSAIdTVvksdkKRLALLeeeaKLMSEIEEGKTEAAERMKEVADELRDIGAdsAEPRARRIlaglgfskemqekpcTDF 228
Cdd:cd03235 81 RDFPI-SV-----RDVVLM----GLYGHKGLFRRLSKADKAKVDEALERVGL--SELADRQI---------------GEL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWK---KTLLIVSHDQGFLDSVCTDIIHLdNQKLH 303
Cdd:cd03235 134 SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRregMTILVVTHDLGLVLEYFDRVLLL-NRTVV 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
84-303 |
1.44e-14 |
|
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: 72.67 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 84 NFDISAQGKLLfDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGarKLAIPSHIDLLYCeqeiqvdstsaidtvvKSDKKR 163
Cdd:cd03226 6 SFSYKKGTEIL-DDLSLDLYAGEIIALTGKNGAGKTTLAKILA--GLIKESSGSILLN----------------GKPIKA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 164 LALLEEEAKLMSEIEEGKTeaaerMKEVADELR---DIGADSAEpRARRILAGLGFSKEMQEKPcTDFSGGWRMRISLAR 240
Cdd:cd03226 67 KERRKSIGYVMQDVDYQLF-----TDSVREELLlglKELDAGNE-QAETVLKDLDLYALKERHP-LSLSGGQKQRLAIAA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 241 ALFLEPTLLMLDEPTNHLD---LNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKLH 303
Cdd:cd03226 140 ALLSGKDLLIFDEPTSGLDyknMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
409-565 |
1.45e-14 |
|
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: 73.42 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 409 DVNFGYGKD---VLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR---------KHRTLR--IGwfdq 474
Cdd:cd03251 5 NVTFRYPGDgppVL-RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILidghdvrdyTLASLRrqIG---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 475 hanealNGEQTPVEFLCTKF-NIDY---QEARKQLGTTGLAAHAHTV----------KIKD----LSGGQKSRVALCNLA 536
Cdd:cd03251 80 ------LVSQDVFLFNDTVAeNIAYgrpGATREEVEEAARAANAHEFimelpegydtVIGErgvkLSGGQRQRIAIARAL 153
|
170 180
....*....|....*....|....*....
gi 17559834 537 LGGPDIIILDEPTNNLDIESIDALAEAIR 565
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALE 182
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
433-585 |
1.55e-14 |
|
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: 73.24 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIGKIDPNDGELR---------------KHRTLRIGWFDQhaNEALNGEQTPVEflctkfNI- 496
Cdd:COG4181 41 VAIVGASGSGKSTLLGLLAGLDRPTSGTVRlagqdlfaldedaraRLRARHVGFVFQ--SFQLLPTLTALE------NVm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 497 ----------DYQEARKQLGTTGLAAHAHTVKiKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIES----IDALAE 562
Cdd:COG4181 113 lplelagrrdARARARALLERVGLGHRLDHYP-AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFE 191
|
170 180
....*....|....*....|...
gi 17559834 563 AIRDFNGGVVMVTHDERLVVRTD 585
Cdd:COG4181 192 LNRERGTTLVLVTHDPALAARCD 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
80-283 |
1.87e-14 |
|
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: 76.17 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGK-LLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPShidllycEQEIQVDSTSAIDTVVK 158
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG--FVDPT-------EGSIAVNGVPLADADAD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 159 SDKKRLALLEE-----EAKLMSEIEEGKTEAAErmKEVADELRDIGADSAEPRArrilaGLGFSKEMQEKPcTDFSGGWR 233
Cdd:TIGR02857 393 SWRDQIAWVPQhpflfAGTIAENIRLARPDASD--AEIREALERAGLDEFVAAL-----PQGLDTPIGEGG-AGLSGGQA 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17559834 234 MRISLARALFLEPTLLMLDEPTNHLDL-NAVIWLDNYLQTWK-KTLLIVSHD 283
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAeTEAEVLEALRALAQgRTVLLVTHR 516
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
409-595 |
2.26e-14 |
|
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: 72.64 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 409 DVNFGY--GKDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGEL---------RKHRTLR--IGWFDQH 475
Cdd:cd03254 7 NVNFSYdeKKPVL-KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdISRKSLRsmIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 476 A---------NEALNGEQTPVEflctkfniDYQEARKQLGTT--------GLAAHAhTVKIKDLSGGQKSRVALCNLALG 538
Cdd:cd03254 86 TflfsgtimeNIRLGRPNATDE--------EVIEAAKEAGAHdfimklpnGYDTVL-GENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17559834 539 GPDIIILDEPTNNLDIESIDALAEAIRDFNGG--VVMVTHdeRLVVRTDCNLWVVENQG 595
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGrtSIIIAH--RLSTIKNADKILVLDDG 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
407-577 |
2.43e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 72.72 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGE--------------LRKHRTlRIGW- 471
Cdd:COG1126 4 IENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTitvdgedltdskkdINKLRR-KVGMv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 472 FdQHAN------------EAlngeqtPVEFLctkfNIDYQEARKQ----LGTTGLAAHAHtVKIKDLSGGQKSRVALCN- 534
Cdd:COG1126 83 F-QQFNlfphltvlenvtLA------PIKVK----KMSKAEAEERamelLERVGLADKAD-AYPAQLSGGQQQRVAIARa 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17559834 535 LALgGPDIIILDEPTNNLDIESIDALAEAIRDF-NGG--VVMVTHD 577
Cdd:COG1126 151 LAM-EPKVMLFDEPTSALDPELVGEVLDVMRDLaKEGmtMVVVTHE 195
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
395-577 |
4.32e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.40 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 395 PETTKLNPPV-LGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKHRTLrigwfd 473
Cdd:PRK11247 2 MNTARLNQGTpLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 474 qhANEALngEQTPVEF-----LCTKFNID----------YQEARKQLGTTGLAAHAHTVKIKdLSGGQKSRVALCNLALG 538
Cdd:PRK11247 76 --LAEAR--EDTRLMFqdarlLPWKKVIDnvglglkgqwRDAALQALAAVGLADRANEWPAA-LSGGQKQRVALARALIH 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17559834 539 GPDIIILDEPTNNLD----IESIDALAEAIRDFNGGVVMVTHD 577
Cdd:PRK11247 151 RPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
79-302 |
5.03e-14 |
|
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: 75.19 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 79 DIKIEN--FDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIgARKLAiPSHidllyceQEIQVDSTSaIDTV 156
Cdd:COG4987 333 SLELEDvsFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALL-LRFLD-PQS-------GSITLGGVD-LRDL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 157 VKSD-KKRLALLEEEAKLMSEieegkTeaaermkeVADELRdIGADSA-EPRARRIL--AGL---------GFSKEMQEK 223
Cdd:COG4987 403 DEDDlRRRIAVVPQRPHLFDT-----T--------LRENLR-LARPDAtDEELWAALerVGLgdwlaalpdGLDTWLGEG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 224 PCTdFSGGWRMRISLARALFLEPTLLMLDEPTNHLD-LNAVIWLDNYLQTWK-KTLLIVSHDQGFLDSVCTdIIHLDNQK 301
Cdd:COG4987 469 GRR-LSGGERRRLALARALLRDAPILLLDEPTEGLDaATEQALLADLLEALAgRTVLLITHRLAGLERMDR-ILVLEDGR 546
|
.
gi 17559834 302 L 302
Cdd:COG4987 547 I 547
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
420-587 |
5.73e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 71.41 E-value: 5.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 420 FKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKHRtlRIGW-FDqhANEALNGEQTPVE---FLCTKFN 495
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--RVSSlLG--LGGGFNPELTGREniyLNGRLLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 496 IDYQEARKQL----GTTGLAAHAHTvKIKDLSGGQKSRVAL-CNLALgGPDIIILDEPTNNLDIE----SIDALAEAIRD 566
Cdd:cd03220 114 LSRKEIDEKIdeiiEFSELGDFIDL-PVKTYSSGMKARLAFaIATAL-EPDILLIDEVLAVGDAAfqekCQRRLRELLKQ 191
|
170 180
....*....|....*....|.
gi 17559834 567 fNGGVVMVTHDERLVVRTdCN 587
Cdd:cd03220 192 -GKTVILVSHDPSSIKRL-CD 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
395-585 |
5.89e-14 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 74.78 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 395 PETTKLNPP--VLGLHDVNFGY--GKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDP-------------- 456
Cdd:COG4618 319 PERMPLPRPkgRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPtagsvrldgadlsq 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 457 -NDGELRKHrtlrIGWFDQHAnEALNGeqTPVEflctkfNI------DYQE----ARkqlgttglAAHAH---------- 515
Cdd:COG4618 399 wDREELGRH----IGYLPQDV-ELFDG--TIAE------NIarfgdaDPEKvvaaAK--------LAGVHemilrlpdgy 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17559834 516 -TVkIKD----LSGGQKSRVALCNlAL-GGPDIIILDEPTNNLDIESIDALAEAIRDF--NGG-VVMVTHDERLVVRTD 585
Cdd:COG4618 458 dTR-IGEggarLSGGQRQRIGLAR-ALyGDPRLVVLDEPNSNLDDEGEAALAAAIRALkaRGAtVVVITHRPSLLAAVD 534
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
80-581 |
6.89e-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: 6.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARKLAIPSHIDLLY----CEQ------------ 143
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYhvalCEKcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 144 ----------EIQVDSTSAIDTVVKSDKKRLALLEEEAKLMSEIEegkteaaERMKEVADELRDIG--ADSAEPRARRIL 211
Cdd:TIGR03269 81 pcpvcggtlePEEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDD-------TVLDNVLEALEEIGyeGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 212 AGLGFSKEMQEKpCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKK----TLLIVSHDQGFL 287
Cdd:TIGR03269 154 EMVQLSHRITHI-ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasgiSMVLTSHWPEVI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 288 DSVCTDIIHLDNqklhtyrgnytlfkkqyaqdmqvheknfdqqqkqlKAMKKEGKSakqaEEQVKQQMAnkakkggkkna 367
Cdd:TIGR03269 233 EDLSDKAIWLEN-----------------------------------GEIKEEGTP----DEVVAVFME----------- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 368 gkvnddddaGAPElLQRRKEYSVKfqfpettklnPPVLGLHDVNFGY-GKDVLFKKLNFGVDMDSR----IAIVGPNGVG 442
Cdd:TIGR03269 263 ---------GVSE-VEKECEVEVG----------EPIIKVRNVSKRYiSVDRGVVKAVDNVSLEVKegeiFGIVGTSGAG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 443 KSTLLKLLIGKIDPNDGELrkhrTLRIG--WFDQ------------------HANEALNGEQTPVEFLCTKFNIDYQE-- 500
Cdd:TIGR03269 323 KTTLSKIIAGVLEPTSGEV----NVRVGdeWVDMtkpgpdgrgrakryigilHQEYDLYPHRTVLDNLTEAIGLELPDel 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 501 AR-------KQLGTTGLAAHAHTVKIKD-LSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAI----RDFN 568
Cdd:TIGR03269 399 ARmkavitlKMVGFDEEKAEEILDKYPDeLSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEME 478
|
570
....*....|...
gi 17559834 569 GGVVMVTHDERLV 581
Cdd:TIGR03269 479 QTFIIVSHDMDFV 491
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
415-580 |
8.08e-14 |
|
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: 70.63 E-value: 8.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 415 GKDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPN--DGELrkhrtlrigWFDQH------ANE-ALNG--- 482
Cdd:cd03217 12 GKEIL-KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEI---------LFKGEditdlpPEErARLGifl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 483 -EQTPVEFlctkfnidyqearkqlgttglaahaHTVKIKDL--------SGGQKSRVALCNLALGGPDIIILDEPTNNLD 553
Cdd:cd03217 82 aFQYPPEI-------------------------PGVKNADFlryvnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190
....*....|....*....|....*....|
gi 17559834 554 IESIDALAEAI---RDFNGGVVMVTHDERL 580
Cdd:cd03217 137 IDALRLVAEVInklREEGKSVLIITHYQRL 166
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
80-282 |
9.80e-14 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 71.27 E-value: 9.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARklaIP----SHIDLL---------------- 139
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGD---LPptygNDVRLFgerrggedvwelrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 140 -YCEQEIQVD---STSAIDTVVksdkkrlalleeeaklmSeieeGKTEAAERMKEVADELRDigadsaepRARRILAGLG 215
Cdd:COG1119 81 gLVSPALQLRfprDETVLDVVL-----------------S----GFFDSIGLYREPTDEQRE--------RARELLELLG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559834 216 FSkEMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNA----VIWLDNYLQTWKKTLLIVSH 282
Cdd:COG1119 132 LA-HLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
403-593 |
1.13e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.15 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 403 PVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR----------KHRTLRIGWF 472
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsraRHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 473 DQHANeaLNGEQTPVEFLCT---KFNIDYQEARKQLGT----TGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIIL 545
Cdd:PRK13537 86 PQFDN--LDPDFTVRENLLVfgrYFGLSAAAARALVPPllefAKLENKADA-KVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 546 DEPTNNLDIESIDALAEAIRDF---NGGVVMVTH----DERLvvrtdCN-LWVVEN 593
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLlarGKTILLTTHfmeeAERL-----CDrLCVIEE 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
96-302 |
1.16e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.89 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 96 DKASLTIVYGRRYGLVGPNGMGKTTLLKHIGarKLAIPSHIDLLyceqeiqVDSTSaidtvVKSDKKRLALLEEEAKL-- 173
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCIN--KLEEITSGDLI-------VDGLK-----VNDPKVDERLIRQEAGMvf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 174 --------MSEIEEgkteaaermkeVA---DELRDIGADSAEPRARRILAGLGFSKEMQEKPcTDFSGGWRMRISLARAL 242
Cdd:PRK09493 84 qqfylfphLTALEN-----------VMfgpLRVRGASKEEAEKQARELLAKVGLAERAHHYP-SELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 243 FLEPTLLMLDEPTNHLD---LNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKL 302
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDpelRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
99-297 |
1.23e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.59 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTT----LLKHIGAR--------KLAIPSHIDLLYCEQEIQV---DSTSAIDtvvksdkKR 163
Cdd:PRK15134 306 SFTLRPGETLGLVGESGSGKSTtglaLLRLINSQgeiwfdgqPLHNLNRRQLLPVRHRIQVvfqDPNSSLN-------PR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 164 LALLEEeaklmseIEEG------KTEAAERMKEVADELRDIGADsAEPRARRilaglgfskemqekPcTDFSGGWRMRIS 237
Cdd:PRK15134 379 LNVLQI-------IEEGlrvhqpTLSAAQREQQVIAVMEEVGLD-PETRHRY--------------P-AEFSGGQRQRIA 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559834 238 LARALFLEPTLLMLDEPTNHLD--LNAVI--WLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHL 297
Cdd:PRK15134 436 IARALILKPSLIILDEPTSSLDktVQAQIlaLLKSLQQKHQLAYLFISHDLHVVRALCHQVIVL 499
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
433-576 |
1.36e-13 |
|
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: 69.50 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIGKIDPN--------DGELRKHRTLR--IGWFDQHanEALNGEQTPVEFLctkfnidyqear 502
Cdd:cd03213 38 TAIMGPSGAGKSTLLNALAGRRTGLgvsgevliNGRPLDKRSFRkiIGYVPQD--DILHPTLTVRETL------------ 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17559834 503 kqlgttglaahAHTVKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDF-NGG--VVMVTH 576
Cdd:cd03213 104 -----------MFAAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGrtIICSIH 169
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
80-303 |
1.89e-13 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 69.53 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRrYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIqVDSTSAIdtvvks 159
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILAT--LTPPSSGTIRIDGQDV-LKQPQKL------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 dKKRLALLEEEAKLMSEIeegkteAAERMKEVADELRDIGADSAEPRARRILAGLGFSkEMQEKPCTDFSGGWRMRISLA 239
Cdd:cd03264 71 -RRRIGYLPQEFGVYPNF------TVREFLDYIAWLKGIPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 240 RALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTW--KKTLLIVSHDQGFLDSVCTDIIHLDNQKLH 303
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELgeDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
407-578 |
1.99e-13 |
|
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: 69.59 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR-----------KHRTLRIGwFDQH 475
Cdd:cd03301 3 LENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdlppKDRDIAMV-FQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 476 A---------NEALNGEQTPVEflctKFNID--YQEARKQLGTTGLAAHahtvKIKDLSGGQKSRVALCNLALGGPDIII 544
Cdd:cd03301 82 AlyphmtvydNIAFGLKLRKVP----KDEIDerVREVAELLQIEHLLDR----KPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 17559834 545 LDEPTNNLD----IESIDALAEAIRDFNGGVVMVTHDE 578
Cdd:cd03301 154 MDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQ 191
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
407-577 |
2.12e-13 |
|
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: 69.48 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGEL-----------RKHRTLR--IGWFD 473
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidglkltddkKNINELRqkVGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 474 QHAN--EALNGEQTPVEFLCTKFNIDYQEA----RKQLGTTGLAAHAHtVKIKDLSGGQKSRVALCN-LALgGPDIIILD 546
Cdd:cd03262 83 QQFNlfPHLTVLENITLAPIKVKGMSKAEAeeraLELLEKVGLADKAD-AYPAQLSGGQQQRVAIARaLAM-NPKVMLFD 160
|
170 180 190
....*....|....*....|....*....|....
gi 17559834 547 EPTNNLDIESIDALAEAIRDF-NGGVVM--VTHD 577
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLaEEGMTMvvVTHE 194
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
96-303 |
2.59e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 69.69 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 96 DKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQvdstsaidtvvKSDKKRLA---------- 165
Cdd:COG1136 25 RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG--LDRPTSGEVLIDGQDIS-----------SLSERELArlrrrhigfv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 166 -----LLEEeaklMSeieegkteAAERMkEVADELRDIGADSAEPRARRILAGLGFSKEMQEKPcTDFSGGWRMRISLAR 240
Cdd:COG1136 92 fqffnLLPE----LT--------ALENV-ALPLLLAGVSRKERRERARELLERVGLGDRLDHRP-SQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 241 ALFLEPTLLMLDEPTNHLD-------LNAviwLDNYLQTWKKTLLIVSHDQgFLDSVCTDIIHLDNQKLH 303
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDsktgeevLEL---LRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
417-583 |
2.84e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.84 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 417 DVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGEL---------------RKHRTLRIGWFDQHAN---- 477
Cdd:PRK11629 23 DVL-HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqpmsklssaakAELRNQKLGFIYQFHHllpd 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 478 -EALNGEQTPVEFLCTKFNIDYQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIES 556
Cdd:PRK11629 102 fTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANH-RPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190
....*....|....*....|....*....|.
gi 17559834 557 IDALAEAIRDFN----GGVVMVTHDERLVVR 583
Cdd:PRK11629 181 ADSIFQLLGELNrlqgTAFLVVTHDLQLAKR 211
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
433-582 |
3.22e-13 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 69.74 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIGKIDPNDGELRKHRTlRIGWFDQHANEALNGeqTPVEFLCTKFNIDYQ------EARKQLG 506
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQYIKADYEG--TVRDLLSSITKDFYThpyfktEIAKPLQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 507 TTGLAAHahtvKIKDLSGGQKSRVALCnLALGGP-DIIILDEPTNNLDIESIDALAEAIRDF----NGGVVMVTHD---- 577
Cdd:cd03237 105 IEQILDR----EVPELSGGELQRVAIA-ACLSKDaDIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHDiimi 179
|
....*....
gi 17559834 578 ----ERLVV 582
Cdd:cd03237 180 dylaDRLIV 188
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
409-585 |
4.75e-13 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 69.04 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 409 DVNFGYGK--DVL-FKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGEL---------RKHRTLrigwfdqHA 476
Cdd:cd03248 16 NVTFAYPTrpDTLvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlldgkpisqYEHKYL-------HS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 477 NEALNGeQTPVEFLCT-KFNIDYQEARKQLGTTGLAA---HAHTV--------------KIKDLSGGQKSRVALCNLALG 538
Cdd:cd03248 89 KVSLVG-QEPVLFARSlQDNIAYGLQSCSFECVKEAAqkaHAHSFiselasgydtevgeKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17559834 539 GPDIIILDEPTNNLDIESIDALAEAIRDFNGG--VVMVTHDERLVVRTD 585
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERrtVLVIAHRLSTVERAD 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
80-299 |
5.45e-13 |
|
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: 68.46 E-value: 5.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIgarkLAIpshidLLYCEQEIQVDSTSaidtVVKS 159
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMI----LGI-----ILPDSGEVLFDGKP----LDIA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 DKKRLALLEEEAKLMSeieegKTEAAERMKEVAdELRDIGADSAEPRARRILAGLGFSkEMQEKPCTDFSGGWRMRISLA 239
Cdd:cd03269 68 ARNRIGYLPEERGLYP-----KMKVIDQLVYLA-QLKGLKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFI 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 240 RALFLEPTLLMLDEPTNHLD-LNAVIWLD--NYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDN 299
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDpVNVELLKDviRELARAGKTVILSTHQMELVEELCDRVLLLNK 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
96-259 |
6.56e-13 |
|
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: 71.25 E-value: 6.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 96 DKASLTIVYGRRYGLVGPNGMGKTTLlkhigARKLA--IPSHIDLLYCEQEIQvdstsaidtvvksDKKRLALLEEEAKL 173
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTL-----GLALLrlIPSEGEIRFDGQDLD-------------GLSRRALRPLRRRM 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 174 --------------MS--EI-EEGkteaaermkevadeLR--DIGADSAEPRAR--RILAGLGFSKEMQEKPCTDFSGGW 232
Cdd:COG4172 365 qvvfqdpfgslsprMTvgQIiAEG--------------LRvhGPGLSAAERRARvaEALEEVGLDPAARHRYPHEFSGGQ 430
|
170 180
....*....|....*....|....*..
gi 17559834 233 RMRISLARALFLEPTLLMLDEPTNHLD 259
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
433-614 |
7.58e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.89 E-value: 7.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIGKIDPND--------------------GELRKHRTlRIGWFDQHAN---------EALNGE 483
Cdd:PRK09984 33 VALLGPSGSGKSTLLRHLSGLITGDKsagshiellgrtvqregrlaRDIRKSRA-NTGYIFQQFNlvnrlsvleNVLIGA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 484 --QTPVEFLCTKF--NIDYQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDA 559
Cdd:PRK09984 112 lgSTPFWRTCFSWftREQKQRALQALTRVGMVHFAHQ-RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARI 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17559834 560 LAEAIRDFN---GGVVMVT-HDERLVVRTdCNLWVVENQGIDEIDGDFEDYKKEVLDAL 614
Cdd:PRK09984 191 VMDTLRDINqndGITVVVTlHQVDYALRY-CERIVALRQGHVFYDGSSQQFDNERFDHL 248
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
81-259 |
8.14e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 67.89 E-value: 8.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 81 KIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIgarklaIPSHIDLLYCEQEIQVDSTSaIDTVvKSD 160
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAI------AGTLSPAFSASGEVLLNGRR-LTAL-PAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 161 KKRLALLEEEAKL---MSEIEE------GKTEAAERMKEVADELRDIGadsaeprarriLAGLGFSKemqekPCTdFSGG 231
Cdd:COG4136 75 QRRIGILFQDDLLfphLSVGENlafalpPTIGRAQRRARVEQALEEAG-----------LAGFADRD-----PAT-LSGG 137
|
170 180
....*....|....*....|....*...
gi 17559834 232 WRMRISLARALFLEPTLLMLDEPTNHLD 259
Cdd:COG4136 138 QRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
410-568 |
9.87e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.86 E-value: 9.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 410 VNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGEL-----------RKHRTLRIGWFDQHA-- 476
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaSKEVARRIGLLAQNAtt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 477 ------NEALNGEQTPVEFLCTKFNIDYQEA-RKQLGTTGLaAHAHTVKIKDLSGGQKSRVALCNLALGGPDIIILDEPT 549
Cdd:PRK10253 93 pgditvQELVARGRYPHQPLFTRWRKEDEEAvTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170
....*....|....*....
gi 17559834 550 NNLDIESIDALAEAIRDFN 568
Cdd:PRK10253 172 TWLDISHQIDLLELLSELN 190
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
74-283 |
1.05e-12 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 68.58 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 74 MENSMD-IKIEN----FDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHI-GarkLAIPShidllycEQEIQV 147
Cdd:COG1116 1 MSAAAPaLELRGvskrFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIaG---LEKPT-------SGEVLV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 148 DstsaiDTVVKSDKKRLALLEEEAKLMseieEGKTeaaermkeVAD------ELRDIGADSAEPRARRILAGLGFSKEMQ 221
Cdd:COG1116 71 D-----GKPVTGPGPDRGVVFQEPALL----PWLT--------VLDnvalglELRGVPKAERRERARELLELVGLAGFED 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559834 222 EKPCTdFSGGWRMRISLARALFLEPTLLMLDEPTNHLD------LNAVIwldnyLQTW---KKTLLIVSHD 283
Cdd:COG1116 134 AYPHQ-LSGGMRQRVAIARALANDPEVLLMDEPFGALDaltrerLQDEL-----LRLWqetGKTVLFVTHD 198
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
80-298 |
1.19e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.24 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARKLAIPSHIDLlyceQEIQVDSTSAID---TV 156
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV----GDITIDTARSLSqqkGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 157 VKSDKKRLALLEEEAKL------MSEIEEGKTEaaermkeVADELRDigadSAEPRARRILAGLGFSKEMQEKPcTDFSG 230
Cdd:PRK11264 80 IRQLRQHVGFVFQNFNLfphrtvLENIIEGPVI-------VKGEPKE----EATARARELLAKVGLAGKETSYP-RRLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559834 231 GWRMRISLARALFLEPTLLMLDEPTNHLD---LNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLD 298
Cdd:PRK11264 148 GQQQRVAIARALAMRPEVILFDEPTSALDpelVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMD 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
96-291 |
1.25e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.60 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 96 DKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQVDSTSAIDTVVKSDKKRLALLEEEAKLM- 174
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAG--VLEPTSGEVNVRVGDEWVDMTKPGPDGRGRAKRYIGILHQEYDLYp 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 175 -SEIEEGKTEAAERmkEVADELrdigadsAEPRARRILAGLGFS----KEMQEKPCTDFSGGWRMRISLARALFLEPTLL 249
Cdd:TIGR03269 379 hRTVLDNLTEAIGL--ELPDEL-------ARMKAVITLKMVGFDeekaEEILDKYPDELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17559834 250 MLDEPTNHLD-LNAVIWLDNYLQTWK---KTLLIVSHDQGFLDSVC 291
Cdd:TIGR03269 450 ILDEPTGTMDpITKVDVTHSILKAREemeQTFIIVSHDMDFVLDVC 495
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
409-582 |
1.50e-12 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 68.25 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 409 DVNFGYGKDVLFKK-----LNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGelrkhrTLRIGWFDQHANEALNGE 483
Cdd:TIGR04521 5 NVSYIYQPGTPFEKkalddVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSG------TVTIDGRDITAKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 484 ----------QTP------------VEFLCTKFNIDYQEARKQ----LGTTGLAahaHTVKIK---DLSGGQKSRVALCN 534
Cdd:TIGR04521 79 dlrkkvglvfQFPehqlfeetvykdIAFGPKNLGLSEEEAEERvkeaLELVGLD---EEYLERspfELSGGQMRRVAIAG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559834 535 -LALGgPDIIILDEPTNNLDIESIDALAEAIRDFNG----GVVMVTHD--------ERLVV 582
Cdd:TIGR04521 156 vLAME-PEVLILDEPTAGLDPKGRKEILDLFKRLHKekglTVILVTHSmedvaeyaDRVIV 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
109-295 |
1.66e-12 |
|
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: 66.93 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 109 GLVGPNGMGKTTLLKHIGARKLAIPSHIDLlycEQEIQVDSTSAIDTvvKSDKKRLALLEEEAKLM------SEIEEGkt 182
Cdd:cd03297 27 GIFGASGAGKSTLLRCIAGLEKPDGGTIVL---NGTVLFDSRKKINL--PPQQRKIGLVFQQYALFphlnvrENLAFG-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 183 eaaerMKEVAD-ELRDigadsaepRARRILAGLGFSKEMQEKPCTdFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLN 261
Cdd:cd03297 100 -----LKRKRNrEDRI--------SVDELLDLLGLDHLLNRYPAQ-LSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 17559834 262 AVIWLDNYLQTWKKTL----LIVSHDQGFLDSVCTDII 295
Cdd:cd03297 166 LRLQLLPELKQIKKNLnipvIFVTHDLSEAEYLADRIV 203
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
90-292 |
1.67e-12 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 67.03 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 90 QGKLL--FDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARKLaiPSHIDLLYCEQEIQVDSTSAidtvvkSDKKRLALL 167
Cdd:TIGR02324 17 GGVRLpvLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYL--PDSGRILVRHEGAWVDLAQA------SPREVLEVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 168 EEEAKLMSEIeegkTEAAERMKE---VADELRDIGA--DSAEPRARRILAGLGFSKEMQEKPCTDFSGGWRMRISLARAL 242
Cdd:TIGR02324 89 RKTIGYVSQF----LRVIPRVSAlevVAEPLLERGVprEAARARARELLARLNIPERLWHLPPATFSGGEQQRVNIARGF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17559834 243 FLEPTLLMLDEPTNHLDLN---AVIWLDNYLQTWKKTLLIVSHDQGFLDSVCT 292
Cdd:TIGR02324 165 IADYPILLLDEPTASLDAAnrqVVVELIAEAKARGAALIGIFHDEEVRELVAD 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
413-587 |
1.73e-12 |
|
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: 67.22 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 413 GYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDG---------------ELRKHRTlRIGWFDQHAN 477
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGsvlvdgtdltllsgkELRKARR-RIGMIFQHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 478 eaLNGEQT-------PVEFLCTKFNIDYQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILDEPTN 550
Cdd:cd03258 93 --LLSSRTvfenvalPLEIAGVPKAEIEERVLELLELVGLEDKADA-YPAQLSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17559834 551 NLDIESIDALAEAIRDFNG----GVVMVTHdERLVVRTDCN 587
Cdd:cd03258 170 ALDPETTQSILALLRDINRelglTIVLITH-EMEVVKRICD 209
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
415-605 |
1.95e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.87 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 415 GKdVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIG--------KIdpNDGEL--------RKHrtlrIGWFDQH--- 475
Cdd:PRK11174 362 GK-TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslKI--NGIELreldpeswRKH----LSWVGQNpql 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 476 -----------ANEALNGEQtpVEFLCTKFNIDyqEARKQLgTTGLaahaHTVkIKD----LSGGQKSRVALCNlALGGP 540
Cdd:PRK11174 435 phgtlrdnvllGNPDASDEQ--LQQALENAWVS--EFLPLL-PQGL----DTP-IGDqaagLSVGQAQRLALAR-ALLQP 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559834 541 -DIIILDEPTNNLDIES----IDALAEAIRDFNggVVMVTHdeRLVVRTDC-NLWVVENQGIDEiDGDFED 605
Cdd:PRK11174 504 cQLLLLDEPTASLDAHSeqlvMQALNAASRRQT--TLMVTH--QLEDLAQWdQIWVMQDGQIVQ-QGDYAE 569
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
96-302 |
1.99e-12 |
|
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: 66.74 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 96 DKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIqvdstSAIDTVVKSDKKR---------LAL 166
Cdd:cd03255 21 KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG--LDRPTSGEVRVDGTDI-----SKLSEKELAAFRRrhigfvfqsFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 167 LEEeaklMSEIEEgkteaaermKEVADELRDIGADSAEPRARRILAGLGFSKEMQEKPcTDFSGGWRMRISLARALFLEP 246
Cdd:cd03255 94 LPD----LTALEN---------VELPLLLAGVPKKERRERAEELLERVGLGDRLNHYP-SELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 247 TLLMLDEPTNHLDL-NAVIWLD---NYLQTWKKTLLIVSHDQgFLDSVCTDIIHLDNQKL 302
Cdd:cd03255 160 KIILADEPTGNLDSeTGKEVMEllrELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
393-607 |
2.03e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.14 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 393 QFPETTKLNP-PVLGL---HDVNFGYGK--DV-LFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR--- 462
Cdd:TIGR00958 463 NIPLTGTLAPlNLEGLiefQDVSFSYPNrpDVpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldg 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 463 ------KHRTLrigwfdqHANEALNGeQTPVEFLCT-KFNIDYQEARK---QLGTTGLAAHAHTVKIKD----------- 521
Cdd:TIGR00958 543 vplvqyDHHYL-------HRQVALVG-QEPVLFSGSvRENIAYGLTDTpdeEIMAAAKAANAHDFIMEFpngydtevgek 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 522 ---LSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGGVVMVTH--------DERLVVRTDCnlwV 590
Cdd:TIGR00958 615 gsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHrlstveraDQILVLKKGS---V 691
|
250
....*....|....*..
gi 17559834 591 VENQGIDEIDGDFEDYK 607
Cdd:TIGR00958 692 VEMGTHKQLMEDQGCYK 708
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
96-299 |
2.14e-12 |
|
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: 67.08 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 96 DKASLTIVYGRRYGLVGPNGMGKTTLLKHI-GARKlaiPSHIDLLYCEQEI-----------------QV----DSTSAI 153
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsGFLR---PTSGSVLFDGEDItglppheiarlgigrtfQIprlfPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 154 DTVvksdkkRLALLEEEAKLMSEIEEGKTEAAERmkevadelrdigadsaePRARRILAGLGFSKEMQEkPCTDFSGGWR 233
Cdd:cd03219 94 ENV------MVAAQARTGSGLLLARARREEREAR-----------------ERAEELLERVGLADLADR-PAGELSYGQQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17559834 234 MRISLARALFLEPTLLMLDEPT---NHLDLNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDN 299
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQ 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
433-582 |
2.33e-12 |
|
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: 69.81 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIGKIDPNDGELRKhrTLRIGWFDQHANEALNGeqtPVEFLCTKFNID-------YQEARKQL 505
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEVDE--DLKISYKPQYISPDYDG---TVEEFLRSANTDdfgssyyKTEIIKPL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 506 GTTGLaahaHTVKIKDLSGG--QKSRVALCnLALGGpDIIILDEPTNNLDIESIDALAEAIRDF---NGGVVMVT-HD-- 577
Cdd:COG1245 444 GLEKL----LDKNVKDLSGGelQRVAIAAC-LSRDA-DLYLLDEPSAHLDVEQRLAVAKAIRRFaenRGKTAMVVdHDiy 517
|
170
....*....|.
gi 17559834 578 ------ERLVV 582
Cdd:COG1245 518 lidyisDRLMV 528
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
80-303 |
2.34e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 66.61 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDIS-AQGKLLFDKASLTI-----VYgrrygLVGPNGMGKTTLLKhigarklaipshidLLYCEQ-----EIQVD 148
Cdd:COG2884 2 IRFENVSKRyPGGREALSDVSLEIekgefVF-----LTGPSGAGKSTLLK--------------LLYGEErptsgQVLVN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 149 STSaidtVVKSDKKRLALLE-------EEAKLMSEieegKTeAAErmkEVADELRDIGADSAE--PRARRILAGLGFSKE 219
Cdd:COG2884 63 GQD----LSRLKRREIPYLRrrigvvfQDFRLLPD----RT-VYE---NVALPLRVTGKSRKEirRRVREVLDLVGLSDK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 220 MQEKPCTdFSGGWRMRISLARALFLEPTLLMLDEPTNHLD-------------LNAViwldnylqtwKKTLLIVSHDQGF 286
Cdd:COG2884 131 AKALPHE-LSGGEQQRVAIARALVNRPELLLADEPTGNLDpetsweimelleeINRR----------GTTVLIATHDLEL 199
|
250
....*....|....*..
gi 17559834 287 LDSVCTDIIHLDNQKLH 303
Cdd:COG2884 200 VDRMPKRVLELEDGRLV 216
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
405-577 |
2.48e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 66.70 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 405 LGLHDVNFGYGKDVLfkKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELrkhrtlrigWFDQHANEALNGEQ 484
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRI---------LWNGQDLTALPPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 485 TPVEFLctkF-------------NI-------------DYQEARKQLGTTGLAAHAhTVKIKDLSGGQKSRVALCNLALG 538
Cdd:COG3840 71 RPVSML---FqennlfphltvaqNIglglrpglkltaeQRAQVEQALERVGLAGLL-DRLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17559834 539 GPDIIILDEPTNNLDI----ESIDALAEAIRDFNGGVVMVTHD 577
Cdd:COG3840 147 KRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMVTHD 189
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
96-290 |
2.92e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.80 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 96 DKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPShidllyceqeiqvdsTSAIDTVVKSDKKRLALLEEEaKLMS 175
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNA--LLLPD---------------TGTIEWIFKDEKNKKKTKEKE-KVLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 176 EIEEGKTEAaERMKEVADELRDIGA-----------------------------DSAEPRARRILAGLGFSKEMQEKPCT 226
Cdd:PRK13651 86 KLVIQKTRF-KKIKKIKEIRRRVGVvfqfaeyqlfeqtiekdiifgpvsmgvskEEAKKRAAKYIELVGLDESYLQRSPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17559834 227 DFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWK---KTLLIVSHDqgfLDSV 290
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNkqgKTIILVTHD---LDNV 228
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
99-283 |
3.38e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 65.72 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLKHI-GARK-----LAIPSHIDLLYCEQEIQVDST---SAIDTVVKSDKKRLALLee 169
Cdd:NF040873 12 DLTIPAGSLTAVVGPNGSGKSTLLKVLaGVLRptsgtVRRAGGARVAYVPQRSEVPDSlplTVRDLVAMGRWARRGLW-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 170 eaklmseieeGKTEAAERMkEVADELRDIGADSAEPRARRILaglgfskemqekpctdfSGGWRMRISLARALFLEPTLL 249
Cdd:NF040873 90 ----------RRLTRDDRA-AVDDALERVGLADLAGRQLGEL-----------------SGGQRQRALLAQGLAQEADLL 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 17559834 250 MLDEPTNHLDLNAVIWLDNYLQTW---KKTLLIVSHD 283
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEharGATVVVVTHD 178
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
386-581 |
3.48e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.14 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 386 KEYSVKFQFPETTKLNPPVLGLHDvNFGYGKDV----LFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGEl 461
Cdd:COG2401 9 VLMRVTKVYSSVLDLSERVAIVLE-AFGVELRVveryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 462 rkhrtlriGWFDQHANEaLNGEQTPVEFLCTKFNIDyqEARKQLGTTGLA-AHAHTVKIKDLSGGQKSRVALCNLALGGP 540
Cdd:COG2401 87 --------GCVDVPDNQ-FGREASLIDAIGRKGDFK--DAVELLNAVGLSdAVLWLRRFKELSTGQKFRFRLALLLAERP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17559834 541 DIIILDEPTNNLDIESIDALA----EAIRDFNGGVVMVTHDERLV 581
Cdd:COG2401 156 KLLVIDEFCSHLDRQTAKRVArnlqKLARRAGITLVVATHHYDVI 200
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
426-581 |
4.18e-12 |
|
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: 66.60 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 426 GVDMD----SRIAIVGPNGVGKSTLLKLLIGKIDPNDGE----------LRKHRTLRIGW---FdQHANeaLNGEQTPVE 488
Cdd:COG0411 22 DVSLEvergEIVGLIGPNGAGKTTLFNLITGFYRPTSGRilfdgrditgLPPHRIARLGIartF-QNPR--LFPELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 489 -------------FLCTKFNID---------YQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRV----ALCnlalGGPDI 542
Cdd:COG0411 99 nvlvaaharlgrgLLAALLRLPrarreereaRERAEELLERVGLADRADE-PAGNLSYGQQRRLeiarALA----TEPKL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17559834 543 IILDEPTNNLDIESIDALAEAIRDFNGG----VVMVTHDERLV 581
Cdd:COG0411 174 LLLDEPAAGLNPEETEELAELIRRLRDErgitILLIEHDMDLV 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
398-585 |
4.95e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.55 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 398 TKLNPPVLGLHDVNFGYGKDVLF--KKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELrkhrtlrigwfdQH 475
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSENNalKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEI------------KI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 476 ANEALNGEQtpVEFLCTKFNIDYQEARKQ-LGTT-------GL--------------AAHAHTVKIKD--------LSGG 525
Cdd:PRK13632 69 DGITISKEN--LKEIRKKIGIIFQNPDNQfIGATveddiafGLenkkvppkkmkdiiDDLAKKVGMEDyldkepqnLSGG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 526 QKSRVALCN-LALgGPDIIILDEPTNNLDIESIDALAEAIRDF----NGGVVMVTHDERLVVRTD 585
Cdd:PRK13632 147 QKQRVAIASvLAL-NPEIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITHDMDEAILAD 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
105-582 |
5.17e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.68 E-value: 5.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 105 GRRYGLVGPNGMGKTTLLKhIGARKLaIPShidllYCEqeiqVDSTSAIDTVVK---------------SDKKRLALLEE 169
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVK-ILSGEL-IPN-----LGD----YEEEPSWDEVLKrfrgtelqnyfkklyNGEIKVVHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 170 EAKLMSEIEEGKT-EAAERMKE--VADELRDIgadsaeprarrilagLGFSKEMqEKPCTDFSGGWRMRISLARALFLEP 246
Cdd:PRK13409 168 YVDLIPKVFKGKVrELLKKVDErgKLDEVVER---------------LGLENIL-DRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 247 TLLMLDEPTNHLD----LNAVIWLDNYLQtwKKTLLIVSHDQGFLDSVcTDIIHLdnqklhTY--RGNYTLFKKQYAQDM 320
Cdd:PRK13409 232 DFYFFDEPTSYLDirqrLNVARLIRELAE--GKYVLVVEHDLAVLDYL-ADNVHI------AYgePGAYGVVSKPKGVRV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 321 QVHE--KNFdqqqkqLKamkkegksakqaEEQVkqqmankakkggkknagkvnddddagapellqRRKEYSVKF-QFPET 397
Cdd:PRK13409 303 GINEylKGY------LP------------EENM--------------------------------RIRPEPIEFeERPPR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 398 TKLNPPVLglhdvnFGYGKdvLFKKL-NFGVDMDSR-------IAIVGPNGVGKSTLLKLLIGKIDPNDGELRKhrTLRI 469
Cdd:PRK13409 333 DESERETL------VEYPD--LTKKLgDFSLEVEGGeiyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--ELKI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 470 GWFDQHANEALNGeqtPVEFLCTKFNIDY------QEARKQLGTTGLaahaHTVKIKDLSGGQKSRVALCnLALGGP-DI 542
Cdd:PRK13409 403 SYKPQYIKPDYDG---TVEDLLRSITDDLgssyykSEIIKPLQLERL----LDKNVKDLSGGELQRVAIA-ACLSRDaDL 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 17559834 543 IILDEPTNNLDIESIDALAEAIRDF---NGGVVMVT-HD--------ERLVV 582
Cdd:PRK13409 475 YLLDEPSAHLDVEQRLAVAKAIRRIaeeREATALVVdHDiymidyisDRLMV 526
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
415-577 |
5.25e-12 |
|
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: 65.82 E-value: 5.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 415 GKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrigwFDQHANEALNGEQTPVEFLCTKF 494
Cdd:cd03299 10 WKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIL---------LNGKDITNLPPEKRDISYVPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 495 ----------NIDY----------QEARKQLGTTGLAAHAHTV--KIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNL 552
Cdd:cd03299 81 alfphmtvykNIAYglkkrkvdkkEIERKVLEIAEMLGIDHLLnrKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180
....*....|....*....|....*....
gi 17559834 553 DIES----IDALAEAIRDFNGGVVMVTHD 577
Cdd:cd03299 161 DVRTkeklREELKKIRKEFGVTVLHVTHD 189
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
434-577 |
5.34e-12 |
|
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: 67.39 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 434 AIVGPNGVGKSTLLKLLIGKIDPN---------DG---------ELRKHRTLRIGW-FdQHANEALN-----GEQTpVEF 489
Cdd:COG0444 35 GLVGESGSGKSTLARAILGLLPPPgitsgeilfDGedllklsekELRKIRGREIQMiF-QDPMTSLNpvmtvGDQI-AEP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 490 LCTKFNIDYQEARKQ----LGTTGLAAHAhtvKIKD-----LSGGQKSRVALCnLAL-GGPDIIILDEPTNNLDIeSIDA 559
Cdd:COG0444 113 LRIHGGLSKAEARERaielLERVGLPDPE---RRLDrypheLSGGMRQRVMIA-RALaLEPKLLIADEPTTALDV-TIQA 187
|
170 180
....*....|....*....|...
gi 17559834 560 -----LAEAIRDFNGGVVMVTHD 577
Cdd:COG0444 188 qilnlLKDLQRELGLAILFITHD 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
405-583 |
5.40e-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: 65.38 E-value: 5.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 405 LGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR--------KHRTlRIGWFDQha 476
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldiAARN-RIGYLPE-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 477 NEALNGEQTPVE---FLCTKFNIDYQEARKQ----LGTTGLAAHAHtVKIKDLSGGQKSRVALCNLALGGPDIIILDEPT 549
Cdd:cd03269 78 ERGLYPKMKVIDqlvYLAQLKGLKKEEARRRidewLERLELSEYAN-KRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 17559834 550 NNLDIESIDALAEAIRDFNGG---VVMVTHDERLVVR 583
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAgktVILSTHQMELVEE 193
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
80-302 |
6.25e-12 |
|
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: 65.77 E-value: 6.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQVDSTSAIDTVvks 159
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG--LLRPDSGEILVDGQDITGLSEKELYEL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 dKKRLALLEEEAKL---MSeIEEgkteaaermkEVA---DELRDIGADSAEPRARRILA--GLgfsKEMQEKPCTDFSGG 231
Cdd:COG1127 81 -RRRIGMLFQGGALfdsLT-VFE----------NVAfplREHTDLSEAEIRELVLEKLElvGL---PGAADKMPSELSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 232 WRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTL----LIVSHDQGFLDSVCTDIIHLDNQKL 302
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELgltsVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
417-580 |
6.34e-12 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 64.10 E-value: 6.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 417 DVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLigkidpndGELRKHRTLRIGwfdqhanealngeqtpvefLCTKFNI 496
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL--------AGLWPWGSGRIG-------------------MPEGEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 497 DY--QEARKQLGTtglaahahtvkIKD---------LSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIR 565
Cdd:cd03223 67 LFlpQRPYLPLGT-----------LREqliypwddvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK 135
|
170
....*....|....*
gi 17559834 566 DFNGGVVMVTHDERL 580
Cdd:cd03223 136 ELGITVISVGHRPSL 150
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
96-298 |
9.03e-12 |
|
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: 65.43 E-value: 9.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 96 DKASLTIVYGRRYGLVGPNGMGKTTLLKHI------------------GARKLAIPSHIDLLYCEQEIQVDSTSAIDTvv 157
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILsgllqptsgevrvaglvpWKRRKKFLRRIGVVFGQKTQLWWDLPVIDS-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 158 ksdkkrLALLEEeaklMSEIEEGktEAAERMKEVADELrDIGadsaeprarRILaglgfskemqEKPCTDFSGGWRMRIS 237
Cdd:cd03267 116 ------FYLLAA----IYDLPPA--RFKKRLDELSELL-DLE---------ELL----------DTPVRQLSLGQRMRAE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 238 LARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKK----TLLIVSHDQGFLDSVCTDIIHLD 298
Cdd:cd03267 164 IAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRergtTVLLTSHYMKDIEALARRVLVID 228
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
380-581 |
1.01e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.93 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 380 ELLQRRKEysVKFQFPETTKLNPPVLGLHDVNFGY--GKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPN 457
Cdd:PRK11160 316 EITEQKPE--VTFPTTSTAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 458 DGE---------------LRKHRTL---RIGWFDQHANEALngeqtpvefLCTKFNIDYQEARKQLGTTGLAAHAHTVKI 519
Cdd:PRK11160 394 QGEillngqpiadyseaaLRQAISVvsqRVHLFSATLRDNL---------LLAAPNASDEALIEVLQQVGLEKLLEDDKG 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 520 KD---------LSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGG--VVMVTHdeRLV 581
Cdd:PRK11160 465 LNawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNktVLMITH--RLT 535
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
414-577 |
1.05e-11 |
|
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: 64.70 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 414 YGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGE--------LRKHRTLR--IGWF--DQHANEALN 481
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvVREPREVRrrIGIVfqDLSVDDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 482 GEQTpVEFLCTKFNIDYQEARKQ----LGTTGLAAHAHTVkIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESI 557
Cdd:cd03265 90 GWEN-LYIHARLYGVPGAERRERidelLDFVGLLEAADRL-VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180
....*....|....*....|....
gi 17559834 558 DALAEAIR----DFNGGVVMVTHD 577
Cdd:cd03265 168 AHVWEYIEklkeEFGMTILLTTHY 191
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
73-254 |
1.15e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.56 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 73 QMENSMDIKIENFdiSAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARKLaiPSHIDLLYCEQEIQVDSTSA 152
Cdd:PRK11831 3 SVANLVDMRGVSF--TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIA--PDHGEILFDGENIPAMSRSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 153 IDTVvksdKKRLALLEEEAKLMSEIEEgkteaaerMKEVADELRDiGADSAEPRARRI----LAGLGFSKEMQEKPcTDF 228
Cdd:PRK11831 79 LYTV----RKRMSMLFQSGALFTDMNV--------FDNVAYPLRE-HTQLPAPLLHSTvmmkLEAVGLRGAAKLMP-SEL 144
|
170 180
....*....|....*....|....*.
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEP 254
Cdd:PRK11831 145 SGGMARRAALARAIALEPDLIMFDEP 170
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
405-574 |
1.25e-11 |
|
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: 64.38 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 405 LGLHDVNFGYGK-DVLFKkLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGE----------LRKHRTLR--IGW 471
Cdd:cd03224 1 LEVENLNAGYGKsQILFG-VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSirfdgrditgLPPHERARagIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 472 FDQHAN--------EAL---------NGEQTPVEFLCTKFNIdYQEARKQLGTTglaahahtvkikdLSGGQKSRVALCN 534
Cdd:cd03224 80 VPEGRRifpeltveENLllgayarrrAKRKARLERVYELFPR-LKERRKQLAGT-------------LSGGEQQMLAIAR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17559834 535 LALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGG---VVMV 574
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgvtILLV 188
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
387-554 |
1.46e-11 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 67.46 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 387 EYSVKFQFPETTKLNPPVLGLH-DVNFGYGKDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGE----- 460
Cdd:TIGR01193 457 EFINKKKRTELNNLNGDIVINDvSYSYGYGSNIL-SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEillng 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 461 -----LRKHrTLR--IGWFDQH---------------ANEalNGEQTPVEFLCTKFNIDYQEARKQLG-TTGLAAHAHTv 517
Cdd:TIGR01193 536 fslkdIDRH-TLRqfINYLPQEpyifsgsilenlllgAKE--NVSQDEIWAACEIAEIKDDIENMPLGyQTELSEEGSS- 611
|
170 180 190
....*....|....*....|....*....|....*..
gi 17559834 518 kikdLSGGQKSRVALCNLALGGPDIIILDEPTNNLDI 554
Cdd:TIGR01193 612 ----ISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
80-283 |
1.54e-11 |
|
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: 64.42 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIEN----FDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPShidllycEQEIQVDstsaiDT 155
Cdd:cd03293 1 LEVRNvsktYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAG--LERPT-------SGEVLVD-----GE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 156 VVKSDKKRLALLEEEAKLMseieEGKTeaaermkeVAD------ELRDIGADSAEPRARRILAGLGFSKEMQEKPcTDFS 229
Cdd:cd03293 67 PVTGPGPDRGYVFQQDALL----PWLT--------VLDnvalglELQGVPKAEARERAEELLELVGLSGFENAYP-HQLS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 230 GGWRMRISLARALFLEPTLLMLDEPTNHLDlnAVI------WLDNYLQTWKKTLLIVSHD 283
Cdd:cd03293 134 GGMRQRVALARALAVDPDVLLLDEPFSALD--ALTreqlqeELLDIWRETGKTVLLVTHD 191
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
416-593 |
1.56e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.21 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 416 KDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGE------------LRKHRTLrIGWFDQHANEAL--- 480
Cdd:PRK13652 17 KEAL-NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSvlirgepitkenIREVRKF-VGLVFQNPDDQIfsp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 481 NGEQTpVEFLCTKFNIDyQEARKQLGTTGLaahaHTVKIKD--------LSGGQKSRVALCNLALGGPDIIILDEPTNNL 552
Cdd:PRK13652 95 TVEQD-IAFGPINLGLD-EETVAHRVSSAL----HMLGLEElrdrvphhLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17559834 553 DIESIDALAEAIRDF----NGGVVMVTHDERLVVRTDCNLWVVEN 593
Cdd:PRK13652 169 DPQGVKELIDFLNDLpetyGMTVIFSTHQLDLVPEMADYIYVMDK 213
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
415-580 |
1.65e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 64.70 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 415 GKDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKID--PNDGELRkhrtlrigwfdqhaneaLNGE--------- 483
Cdd:COG0396 12 GKEIL-KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSIL-----------------LDGEdilelspde 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 484 ----------QTPVE--------FLCTKFN------IDYQEARKQLGttglaAHAHTVKIKD----------LSGGQKSR 529
Cdd:COG0396 74 raragiflafQYPVEipgvsvsnFLRTALNarrgeeLSAREFLKLLK-----EKMKELGLDEdfldryvnegFSGGEKKR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17559834 530 VALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDF---NGGVVMVTHDERL 580
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLrspDRGILIITHYQRI 202
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
404-585 |
1.75e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.82 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 404 VLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGElrkhrtlrIGWFDQHANEALNGE 483
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGE--------ILFERQSIKKDLCTY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 484 QTPVEFLCTKFNI------------DYQEARKQLGTTGLA-----AHAHTVKIKDLSGGQKSRVALCNLALGGPDIIILD 546
Cdd:PRK13540 73 QKQLCFVGHRSGInpyltlrenclyDIHFSPGAVGITELCrlfslEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17559834 547 EPTNNLD---IESIDALAEAIRDFNGGVVMVTHDERLVVRTD 585
Cdd:PRK13540 153 EPLVALDelsLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
405-577 |
1.82e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 64.65 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 405 LGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKH---------RTL--RIGWFD 473
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGdkpismlssRQLarRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 474 QH--ANEALNGEQTpVEF-----------LCTKFNIDYQEARKQLGTTGLAAHahtvKIKDLSGGQKSRVALCNLALGGP 540
Cdd:PRK11231 83 QHhlTPEGITVREL-VAYgrspwlslwgrLSAEDNARVNQAMEQTRINHLADR----RLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17559834 541 DIIILDEPTNNLDIESIDALAEAIRDFNGG---VVMVTHD 577
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQgktVVTVLHD 197
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
80-282 |
2.11e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 65.21 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQVDSTSAidtvvks 159
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLG--LTHPDAGSISLCGEPVPSRARHA------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 dKKRLALLEEEAKLMSEIEegkteaaermkeVADEL----RDIGADSAEPRARrILAGLGFSKEMQ--EKPCTDFSGGWR 233
Cdd:PRK13537 79 -RQRVGVVPQFDNLDPDFT------------VRENLlvfgRYFGLSAAAARAL-VPPLLEFAKLENkaDAKVGELSGGMK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17559834 234 MRISLARALFLEPTLLMLDEPTNHLDLNA--VIW--LDNYLQTwKKTLLIVSH 282
Cdd:PRK13537 145 RRLTLARALVNDPDVLVLDEPTTGLDPQArhLMWerLRSLLAR-GKTILLTTH 196
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
407-582 |
2.17e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 65.55 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKH----------RTLRIGWFDQHA 476
Cdd:COG1118 5 VRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNgrdlftnlppRERRVGFVFQHY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 477 neAL--------NgeqtpVEFLCTKFNIDYQEARK----QLGTTGLAAHAHtVKIKDLSGGQKSRVALCN-LALgGPDII 543
Cdd:COG1118 85 --ALfphmtvaeN-----IAFGLRVRPPSKAEIRArveeLLELVQLEGLAD-RYPSQLSGGQRQRVALARaLAV-EPEVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 544 ILDEPTNNLDIesidALAEAIR--------DFNGGVVMVTHD--------ERLVV 582
Cdd:COG1118 156 LLDEPFGALDA----KVRKELRrwlrrlhdELGGTTVFVTHDqeealelaDRVVV 206
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
407-602 |
2.31e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 64.34 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLK------------LLIGKIDPNDGElRKHRTLRI--GWF 472
Cdd:PRK09493 4 FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdLIVDGLKVNDPK-VDERLIRQeaGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 473 DQHANeaLNGEQTPVEflctkfNIDY----------QEARKQ----LGTTGLAAHAHTVKiKDLSGGQKSRVALCN-LAL 537
Cdd:PRK09493 83 FQQFY--LFPHLTALE------NVMFgplrvrgaskEEAEKQarelLAKVGLAERAHHYP-SELSGGQQQRVAIARaLAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17559834 538 gGPDIIILDEPTNNLDIESIDALAEAIRDF-NGGVVM--VTHDERLVVRTDCNLWVVENQGIDEiDGD 602
Cdd:PRK09493 154 -KPKLMLFDEPTSALDPELRHEVLKVMQDLaEEGMTMviVTHEIGFAEKVASRLIFIDKGRIAE-DGD 219
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
80-282 |
2.33e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.14 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQ------GKLLFDkASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPShidllycEQEIQVDSTSAI 153
Cdd:PRK13643 2 IKFEKVNYTYQpnspfaSRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNG--LLQPT-------EGKVTVGDIVVS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 154 DTvvkSDKKRLALLEEEAKLMSEIEEGKTEAAERMKEVADELRDIG--ADSAEPRARRILAGLGFSKEMQEKPCTDFSGG 231
Cdd:PRK13643 72 ST---SKQKEIKPVRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGipKEKAEKIAAEKLEMVGLADEFWEKSPFELSGG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17559834 232 WRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWK---KTLLIVSH 282
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHqsgQTVVLVTH 202
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
295-353 |
2.50e-11 |
|
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: 59.89 E-value: 2.50e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 295 IHLDNQKLHTYRGNYTLFKKQYAQDMQVHEKNFDQQQKQLKAM-------KKEGKSAKQAEEQVKQ 353
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLeefidrfRAKASKAKQAQSRIKA 66
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
96-302 |
2.79e-11 |
|
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: 63.54 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 96 DKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArklaipshidLLyceqeiQVDSTSAI----DTVVKSDK--KRLALLEE 169
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTT----------LL------KPTSGRATvaghDVVREPREvrRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 170 EAKLmseieEGKTEAAERMkEVADELRDIGADSAEPRARRILAGLGFSkEMQEKPCTDFSGGWRMRISLARALFLEPTLL 249
Cdd:cd03265 81 DLSV-----DDELTGWENL-YIHARLYGVPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17559834 250 MLDEPTNHLDLNAVIWLDNYLQTWKK----TLLIVSHDQGFLDSVCTDIIHLDNQKL 302
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEefgmTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
433-583 |
3.46e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.94 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIGKIDPNDGELR------------KHRTLR--IGWFDQHANEALNGEQT-------PVEFLc 491
Cdd:PRK10419 41 VALLGRSGCGKSTLARLLVGLESPSQGNVSwrgeplaklnraQRKAFRrdIQMVFQDSISAVNPRKTvreiirePLRHL- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 492 TKFNIDYQEARKQ--LGTTGLAAHAHTVKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDI----ESIDALAEAIR 565
Cdd:PRK10419 120 LSLDKAERLARASemLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQ 199
|
170
....*....|....*...
gi 17559834 566 DFNGGVVMVTHDERLVVR 583
Cdd:PRK10419 200 QFGTACLFITHDLRLVER 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
404-576 |
3.94e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 64.37 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 404 VLGLHDVNFGYGKDVLF-KKLNFGVDMD----SRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR----------KHRTLR 468
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFaSRALFDIDLEvkkgSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdivvsstsKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 469 -----IGWFDQHANEALNGEQT--PVEFLCTKFNIDYQEARK----QLGTTGLAAHAHTVKIKDLSGGQKSRVALCNLAL 537
Cdd:PRK13643 81 pvrkkVGVVFQFPESQLFEETVlkDVAFGPQNFGIPKEKAEKiaaeKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17559834 538 GGPDIIILDEPTNNLDIES---IDALAEAIRDFNGGVVMVTH 576
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH 202
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
80-297 |
4.12e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 62.54 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKhigarklAIPSHIDLLYCEQEIQVDSTSAIDTVVks 159
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAK-------TIMGHPKYEVTEGEILFKGEDITDLPP-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 dkkrlallEEEAKL---MS-----EIEEGKteaaermkeVADELRDIGADsaeprarrilaglgfskemqekpctdFSGG 231
Cdd:cd03217 72 --------EERARLgifLAfqyppEIPGVK---------NADFLRYVNEG--------------------------FSGG 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17559834 232 WRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTW---KKTLLIVSHDQGFLDSVCTDIIHL 297
Cdd:cd03217 109 EKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreeGKSVLIITHYQRLLDYIKPDRVHV 177
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
421-565 |
4.18e-11 |
|
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: 63.16 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 421 KKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGelrkhrTLRIGWFDQHAN--EALNGeqtpVEFLCTKFNI-D 497
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAG------FATVDGFDVVKEpaEARRR----LGFVSDSTGLyD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 498 YQEARKQL----GTTGLAAHAHTVKIKDL-----------------SGGQKSRVALCNLALGGPDIIILDEPTNNLDIES 556
Cdd:cd03266 92 RLTARENLeyfaGLYGLKGDELTARLEELadrlgmeelldrrvggfSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
....*....
gi 17559834 557 IDALAEAIR 565
Cdd:cd03266 172 TRALREFIR 180
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
414-578 |
4.60e-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: 63.02 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 414 YGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKH--RTLRIGWFDQHANE-----ALNGEQT- 485
Cdd:cd03300 10 YGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgkDITNLPPHKRPVNTvfqnyALFPHLTv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 486 ------PVEFLCTKFNIDYQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDA 559
Cdd:cd03300 90 feniafGLRLKKLPKAEIKERVAEALDLVQLEGYANR-KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKD 168
|
170 180
....*....|....*....|...
gi 17559834 560 LAEAIRDFNGGV----VMVTHDE 578
Cdd:cd03300 169 MQLELKRLQKELgitfVFVTHDQ 191
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
403-577 |
4.62e-11 |
|
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: 63.82 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 403 PVLGLHDVNFgygkDVlfkklnfgvdMDSRI-AIVGPNGVGKSTLLKLLIGKIDP---------------NDGELRKHRT 466
Cdd:cd03294 36 QTVGVNDVSL----DV----------REGEIfVIMGLSGSGKSTLLRCINRLIEPtsgkvlidgqdiaamSRKELRELRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 467 LRIGWFDQH----------ANEALngeqtPVEFLCTKFNIDYQEARKQLGTTGLAAHAHtVKIKDLSGGQKSRVALCNLA 536
Cdd:cd03294 102 KKISMVFQSfallphrtvlENVAF-----GLEVQGVPRAEREERAAEALELVGLEGWEH-KYPDELSGGMQQRVGLARAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17559834 537 LGGPDIIILDEPTNNLD----IESIDALAEAIRDFNGGVVMVTHD 577
Cdd:cd03294 176 AVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHD 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
426-577 |
5.41e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.23 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 426 GVDMDSR----IAIVGPNGVGKSTLLKLLIGKIDPNDGelrkhrTLRIGWFDQHANEALNGEQT-------PVEFLCTKF 494
Cdd:PRK11264 21 GIDLEVKpgevVAIIGPSGSGKTTLLRCINLLEQPEAG------TIRVGDITIDTARSLSQQKGlirqlrqHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 495 NI------------------------DYQEARKQLGTTGLAAHAHTVKiKDLSGGQKSRVALCNLALGGPDIIILDEPTN 550
Cdd:PRK11264 95 NLfphrtvleniiegpvivkgepkeeATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190
....*....|....*....|....*....|....
gi 17559834 551 NLDIE-------SIDALAEAIRDfnggVVMVTHD 577
Cdd:PRK11264 174 ALDPElvgevlnTIRQLAQEKRT----MVIVTHE 203
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
96-299 |
5.60e-11 |
|
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: 63.13 E-value: 5.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 96 DKASLTIVYGRRYGLVGPNGMGKTTLLKHI-GARKlaiPSHIDLLYCEQEI-----------------QV----DSTSAI 153
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLItGFYR---PTSGRILFDGRDItglpphriarlgiartfQNprlfPELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 154 DTVvksdkkRLALLeeeaklmSEIEEGKTEAAERMKEVADELRDIGAdsaepRARRILAGLGFSkEMQEKPCTDFSGGWR 233
Cdd:COG0411 98 ENV------LVAAH-------ARLGRGLLAALLRLPRARREEREARE-----RAEELLERVGLA-DRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 234 MRISLARALFLEPTLLMLDEPT---NHLDLNAVI-WLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDN 299
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAaglNPEETEELAeLIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
78-259 |
5.70e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 63.61 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 78 MDIKIENFDISAQ------GKLLFDkASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPShidllycEQEIQVDSTS 151
Cdd:PRK13649 1 MGINLQNVSYTYQagtpfeGRALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNG--LHVPT-------QGSVRVDDTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 152 AIDTVVKSDKKRLallEEEAKLMSEIEEGKTEAAERMKEVADELRDIGA--DSAEPRARRILAGLGFSKEMQEKPCTDFS 229
Cdd:PRK13649 71 ITSTSKNKDIKQI---RKKVGLVFQFPESQLFEETVLKDVAFGPQNFGVsqEEAEALAREKLALVGISESLFEKNPFELS 147
|
170 180 190
....*....|....*....|....*....|
gi 17559834 230 GGWRMRISLARALFLEPTLLMLDEPTNHLD 259
Cdd:PRK13649 148 GGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
407-577 |
5.97e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.11 E-value: 5.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKD-VLFKkLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGEL---------------RKHRTLR-- 468
Cdd:PRK11124 5 LNGINCFYGAHqALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdfsktpsdKAIRELRrn 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 469 IGWFDQHAN--EALNGEQTPVEFLCTKFNIDYQEARKQ----LGTTGLAAHAHTVKIKdLSGGQKSRVALCNLALGGPDI 542
Cdd:PRK11124 84 VGMVFQQYNlwPHLTVQQNLIEAPCRVLGLSKDQALARaeklLERLRLKPYADRFPLH-LSGGQQQRVAIARALMMEPQV 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 17559834 543 IILDEPTNNLDIESIDALAEAIRDFNG-GV--VMVTHD 577
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAEtGItqVIVTHE 200
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
90-283 |
6.01e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.91 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 90 QGKLLFD---KASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQVDSTSAidtvvKSD--KKRL 164
Cdd:PRK11629 17 EGSVQTDvlhNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGG--LDTPTSGDVIFNGQPMSKLSSAA-----KAElrNQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 165 ALLEEEAKLMSEIEEgkteaaerMKEVADELRdIGA---DSAEPRARRILAGLGFSKEMQEKPcTDFSGGWRMRISLARA 241
Cdd:PRK11629 90 GFIYQFHHLLPDFTA--------LENVAMPLL-IGKkkpAEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17559834 242 LFLEPTLLMLDEPTNHLDL---NAVIWLDNYLQTWKKT-LLIVSHD 283
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGTaFLVVTHD 205
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
418-580 |
6.93e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.21 E-value: 6.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 418 VLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLL-------IGKID-PNDGEL----RK----HRTLRigwfDQ----HAN 477
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygSGRIArPAGARVlflpQRpylpLGTLR----EAllypATA 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 478 EALNGEQtpveflctkfnidYQEARKQLGTTGLAAHAHTVKIKD--LSGGQKSRVALCNLALGGPDIIILDEPTNNLDIE 555
Cdd:COG4178 453 EAFSDAE-------------LREALEAVGLGHLAERLDEEADWDqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180
....*....|....*....|....*..
gi 17559834 556 SIDALAEAIRD--FNGGVVMVTHDERL 580
Cdd:COG4178 520 NEAALYQLLREelPGTTVISVGHRSTL 546
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
74-297 |
7.46e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 62.42 E-value: 7.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 74 MENSMDIKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQVDSTSAI 153
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVAS--LISPTSGTLLFEGEDISTLKPEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 154 DTVVKSDKKRLALLeeeaklmseieeGKTeaaermkeVADELR---DIGADSAEPRA-RRILAGLGFSKEMQEKPCTDFS 229
Cdd:PRK10247 80 RQQVSYCAQTPTLF------------GDT--------VYDNLIfpwQIRNQQPDPAIfLDDLERFALPDTILTKNIAELS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 230 GGWRMRISLARALFLEPTLLMLDEPTNHLD------LNAVIwlDNYLQTWKKTLLIVSHDQgflDSV--CTDIIHL 297
Cdd:PRK10247 140 GGEKQRISLIRNLQFMPKVLLLDEITSALDesnkhnVNEII--HRYVREQNIAVLWVTHDK---DEInhADKVITL 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
80-298 |
8.15e-11 |
|
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: 62.16 E-value: 8.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPShidllycEQEIQVDstsaiDTVVKS 159
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINL--LEEPD-------SGTIIID-----GLKLTD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 DKKRLALLEEEAKL----------MSeIEEGKTEAAERMKEVADelrdigaDSAEPRARRILAGLGFSKEMQEKPCTdFS 229
Cdd:cd03262 67 DKKNINELRQKVGMvfqqfnlfphLT-VLENITLAPIKVKGMSK-------AEAEERALELLEKVGLADKADAYPAQ-LS 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559834 230 GGWRMRISLARALFLEPTLLMLDEPTNHLD---LNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLD 298
Cdd:cd03262 138 GGQQQRVAIARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMD 209
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
405-596 |
8.53e-11 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 61.80 E-value: 8.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 405 LGLHDVNFGYgkDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELrkhrtlrigWFDQHANEALNGEQ 484
Cdd:TIGR01277 1 LALDKVRYEY--EHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSI---------KVNDQSHTGLAPYQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 485 TPVEFLCTKFNI-DYQEARKQLG-------------TTGLAAHAHTVKIKD--------LSGGQKSRVALCNLALGGPDI 542
Cdd:TIGR01277 70 RPVSMLFQENNLfAHLTVRQNIGlglhpglklnaeqQEKVVDAAQQVGIADyldrlpeqLSGGQRQRVALARCLVRPNPI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17559834 543 IILDEPTNNLD----IESIDALAEAIRDFNGGVVMVTHDERLVVRTDCNLWVVENQGI 596
Cdd:TIGR01277 150 LLLDEPFSALDpllrEEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
420-613 |
9.88e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.41 E-value: 9.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 420 FKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhRTLRIGW-------FDQHaneaLNGEQTpVEFLCT 492
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE--VNGRVSAllelgagFHPE----LTGREN-IYLNGR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 493 KFNIDYQEARKQLGT----TGLAAHAHTvKIKDLSGGQKSRVAL-CNLALgGPDIIILDEptnnldiesidALA------ 561
Cdd:COG1134 115 LLGLSRKEIDEKFDEivefAELGDFIDQ-PVKTYSSGMRARLAFaVATAV-DPDILLVDE-----------VLAvgdaaf 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559834 562 -----EAIRDF---NGGVVMVTHDERLVVRTdCN--LWVveNQGIDEIDGDFEdykkEVLDA 613
Cdd:COG1134 182 qkkclARIRELresGRTVIFVSHSMGAVRRL-CDraIWL--EKGRLVMDGDPE----EVIAA 236
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
407-565 |
1.05e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.35 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKD-VLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR---------KHRTLRigwfdqha 476
Cdd:PRK10790 343 IDNVSFAYRDDnLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRldgrplsslSHSVLR-------- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 477 nealNG----EQTPVEFLCTKF-NI----DYQEAR--KQLGTTGLAAHAHTV----------KIKDLSGGQKSRVALCNL 535
Cdd:PRK10790 415 ----QGvamvQQDPVVLADTFLaNVtlgrDISEEQvwQALETVQLAELARSLpdglytplgeQGNNLSVGQKQLLALARV 490
|
170 180 190
....*....|....*....|....*....|
gi 17559834 536 ALGGPDIIILDEPTNNLDIESIDALAEAIR 565
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALA 520
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
99-283 |
1.07e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.87 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQVDSTsaiDTVVKSDKKRLALLEE--EAKLMS- 175
Cdd:PRK13646 27 NTEFEQGKYYAIVGQTGSGKSTLIQNINA--LLKPTTGTVTVDDITITHKTK---DKYIRPVRKRIGMVFQfpESQLFEd 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 176 ----EIEEGKTEAAERMKEVADelrdigadsaepRARRILAGLGFSKEMQEKPCTDFSGGWRMRISLARALFLEPTLLML 251
Cdd:PRK13646 102 tverEIIFGPKNFKMNLDEVKN------------YAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 17559834 252 DEPTNHLDLNA---VIWLDNYLQTWK-KTLLIVSHD 283
Cdd:PRK13646 170 DEPTAGLDPQSkrqVMRLLKSLQTDEnKTIILVSHD 205
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
401-577 |
1.17e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 62.06 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 401 NPPVLGLHDVNFGYGKdvlFK---KLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDG-------ELRKHRTLRIG 470
Cdd:COG4674 7 HGPILYVEDLTVSFDG---FKalnDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGsvlfggtDLTGLDEHEIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 471 W------------FDQHANE-----ALNGEQTPVEFLCTKFNidyQEARKQ----LGTTGLAAHAHTvKIKDLSGGQKSR 529
Cdd:COG4674 84 RlgigrkfqkptvFEELTVFenlelALKGDRGVFASLFARLT---AEERDRieevLETIGLTDKADR-LAGLLSHGQKQW 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17559834 530 VALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGG--VVMVTHD 577
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKhsVVVVEHD 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
407-577 |
1.33e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 61.95 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGEL---------------RKHRTLR--I 469
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLniaghqfdfsqkpseKAIRLLRqkV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 470 GWFDQHAN--EALNGEQTPVEFLCTKFNIDYQEARKQ----LGTTGLAAHAHTVKIKdLSGGQKSRVALCNLALGGPDII 543
Cdd:COG4161 85 GMVFQQYNlwPHLTVMENLIEAPCKVLGLSKEQAREKamklLARLRLTDKADRFPLH-LSGGQQQRVAIARALMMEPQVL 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 17559834 544 ILDEPTNNLDIESIDALAEAIRDFNG-GV--VMVTHD 577
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIRELSQtGItqVIVTHE 200
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
426-583 |
1.60e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.43 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 426 GVDMDSRIA----IVGPNGVGKSTLLKLLIGKIDPNDGELrkhrtlrigWFDQHANEALNGEQTPveFLCTKFNIDYQE- 500
Cdd:PRK10908 20 GVTFHMRPGemafLTGHSGAGKSTLLKLICGIERPSAGKI---------WFSGHDITRLKNREVP--FLRRQIGMIFQDh 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 501 -------------------------ARKQ----LGTTGLAAHAHTVKIKdLSGGQKSRVALCNLALGGPDIIILDEPTNN 551
Cdd:PRK10908 89 hllmdrtvydnvaipliiagasgddIRRRvsaaLDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 17559834 552 LDiesiDALAEAI----RDFNG---GVVMVTHDERLVVR 583
Cdd:PRK10908 168 LD----DALSEGIlrlfEEFNRvgvTVLMATHDIGLISR 202
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
80-284 |
1.81e-10 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 61.48 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQVDSTS--AIDTVV 157
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAG--FETPTSGEILLDGKDITNLPPHkrPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 158 KSdkkrLAL---LEEEAKLMSEIEEGKTEAAERMKEVADELRDIGADSAEPRarrilaglgfskemqeKPcTDFSGGWRM 234
Cdd:cd03300 79 QN----YALfphLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANR----------------KP-SQLSGGQQQ 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17559834 235 RISLARALFLEPTLLMLDEPTNHLDL----NAVIWLDNYLQTWKKTLLIVSHDQ 284
Cdd:cd03300 138 RVAIARALVNEPKVLLLDEPLGALDLklrkDMQLELKRLQKELGITFVFVTHDQ 191
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
409-581 |
1.91e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 62.02 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 409 DVNFGYGKD-VLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGE-LRKHRTLR------------IGWFDQ 474
Cdd:PRK13639 6 DLKYSYPDGtEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEvLIKGEPIKydkksllevrktVGIVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 475 HANEALNGE--QTPVEF--LCTKFNID-----YQEARKQLGTTGLAAHA-HtvkikDLSGGQKSRVALCNLALGGPDIII 544
Cdd:PRK13639 86 NPDDQLFAPtvEEDVAFgpLNLGLSKEevekrVKEALKAVGMEGFENKPpH-----HLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17559834 545 LDEPTNNLDIESIDALAEAIRDFNG---GVVMVTHDERLV 581
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNKegiTIIISTHDVDLV 200
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
519-595 |
2.13e-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: 60.70 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 519 IKDLSGGQKS------RVALCNLALGGPDIIILDEPTNNLDIESID-ALAEAIRDFNGG----VVMVTHDERLVVRTDcN 587
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQknfqLIVITHDEELVDAAD-H 191
|
....*...
gi 17559834 588 LWVVENQG 595
Cdd:cd03240 192 IYRVEKDG 199
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
407-577 |
2.28e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 62.40 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrIGwfDQHANEALNGE--- 483
Cdd:COG3839 6 LENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIL------IG--GRDVTDLPPKDrni 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 484 ----QTPV--------EflctkfNIDY---------QEARKQ----LGTTGLAAHAHtVKIKDLSGGQKSRVALcnlalg 538
Cdd:COG3839 78 amvfQSYAlyphmtvyE------NIAFplklrkvpkAEIDRRvreaAELLGLEDLLD-RKPKQLSGGQRQRVAL------ 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17559834 539 G------PDIIILDEPTNNLD----IESIDALAEAIRDFNGGVVMVTHD 577
Cdd:COG3839 145 GralvrePKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
80-284 |
2.38e-10 |
|
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: 60.73 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPShidllycEQEIQVDSTSAIDtvVKS 159
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAG--LEEPT-------SGRIYIGGRDVTD--LPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 DKKRLALLEEEAKL---MSeieegkteAAERMkEVADELRDIGADSAEPRARRILAGLGFSKEMQEKPcTDFSGGWRMRI 236
Cdd:cd03301 70 KDRDIAMVFQNYALyphMT--------VYDNI-AFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKP-KQLSGGQRQRV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17559834 237 SLARALFLEPTLLMLDEPTNHLD----LNAVIWLDNYLQTWKKTLLIVSHDQ 284
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQ 191
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
80-284 |
2.56e-10 |
|
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: 60.81 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAqGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHI-GARKlaiPSHIDLLYCEQEIqvdstsaidTVVK 158
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIaGFIK---PDSGKILLNGKDI---------TNLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 159 SDKKRLALLEEEAKL---MS---EIEEGKTEAAERMKEVADELRDIGADsaeprarrilagLGFSKEMQEKPCTdFSGGW 232
Cdd:cd03299 68 PEKRDISYVPQNYALfphMTvykNIAYGLKKRKVDKKEIERKVLEIAEM------------LGIDHLLNRKPET-LSGGE 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 233 RMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKK----TLLIVSHDQ 284
Cdd:cd03299 135 QQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKefgvTVLHVTHDF 190
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
434-585 |
2.63e-10 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 59.30 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 434 AIVGPNGVGKSTLLK---LLIGkidpndgeLRKHRTLRIGWFDQHANEALngeqtpveflctkFNIDYQEARKQLgttgl 510
Cdd:cd03227 25 IITGPNGSGKSTILDaigLALG--------GAQSATRRRSGVKAGCIVAA-------------VSAELIFTRLQL----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 511 aahahtvkikdlSGGQKSRVALCN---LALGGPD-IIILDEPTNNLDIESIDALAEAIRDFNGG---VVMVTHDERLVVR 583
Cdd:cd03227 79 ------------SGGEKELSALALilaLASLKPRpLYILDEIDRGLDPRDGQALAEAILEHLVKgaqVIVITHLPELAEL 146
|
..
gi 17559834 584 TD 585
Cdd:cd03227 147 AD 148
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
80-297 |
2.65e-10 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 61.12 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKhigarklAIPSHIDLLYCEQEIQVDSTSAIDTVVKs 159
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSK-------TIAGHPSYEVTSGTILFKGQDLLELEPD- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 DKKRLALL-----EEEAKLMSEIEEGKTEAAERMKEVADElrDIGADSAEPRARRILAGLGFSKEMQEKPCTD-FSGGWR 233
Cdd:TIGR01978 73 ERARAGLFlafqyPEEIPGVSNLEFLRSALNARRSARGEE--PLDLLDFEKLLKEKLALLDMDEEFLNRSVNEgFSGGEK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17559834 234 MRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWK---KTLLIVSHDQGFLDSVCTDIIHL 297
Cdd:TIGR01978 151 KRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLRepdRSFLIITHYQRLLNYIKPDYVHV 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
407-553 |
2.78e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.16 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGEL-----------RKHRTlRIGWFDQH 475
Cdd:PRK13536 44 LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvlgvpvparaRLARA-RIGVVPQF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 476 ANeaLNGEQTPVEFLCT---KFNIDYQEARKQLGT----TGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILDEP 548
Cdd:PRK13536 123 DN--LDLEFTVRENLLVfgrYFGMSTREIEAVIPSllefARLESKADA-RVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
....*
gi 17559834 549 TNNLD 553
Cdd:PRK13536 200 TTGLD 204
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
403-595 |
2.84e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 62.55 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 403 PVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR---------KHRTL--RIGW 471
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagddvealSARAAsrRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 472 FDQHANEALN--GEQTpVEF--------LCTKFNIDYQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCN-LALGGP 540
Cdd:PRK09536 82 VPQDTSLSFEfdVRQV-VEMgrtphrsrFDTWTETDRAAVERAMERTGVAQFADR-PVTSLSGGERQRVLLARaLAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559834 541 dIIILDEPTNNLDI-------ESIDALAEAIRdfngGVVMVTHDERLVVRTdCNLWVVENQG 595
Cdd:PRK09536 160 -VLLLDEPTASLDInhqvrtlELVRRLVDDGK----TAVAAIHDLDLAARY-CDELVLLADG 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
434-576 |
3.86e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.35 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 434 AIVGPNGVGKSTLLKLLIGKIDPNDGELRKH------------RTLRIGWFDQH----------ANEALNGEQTPveflc 491
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvrirsprdaIALGIGMVHQHfmlvpnltvaENIVLGLEPTK----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 492 tKFNIDYQEARKQL----GTTGLAAHAHTvKIKDLSGGQKSRV----ALcnlaLGGPDIIILDEPTNNLDIESIDALAEA 563
Cdd:COG3845 110 -GGRLDRKAARARIrelsERYGLDVDPDA-KVEDLSVGEQQRVeilkAL----YRGARILILDEPTAVLTPQEADELFEI 183
|
170
....*....|....*.
gi 17559834 564 IRDF--NG-GVVMVTH 576
Cdd:COG3845 184 LRRLaaEGkSIIFITH 199
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
405-576 |
4.04e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 60.37 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 405 LGLHDVNFGYgkDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrigwfdqhaneaLNGE- 483
Cdd:PRK10771 2 LKLTDITWLY--HHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLT-----------------LNGQd 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 484 -------QTPVEFLCTKFNI---------------------DYQeaRKQLGTTglaahAHTVKIKD--------LSGGQK 527
Cdd:PRK10771 63 htttppsRRPVSMLFQENNLfshltvaqniglglnpglklnAAQ--REKLHAI-----ARQMGIEDllarlpgqLSGGQR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17559834 528 SRVALCNLALGGPDIIILDEPTNNLD----IESIDALAEAIRDFNGGVVMVTH 576
Cdd:PRK10771 136 QRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
80-283 |
4.25e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.51 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHI------GARKLAIPSHIDLLYCEQEIQVDSTSAI 153
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVlglvapDEGVIKRNGKLRIGYVPQKLYLDTTLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 154 dTVvksdkKRLALLEEEAKLmseieegkteaaermkevadelRDIGadsaePRARRILAGlgfskEMQEKPCTDFSGGWR 233
Cdd:PRK09544 85 -TV-----NRFLRLRPGTKK----------------------EDIL-----PALKRVQAG-----HLIDAPMQKLSGGET 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17559834 234 MRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTL----LIVSHD 283
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcavLMVSHD 180
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
78-282 |
4.36e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.22 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 78 MDIKIENFD-ISAQG----KLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPShidllycEQEIQVDSTSA 152
Cdd:PRK13637 1 MSIKIENLThIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNG--LLKPT-------SGKIIIDGVDI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 153 IDTVVK-SD-KKRLALLEE--EAKLMSEIEEgkteaaermKEVADELRDIG--ADSAEPRARRILAGLGFSKE-MQEKPC 225
Cdd:PRK13637 72 TDKKVKlSDiRKKVGLVFQypEYQLFEETIE---------KDIAFGPINLGlsEEEIENRVKRAMNIVGLDYEdYKDKSP 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 226 TDFSGGWRMRISLARALFLEPTLLMLDEPTNHLD-------LNAVIWL-DNYlqtwKKTLLIVSH 282
Cdd:PRK13637 143 FELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgrdeiLNKIKELhKEY----NMTIILVSH 203
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
90-302 |
4.40e-10 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 60.59 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 90 QGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEI-QVDSTSAidtvvKSDKKRLALLE 168
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLG--LEKPAQGTVSFRGQDLyQLDRKQR-----RAFRRDVQLVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 169 EEAklMSEIEEGKTeAAERMKEVADELRDIGADSAEPRARRILAGLGFSKEMQEKPCTDFSGGWRMRISLARALFLEPTL 248
Cdd:TIGR02769 95 QDS--PSAVNPRMT-VRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17559834 249 LMLDEPTNHLD--LNAVI--WLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKL 302
Cdd:TIGR02769 172 IVLDEAVSNLDmvLQAVIleLLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
433-600 |
4.44e-10 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 60.59 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIGKIDPNDGEL----------------RKHRTLRIGWfdQHANEALNGEQT-------PVEF 489
Cdd:TIGR02769 40 VGLLGRSGCGKSTLARLLLGLEKPAQGTVsfrgqdlyqldrkqrrAFRRDVQLVF--QDSPSAVNPRMTvrqiigePLRH 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 490 LcTKFNIDYQEARKQ--LGTTGLAAHAHTVKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDI---ESIDALAEAI 564
Cdd:TIGR02769 118 L-TSLDESEQKARIAelLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqAVILELLRKL 196
|
170 180 190
....*....|....*....|....*....|....*...
gi 17559834 565 R-DFNGGVVMVTHDERLVVRTDCNLWVVEN-QGIDEID 600
Cdd:TIGR02769 197 QqAFGTAYLFITHDLRLVQSFCQRVAVMDKgQIVEECD 234
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
100-283 |
4.56e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.46 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 100 LTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLyceqeiqvdSTSAIDTVVKSDKKrlaLLEEEAKLMSeiee 179
Cdd:PRK11247 33 LHIPAGQFVAVVGRSGCGKSTLLRLLAG--LETPSAGELL---------AGTAPLAEAREDTR---LMFQDARLLP---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 180 gkteaaerMKEVADelrDIG---ADSAEPRARRILAGLGFSKEMQEKPCTdFSGGWRMRISLARALFLEPTLLMLDEPTN 256
Cdd:PRK11247 95 --------WKKVID---NVGlglKGQWRDAALQALAAVGLADRANEWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190
....*....|....*....|....*....|.
gi 17559834 257 HLDLNAVIWLDNYLQT-WKK---TLLIVSHD 283
Cdd:PRK11247 163 ALDALTRIEMQDLIESlWQQhgfTVLLVTHD 193
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
99-302 |
5.63e-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: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLKHIGARKLaiPShidllycEQEIQVDSTSaidtVVKSDKKRLALLE-------EEA 171
Cdd:cd03292 21 NISISAGEFVFLVGPSGAGKSTLLKLIYKEEL--PT-------SGTIRVNGQD----VSDLRGRAIPYLRrkigvvfQDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 172 KLMSeieegKTEAAErmkEVADELRDIGADSAEPRAR--RILAGLGFSKEMQEKPcTDFSGGWRMRISLARALFLEPTLL 249
Cdd:cd03292 88 RLLP-----DRNVYE---NVAFALEVTGVPPREIRKRvpAALELVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 250 MLDEPTNHLD---LNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKL 302
Cdd:cd03292 159 IADEPTGNLDpdtTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
194-304 |
5.94e-10 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 59.75 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 194 ELRdiGADSAEPRARRILAGLGFSKEMQEKPcTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLD-------------L 260
Cdd:COG4181 116 ELA--GRRDARARARALLERVGLGHRLDHYP-AQLSGGEQQRVALARAFATEPAILFADEPTGNLDaatgeqiidllfeL 192
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 17559834 261 NaviwldnylQTWKKTLLIVSHDQGfLDSVCTDIIHLDNQKLHT 304
Cdd:COG4181 193 N---------RERGTTLVLVTHDPA-LAARCDRVLRLRAGRLVE 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
402-578 |
6.02e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.96 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 402 PPVLGLHDVNFgygkdvlfkKLNFGvdmdsRI-AIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrigwfdqhaneaL 480
Cdd:COG1129 15 GGVKALDGVSL---------ELRPG-----EVhALLGENGAGKSTLMKILSGVYQPDSGEIL-----------------L 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 481 NGEqtPVEF-------------------LC----------------TKFNID----YQEARKQLGTTGLAAHAHTvKIKD 521
Cdd:COG1129 64 DGE--PVRFrsprdaqaagiaiihqelnLVpnlsvaeniflgreprRGGLIDwramRRRARELLARLGLDIDPDT-PVGD 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 522 LSGGQKSRVALCNlAL-GGPDIIILDEPTNNLDIESIDALAEAIRDF--NG-GVVMVTH--DE 578
Cdd:COG1129 141 LSVAQQQLVEIAR-ALsRDARVLILDEPTASLTEREVERLFRIIRRLkaQGvAIIYISHrlDE 202
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
228-282 |
6.48e-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: 58.38 E-value: 6.48e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559834 228 FSGGWRMRISLARALFLEPTLLMLDEPTNHLD------LNAVIwldNYLQTWKKTLLIVSH 282
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDvegeraLNQAI---AALKAAGATRIVIAH 154
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
78-284 |
8.86e-10 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 60.55 E-value: 8.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 78 MDIKIENfdISAQ--GKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHI-GarkLAIPShidllycEQEIQVDstsaiD 154
Cdd:COG1118 1 MSIEVRN--ISKRfgSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIaG---LETPD-------SGRIVLN-----G 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 155 TVVKSD----KKRLALLEEEAKL---MSeieegkteaaermkeVADE----LRDIGADSAEPRAR------RI-LAGLGf 216
Cdd:COG1118 64 RDLFTNlpprERRVGFVFQHYALfphMT---------------VAENiafgLRVRPPSKAEIRARveelleLVqLEGLA- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 217 skemQEKPcTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDlNAV-----IWLDNYLQTWKKTLLIVSHDQ 284
Cdd:COG1118 128 ----DRYP-SQLSGGQRQRVALARALAVEPEVLLLDEPFGALD-AKVrkelrRWLRRLHDELGGTTVFVTHDQ 194
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
78-259 |
9.06e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.03 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 78 MDIKIENFDISAQGKLLFDKASL-----TIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQvDSTSA 152
Cdd:PRK13634 1 MDITFQKVEHRYQYKTPFERRALydvnvSIPSGSYVAIIGHTGSGKSTLLQHLNG--LLQPTSGTVTIGERVIT-AGKKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 153 IDtvVKSDKKRLALLEE--EAKLMSEIEEgkteaaermKEVADELRDIGA--DSAEPRARRILAGLGFSKEMQEKPCTDF 228
Cdd:PRK13634 78 KK--LKPLRKKVGIVFQfpEHQLFEETVE---------KDICFGPMNFGVseEDAKQKAREMIELVGLPEELLARSPFEL 146
|
170 180 190
....*....|....*....|....*....|.
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEPTNHLD 259
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
423-577 |
9.07e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 9.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 423 LNFGVDMDSRIAIVGPNGVGKSTLLKLLI------GKIDPND--------GELRKHRtlriGWFDQ-------------- 474
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAgllpgsGSIQFAGqpleawsaAELARHR----AYLSQqqtppfampvfqyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 475 ----HANEALNGEQTPVEFLCTKFNIDYQearkqlgttgLAAHAHTvkikdLSGGQKSRVALCNLALG-GPDI------I 543
Cdd:PRK03695 91 tlhqPDKTRTEAVASALNEVAEALGLDDK----------LGRSVNQ-----LSGGEWQRVRLAAVVLQvWPDInpagqlL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 17559834 544 ILDEPTNNLDIESIDALAEAIRDF---NGGVVMVTHD 577
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELcqqGIAVVMSSHD 192
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
78-302 |
9.08e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 60.23 E-value: 9.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 78 MDIKIENFD-ISAQGKLL----FDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQVDSTSa 152
Cdd:PRK13641 1 MSIKFENVDyIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNA--LLKPSSGTITIAGYHITPETGN- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 153 idtvvksdkKRLALLEEEAKLMSEIEEGKTEAAERMKEVADELRDIGA--DSAEPRARRILAGLGFSKEMQEKPCTDFSG 230
Cdd:PRK13641 78 ---------KNLKKLRKKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFseDEAKEKALKWLKKVGLSEDLISKSPFELSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 231 GWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKK---TLLIVSHDQGFLDSVCTDIIHLDNQKL 302
Cdd:PRK13641 149 GQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
97-283 |
1.05e-09 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 60.51 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 97 KASLTIVYGRRYGLVGPNGMGKTTLLKHIGARKLAIPSHIDLlycEQEIQVDSTSAIDTvvKSDKKRLALLEEEAKLM-- 174
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVL---NGRTLFDSRKGIFL--PPEKRRIGYVFQEARLFph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 175 ----SEIEEGkteaaerMKEVADELRDIGADsaeprarRILAGLGFSKEMQEKPcTDFSGGWRMRISLARALFLEPTLLM 250
Cdd:TIGR02142 90 lsvrGNLRYG-------MKRARPSERRISFE-------RVIELLGIGHLLGRLP-GRLSGGEKQRVAIGRALLSSPRLLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 17559834 251 LDEPTNHLDL---NAVI-WLDNYLQTWKKTLLIVSHD 283
Cdd:TIGR02142 155 MDEPLAALDDprkYEILpYLERLHAEFGIPILYVSHS 191
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
77-282 |
1.08e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 60.23 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 77 SMDIKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHI------------------------GARKLAI 132
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIlgmtspdagkitvlgvpvpararlARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 133 PSHIDLLycEQEIQVDStsaiDTVVKSDKKRLALLEEEAKLMSEIEEGKTEAAermkevadelrdigADSaeprarrila 212
Cdd:PRK13536 119 VPQFDNL--DLEFTVRE----NLLVFGRYFGMSTREIEAVIPSLLEFARLESK--------------ADA---------- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559834 213 glgfskemqekPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNA--VIW--LDNYLqTWKKTLLIVSH 282
Cdd:PRK13536 169 -----------RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHArhLIWerLRSLL-ARGKTILLTTH 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
80-283 |
1.12e-09 |
|
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: 58.73 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHI-GARKLAIPSHID--LLYCEQEIqvdstSAIDTV 156
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnRLNDLIPGAPDEgeVLLDGKDI-----YDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 157 VKSDKKRLALLEEEAKL--MS---EIEEGKTEAAERMKEVADElrdigadsaepRARRILAGLGFSKEMQEKP-CTDFSG 230
Cdd:cd03260 76 VLELRRRVGMVFQKPNPfpGSiydNVAYGLRLHGIKLKEELDE-----------RVEEALRKAALWDEVKDRLhALGLSG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 231 GWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKK--TLLIVSHD 283
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
434-576 |
1.12e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 434 AIVGPNGVGKSTLLKLLIGKIDPNDGELR-KHRTLRIgwfdQHANEALNG-------------EQTPVEFLC-----TKF 494
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDAGSILiDGQEMRF----ASTTAALAAgvaiiyqelhlvpEMTVAENLYlgqlpHKG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 495 N-ID----YQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDF-- 567
Cdd:PRK11288 110 GiVNrrllNYEAREQLEHLGVDIDPDT-PLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELra 188
|
170
....*....|
gi 17559834 568 NGGVVM-VTH 576
Cdd:PRK11288 189 EGRVILyVSH 198
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
80-260 |
1.33e-09 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 59.36 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHI-GARKlaiPSHIDLLYCEQEIqvdstSAIDTVVK 158
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGELT---PSSGEVRLNGRPL-----AAWSPWEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 159 SdkKRLALLEEEAKLmseieegktEAAERMKEVAdEL-RDIGADSAEPRARRI-----LAGLGfskEMQEKPCTDFSGGW 232
Cdd:COG4559 74 A--RRRAVLPQHSSL---------AFPFTVEEVV-ALgRAPHGSSAAQDRQIVrealaLVGLA---HLAGRSYQTLSGGE 138
|
170 180 190
....*....|....*....|....*....|....*
gi 17559834 233 RMRISLARAL-------FLEPTLLMLDEPTNHLDL 260
Cdd:COG4559 139 QQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDL 173
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
409-596 |
1.35e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 59.65 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 409 DVNFGYGKDVLFKKL-----NFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR-------------KHRTLR-- 468
Cdd:PRK13634 7 KVEHRYQYKTPFERRalydvNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigervitagkknkKLKPLRkk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 469 IGWFDQHANEALNgEQTPVEFLC---TKFNIDYQEA----RKQLGTTGLAAHAHTVKIKDLSGGQKSRVALCN-LALGgP 540
Cdd:PRK13634 87 VGIVFQFPEHQLF-EETVEKDICfgpMNFGVSEEDAkqkaREMIELVGLPEELLARSPFELSGGQMRRVAIAGvLAME-P 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 541 DIIILDEPTNNLD----IESIDALAEAIRDFNGGVVMVTHDERLVVRTDCNLWVVENQGI 596
Cdd:PRK13634 165 EVLVLDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
409-577 |
1.37e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.39 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 409 DVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELrkhrtlrigWFDqhanealnGEQTPve 488
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI---------LFD--------GENIP-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 489 flcTKFNIDYQEARKQ---LGTTG---------------LAAHAH--------TVKIK---------------DLSGGQK 527
Cdd:PRK11831 73 ---AMSRSRLYTVRKRmsmLFQSGalftdmnvfdnvaypLREHTQlpapllhsTVMMKleavglrgaaklmpsELSGGMA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17559834 528 SRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNG--GV--VMVTHD 577
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVtcVVVSHD 203
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
435-577 |
1.49e-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: 58.92 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 435 IVGPNGVGKSTLLKLLIGKIDPN----------DGELRKHR--TLRIgWFDQHANEALNGEQTP--VEFLCTKF------ 494
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNlgkfddppdwDEILDEFRgsELQN-YFTKLLEGDVKVIVKPqyVDLIPKAVkgkvge 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 495 NIDYQEAR-------KQLGTTGLAAHahtvKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDF 567
Cdd:cd03236 110 LLKKKDERgkldelvDQLELRHVLDR----NIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIREL 185
|
170
....*....|...
gi 17559834 568 N---GGVVMVTHD 577
Cdd:cd03236 186 AeddNYVLVVEHD 198
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
410-585 |
1.54e-09 |
|
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: 58.65 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 410 VNFGYGKD--VLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGE---------------LRKhrtlRIGWF 472
Cdd:cd03252 6 VRFRYKPDgpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRvlvdghdlaladpawLRR----QVGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 473 DQHA---------NEALNGEQTPVEflctkfniDYQEARKQLGttglaAHAHTVKIKD------------LSGGQKSRVA 531
Cdd:cd03252 82 LQENvlfnrsirdNIALADPGMSME--------RVIEAAKLAG-----AHDFISELPEgydtivgeqgagLSGGQRQRIA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 532 LCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGG--VVMVTHDERLVVRTD 585
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGrtVIIIAHRLSTVKNAD 204
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
432-610 |
1.61e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 59.72 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 432 RIAIVGPNGVGKSTLLKLLIGKIDPNDGELR-------KHRT---LRIG---------WFDQHANEALngeqtpvEFLCT 492
Cdd:COG4586 50 IVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgyvpfKRRKefaRRIGvvfgqrsqlWWDLPAIDSF-------RLLKA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 493 KFNIDYQEARKQLGTTglaahAHTVKIKD--------LSGGQKSRvalCNLA---LGGPDIIILDEPTNNLDIESIDALA 561
Cdd:COG4586 123 IYRIPDAEYKKRLDEL-----VELLDLGElldtpvrqLSLGQRMR---CELAaalLHRPKILFLDEPTIGLDVVSKEAIR 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17559834 562 EAIRDFN---GGVVMVT-HD----ERLvvrtdCNLWVVENQGidEI--DGDFEDYKKEV 610
Cdd:COG4586 195 EFLKEYNrerGTTILLTsHDmddiEAL-----CDRVIVIDHG--RIiyDGSLEELKERF 246
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
80-283 |
1.79e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.94 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSH--IDLlyceQEIQVDSTSAIDTVV 157
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAG--FVPYQHgsITL----DGKPVEGPGAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 158 KSDKkrlALLEEEaKLMSEIEEGKteaaermkevadELRDIGADSAEPRARRILAGLGFSkEMQEKPCTDFSGGWRMRIS 237
Cdd:PRK11248 76 FQNE---GLLPWR-NVQDNVAFGL------------QLAGVEKMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 238 LARALFLEPTLLMLDEPTNHLD---------LNAVIWLDnylqTWKKTLLIvSHD 283
Cdd:PRK11248 139 IARALAANPQLLLLDEPFGALDaftreqmqtLLLKLWQE----TGKQVLLI-THD 188
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
80-259 |
2.00e-09 |
|
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: 58.35 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDIS-AQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGarKLAIPSHIDLLYCEQEIQVDSTSAIDTVvk 158
Cdd:cd03256 1 IEVENLSKTyPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLN--GLVEPTSGSVLIDGTDINKLKGKALRQL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 159 sdKKRLALLEEEAKL---MSEIEEGKTEAAERMKEVADELRdiGADSAE-PRARRILAGLGFSkEMQEKPCTDFSGGWRM 234
Cdd:cd03256 77 --RRQIGMIFQQFNLierLSVLENVLSGRLGRRSTWRSLFG--LFPKEEkQRALAALERVGLL-DKAYQRADQLSGGQQQ 151
|
170 180
....*....|....*....|....*
gi 17559834 235 RISLARALFLEPTLLMLDEPTNHLD 259
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLD 176
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
398-580 |
2.15e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.50 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 398 TKLNPPVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIG-------------------KIDPnd 458
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaykilegdilfkgesilDLEP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 459 gELRKHRTLRIGWfdqhanealngeQTPVE--------FLCTKFN----------ID----YQEARKQLGTTGLAAHAHT 516
Cdd:CHL00131 79 -EERAHLGIFLAF------------QYPIEipgvsnadFLRLAYNskrkfqglpeLDplefLEIINEKLKLVGMDPSFLS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17559834 517 VKIKD-LSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDF---NGGVVMVTHDERL 580
Cdd:CHL00131 146 RNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLmtsENSIILITHYQRL 213
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
409-577 |
2.23e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.04 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 409 DVNFGY--GKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPND---------GELRKHRTL-----RIGWF 472
Cdd:PRK13640 10 HVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnskitvdGITLTAKTVwdireKVGIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 473 DQHANEALNGEQT--PVEFLCTKFNIDYQE----ARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILD 546
Cdd:PRK13640 90 FQNPDNQFVGATVgdDVAFGLENRAVPRPEmikiVRDVLADVGMLDYIDS-EPANLSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190
....*....|....*....|....*....|....*
gi 17559834 547 EPTNNLDIESIDALAEAIRDF----NGGVVMVTHD 577
Cdd:PRK13640 169 ESTSMLDPAGKEQILKLIRKLkkknNLTVISITHD 203
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
407-593 |
2.24e-09 |
|
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: 57.89 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLfkKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrIGWFDQHANEAlngEQTP 486
Cdd:cd03298 3 LDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVL------INGVDVTAAPP---ADRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 487 VEFLCTKFNI-----------------------DYQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDII 543
Cdd:cd03298 72 VSMLFQENNLfahltveqnvglglspglkltaeDRQAIEVALARVGLAGLEKR-LPGELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17559834 544 ILDEPTNNLD----IESIDALAEAIRDFNGGVVMVTHDERLVVRTDCNLWVVEN 593
Cdd:cd03298 151 LLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDN 204
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
421-582 |
2.31e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 58.59 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 421 KKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR-----------KHRTLRIGWFDQHANEALNGEQT--PV 487
Cdd:PRK13647 22 KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvmgrevnaeneKWVRSKVGLVFQDPDDQVFSSTVwdDV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 488 EFLCTKFNIDYQEARKQLGTtGLAAhahtVKIKD--------LSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDA 559
Cdd:PRK13647 102 AFGPVNMGLDKDEVERRVEE-ALKA----VRMWDfrdkppyhLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180
....*....|....*....|....*.
gi 17559834 560 LAEAIRDFN--GGVVMV-THDERLVV 582
Cdd:PRK13647 177 LMEILDRLHnqGKTVIVaTHDVDLAA 202
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
433-616 |
2.52e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 59.33 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIGKIDPNDGELRKH---------RTLRIGWFDQHAneALNGEQTPVEflctkfNIDYqeark 503
Cdd:PRK10851 31 VALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgtdvsrlhaRDRKVGFVFQHY--ALFRHMTVFD------NIAF----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 504 qlGTTGLAAH----AHTVKIK-------------------DLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDAL 560
Cdd:PRK10851 98 --GLTVLPRRerpnAAAIKAKvtqllemvqlahladrypaQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKEL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17559834 561 AEAIR----DFNGGVVMVTHD--ERLVVrtdCNLWVVENQGIDEIDGDFEDYKKE-----VLDALGE 616
Cdd:PRK10851 176 RRWLRqlheELKFTSVFVTHDqeEAMEV---ADRVVVMSQGNIEQAGTPDQVWREpatrfVLEFMGE 239
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
99-259 |
2.69e-09 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 58.01 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLKhigarklAIPSHIDllYCEQEIQVDSTSAIDTVVKSDKKRLALLEEEAKLMSE-I 177
Cdd:cd03251 22 SLDIPAGETVALVGPSGSGKSTLVN-------LIPRFYD--VDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDtV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 178 EE----GKTEAAErmKEVADELRDIGADSaeprarrilaglgFSKEMQEKPCTD-------FSGGWRMRISLARALFLEP 246
Cdd:cd03251 93 AEniayGRPGATR--EEVEEAARAANAHE-------------FIMELPEGYDTVigergvkLSGGQRQRIAIARALLKDP 157
|
170
....*....|...
gi 17559834 247 TLLMLDEPTNHLD 259
Cdd:cd03251 158 PILILDEATSALD 170
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
374-566 |
2.82e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 59.83 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 374 DDAGAPELLQRRKEysVKFQfpettklnppvlglhDVNFGYGKD--VLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLI 451
Cdd:COG5265 344 DAPDAPPLVVGGGE--VRFE---------------NVSFGYDPErpIL-KGVSFEVPAGKTVAIVGPSGAGKSTLARLLF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 452 GKIDPNDGELR---------KHRTLR--IGWFdqhanealngEQTPVEFLCT-KFNIDY-----------QEARkqlgtt 508
Cdd:COG5265 406 RFYDVTSGRILidgqdirdvTQASLRaaIGIV----------PQDTVLFNDTiAYNIAYgrpdaseeeveAAAR------ 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17559834 509 glAAHAHT-----------------VKikdLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIES---I-DALAEAIRD 566
Cdd:COG5265 470 --AAQIHDfieslpdgydtrvgergLK---LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTeraIqAALREVARG 543
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
434-587 |
2.83e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 58.94 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 434 AIVGPNGVGKSTLLKLL-----------------IGKIDPNdgELRKHRtLRIGWFDQHANeaLNGEQTPVEflctkfNI 496
Cdd:COG1135 35 GIIGYSGAGKSTLIRCInllerptsgsvlvdgvdLTALSER--ELRAAR-RKIGMIFQHFN--LLSSRTVAE------NV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 497 DY--------QEARKQ-----LGTTGLAAHAHtVKIKDLSGGQKSRV----ALCNlalgGPDIIILDEPTNNLDIESIDA 559
Cdd:COG1135 104 ALpleiagvpKAEIRKrvaelLELVGLSDKAD-AYPSQLSGGQKQRVgiarALAN----NPKVLLCDEATSALDPETTRS 178
|
170 180 190
....*....|....*....|....*....|..
gi 17559834 560 LAEAIRDFNG--G--VVMVTHdERLVVRTDCN 587
Cdd:COG1135 179 ILDLLKDINRelGltIVLITH-EMDVVRRICD 209
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
421-554 |
3.37e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 58.26 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 421 KKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGEL-----------RKHRTLRIGWFDQHANEALNGEQTPVEF 489
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhplhfgdYSYRSQRIRMIFQDPSTSLNPRQRISQI 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 490 L--CTKFNIDY--QEARKQLGTT----GLAAHAHTVKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDI 554
Cdd:PRK15112 110 LdfPLRLNTDLepEQREKQIIETlrqvGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
78-299 |
3.42e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 57.72 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 78 MDIKIENFDIS-AQGKLLFDkASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLlyceqEIqvdSTSAIDTV 156
Cdd:PRK11124 1 MSIQLNGINCFyGAHQALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNL--LEMPRSGTL-----NI---AGNHFDFS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 157 VKSDKKRLALLEEEAKLMSE---------IEEGKTEAAERMKEVADElrdigadSAEPRARRILAGLGFSKEMQEKPcTD 227
Cdd:PRK11124 70 KTPSDKAIRELRRNVGMVFQqynlwphltVQQNLIEAPCRVLGLSKD-------QALARAEKLLERLRLKPYADRFP-LH 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 228 FSGGWRMRISLARALFLEPTLLMLDEPTNHLD---LNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDN 299
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeiTAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMEN 216
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
99-260 |
3.74e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.44 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLlkhigARKLAI---PSHIDLLYCEQEiqvdstsaidtVVKSDKKRLALLEEEAKLMS 175
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTL-----ARLLTMietPTGGELYYQGQD-----------LLKADPEAQKLLRQKIQIVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 176 EIEEGKTEAAERMKEVADELRDIGAD-SAEPRARRILAGL---GFSKEMQEKPCTDFSGGWRMRISLARALFLEPTLLML 251
Cdd:PRK11308 99 QNPYGSLNPRKKVGQILEEPLLINTSlSAAERREKALAMMakvGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVA 178
|
....*....
gi 17559834 252 DEPTNHLDL 260
Cdd:PRK11308 179 DEPVSALDV 187
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
398-577 |
3.83e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.63 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 398 TKLNPPVLGLHDVNFG-YGKDVLfkklnfgvdmdsriAIVGPNGVGKSTLLKLLIGKIDPNDG----------------- 459
Cdd:PRK11701 13 TKLYGPRKGCRDVSFDlYPGEVL--------------GIVGESGSGKTTLLNALSARLAPDAGevhyrmrdgqlrdlyal 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 460 -ELRKHRTLRIGW--FDQHANEALNGEQTP----VEFLCTKFNIDYQEARKQ----LGTTGLAAHahtvKIKDL----SG 524
Cdd:PRK11701 79 sEAERRRLLRTEWgfVHQHPRDGLRMQVSAggniGERLMAVGARHYGDIRATagdwLERVEIDAA----RIDDLpttfSG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17559834 525 GQKSRVALC-NLaLGGPDIIILDEPTNNLDIeSI-----DALAEAIRDFNGGVVMVTHD 577
Cdd:PRK11701 155 GMQQRLQIArNL-VTHPRLVFMDEPTGGLDV-SVqarllDLLRGLVRELGLAVVIVTHD 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
409-577 |
4.05e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 58.30 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 409 DVNFGYGKDVLFKK-----LNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR---KHRTL------------R 468
Cdd:PRK13641 7 NVDYIYSPGTPMEKkgldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagYHITPetgnknlkklrkK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 469 IGWFDQHANEAL--NGEQTPVEFLCTKFNIDYQEARKQ----LGTTGLAAHAHTVKIKDLSGGQKSRVALCNLALGGPDI 542
Cdd:PRK13641 87 VSLVFQFPEAQLfeNTVLKDVEFGPKNFGFSEDEAKEKalkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 17559834 543 IILDEPTNNLDIESIDALAEAIRDFNGG---VVMVTHD 577
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHN 204
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
407-577 |
4.39e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 57.82 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLN---FGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPN------DGELRKHRTL-----RIGWF 472
Cdd:PRK13650 7 VKNLTFKYKEDQEKYTLNdvsFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsgqiiiDGDLLTEENVwdirhKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 473 DQHANEALNGE--QTPVEFLCTKFNIDYQEARKQ----LGTTGLAAHAhTVKIKDLSGGQKSRVALCNLALGGPDIIILD 546
Cdd:PRK13650 87 FQNPDNQFVGAtvEDDVAFGLENKGIPHEEMKERvneaLELVGMQDFK-EREPARLSGGQKQRVAIAGAVAMRPKIIILD 165
|
170 180 190
....*....|....*....|....*....|....*
gi 17559834 547 EPTNNLDIESIDALAEAIR----DFNGGVVMVTHD 577
Cdd:PRK13650 166 EATSMLDPEGRLELIKTIKgirdDYQMTVISITHD 200
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
435-579 |
4.57e-09 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 58.27 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 435 IVGPNGVGKSTLLKLLIGKIDPNDGELRKHRT--------LR-IGWFDQhaNEALNGEQTPVEflctkfNIDY------- 498
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEdvtnvpphLRhINMVFQ--SYALFPHMTVEE------NVAFglkmrkv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 499 ------QEARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNG--- 569
Cdd:TIGR01187 73 praeikPRVLEALRLVQLEEFADR-KPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEqlg 151
|
170
....*....|.
gi 17559834 570 -GVVMVTHDER 579
Cdd:TIGR01187 152 iTFVFVTHDQE 162
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
434-595 |
5.41e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.87 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 434 AIVGPNGVGKSTLLKLLIGKIDPNDGELR------------KH-RTLR--IGWFDQHANEAL--NGEQTPVEFLCTKFNI 496
Cdd:PRK13646 37 AIVGQTGSGKSTLIQNINALLKPTTGTVTvdditithktkdKYiRPVRkrIGMVFQFPESQLfeDTVEREIIFGPKNFKM 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 497 DYQEAR----KQLGTTGLAAHAHTVKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDF----N 568
Cdd:PRK13646 117 NLDEVKnyahRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqtdeN 196
|
170 180
....*....|....*....|....*..
gi 17559834 569 GGVVMVTHDERLVVRTDCNLwVVENQG 595
Cdd:PRK13646 197 KTIILVSHDMNEVARYADEV-IVMKEG 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
434-580 |
5.63e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 57.81 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 434 AIVGPNGVGKSTLLKLLIGKIDPNDGELR--------KHRTlRIGW-------------FDQ---HAneALNGeqtpvef 489
Cdd:COG4152 31 GLLGPNGAGKTTTIRIILGILAPDSGEVLwdgepldpEDRR-RIGYlpeerglypkmkvGEQlvyLA--RLKG------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 490 lctkfnIDYQEARKQ----LGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIR 565
Cdd:COG4152 101 ------LSKAEAKRRadewLERLGLGDRANK-KVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIR 173
|
170 180
....*....|....*....|..
gi 17559834 566 DF--NG-GVVMVTHD----ERL 580
Cdd:COG4152 174 ELaaKGtTVIFSSHQmelvEEL 195
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
422-593 |
5.78e-09 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 58.20 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 422 KLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKHRTLrigWFDQHAnealnGEQTPVEFlcTKFNIDYQEA 501
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRT---LFDSRK-----GIFLPPEK--RRIGYVFQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 502 R--KQLGTTG-----------------------LAAHAHTVK--IKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDI 554
Cdd:TIGR02142 85 RlfPHLSVRGnlrygmkrarpserrisfervieLLGIGHLLGrlPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17559834 555 ----ESIDALAEAIRDFNGGVVMVTHDERLVVRTDCNLWVVEN 593
Cdd:TIGR02142 165 prkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLED 207
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
229-290 |
6.38e-09 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 58.61 E-value: 6.38e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEPTNHLD------LNAVIwldNYLQTWKKTLLIVSHDQGFLDSV 290
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaaLAAAI---RALKARGATVVVITHRPSLLAAV 533
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
407-553 |
6.78e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.12 E-value: 6.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLK------------LLIGKIDPNDGELRKHRtlrIGWFDQ 474
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRmiagleditsgdLFIGEKRMNDVPPAERG---VGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 475 ------HANEALNgeqtpVEFLCTKFNIDYQEARK---QLGTTGLAAHAHTVKIKDLSGGQKSRVALCNLALGGPDIIIL 545
Cdd:PRK11000 83 syalypHLSVAEN-----MSFGLKLAGAKKEEINQrvnQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
....*...
gi 17559834 546 DEPTNNLD 553
Cdd:PRK11000 158 DEPLSNLD 165
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
409-582 |
7.20e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.49 E-value: 7.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 409 DVNFGY-GKDVL-FKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGE---------------LRKHRTL---R 468
Cdd:PRK11176 346 NVTFTYpGKEVPaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEilldghdlrdytlasLRNQVALvsqN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 469 IGWF-DQHANealngeqtpveflctkfNIDY----QEARKQLGTTGLAAHA-----------HTVkIKD----LSGGQKS 528
Cdd:PRK11176 426 VHLFnDTIAN-----------------NIAYarteQYSREQIEEAARMAYAmdfinkmdnglDTV-IGEngvlLSGGQRQ 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559834 529 RVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDF--NGGVVMVTH--------DERLVV 582
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELqkNRTSLVIAHrlstiekaDEILVV 551
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
433-577 |
8.45e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.40 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIGKIDPNDGEL--------RKHRTLRIGWFD---------------------------QHAN 477
Cdd:PRK13651 36 IAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdekNKKKTKEKEKVLeklviqktrfkkikkikeirrrvgvvfQFAE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 478 EALNgEQT--------PVEFLCTKfNIDYQEARKQLGTTGLAAHAHTVKIKDLSGGQKSRVALCNLALGGPDIIILDEPT 549
Cdd:PRK13651 116 YQLF-EQTiekdiifgPVSMGVSK-EEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPT 193
|
170 180 190
....*....|....*....|....*....|.
gi 17559834 550 NNLDIESIDALAEAIRDFNGG---VVMVTHD 577
Cdd:PRK13651 194 AGLDPQGVKEILEIFDNLNKQgktIILVTHD 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
401-583 |
8.91e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 58.16 E-value: 8.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 401 NPPVLGLHD--VNFGYGKDVLF--KKLNFGVDMDSRIAIVGPNGVGKS----TLLKLL-------IGKI--------DPN 457
Cdd:COG4172 3 SMPLLSVEDlsVAFGQGGGTVEavKGVSFDIAAGETLALVGESGSGKSvtalSILRLLpdpaahpSGSIlfdgqdllGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 458 DGELRKHRTLRIGWFDQHANEALNgeqtPVeflctkFNIDYQ--EA-RKQLGTTGLAAHAHT------VKIKD------- 521
Cdd:COG4172 83 ERELRRIRGNRIAMIFQEPMTSLN----PL------HTIGKQiaEVlRLHRGLSGAAARARAlellerVGIPDperrlda 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559834 522 ----LSGGQKSRV----ALCNlalgGPDIIILDEPTNNLDI----ESIDALAEAIRDFNGGVVMVTHDERLVVR 583
Cdd:COG4172 153 yphqLSGGQRQRVmiamALAN----EPDLLIADEPTTALDVtvqaQILDLLKDLQRELGMALLLITHDLGVVRR 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
404-577 |
9.35e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 57.17 E-value: 9.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 404 VLGLHDVNFGY--GKDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGEL----------RKH-RTLR-- 468
Cdd:PRK13636 5 ILKVEELNYNYsdGTHAL-KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysRKGlMKLRes 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 469 IGWFDQHANEALNGEQT--PVEFLCTKFNIDYQEARKQ----LGTTGLAaHAHTVKIKDLSGGQKSRVALCNLALGGPDI 542
Cdd:PRK13636 84 VGMVFQDPDNQLFSASVyqDVSFGAVNLKLPEDEVRKRvdnaLKRTGIE-HLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 17559834 543 IILDEPTNNLD----IESIDALAEAIRDFNGGVVMVTHD 577
Cdd:PRK13636 163 LVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
402-576 |
1.24e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 56.20 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 402 PPVLGLHDVNFGYG-KDVLFkklnfGVDMD---SRI-AIVGPNGVGKSTLLK------------------LLIGK----- 453
Cdd:COG1117 9 EPKIEVRNLNVYYGdKQALK-----DINLDipeNKVtALIGPSGCGKSTLLRclnrmndlipgarvegeiLLDGEdiydp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 454 -IDPNdgELRKhrtlRIGW-FdqhanealngeQTPVEFLCTKF-NIDYqearkqlgttGLAAHAHTVK------------ 518
Cdd:COG1117 84 dVDVV--ELRR----RVGMvF-----------QKPNPFPKSIYdNVAY----------GLRLHGIKSKseldeiveeslr 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 519 -------IKD--------LSGGQKSRvaLC---NLALgGPDIIILDEPTNNLD------IES-IDALAEairDFngGVVM 573
Cdd:COG1117 137 kaalwdeVKDrlkksalgLSGGQQQR--LCiarALAV-EPEVLLMDEPTSALDpistakIEElILELKK---DY--TIVI 208
|
...
gi 17559834 574 VTH 576
Cdd:COG1117 209 VTH 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
96-284 |
1.29e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.04 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 96 DKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPShidllycEQEIQVDSTsaiDTVVKSDKKR--------LALL 167
Cdd:PRK11432 23 DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAG--LEKPT-------EGQIFIDGE---DVTHRSIQQRdicmvfqsYALF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 168 EEeaklMSEIEE----------GKTEAAERMKEvADELRDigadsaeprarriLAGlgfskeMQEKPCTDFSGGWRMRIS 237
Cdd:PRK11432 91 PH----MSLGENvgyglkmlgvPKEERKQRVKE-ALELVD-------------LAG------FEDRYVDQISGGQQQRVA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 238 LARALFLEPTLLMLDEPTNHLDLNaviwLDNYL--------QTWKKTLLIVSHDQ 284
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLDAN----LRRSMrekirelqQQFNITSLYVTHDQ 197
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
96-283 |
1.44e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 56.66 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 96 DKASLTIVYGRRYGLVGPNGMGKTTLLK-------------HIGARKLAIPSHIDLLYCEQEIQV---DSTSAID---TV 156
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRlllrleeptsgeiLFDGQDITGLSGRELRPLRRRMQMvfqDPYASLNprmTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 157 vksdkkrLALLEEEAKLMseieeGKTEAAERMKEVADELRDIGADSAepRARRilaglgFSKEmqekpctdFSGGWRMRI 236
Cdd:COG4608 115 -------GDIIAEPLRIH-----GLASKAERRERVAELLELVGLRPE--HADR------YPHE--------FSGGQRQRI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17559834 237 SLARALFLEPTLLMLDEPTNHLDLN--A-VIwldNYLQTWKK----TLLIVSHD 283
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDVSiqAqVL---NLLEDLQDelglTYLFISHD 217
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
415-609 |
1.45e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.87 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 415 GKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKHRTLRIGWFDQ-------------------- 474
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQetpalpqpaleyvidgdrey 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 475 --------HANEALNGEQtpVEFLCTKFN-IDYQEARKQ----LGTTGLAAHAHTVKIKDLSGGQKSRVALCNLALGGPD 541
Cdd:PRK10636 92 rqleaqlhDANERNDGHA--IATIHGKLDaIDAWTIRSRaaslLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17559834 542 IIILDEPTNNLDIESIDALAEAIRDFNGGVVMVTHDERLVVRTDCNLWVVENQGIDEIDGDFEDYKKE 609
Cdd:PRK10636 170 LLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQ 237
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
407-577 |
1.60e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 55.86 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGE----------------------LRK- 463
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEvlvdgldvattpsrelakrlaiLRQe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 464 -HRTLRI--------GWFdQHANEALNGEqtpveflctkfniDYQ---EARKQLGTTGLAaHAHtvkIKDLSGGQKSR-- 529
Cdd:COG4604 84 nHINSRLtvrelvafGRF-PYSKGRLTAE-------------DREiidEAIAYLDLEDLA-DRY---LDELSGGQRQRaf 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17559834 530 VA--LCNlalgGPDIIILDEPTNNLDI----ESIDALAEAIRDFNGGVVMVTHD 577
Cdd:COG4604 146 IAmvLAQ----DTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
433-577 |
1.73e-08 |
|
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: 57.49 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIGKIDPNDGE----------LRKHRTLRIG-WFDQHANEALNGEQTP--VEFLCTKF----- 494
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDydeepswdevLKRFRGTELQdYFKKLANGEIKVAHKPqyVDLIPKVFkgtvr 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 495 ----NID----YQEARKQLGTTGLAAHahtvKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRD 566
Cdd:COG1245 182 elleKVDergkLDELAEKLGLENILDR----DISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRE 257
|
170
....*....|....
gi 17559834 567 F---NGGVVMVTHD 577
Cdd:COG1245 258 LaeeGKYVLVVEHD 271
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
78-284 |
1.75e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.63 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 78 MDIKIENFDIS-AQGKLLFDkASLTIVYGRRYGLVGPNGMGKTTLLKHIGARKLAIPSHIDLlyceQEIQVDSTSAIDTV 156
Cdd:PRK10851 1 MSIEIANIKKSfGRTQVLND-ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRF----HGTDVSRLHARDRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 157 VKSDKKRLALLEEeAKLMSEIEEGKTEAAERMKEVADELRDigadsaepRARRILAGLGFSKEMQEKPcTDFSGGWRMRI 236
Cdd:PRK10851 76 VGFVFQHYALFRH-MTVFDNIAFGLTVLPRRERPNAAAIKA--------KVTQLLEMVQLAHLADRYP-AQLSGGQKQRV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17559834 237 SLARALFLEPTLLMLDEPTNHLDLNAVI----WLDNYLQTWKKTLLIVSHDQ 284
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKelrrWLRQLHEELKFTSVFVTHDQ 197
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
407-576 |
1.80e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.91 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFK-KLNFGVDMD----SRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR----------KHRTLR--- 468
Cdd:PRK13649 5 LQNVSYTYQAGTPFEgRALFDVNLTiedgSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlitstsKNKDIKqir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 469 --IGWFDQHANEALNGEQT--PVEFLCTKFNIDYQEA----RKQLGTTGLAAHAHTVKIKDLSGGQKSRVALCNLALGGP 540
Cdd:PRK13649 85 kkVGLVFQFPESQLFEETVlkDVAFGPQNFGVSQEEAealaREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEP 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 17559834 541 DIIILDEPTNNLDIESIDALAEAIRDFNGG---VVMVTH 576
Cdd:PRK13649 165 KILVLDEPTAGLDPKGRKELMTLFKKLHQSgmtIVLVTH 203
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
402-549 |
2.04e-08 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 55.37 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 402 PPVLGLHDVNFGYGK-DVLFkklnfGVDMD----SRIAIVGPNGVGKSTLLKLLIGKIDPNDGE----------LRKHRT 466
Cdd:COG0410 1 MPMLEVENLHAGYGGiHVLH-----GVSLEveegEIVALLGRNGAGKTTLLKAISGLLPPRSGSirfdgeditgLPPHRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 467 -----------------------LRIGWFdqhANEALNGEQTPVEFLCTKFNIdYQEARKQLGTTglaahahtvkikdLS 523
Cdd:COG0410 76 arlgigyvpegrrifpsltveenLLLGAY---ARRDRAEVRADLERVYELFPR-LKERRRQRAGT-------------LS 138
|
170 180
....*....|....*....|....*..
gi 17559834 524 GGQKSRVALCNlAL-GGPDIIILDEPT 549
Cdd:COG0410 139 GGEQQMLAIGR-ALmSRPKLLLLDEPS 164
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
421-600 |
2.41e-08 |
|
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: 54.73 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 421 KKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDG--ELRKHRTLRIGWFDQHANEALNgEQTPVEFLCT-KFNID 497
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGkiEIDGIDISTIPLEDLRSSLTII-PQDPTLFSGTiRSNLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 498 -YQE-ARKQLGTTglaahahtVKIK----DLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGGV 571
Cdd:cd03369 104 pFDEySDEEIYGA--------LRVSegglNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNS 175
|
170 180 190
....*....|....*....|....*....|
gi 17559834 572 VMVTHDERLVVRTDCNLWVVENQG-IDEID 600
Cdd:cd03369 176 TILTIAHRLRTIIDYDKILVMDAGeVKEYD 205
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
395-577 |
2.42e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.27 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 395 PETTKLNPPVLGLHD--VNFGY--GKDVLFKKLNFGVDMDSRIAIVGPNGVGKS----TLLKLLI--GKIDP-------- 456
Cdd:PRK09473 3 PLAQQQADALLDVKDlrVTFSTpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGRIGGsatfngre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 457 ----NDGELRKHRTLRIGWFDQHANEALN-----GEQ-TPVEFLCTKFN--------------IDYQEARKQLGTtglaa 512
Cdd:PRK09473 83 ilnlPEKELNKLRAEQISMIFQDPMTSLNpymrvGEQlMEVLMLHKGMSkaeafeesvrmldaVKMPEARKRMKM----- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 513 HAHtvkikDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIeSIDA-----LAEAIRDFNGGVVMVTHD 577
Cdd:PRK09473 158 YPH-----EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAqimtlLNELKREFNTAIIMITHD 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
83-263 |
2.47e-08 |
|
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: 54.42 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 83 ENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQeiqvdstsAIDTVVKSDKK 162
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAG--LSPPLAGRVLLNGG--------PLDFQRDSIAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 163 RLALLEEEAKLmseieEGKTEAAERMKEvadeLRDIGADSA--EPRARRILAGLGfskemqEKPCTDFSGGWRMRISLAR 240
Cdd:cd03231 74 GLLYLGHAPGI-----KTTLSVLENLRF----WHADHSDEQveEALARVGLNGFE------DRPVAQLSAGQQRRVALAR 138
|
170 180
....*....|....*....|...
gi 17559834 241 ALFLEPTLLMLDEPTNHLDLNAV 263
Cdd:cd03231 139 LLLSGRPLWILDEPTTALDKAGV 161
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
78-305 |
2.53e-08 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 54.85 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 78 MDIKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGarklaipshidllyceQEIQVDSTSaidtvV 157
Cdd:cd03220 21 KKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLA----------------GIYPPDSGT-----V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 158 KSDKKRLALLEEEAKLMSEI--EEG-----------KTEAAERMKEVADelrdigadsaeprarriLAGLGfskEMQEKP 224
Cdd:cd03220 80 TVRGRVSSLLGLGGGFNPELtgRENiylngrllglsRKEIDEKIDEIIE-----------------FSELG---DFIDLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 225 CTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKK---TLLIVSHDQGFLDSVCTDIIHLDNQK 301
Cdd:cd03220 140 VKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKqgkTVILVSHDPSSIKRLCDRALVLEKGK 219
|
....
gi 17559834 302 LHTY 305
Cdd:cd03220 220 IRFD 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
423-610 |
2.82e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 55.44 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 423 LNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDG-----------------ELRKhrtlRIGWFDQHANEALNgEQT 485
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGkiiidgvditdkkvklsDIRK----KVGLVFQYPEYQLF-EET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 486 ---PVEFLCTKFNIDYQE----ARKQLGTTGLAAHahTVKIK---DLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIE 555
Cdd:PRK13637 101 iekDIAFGPINLGLSEEEienrVKRAMNIVGLDYE--DYKDKspfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 556 SIDALAEAIRD----FNGGVVMVTHD----ERLVVRTdcnlwVVENQGIDEIDGDFEDYKKEV 610
Cdd:PRK13637 179 GRDEILNKIKElhkeYNMTIILVSHSmedvAKLADRI-----IVMNKGKCELQGTPREVFKEV 236
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
80-284 |
3.21e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 56.00 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIqvdstsaidTVVKS 159
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG--FEQPTAGQIMLDGVDL---------SHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 DKKRLALLEEEAKLMSE--IEEGKTEAAERMKEVADELRDigadsaepRARRILAGLGFSKEMQEKPcTDFSGGWRMRIS 237
Cdd:PRK11607 89 YQRPINMMFQSYALFPHmtVEQNIAFGLKQDKLPKAEIAS--------RVNEMLGLVHMQEFAKRKP-HQLSGGQRQRVA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17559834 238 LARALFLEPTLLMLDEPTNHLD--LNAVIWLD--NYLQTWKKTLLIVSHDQ 284
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQ 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
78-284 |
5.20e-08 |
|
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: 54.27 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 78 MDIKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEiqVDSTSAIDTVV 157
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG--LERPDSGTILFGGED--ATDVPVQERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 158 KSDKKRLALLeeeaKLMSEIEE---GKTEAAERMKEVADELRDigadsaepRARRILAGLGFSKEMQEKPcTDFSGGWRM 234
Cdd:cd03296 77 GFVFQHYALF----RHMTVFDNvafGLRVKPRSERPPEAEIRA--------KVHELLKLVQLDWLADRYP-AQLSGGQRQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17559834 235 RISLARALFLEPTLLMLDEPTNHLDLNaviwLDNYLQTWKK--------TLLIVSHDQ 284
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAK----VRKELRRWLRrlhdelhvTTVFVTHDQ 197
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
433-577 |
5.41e-08 |
|
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: 52.96 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIGKIDPNDGELRKHRtLRIGWFDQHAnealngeqtpveflctkfnidyqearkqlgttglaa 512
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-ITPVYKPQYI------------------------------------ 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17559834 513 hahtvkikDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDF----NGGVVMVTHD 577
Cdd:cd03222 71 --------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHD 131
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
417-577 |
5.47e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.89 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 417 DVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLiGKID-PNDGELR---------------KHRTLRIGWFDQ------ 474
Cdd:PRK10535 22 EVL-KGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLDkPTSGTYRvagqdvatldadalaQLRREHFGFIFQryhlls 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 475 HANEALNGEqTPVEFLCTKFNIDYQEARKQLGTTGLAAHAHtVKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDI 554
Cdd:PRK10535 100 HLTAAQNVE-VPAVYAGLERKQRLLRAQELLQRLGLEDRVE-YQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180
....*....|....*....|....*.
gi 17559834 555 ES---IDALAEAIRDFNGGVVMVTHD 577
Cdd:PRK10535 178 HSgeeVMAILHQLRDRGHTVIIVTHD 203
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
407-578 |
5.73e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.11 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPN------DGELRKHRTLrigwfdQHANeal 480
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTegqifiDGEDVTHRSI------QQRD--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 481 ngeqtpvefLCTKF-------------NIDY--------QEARKQ-----LGTTGLAAHAHTVkIKDLSGGQKSRVALCN 534
Cdd:PRK11432 80 ---------ICMVFqsyalfphmslgeNVGYglkmlgvpKEERKQrvkeaLELVDLAGFEDRY-VDQISGGQQQRVALAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17559834 535 LALGGPDIIILDEPTNNLDIESIDALAEAIRD----FNGGVVMVTHDE 578
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRElqqqFNITSLYVTHDQ 197
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
80-302 |
5.94e-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: 53.74 E-value: 5.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIEN----FDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPShidllycEQEIQVDSTSaIDT 155
Cdd:cd03258 2 IELKNvskvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING--LERPT-------SGSVLVDGTD-LTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 156 VVKSD----KKRLALLEEEAKLMSEieegKTeAAErmkEVADELRDIGADSAE--PRARRILAGLGFSKEMQEKPcTDFS 229
Cdd:cd03258 72 LSGKElrkaRRRIGMIFQHFNLLSS----RT-VFE---NVALPLEIAGVPKAEieERVLELLELVGLEDKADAYP-AQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 230 GGWRMRISLARALFLEPTLLMLDEPTNHLDLNAViwlDNYLQTWKK-------TLLIVSHDQGFLDSVCTDIIHLDNQKL 302
Cdd:cd03258 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETT---QSILALLRDinrelglTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
99-283 |
6.40e-08 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 53.62 E-value: 6.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQvdstsaidtvvKSDKKRLALLEEEAKL--MSE 176
Cdd:TIGR01184 5 NLTIQQGEFISLIGHSGCGKSTLLNLISG--LAQPTSGGVILEGKQIT-----------EPGPDRMVVFQNYSLLpwLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 177 IEEgkteaaermkeVADELRDIGADSAEPRARRI------LAGLGfskEMQEKPCTDFSGGWRMRISLARALFLEPTLLM 250
Cdd:TIGR01184 72 REN-----------IALAVDRVLPDLSKSERRAIveehiaLVGLT---EAADKRPGQLSGGMKQRVAIARALSIRPKVLL 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 17559834 251 LDEPTNHLD-LNAVIWLDNYLQTWKK---TLLIVSHD 283
Cdd:TIGR01184 138 LDEPFGALDaLTRGNLQEELMQIWEEhrvTVLMVTHD 174
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
433-579 |
6.59e-08 |
|
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: 51.99 E-value: 6.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIGKIDPNDGelrkhrtlrigwfdqhanealngeqtPVEFLCTKFNIDYQEARKQLGTTGlaa 512
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGG--------------------------GVIYIDGEDILEEVLDQLLLIIVG--- 55
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 513 hahtVKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDF---------NGGVVMVTHDER 579
Cdd:smart00382 56 ----GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRlllllksekNLTVILTTNDEK 127
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
78-283 |
6.83e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 54.36 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 78 MDIKIENFDIS---AQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARKLAIPSHIDLLycEQEIQVDSTSAId 154
Cdd:PRK13647 1 MDNIIEVEDLHfryKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVM--GREVNAENEKWV- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 155 tvvksdKKRLALL---EEEAKLMSEIEEGKTEAAERMKEVADELrdigadsaEPRARRILAGLGFsKEMQEKPCTDFSGG 231
Cdd:PRK13647 78 ------RSKVGLVfqdPDDQVFSSTVWDDVAFGPVNMGLDKDEV--------ERRVEEALKAVRM-WDFRDKPPYHLSYG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17559834 232 WRMRISLARALFLEPTLLMLDEPTNHLD------LNAVIWLdnyLQTWKKTLLIVSHD 283
Cdd:PRK13647 143 QKKRVAIAGVLAMDPDVIVLDEPMAYLDprgqetLMEILDR---LHNQGKTVIVATHD 197
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
91-283 |
6.95e-08 |
|
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: 53.84 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 91 GKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGarKLAIPShidllycEQEIQVD--STSAIDTVvkSDKKRLALLE 168
Cdd:cd03295 13 GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMIN--RLIEPT-------SGEIFIDgeDIREQDPV--ELRRKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 169 EEAKLMSE--IEEG-------KTEAAERMKEVADEL-RDIGADSAEPRARrilaglgFSKEMqekpctdfSGGWRMRISL 238
Cdd:cd03295 82 QQIGLFPHmtVEENialvpklLKWPKEKIRERADELlALVGLDPAEFADR-------YPHEL--------SGGQQQRVGV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17559834 239 ARALFLEPTLLMLDEPTNHLDLNAVIWLDNYL----QTWKKTLLIVSHD 283
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFkrlqQELGKTIVFVTHD 195
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
404-577 |
7.71e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 54.33 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 404 VLGLHDVNFGYGKDVLFKKLN---FGVDMDSRIAIVGPNGVGKSTLLKLLIG---------KID------PNDGELRKhr 465
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGlfeefegkvKIDgelltaENVWNLRR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 466 tlRIGWFDQHANEALNGE--QTPVEFLCTKFNIDYQEARKQLGTTGLAAHAHTVKIKD---LSGGQKSRVALCNLALGGP 540
Cdd:PRK13642 82 --KIGMVFQNPDNQFVGAtvEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREparLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17559834 541 DIIILDEPTNNLD----IESIDALAEAIRDFNGGVVMVTHD 577
Cdd:PRK13642 160 EIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
433-553 |
8.03e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.27 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIGKID---------PNDGELRKHRTLRIGWFDQhaNEALNGEQTPVEFL--CTKF----NID 497
Cdd:PLN03211 97 LAVLGPSGSGKSTLLNALAGRIQgnnftgtilANNRKPTKQILKRTGFVTQ--DDILYPHLTVRETLvfCSLLrlpkSLT 174
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559834 498 YQE----ARKQLGTTGLAAHAHTVK----IKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLD 553
Cdd:PLN03211 175 KQEkilvAESVISELGLTKCENTIIgnsfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
403-553 |
8.70e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.63 E-value: 8.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 403 PVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLL------------IGKIDPNDGELRKHRT---- 466
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGSIVYNGHNIYSPRTdtvd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 467 LR--IGWFDQHANE-------------ALNGEQ------TPVEFLCTKFNIdYQEARKQLGTTGLAahahtvkikdLSGG 525
Cdd:PRK14239 84 LRkeIGMVFQQPNPfpmsiyenvvyglRLKGIKdkqvldEAVEKSLKGASI-WDEVKDRLHDSALG----------LSGG 152
|
170 180
....*....|....*....|....*...
gi 17559834 526 QKSRVALCNLALGGPDIIILDEPTNNLD 553
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
404-581 |
9.16e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.64 E-value: 9.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 404 VLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKID--PNDGELR-KHRTLRIGWFDQHANEAL 480
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEfKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 481 -NGEQTPVE--------FLCTKFNI----------------DYQEARKQLGTTGLAAHAHTVKIkDLSGGQKSRVALCNL 535
Cdd:PRK09580 81 fMAFQYPVEipgvsnqfFLQTALNAvrsyrgqepldrfdfqDLMEEKIALLKMPEDLLTRSVNV-GFSGGEKKRNDILQM 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17559834 536 ALGGPDIIILDEPTNNLDIESIDALAE---AIRDFNGGVVMVTHDERLV 581
Cdd:PRK09580 160 AVLEPELCILDESDSGLDIDALKIVADgvnSLRDGKRSFIIVTHYQRIL 208
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
108-283 |
9.33e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.51 E-value: 9.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 108 YGLVGPNGMGKTTLLK------HIGARKLAIPSHIdlLYCEQEI-QVDSTSAidtvvksdKKRLALLEEEAKLMSEIEEG 180
Cdd:PRK14246 39 FGIMGPSGSGKSTLLKvlnrliEIYDSKIKVDGKV--LYFGKDIfQIDAIKL--------RKEVGMVFQQPNPFPHLSIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 181 KTEAAERMKEVADELRDIGADSAEPrarriLAGLGFSKEMQEK---PCTDFSGGWRMRISLARALFLEPTLLMLDEPTNH 257
Cdd:PRK14246 109 DNIAYPLKSHGIKEKREIKKIVEEC-----LRKVGLWKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180
....*....|....*....|....*...
gi 17559834 258 LDLNAVIWLDNYLQTWKK--TLLIVSHD 283
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
405-585 |
9.35e-08 |
|
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: 52.86 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 405 LGLHDVNFGYGKDV-----LFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKHRtlRIGWFDQhanEA 479
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQ---EP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 480 --LNGeqtpveflcT-KFNI----DYQEAR--------------KQL-----------GTTglaahahtvkikdLSGGQK 527
Cdd:cd03250 76 wiQNG---------TiRENIlfgkPFDEERyekvikacalepdlEILpdgdlteigekGIN-------------LSGGQK 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559834 528 SRVALCNLALGGPDIIILDEPTNNLDIESIDALAE-AIRDF---NGGVVMVTHDERLVVRTD 585
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLllnNKTRILVTHQLQLLPHAD 195
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
433-553 |
1.02e-07 |
|
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: 53.04 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIGKIDP----------NDGELRKHRTL-RIGWFDQHanEALNGEQTPVEFL--CTKF---NI 496
Cdd:cd03234 36 MAILGSSGSGKTTLLDAISGRVEGggttsgqilfNGQPRKPDQFQkCVAYVRQD--DILLPGLTVRETLtyTAILrlpRK 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559834 497 DYQEARKQL-GTTGLAAHAHTV----KIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLD 553
Cdd:cd03234 114 SSDAIRKKRvEDVLLRDLALTRiggnLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
78-318 |
1.04e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 53.48 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 78 MDIKIENFDIS-AQGKLLFDkASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIqvdstsaiDTV 156
Cdd:COG4161 1 MSIQLKNINCFyGSHQALFD-INLECPSGETLVLLGPSGAGKSSLLRVLNL--LETPDSGQLNIAGHQF--------DFS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 157 VKSDKKRLALLEEEAKLMSE---------IEEGKTEAAERM----KEVADElrdigadsaepRARRILAGLGFSKEMQEK 223
Cdd:COG4161 70 QKPSEKAIRLLRQKVGMVFQqynlwphltVMENLIEAPCKVlglsKEQARE-----------KAMKLLARLRLTDKADRF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 224 PcTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLD---LNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQ 300
Cdd:COG4161 139 P-LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeiTAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKG 217
|
250 260
....*....|....*....|..
gi 17559834 301 KLHTYrGNYTLFK----KQYAQ 318
Cdd:COG4161 218 RIIEQ-GDASHFTqpqtEAFAH 238
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
404-549 |
1.11e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 404 VLGLHDVNFGYGKDVlfkKLNfGVDMD----SRIAIVGPNGVGKSTLLKLLIG--KIdpNDGEL---------RKHRTL- 467
Cdd:NF033858 1 VARLEGVSHRYGKTV---ALD-DVSLDipagCMVGLIGPDGVGKSSLLSLIAGarKI--QQGRVevlggdmadARHRRAv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 468 --RIGWFDQ------------HANealngeqtpVEFLCTKFNIDYQEaRKQ-----LGTTGLAAHAhtvkikD-----LS 523
Cdd:NF033858 75 cpRIAYMPQglgknlyptlsvFEN---------LDFFGRLFGQDAAE-RRRridelLRATGLAPFA------DrpagkLS 138
|
170 180
....*....|....*....|....*..
gi 17559834 524 GGQKSRVALCnLAL-GGPDIIILDEPT 549
Cdd:NF033858 139 GGMKQKLGLC-CALiHDPDLLILDEPT 164
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
405-605 |
1.17e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 53.43 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 405 LGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLL-----------------IGKIDPNDGELR---KH 464
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsegsivvngqtINLVRDKDGQLKvadKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 465 -----RTlRIGWFDQHAN-----EAL-NGEQTPVEFLCTKFNIDYQEARKQLGTTGLAAHAHTVKIKDLSGGQKSRVALC 533
Cdd:PRK10619 86 qlrllRT-RLTMVFQHFNlwshmTVLeNVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 534 NLALGGPDIIILDEPTNNLDIESIDA---LAEAIRDFNGGVVMVTHdERLVVRTDCNLWVVENQGIDEIDGDFED 605
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEvlrIMQQLAEEGKTMVVVTH-EMGFARHVSSHVIFLHQGKIEEEGAPEQ 238
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
407-577 |
1.18e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 53.45 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGY--GKDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLL------------KLLIGKIDPND-GELRKHRTLrIGW 471
Cdd:PRK13644 4 LENVSYSYpdGTPAL-ENINLVIKKGEYIGIIGKNGSGKSTLAlhlngllrpqkgKVLVSGIDTGDfSKLQGIRKL-VGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 472 FDQHANEALNGE--QTPVEFLCTKFNIDYQEARKQ----LGTTGLAAHAHTVKiKDLSGGQKSRVALCNLALGGPDIIIL 545
Cdd:PRK13644 82 VFQNPETQFVGRtvEEDLAFGPENLCLPPIEIRKRvdraLAEIGLEKYRHRSP-KTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190
....*....|....*....|....*....|....*
gi 17559834 546 DEPTNNLDIESIDALAEAIRDFN---GGVVMVTHD 577
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHekgKTIVYITHN 195
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
80-283 |
1.28e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.12 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGaRKLAIPSHIDLlycEQEIQVDSTSAIDTVVKS 159
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRV---EGRVEFFNQNIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 DKKR--LALLEEEAKL--MS----------------EIE-EGKTEAAERMKEVADELrdigadsaeprarrilaglgfsK 218
Cdd:PRK14258 84 NRLRrqVSMVHPKPNLfpMSvydnvaygvkivgwrpKLEiDDIVESALKDADLWDEI----------------------K 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17559834 219 EMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWK----KTLLIVSHD 283
Cdd:PRK14258 142 HKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHN 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
421-585 |
1.45e-07 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 52.85 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 421 KKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR-----------------KHRTLrIGWFDQHANEALnge 483
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIlegkqitepgpdrmvvfQNYSL-LPWLTVRENIAL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 484 qtPVEFLCTKFNIDYQEA--RKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDI----ESI 557
Cdd:TIGR01184 78 --AVDRVLPDLSKSERRAivEEHIALVGLTEAADK-RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgNLQ 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 17559834 558 DALAEAIRDFNGGVVMVTHD--------ERLVVRTD 585
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDvdealllsDRVVMLTN 190
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
85-259 |
1.51e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.58 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 85 FDISAQGklLFDkASLTIVYGRRYGLVGPNGMGKTTLlkhigarklaipshIDLLYCEQE-----IQVDSTSAIDTVVKS 159
Cdd:PRK13657 344 YDNSRQG--VED-VSFEAKPGQTVAIVGPTGAGKSTL--------------INLLQRVFDpqsgrILIDGTDIRTVTRAS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 DKKRLALLEEEAKLMSE-IEE----GKTEAA-ERMKEVADelRDIGADSAEPRARRILAGLGFSKEMqekpctdFSGGWR 233
Cdd:PRK13657 407 LRRNIAVVFQDAGLFNRsIEDnirvGRPDATdEEMRAAAE--RAQAHDFIERKPDGYDTVVGERGRQ-------LSGGER 477
|
170 180
....*....|....*....|....*.
gi 17559834 234 MRISLARALFLEPTLLMLDEPTNHLD 259
Cdd:PRK13657 478 QRLAIARALLKDPPILILDEATSALD 503
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
432-577 |
1.58e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 52.92 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 432 RIAIVGPNGVGKSTLLKLLIGKIDPN-----DG---------ELRKHRtlriGWFDQHanealngeQTPVeflctkFNID 497
Cdd:COG4138 24 LIHLIGPNGAGKSTLLARMAGLLPGQgeillNGrplsdwsaaELARHR----AYLSQQ--------QSPP------FAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 498 -YQ--------EARKQLGTTGLAAHAHTVKIKD--------LSGGQKSRVALCNLAL-----GGPD--IIILDEPTNNLD 553
Cdd:COG4138 86 vFQylalhqpaGASSEAVEQLLAQLAEALGLEDklsrpltqLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPMNSLD 165
|
170 180
....*....|....*....|....*..
gi 17559834 554 IE---SIDALAEAIRDFNGGVVMVTHD 577
Cdd:COG4138 166 VAqqaALDRLLRELCQQGITVVMSSHD 192
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
401-590 |
1.60e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 52.94 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 401 NPPVLGLHDVNFGYGKDVLfkklnfgvdmdsrIAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrigwFDQHA---- 476
Cdd:COG4525 17 GQPQPALQDVSLTIESGEF-------------VVALGASGCGKTTLLNLIAGFLAPSSGEIT---------LDGVPvtgp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 477 ---------NEALNGEQTPVEflctkfNIDY-------------QEARKQLGTTGLAaHAHTVKIKDLSGGQKSRVALCN 534
Cdd:COG4525 75 gadrgvvfqKDALLPWLNVLD------NVAFglrlrgvpkaerrARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 535 lALGG-PDIIILDEPTNNLDI---ESIDALAEAI-RDFNGGVVMVTHD--ERLVVRTDcnLWV 590
Cdd:COG4525 148 -ALAAdPRFLLMDEPFGALDAltrEQMQELLLDVwQRTGKGVFLITHSveEALFLATR--LVV 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
194-284 |
1.64e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 53.56 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 194 ELRDIGADSAEPRARRILA--GLGfskEMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNA----VIWLD 267
Cdd:COG3842 103 RMRGVPKAEIRARVAELLElvGLE---GLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLreemREELR 179
|
90
....*....|....*..
gi 17559834 268 NYLQTWKKTLLIVSHDQ 284
Cdd:COG3842 180 RLQRELGITFIYVTHDQ 196
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
109-259 |
1.64e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.09 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 109 GLVGPNGMGKTTLLKHIGArklaipshidLLYCEQEIQVDSTSAIDTvvkSDKKRLALLEEEAKLMSEIEEgKTEAAERM 188
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSG----------LLRPQKGAVLWQGKPLDY---SKRGLLALRQQVATVFQDPEQ-QIFYTDID 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 189 KEVADELRDIGADSAEPrARRILAGLGF--SKEMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLD 259
Cdd:PRK13638 97 SDIAFSLRNLGVPEAEI-TRRVDEALTLvdAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
80-260 |
1.80e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 52.85 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIgARKLAiPSHIDLLYCEQEIqvDSTSAIDTVvks 159
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL-SGELS-PDSGEVRLNGRPL--ADWSPAELA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 dkKRLALLEEEAKLmseieegktEAAERMKEVADELRDIGADSAEpRARRILAglgfsKEMQEKPCTDF--------SGG 231
Cdd:PRK13548 76 --RRRAVLPQHSSL---------SFPFTVEEVVAMGRAPHGLSRA-EDDALVA-----AALAQVDLAHLagrdypqlSGG 138
|
170 180 190
....*....|....*....|....*....|....*
gi 17559834 232 WRMRISLARAL------FLEPTLLMLDEPTNHLDL 260
Cdd:PRK13548 139 EQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDL 173
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
426-617 |
1.81e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 52.68 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 426 GVDMDSR----IAIVGPNGVGKSTLLKLLIGKIDPNDGELR----------KHRTLRIGWFDQHANEALNGEQTPVE--- 488
Cdd:PRK11300 23 NVNLEVReqeiVSLIGPNGAGKTTVFNCLTGFYKPTGGTILlrgqhieglpGHQIARMGVVRTFQHVRLFREMTVIEnll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 489 ----------FLCTKFNI-DYQEARKQ--------LGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILDEPT 549
Cdd:PRK11300 103 vaqhqqlktgLFSGLLKTpAFRRAESEaldraatwLERVGLLEHANR-QAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 550 NNLDIESIDALAEAI----RDFNGGVVMVTHDERLVVRTDCNLWVVeNQGIDEIDGDFEDYKK--EVLDA-LGEA 617
Cdd:PRK11300 182 AGLNPKETKELDELIaelrNEHNVTVLLIEHDMKLVMGISDRIYVV-NQGTPLANGTPEEIRNnpDVIKAyLGEA 255
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
408-596 |
1.87e-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: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 408 HDVNFGY---GKDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLL------------KLLIGKIDPNDGELRKHRTlRIGWF 472
Cdd:cd03244 6 KNVSLRYrpnLPPVL-KNISFSIKPGEKVGIVGRTGSGKSSLLlalfrlvelssgSILIDGVDISKIGLHDLRS-RISII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 473 dqhanealngEQTPVEFLCT-KFNID----YQEAR--KQLGTTGLAAHAHTVKIKD----------LSGGQKSRVALCNL 535
Cdd:cd03244 84 ----------PQDPVLFSGTiRSNLDpfgeYSDEElwQALERVGLKEFVESLPGGLdtvveeggenLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 536 ALGGPDIIILDEPTNNLDIESIDALAEAIRDF--NGGVVMVTHdeRLVVRTDCNLWVVENQGI 596
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAH--RLDTIIDSDRILVLDKGR 214
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
99-297 |
1.96e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLKHIGarKLAIPSHIDLLYCEQEIQVDSTsaidtvvKSDKKRLALLEEEAKLMSEIE 178
Cdd:PRK10253 27 TVEIPDGHFTAIIGPNGCGKSTLLRTLS--RLMTPAHGHVWLDGEHIQHYAS-------KEVARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 179 EGKTEAAERMKEVADELRDIGADsaEPRARRILAGLGFSkEMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHL 258
Cdd:PRK10253 98 VQELVARGRYPHQPLFTRWRKED--EEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17559834 259 DLNAVIWLDNYLQTWKK----TLLIVSHDqgfLDSVCTDIIHL 297
Cdd:PRK10253 175 DISHQIDLLELLSELNRekgyTLAAVLHD---LNQACRYASHL 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
99-282 |
2.15e-07 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 52.09 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLkhigarklaipSHIDLLYCEQ--EIQVDSTSAIDTVVKSDKKRLALLEEEAKLMS- 175
Cdd:cd03248 34 SFTLHPGEVTALVGPSGSGKSTVV-----------ALLENFYQPQggQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 176 ----EIEEGKTEAA-ERMKEVADElrdIGADSaeprarrilaglgFSKEMQEKPCTD-------FSGGWRMRISLARALF 243
Cdd:cd03248 103 slqdNIAYGLQSCSfECVKEAAQK---AHAHS-------------FISELASGYDTEvgekgsqLSGGQKQRVAIARALI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17559834 244 LEPTLLMLDEPTNHLDLNAVIWLDNYLQTW--KKTLLIVSH 282
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH 207
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
92-282 |
2.25e-07 |
|
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: 51.89 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 92 KLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARklaIPSHI----DLLYCEQEIQVDSTsaidtvvksdKKRLALL 167
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR---VEGGGttsgQILFNGQPRKPDQF----------QKCVAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 168 EEEAKLMSE--IEEG-----------KTEAAERMKEVADE-LRDIG-ADSAEPRARRIlaglgfskemqekpctdfSGGW 232
Cdd:cd03234 87 RQDDILLPGltVRETltytailrlprKSSDAIRKKRVEDVlLRDLAlTRIGGNLVKGI------------------SGGE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17559834 233 RMRISLARALFLEPTLLMLDEPTNHLD----LNAVIWLDNYLQTwKKTLLIVSH 282
Cdd:cd03234 149 RRRVSIAVQLLWDPKVLILDEPTSGLDsftaLNLVSTLSQLARR-NRIVILTIH 201
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
84-282 |
2.44e-07 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 53.98 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 84 NFDISAQ--------GKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLK-------------HIGARKLA-IPSHI---DL 138
Cdd:TIGR01193 471 NGDIVINdvsysygyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKllvgffqarsgeiLLNGFSLKdIDRHTlrqFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 139 LYCEQEIQVDSTSAIDTVVKSDKKRLAllEEEAKLMSEIEEGKTEAaERMKevadelrdigadsaeprarrilagLGFSK 218
Cdd:TIGR01193 551 NYLPQEPYIFSGSILENLLLGAKENVS--QDEIWAACEIAEIKDDI-ENMP------------------------LGYQT 603
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 219 EMQEKPcTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLD-LNAVIWLDNYLQTWKKTLLIVSH 282
Cdd:TIGR01193 604 ELSEEG-SSISGGQKQRIALARALLTDSKVLILDESTSNLDtITEKKIVNNLLNLQDKTIIFVAH 667
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
408-564 |
2.46e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 53.81 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 408 HDVNFGY-GKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR---------KHRTLR--IGWFDQh 475
Cdd:PRK13657 338 DDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidgtdirtvTRASLRrnIAVVFQ- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 476 anEALNGEQTPVEflctkfNI-----DYQEARKQLGTTGLAAHAHTVKIKD------------LSGGQKSRVALCNLALG 538
Cdd:PRK13657 417 --DAGLFNRSIED------NIrvgrpDATDEEMRAAAERAQAHDFIERKPDgydtvvgergrqLSGGERQRLAIARALLK 488
|
170 180
....*....|....*....|....*.
gi 17559834 539 GPDIIILDEPTNNLDIESIDALAEAI 564
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAAL 514
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
109-283 |
2.48e-07 |
|
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: 52.03 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 109 GLVGPNGMGKTTLLKHI-GARKlaiPSHIDLL-------YCEQEIQVDSTSAIDtvvksdkkrlalleeeaKLMSEIEEG 180
Cdd:cd03237 29 GILGPNGIGKTTFIKMLaGVLK---PDEGDIEieldtvsYKPQYIKADYEGTVR-----------------DLLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 181 KTEAAERMKEVADELRDIGadsaeprarrilaglgfskeMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLD- 259
Cdd:cd03237 89 FYTHPYFKTEIAKPLQIEQ--------------------ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDv 148
|
170 180
....*....|....*....|....*..
gi 17559834 260 ---LNAVIWLDNYLQTWKKTLLIVSHD 283
Cdd:cd03237 149 eqrLMASKVIRRFAENNEKTAFVVEHD 175
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
410-556 |
2.52e-07 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 53.57 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 410 VNFGY---GKDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR------KHRTLRigwfDQHANEAL 480
Cdd:TIGR02203 336 VTFRYpgrDRPAL-DSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILldghdlADYTLA----SLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 481 NGEQTpVEFLCTKF-NIDY----QEARKQLGTTGLAAHA-----------HT---VKIKDLSGGQKSRVALCNLALGGPD 541
Cdd:TIGR02203 411 VSQDV-VLFNDTIAnNIAYgrteQADRAEIERALAAAYAqdfvdklplglDTpigENGVLLSGGQRQRLAIARALLKDAP 489
|
170
....*....|....*
gi 17559834 542 IIILDEPTNNLDIES 556
Cdd:TIGR02203 490 ILILDEATSALDNES 504
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
417-576 |
2.54e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.60 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 417 DVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLiGKIDP-NDGELRKHRTLRIGWFDQHANEALNGEQTPVEFLCTKFn 495
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPvYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSE- 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 496 idyQEARKQLGTTGLAAHAHTVKIKD-----------------LSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESID 558
Cdd:TIGR00954 543 ---DMKRRGLSDKDLEQILDNVQLTHilereggwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG 619
|
170
....*....|....*...
gi 17559834 559 ALAEAIRDFNGGVVMVTH 576
Cdd:TIGR00954 620 YMYRLCREFGITLFSVSH 637
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
99-302 |
2.54e-07 |
|
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: 51.73 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLKHIGARKLAIPSHIDLlyceqeIQVDSTSAidtvvKSDKKRLALLEEEAKLMSEIE 178
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLI------NGVDVTAA-----PPADRPVSMLFQENNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 179 EGKTEAAERMKEVadELRdigadsAEPRAR--RILAGLGFSKEMQEKPCTdFSGGWRMRISLARALFLEPTLLMLDEPTN 256
Cdd:cd03298 87 VEQNVGLGLSPGL--KLT------AEDRQAieVALARVGLAGLEKRLPGE-LSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17559834 257 HLD------LNAVIwLDNYLQTwKKTLLIVSHDQGFLDSVCTDIIHLDNQKL 302
Cdd:cd03298 158 ALDpalraeMLDLV-LDLHAET-KMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
77-282 |
2.72e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.56 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 77 SMDIKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKhigarklAIPSHIDLlyCEQEIQVDSTSAIDTV 156
Cdd:PRK10789 313 ELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLS-------LIQRHFDV--SEGDIRFHDIPLTKLQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 157 VKSDKKRLALLEEEAKLMSE-----IEEGKTEAAERMKEVADELRDIGADsaeprarrILA-GLGFSKEMQEKPCTdFSG 230
Cdd:PRK10789 384 LDSWRSRLAVVSQTPFLFSDtvannIALGRPDATQQEIEHVARLASVHDD--------ILRlPQGYDTEVGERGVM-LSG 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559834 231 GWRMRISLARALFLEPTLLMLDEPtnhldLNAV-------IwLDNyLQTW--KKTLLIVSH 282
Cdd:PRK10789 455 GQKQRISIARALLLNAEILILDDA-----LSAVdgrtehqI-LHN-LRQWgeGRTVIISAH 508
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
99-553 |
2.81e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLlkhigARKLAipSHIDLLYCEQEIQVDSTSAIdtvvkSDKKRLALLEEEAK-----L 173
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSAL-----ARALA--GELPLLSGERQSQFSHITRL-----SFEQLQKLVSDEWQrnntdM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 174 MSEIEE--GKTeAAERMKevaDELRDigadsaEPRARRILAGLGFSKeMQEKPCTDFSGGWRMRISLARALFLEPTLLML 251
Cdd:PRK10938 91 LSPGEDdtGRT-TAEIIQ---DEVKD------PARCEQLAQQFGITA-LLDRRFKYLSTGETRKTLLCQALMSEPDLLIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 252 DEPTNHLDLNAViwldnylQTWKKTLLIVSHDQGFLDSVCT---DIihldnqklhtyrgnytlfkkqyaqdmqvheKNFD 328
Cdd:PRK10938 160 DEPFDGLDVASR-------QQLAELLASLHQSGITLVLVLNrfdEI------------------------------PDFV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 329 QQQKQL--KAMKKEGKSAKQAEEQVKQQMANKAKKggkknagkvnddDDAGAPEllqrRKEYSVKFQFPETTklnPPVLg 406
Cdd:PRK10938 203 QFAGVLadCTLAETGEREEILQQALVAQLAHSEQL------------EGVQLPE----PDEPSARHALPANE---PRIV- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKiDP----ND----------GE----LRKH---- 464
Cdd:PRK10938 263 LNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPqgysNDltlfgrrrgsGEtiwdIKKHigyv 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 465 --------------RTLRI-GWFD-----QHANEALNgeqtpveflctkfnidyQEARKQLGTTGLAAHAHTVKIKDLSG 524
Cdd:PRK10938 342 ssslhldyrvstsvRNVILsGFFDsigiyQAVSDRQQ-----------------KLAQQWLDILGIDKRTADAPFHSLSW 404
|
490 500 510
....*....|....*....|....*....|
gi 17559834 525 GQKsRVALCNLAL-GGPDIIILDEPTNNLD 553
Cdd:PRK10938 405 GQQ-RLALIVRALvKHPTLLILDEPLQGLD 433
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
415-577 |
3.49e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 52.01 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 415 GKDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR-----------------KHRTLrIGWFDQHAN 477
Cdd:PRK11248 13 GKPAL-EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITldgkpvegpgaergvvfQNEGL-LPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 478 EALNGEQTPVEFLCTKfnidyQEARKQLGTTGLAAhAHTVKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESI 557
Cdd:PRK11248 91 VAFGLQLAGVEKMQRL-----EIAHQMLKKVGLEG-AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180
....*....|....*....|....
gi 17559834 558 DALAEAI----RDFNGGVVMVTHD 577
Cdd:PRK11248 165 EQMQTLLlklwQETGKQVLLITHD 188
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
99-259 |
4.17e-07 |
|
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: 51.39 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLkhigarklaipSHIDLLY--CEQEIQVDSTSAIDTVVKSDKKRLALLEEEAKLMS- 175
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKSTVV-----------SLLERFYdpTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 176 ----EIEEGKTEAAerMKEVADELRDIGADSaeprarrILAGL--GFSKEMQEKPCTdFSGGWRMRISLARALFLEPTLL 249
Cdd:cd03249 92 tiaeNIRYGKPDAT--DEEVEEAAKKANIHD-------FIMSLpdGYDTLVGERGSQ-LSGGQKQRIAIARALLRNPKIL 161
|
170
....*....|
gi 17559834 250 MLDEPTNHLD 259
Cdd:cd03249 162 LLDEATSALD 171
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
79-283 |
4.28e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.40 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 79 DIKIeNFDIsAQGKLLF----------DKASLTIVYGRRYGLVGPNGMGKTTLlkhigARklaipshidllyceqeiqvd 148
Cdd:PRK15079 13 DLKV-HFDI-KDGKQWFwqppktlkavDGVTLRLYEGETLGVVGESGCGKSTF-----AR-------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 149 stsAIDTVVKSDKKRLALLEEEAKLMSEieegkteaaERMKEVADELRDIGADS--------------AEP--------- 205
Cdd:PRK15079 66 ---AIIGLVKATDGEVAWLGKDLLGMKD---------DEWRAVRSDIQMIFQDPlaslnprmtigeiiAEPlrtyhpkls 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 206 ------RARRILAGLGFSKEMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKK---- 275
Cdd:PRK15079 134 rqevkdRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemgl 213
|
....*...
gi 17559834 276 TLLIVSHD 283
Cdd:PRK15079 214 SLIFIAHD 221
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
80-314 |
4.73e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.33 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARklaipshidllyceQEIQVDSTSaidtVVKS 159
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGR--------------EDYEVTGGT----VEFK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 DKKRLALLEEEaklmsEIEEGKTEAAERMKEVADELRDIGADSA-----EPRARRILAGLGFSKEMQEK------PC--- 225
Cdd:PRK09580 64 GKDLLELSPED-----RAGEGIFMAFQYPVEIPGVSNQFFLQTAlnavrSYRGQEPLDRFDFQDLMEEKiallkmPEdll 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 226 -----TDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLD---NYLQTWKKTLLIVSHDQGFLDSVCTDIIHL 297
Cdd:PRK09580 139 trsvnVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAdgvNSLRDGKRSFIIVTHYQRILDYIKPDYVHV 218
|
250
....*....|....*..
gi 17559834 298 DNQKLHTYRGNYTLFKK 314
Cdd:PRK09580 219 LYQGRIVKSGDFTLVKQ 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
94-255 |
5.36e-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: 50.90 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 94 LFDkASLTIVYGRRYGLVGPNGMGKTTLLKHI--------------GARKLAIPSH----IDLLYCEQEIQVDSTSaidT 155
Cdd:cd03224 16 LFG-VSLTVPEGEIVALLGRNGAGKTTLLKTImgllpprsgsirfdGRDITGLPPHerarAGIGYVPEGRRIFPEL---T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 156 VvksdkkrlalleEEAKLMSEIEEGKTEAAERMKEVADELrdigadsaePRarrilagLgfsKEMQEKPCTDFSGGWRMR 235
Cdd:cd03224 92 V------------EENLLLGAYARRRAKRKARLERVYELF---------PR-------L---KERRKQLAGTLSGGEQQM 140
|
170 180
....*....|....*....|
gi 17559834 236 ISLARALFLEPTLLMLDEPT 255
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPS 160
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
99-305 |
5.75e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 51.24 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLKHIGarKLAIPShidllycEQEIQVDSTSAidtvvksdkkrlALLE---------- 168
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIA--GILEPT-------SGRVEVNGRVS------------ALLElgagfhpelt 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 169 --EEAKL------MSeieegKTEAAERMKEVADelrdigadsaeprarriLAGLGfskemqekpctDF--------SGGW 232
Cdd:COG1134 105 grENIYLngrllgLS-----RKEIDEKFDEIVE-----------------FAELG-----------DFidqpvktySSGM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 233 RMRISLARALFLEPTLLMLDEptnhldlnaviWL---DNYLQtwKK-------------TLLIVSHDQGFLDSVCTDIIH 296
Cdd:COG1134 152 RARLAFAVATAVDPDILLVDE-----------VLavgDAAFQ--KKclarirelresgrTVIFVSHSMGAVRRLCDRAIW 218
|
....*....
gi 17559834 297 LDNQKLHTY 305
Cdd:COG1134 219 LEKGRLVMD 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
424-582 |
5.86e-07 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 52.03 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 424 NFGVDMDSRI------AIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrIG---WFDQHANEALngeqtPVEflctKF 494
Cdd:COG4148 13 GFTLDVDFTLpgrgvtALFGPSGSGKTTLLRAIAGLERPDSGRIR------LGgevLQDSARGIFL-----PPH----RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 495 NIDY--QEAR-------------------KQLGTTGLAAHAHTVKIKD--------LSGGQKSRVALCNLALGGPDIIIL 545
Cdd:COG4148 78 RIGYvfQEARlfphlsvrgnllygrkrapRAERRISFDEVVELLGIGHlldrrpatLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17559834 546 DEPTNNLDIES----IDALAEAIRDFNGGVVMVTHD--------ERLVV 582
Cdd:COG4148 158 DEPLAALDLARkaeiLPYLERLRDELDIPILYVSHSldevarlaDHVVL 206
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
434-574 |
6.62e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 434 AIVGPNGVGKSTLLKLLIGKIDPNDGELRKH--RTLRIG-----------WfdQHANEALNGE------QTPVEFLC--T 492
Cdd:PRK10938 33 AFVGANGSGKSALARALAGELPLLSGERQSQfsHITRLSfeqlqklvsdeW--QRNNTDMLSPgeddtgRTTAEIIQdeV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 493 KFNIDYQEARKQLGTTGLAAHahtvKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFN-GGV 571
Cdd:PRK10938 111 KDPARCEQLAQQFGITALLDR----RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHqSGI 186
|
...
gi 17559834 572 VMV 574
Cdd:PRK10938 187 TLV 189
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
407-577 |
6.69e-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: 50.76 E-value: 6.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKD-VLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDG---------------ELRKhrtlRIG 470
Cdd:cd03295 3 FENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGeifidgedireqdpvELRR----KIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 471 WFDQ------HANEALNGEQTPVEFLCTKFNIDyQEARKQLGTTGLAAHAHTVKIKD-LSGGQKSRVALCNLALGGPDII 543
Cdd:cd03295 79 YVIQqiglfpHMTVEENIALVPKLLKWPKEKIR-ERADELLALVGLDPAEFADRYPHeLSGGQQQRVGVARALAADPPLL 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 17559834 544 ILDEPTNNLDIESIDALAEAI----RDFNGGVVMVTHD 577
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFkrlqQELGKTIVFVTHD 195
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
434-578 |
6.88e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 51.76 E-value: 6.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 434 AIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrigwFDQHANEALNGEQTPVEFLCTKF----------NIDYQEARK 503
Cdd:PRK11607 49 ALLGASGCGKSTLLRMLAGFEQPTAGQIM---------LDGVDLSHVPPYQRPINMMFQSYalfphmtveqNIAFGLKQD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 504 QLGTTGLAAHAHTV------------KIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGGV 571
Cdd:PRK11607 120 KLPKAEIASRVNEMlglvhmqefakrKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERV 199
|
170
....*....|.
gi 17559834 572 ----VMVTHDE 578
Cdd:PRK11607 200 gvtcVMVTHDQ 210
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
99-282 |
8.48e-07 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 52.09 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLKHIgARklaipshidlLY--CEQEIQVDSTSaIDTVVKSD-KKRLALLEEEAKLMS 175
Cdd:COG1132 360 SLTIPPGETVALVGPSGSGKSTLVNLL-LR----------FYdpTSGRILIDGVD-IRDLTLESlRRQIGVVPQDTFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 176 E-IEE----GKTEAAErmKEVADELRDIGADsaeprarRILAGL--GFSKEMQEKPcTDFSGGWRMRISLARALFLEPTL 248
Cdd:COG1132 428 GtIREniryGRPDATD--EEVEEAAKAAQAH-------EFIEALpdGYDTVVGERG-VNLSGGQRQRIAIARALLKDPPI 497
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17559834 249 LMLDEPTNHLD-------LNAviwLDNYLQtwKKTLLIVSH 282
Cdd:COG1132 498 LILDEATSALDtetealiQEA---LERLMK--GRTTIVIAH 533
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
420-578 |
9.31e-07 |
|
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: 50.42 E-value: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 420 FKKLNfGVDMDSR----IAIVGPNGVGKSTLLKLLIGKIDPNDGEL---------RKHRTLRIGWFDQH----------A 476
Cdd:cd03296 15 FVALD-DVSLDIPsgelVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggedatdVPVQERNVGFVFQHyalfrhmtvfD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 477 NEALNGEQTPVEFLCTKFNIDyQEARKQLGTTGLAAHAHTVKiKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIES 556
Cdd:cd03296 94 NVAFGLRVKPRSERPPEAEIR-AKVHELLKLVQLDWLADRYP-AQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKV 171
|
170 180
....*....|....*....|....*.
gi 17559834 557 IDALAEAIRDFNGGV----VMVTHDE 578
Cdd:cd03296 172 RKELRRWLRRLHDELhvttVFVTHDQ 197
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
99-282 |
1.08e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 51.65 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTT---LLKHigarkLAIPSHIDLLYCEQEI-QVDStsaidtvvKSDKKRLALLEEEAKLM 174
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTvaaLLQN-----LYQPTGGQVLLDGVPLvQYDH--------HYLHRQVALVGQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 175 S-----EIEEGKTEAaermkevadELRDIGADSAEPRARRILAGL--GFSKEMQEKPcTDFSGGWRMRISLARALFLEPT 247
Cdd:TIGR00958 568 SgsvreNIAYGLTDT---------PDEEIMAAAKAANAHDFIMEFpnGYDTEVGEKG-SQLSGGQKQRIAIARALVRKPR 637
|
170 180 190
....*....|....*....|....*....|....*....
gi 17559834 248 LLMLDEPTNHLDLNAviwlDNYLQTWKK----TLLIVSH 282
Cdd:TIGR00958 638 VLILDEATSALDAEC----EQLLQESRSrasrTVLLIAH 672
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
91-263 |
1.16e-06 |
|
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: 49.66 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 91 GKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLkhigaRKLAIPSHIDllycEQEIQVDSTsAIDTVVKSDKKRLALLEEE 170
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLL-----RILAGLLRPD----SGEVRWNGT-PLAEQRDEPHENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 171 AKLMSEIEegkteAAERMKEVADELRDIGADSAEPRARRILAGLgfskemQEKPCTDFSGGWRMRISLARALFLEPTLLM 250
Cdd:TIGR01189 82 PGLKPELS-----ALENLHFWAAIHGGAQRTIEDALAAVGLTGF------EDLPAAQLSAGQQRRLALARLWLSRRPLWI 150
|
170
....*....|...
gi 17559834 251 LDEPTNHLDLNAV 263
Cdd:TIGR01189 151 LDEPTTALDKAGV 163
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
109-295 |
1.19e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.71 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 109 GLVGPNGMGKTTLlkhigARKLA---------IPSHIDLLYCEQEIQVDSTsaiDTVvksdkkrlalleeEAKLMSEIEE 179
Cdd:COG1245 370 GIVGPNGIGKTTF-----AKILAgvlkpdegeVDEDLKISYKPQYISPDYD---GTV-------------EEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 180 G------KTEAAERMkevadelrdigadsaeprarrilaGLgfsKEMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDE 253
Cdd:COG1245 429 DfgssyyKTEIIKPL------------------------GL---EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17559834 254 PTNHLD----LNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDII 295
Cdd:COG1245 482 PSAHLDveqrLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
65-282 |
1.35e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 51.38 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 65 SKTGTQLAQMENSMDIKIENFDI-SAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIgarklaipshIDLLYCEQ 143
Cdd:PRK11174 335 PQQGEKELASNDPVTIEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL----------LGFLPYQG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 144 EIQVDSTSAIDTVVKSDKKRLALLEEE-----AKLMSEIEEGKTEAAErmKEVADELRDIGADSAEPRarriLAgLGFSK 218
Cdd:PRK11174 405 SLKINGIELRELDPESWRKHLSWVGQNpqlphGTLRDNVLLGNPDASD--EQLQQALENAWVSEFLPL----LP-QGLDT 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17559834 219 EMQEKPCTdFSGGWRMRISLARALFLEPTLLMLDEPTNHLDL---NAVIwldNYLQ--TWKKTLLIVSH 282
Cdd:PRK11174 478 PIGDQAAG-LSVGQAQRLALARALLQPCQLLLLDEPTASLDAhseQLVM---QALNaaSRRQTTLMVTH 542
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
404-584 |
1.58e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.17 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 404 VLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLK------------------------LLIGKIDPNdg 459
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndlipgfrvegkvtfhgknLYAPDVDPV-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 460 ELRKhrtlRIGWFDQHAN-------------EALNGEQTPVEFLCTKF---NIDYQEARKQLGTTGLAahahtvkikdLS 523
Cdd:PRK14243 88 EVRR----RIGMVFQKPNpfpksiydniaygARINGYKGDMDELVERSlrqAALWDEVKDKLKQSGLS----------LS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 524 GGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNG--GVVMVTHDERLVVRT 584
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTHNMQQAARV 216
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
84-283 |
1.59e-06 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 49.86 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 84 NFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLkHIGARKLAiPShidllycEQEIQVDSTsaidTVVKSDKKR 163
Cdd:COG4525 12 RYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLL-NLIAGFLA-PS-------SGEITLDGV----PVTGPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 164 LALLEEEAKL--MSEIEEgkteaaermkeVADELRDIGADSAE--PRARRILAGLGFsKEMQEKPCTDFSGGWRMRISLA 239
Cdd:COG4525 79 GVVFQKDALLpwLNVLDN-----------VAFGLRLRGVPKAErrARAEELLALVGL-ADFARRRIWQLSGGMRQRVGIA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17559834 240 RALFLEPTLLMLDEPTNHLD------LNAVIwldnyLQTWKKT---LLIVSHD 283
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDaltreqMQELL-----LDVWQRTgkgVFLITHS 194
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
433-577 |
1.65e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.35 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrigwfdQHANEALNGEQTPVEFLCTKFNIDYQEA------RKQLG 506
Cdd:PRK11308 44 LAVVGESGCGKSTLARLLTMIETPTGGELY-----------YQGQDLLKADPEAQKLLRQKIQIVFQNPygslnpRKKVG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 507 T---------TGLAAHAHTVKIKDL------------------SGGQKSRVALCNLALGGPDIIILDEPTNNLDIeSIDA 559
Cdd:PRK11308 113 QileepllinTSLSAAERREKALAMmakvglrpehydryphmfSGGQRQRIAIARALMLDPDVVVADEPVSALDV-SVQA 191
|
170 180
....*....|....*....|...
gi 17559834 560 -----LAEAIRDFNGGVVMVTHD 577
Cdd:PRK11308 192 qvlnlMMDLQQELGLSYVFISHD 214
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
426-583 |
1.70e-06 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 50.50 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 426 GVDMDSR----IAIVGPNGVGKSTLLKLLIGKIDPNDGELR---------KHRTLR--------IgwF-DQHAneALNGE 483
Cdd:COG4608 36 GVSFDIRrgetLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqditglSGRELRplrrrmqmV--FqDPYA--SLNPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 484 QT-------PVEFlctkFNIDYQEARKQ-----LGTTGL-AAHA----HtvkikDLSGGQKSRVALCN-LALGgPDIIIL 545
Cdd:COG4608 112 MTvgdiiaePLRI----HGLASKAERRErvaelLELVGLrPEHAdrypH-----EFSGGQRQRIGIARaLALN-PKLIVC 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17559834 546 DEPTNNLDIeSIDA-----LAEAIRDFNGGVVMVTHDerL-VVR 583
Cdd:COG4608 182 DEPVSALDV-SIQAqvlnlLEDLQDELGLTYLFISHD--LsVVR 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
84-282 |
1.71e-06 |
|
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: 48.46 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 84 NFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHI-GARKlaiPSHidllyceQEIQVDSTSaIDTVVKSDKK 162
Cdd:cd03247 7 SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLtGDLK---PQQ-------GEITLDGVP-VSDLEKALSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 163 RLALLEEEAKLMSeieegkteaaermkevaDELRDigadsaeprarrilaGLGfskemqekpcTDFSGGWRMRISLARAL 242
Cdd:cd03247 76 LISVLNQRPYLFD-----------------TTLRN---------------NLG----------RRFSGGERQRLALARIL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17559834 243 FLEPTLLMLDEPTNHLD-------LNAViwldnYLQTWKKTLLIVSH 282
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDpiterqlLSLI-----FEVLKDKTLIWITH 155
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
406-554 |
1.75e-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: 51.45 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 406 GLHDVNFG-YGKDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhrtlrigwfdqHANEALNGEQ 484
Cdd:TIGR01271 428 GLFFSNFSlYVTPVL-KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK------------HSGRISFSPQ 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 485 TPVEFLCT-----KFNIDYQEARK-------QL--GTTGLAAHAHTVKIK---DLSGGQKSRVALCNLALGGPDIIILDE 547
Cdd:TIGR01271 495 TSWIMPGTikdniIFGLSYDEYRYtsvikacQLeeDIALFPEKDKTVLGEggiTLSGGQRARISLARAVYKDADLYLLDS 574
|
....*..
gi 17559834 548 PTNNLDI 554
Cdd:TIGR01271 575 PFTHLDV 581
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
83-283 |
1.81e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.51 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 83 ENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIgarkLAIpshidllyceqeIQVDSTSAIdtvvkSDKK 162
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMV----VGI------------VPRDAGNII-----IDDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 163 RLALLEEEAKLMSEIEEGKTEAAE-RMKEVADEL-------RDIGADSAEPRARRILAGLGFSkEMQEKPCTDFSGGWRM 234
Cdd:PRK10895 66 DISLLPLHARARRGIGYLPQEASIfRRLSVYDNLmavlqirDDLSAEQREDRANELMEEFHIE-HLRDSMGQSLSGGERR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17559834 235 RISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKT---LLIVSHD 283
Cdd:PRK10895 145 RVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSglgVLITDHN 196
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
90-302 |
1.89e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 49.69 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 90 QGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLlkhigARKLaipshidlLYCEQEIQVDSTSAIDTVVKSDKKRLALLEE 169
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTL-----ARLL--------VGLESPSQGNVSWRGEPLAKLNRAQRKAFRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 170 EAKLMSEIEEGKTEAAERMKEVADE-LRDIGADSAEPRARRILAGL---GFSKEMQEKPCTDFSGGWRMRISLARALFLE 245
Cdd:PRK10419 90 DIQMVFQDSISAVNPRKTVREIIREpLRHLLSLDKAERLARASEMLravDLDDSVLDKRPPQLSGGQLQRVCLARALAVE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559834 246 PTLLMLDEPTNHLDLN---AVIWLDNYLQTWKKT-LLIVSHDQGFLDSVCTDIIHLDNQKL 302
Cdd:PRK10419 170 PKLLILDEAVSNLDLVlqaGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
425-577 |
1.96e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.88 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 425 FGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGElrkhrtlrIGWFDQHANEALngEQTPVEFLCTKFNIDY------ 498
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGK--------ISILGQPTRQAL--QKNLVAYVPQSEEVDWsfpvlv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 499 -----------------------QEARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIE 555
Cdd:PRK15056 98 edvvmmgryghmgwlrrakkrdrQIVTAALARVDMVEFRHR-QIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180
....*....|....*....|....*
gi 17559834 556 S---IDALAEAIRDFNGGVVMVTHD 577
Cdd:PRK15056 177 TearIISLLRELRDEGKTMLVSTHN 201
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
229-595 |
1.97e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.86 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEPTNHLDLN--AVIW--LDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKLHT 304
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSvqAQILqlLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 305 YRGNYTLF---KKQYAQdmqvheknfdqqqkQLKAMKKEGKSAKQAEEqvkqqmankakkggkknagkvnddddagAPEL 381
Cdd:PRK15134 238 QNRAATLFsapTHPYTQ--------------KLLNSEPSGDPVPLPEP----------------------------ASPL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 382 LQRRKeysVKFQFPETTKLNPPVLGLHDVnfgygkdvlFKKLNFGVDMDSRIAIVGPNGVGKST----LLKLLI--GKID 455
Cdd:PRK15134 276 LDVEQ---LQVAFPIRKGILKRTVDHNVV---------VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEIW 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 456 PNDGELRK--HRTL-----RIGWFDQHANEALNG----EQTPVEFLCT---KFNIDYQEAR--KQLGTTGLAAHAHTVKI 519
Cdd:PRK15134 344 FDGQPLHNlnRRQLlpvrhRIQVVFQDPNSSLNPrlnvLQIIEEGLRVhqpTLSAAQREQQviAVMEEVGLDPETRHRYP 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 520 KDLSGGQKSRVALCNLALGGPDIIILDEPTNNLD---IESIDALAEAIRDFNG-GVVMVTHDERlVVRTDCNLWVVENQG 595
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvQAQILALLKSLQQKHQlAYLFISHDLH-VVRALCHQVIVLRQG 502
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
82-260 |
1.97e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.79 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 82 IENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARKlaIPSHIDLLYCEQEIQVDSTsaidtvvKSDK 161
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQ--PPSEGEILLDAQPLESWSS-------KAFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 162 KRLALLEEEaklmseieegkTEAAERMkeVADELRDIG-------------ADSAEPRARRILAGLgfsKEMQEKPCTDF 228
Cdd:PRK10575 85 RKVAYLPQQ-----------LPAAEGM--TVRELVAIGrypwhgalgrfgaADREKVEEAISLVGL---KPLAHRLVDSL 148
|
170 180 190
....*....|....*....|....*....|..
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEPTNHLDL 260
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
79-282 |
2.09e-06 |
|
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: 49.15 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 79 DIKIENFDIS-AQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIgaRKLAIPSHIDLLYCEQEIQvdstsaiDTVV 157
Cdd:cd03254 2 EIEFENVNFSyDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLL--MRFYDPQKGQILIDGIDIR-------DISR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 158 KSDKKRLALLEEEAKL-----MSEIEEGKTEAaeRMKEVADELRDIGADsaeprarRILAGL--GFSKEMQEKPcTDFSG 230
Cdd:cd03254 73 KSLRSMIGVVLQDTFLfsgtiMENIRLGRPNA--TDEEVIEAAKEAGAH-------DFIMKLpnGYDTVLGENG-GNLSQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17559834 231 GWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKK--TLLIVSH 282
Cdd:cd03254 143 GERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKgrTSIIIAH 196
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
433-553 |
2.31e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.82 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIGKIDPN---------DGEL--RKHRTLRIGWFDQH--------ANEALN-------GEQTP 486
Cdd:TIGR00955 54 LAVMGSSGAGKTTLMNALAFRSPKGvkgsgsvllNGMPidAKEMRAISAYVQQDdlfiptltVREHLMfqahlrmPRRVT 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 487 VEflcTKfnidyQEARKQLGT-TGLAAHAHTV-----KIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLD 553
Cdd:TIGR00955 134 KK---EK-----RERVDEVLQaLGLRKCANTRigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
399-606 |
2.37e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 399 KLNPPVLgLHDVNFgygkDVLFKKLNfgvdmdsriAIVGPNGVGKSTLLKLLIGKIDPNDGELRKHR------------- 465
Cdd:PTZ00243 669 ELEPKVL-LRDVSV----SVPRGKLT---------VVLGATGSGKSTLLQSLLSQFEISEGRVWAERsiayvpqqawimn 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 466 -TLR--IGWFDQHANEALngeQTPVEflCTKFNIDYQearkQLGTtGLAAHAHTVKIkDLSGGQKSRVALCNLALGGPDI 542
Cdd:PTZ00243 735 aTVRgnILFFDEEDAARL---ADAVR--VSQLEADLA----QLGG-GLETEIGEKGV-NLSGGQKARVSLARAVYANRDV 803
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 543 IILDEPTNNLD-------IES--IDALAEAIRdfnggvVMVTHDERLVVRTDCnlWVVENQGIDEIDGDFEDY 606
Cdd:PTZ00243 804 YLLDDPLSALDahvgervVEEcfLGALAGKTR------VLATHQVHVVPRADY--VVALGDGRVEFSGSSADF 868
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
99-301 |
3.06e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.46 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQVDstsaidtvvksdKKRLALLEEEAKLMSEIE 178
Cdd:PRK13636 26 NINIKKGEVTAILGGNGAGKSTLFQNLNG--ILKPSSGRILFDGKPIDYS------------RKGLMKLRESVGMVFQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 179 EGKTEAAERMKEVADELRDIG--ADSAEPRARRILAGLGFSkEMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPTN 256
Cdd:PRK13636 92 DNQLFSASVYQDVSFGAVNLKlpEDEVRKRVDNALKRTGIE-HLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17559834 257 HLDLNAVIWLDNYLQTWKK----TLLIVSHDQGFLDSVCTDIIHLDNQK 301
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQKelglTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
80-283 |
3.44e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.08 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDiSAQGKLLFD-KASLTIvygrrygLVGPNGMGKTTLLKHI-----GARKLAIPSHIDLL-----YCEQEIQVD 148
Cdd:COG0419 5 LRLENFR-SYRDTETIDfDDGLNL-------IVGPNGAGKSTILEAIryalyGKARSRSKLRSDLInvgseEASVELEFE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 149 STSAIDTVVKSDKKRLALLEEEAKLMSEI--EEGKTEAAERMKEVADELRD-IGADSAEPRARRILAGLGFSKEMQEKPC 225
Cdd:COG0419 77 HGGKRYRIERRQGEFAEFLEAKPSERKEAlkRLLGLEIYEELKERLKELEEaLESALEELAELQKLKQEILAQLSGLDPI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17559834 226 TDFSGGWRMRISLARALfleptLLMLDepTNHLDLNAviwLDNYLQTwKKTLLIVSHD 283
Cdd:COG0419 157 ETLSGGERLRLALADLL-----SLILD--FGSLDEER---LERLLDA-LEELAIITHV 203
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
180-259 |
3.53e-06 |
|
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: 49.28 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 180 GKTEAAERMKEVADELRDIGADSAEPRARRilaglgFSKEmqekpctdFSGGWRMRISLARALFLEPTLLMLDEPTNHLD 259
Cdd:COG0444 117 GGLSKAEARERAIELLERVGLPDPERRLDR------YPHE--------LSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
409-576 |
3.54e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 48.93 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 409 DVNFGYGKD------VLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDG----------------ELRKhrt 466
Cdd:PRK13633 9 NVSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGkvyvdgldtsdeenlwDIRN--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 467 lRIGWFDQHANEALNGeqTPVE----FLCTKFNIDYQEAR-------KQLGTTGLAAHA-HTvkikdLSGGQKSRVALCN 534
Cdd:PRK13633 86 -KAGMVFQNPDNQIVA--TIVEedvaFGPENLGIPPEEIRervdeslKKVGMYEYRRHApHL-----LSGGQKQRVAIAG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17559834 535 LALGGPDIIILDEPTNNLD----IESIDALAEAIRDFNGGVVMVTH 576
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH 203
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
81-296 |
3.56e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 48.52 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 81 KIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIgarkLAIPSHI----DLLYCEQEIqvdstsaidtv 156
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL----MGHPKYEvtsgSILLDGEDI----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 157 vksdkkrLALL-EEEAKL---MS-----EIEeG-------KTEAAERMKEvadelrDIGADSAEPRARRILAGLGFSKEM 220
Cdd:COG0396 67 -------LELSpDERARAgifLAfqypvEIP-GvsvsnflRTALNARRGE------ELSAREFLKLLKEKMKELGLDEDF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 221 QEKPC-TDFSGGWRMRISLARALFLEPTLLMLDEPTNHLD---LNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIH 296
Cdd:COG0396 133 LDRYVnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDidaLRIVAEGVNKLRSPDRGILIITHYQRILDYIKPDFVH 212
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
499-576 |
3.92e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 49.08 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 499 QEARKQLGTTGLAAHAHTVKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDF---NGGVVMVT 575
Cdd:PRK13631 154 KLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkanNKTVFVIT 233
|
.
gi 17559834 576 H 576
Cdd:PRK13631 234 H 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
422-576 |
4.31e-06 |
|
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: 50.01 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 422 KLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGelrkhrTLRIGWFDQHANeaLNGEQTPVEfLCTKFNIDYQ-- 499
Cdd:TIGR01257 948 RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSG------TVLVGGKDIETN--LDAVRQSLG-MCPQHNILFHhl 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 500 ----------------------EARKQLGTTGLAaHAHTVKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESI 557
Cdd:TIGR01257 1019 tvaehilfyaqlkgrsweeaqlEMEAMLEDTGLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180
....*....|....*....|.
gi 17559834 558 DALAEAIRDFNGG--VVMVTH 576
Cdd:TIGR01257 1098 RSIWDLLLKYRSGrtIIMSTH 1118
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
72-284 |
4.42e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 49.18 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 72 AQMENSMDIKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARKLAIPSHIDLlyceQEIQVDSTS 151
Cdd:PRK09452 7 QPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIML----DGQDITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 152 A----IDTVVKSdkkrLALLEEeaklMSEIEegKTEAAERMKEVAdelrdigADSAEPRARRILAGLGFSKEMQEKPcTD 227
Cdd:PRK09452 83 AenrhVNTVFQS----YALFPH----MTVFE--NVAFGLRMQKTP-------AAEITPRVMEALRMVQLEEFAQRKP-HQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559834 228 FSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTLLI----VSHDQ 284
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGItfvfVTHDQ 205
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
205-291 |
4.54e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.95 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 205 PRARrilaglgfsKEMQEKPcTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNA---VIWLDNYLQTWKKTLLI-V 280
Cdd:PRK09473 149 PEAR---------KRMKMYP-HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELKREFNTAIImI 218
|
90
....*....|.
gi 17559834 281 SHDQGFLDSVC 291
Cdd:PRK09473 219 THDLGVVAGIC 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
435-587 |
4.72e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 49.03 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 435 IVGPNGVGKSTLLKLL-------IGKI--DPND------GELRKHRtLRIGWFDQH----------ANEALngeqtPVEF 489
Cdd:PRK11153 36 VIGASGAGKSTLIRCInllerptSGRVlvDGQDltalseKELRKAR-RQIGMIFQHfnllssrtvfDNVAL-----PLEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 490 LctkfNIDYQEARKQ----LGTTGLAAHAHTVKiKDLSGGQKSRVALCNlALG-GPDIIILDEPTNNLDIE---SI-DAL 560
Cdd:PRK11153 110 A----GTPKAEIKARvtelLELVGLSDKADRYP-AQLSGGQKQRVAIAR-ALAsNPKVLLCDEATSALDPAttrSIlELL 183
|
170 180
....*....|....*....|....*..
gi 17559834 561 AEAIRDFNGGVVMVTHdERLVVRTDCN 587
Cdd:PRK11153 184 KDINRELGLTIVLITH-EMDVVKRICD 209
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
85-259 |
5.22e-06 |
|
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: 48.25 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 85 FDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIgaRKLAIPSHIDLLYCEQEIQ-VDSTSAidtvvksdKKR 163
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLI--QRFYVPENGRVLVDGHDLAlADPAWL--------RRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 164 LALLEEEAKLMSeieegkteaaermKEVADELRDigADSAEPRARRI----LAGL-GFSKEMQEKPCT-------DFSGG 231
Cdd:cd03252 78 VGVVLQENVLFN-------------RSIRDNIAL--ADPGMSMERVIeaakLAGAhDFISELPEGYDTivgeqgaGLSGG 142
|
170 180
....*....|....*....|....*...
gi 17559834 232 WRMRISLARALFLEPTLLMLDEPTNHLD 259
Cdd:cd03252 143 QRQRIAIARALIHNPRILIFDEATSALD 170
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
80-282 |
5.71e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 47.99 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKhigarklaIPSHIDLLYCEQEIQVDSTSAIDTVVKS 159
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLR--------VFNRLIELYPEARVSGEVYLDGQDIFKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 DkkrLALLEEEAKLMSEIEE--------GKTEAAERMKEVADELRDIgadsaEPRARRILAGLGFSKEMQEK---PCTDF 228
Cdd:PRK14247 76 D---VIELRRRVQMVFQIPNpipnlsifENVALGLKLNRLVKSKKEL-----QERVRWALEKAQLWDEVKDRldaPAGKL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKK--TLLIVSH 282
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
111-284 |
5.94e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 48.87 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 111 VGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQvD---STSAIDTVVKSDK--KRLALLEEEAKLMSEIEEGKTEAA 185
Cdd:PRK11000 35 VGPSGCGKSTLLRMIAG--LEDITSGDLFIGEKRMN-DvppAERGVGMVFQSYAlyPHLSVAENMSFGLKLAGAKKEEIN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 186 ERMKEVADELRdigadsaeprarriLAGLgfskeMQEKPcTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLD----LN 261
Cdd:PRK11000 112 QRVNQVAEVLQ--------------LAHL-----LDRKP-KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQ 171
|
170 180
....*....|....*....|...
gi 17559834 262 AVIWLDNYLQTWKKTLLIVSHDQ 284
Cdd:PRK11000 172 MRIEISRLHKRLGRTMIYVTHDQ 194
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
407-611 |
6.14e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.47 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 407 LHDVNFGYGKDVLF--KKLNfGVDM---DSRIA-IVGPNGVGKSTLLKLLIG--------------KIDPNDGELRKHRT 466
Cdd:PRK13645 9 LDNVSYTYAKKTPFefKALN-NTSLtfkKNKVTcVIGTTGSGKSTMIQLTNGliisetgqtivgdyAIPANLKKIKEVKR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 467 LR--IGWFDQHANEALNGE--QTPVEFLCTKFNIDYQEARKQ----LGTTGLAAHAHTVKIKDLSGGQKSRVALCNLALG 538
Cdd:PRK13645 88 LRkeIGLVFQFPEYQLFQEtiEKDIAFGPVNLGENKQEAYKKvpelLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17559834 539 GPDIIILDEPTNNLDIES----IDALAEAIRDFNGGVVMVTHDERLVVRTDCNLWVVENQGIDEIDGDFEDYKKEVL 611
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQEL 244
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
434-580 |
7.12e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.33 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 434 AIVGPNGVGKSTLLKLLIGKIDPNDGELR-KHRTLrigwFDQHanealNGEQTPVEflctKFNIDY--QEARkqlgttgL 510
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVlNGRVL----FDAE-----KGICLPPE----KRRIGYvfQDAR-------L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 511 AAHaHTVK-----------------------IK--------DLSGGQKSRVALCNLALGGPDIIILDEPTNNLDI----E 555
Cdd:PRK11144 88 FPH-YKVRgnlrygmaksmvaqfdkivallgIEplldrypgSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrE 166
|
170 180
....*....|....*....|....*..
gi 17559834 556 SIDALAEAIRDFNGGVVMVTH--DERL 580
Cdd:PRK11144 167 LLPYLERLAREINIPILYVSHslDEIL 193
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
99-283 |
7.16e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 48.95 E-value: 7.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIqvdSTSAIDTVVKSDKKRLALLEEEAKLMSEIe 178
Cdd:PRK10535 28 SLDIYAGEMVAIVGASGSGKSTLMNILGC--LDKPTSGTYRVAGQDV---ATLDADALAQLRREHFGFIFQRYHLLSHL- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 179 egkteAAERMKEVADELRDIGADSAEPRARRILAGLGFSKEMQEKPcTDFSGGWRMRISLARALFLEPTLLMLDEPTNHL 258
Cdd:PRK10535 102 -----TAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180
....*....|....*....|....*...
gi 17559834 259 DLNA---VIWLDNYLQTWKKTLLIVSHD 283
Cdd:PRK10535 176 DSHSgeeVMAILHQLRDRGHTVIIVTHD 203
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
91-263 |
7.25e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 47.18 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 91 GKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQVDS-TSAIDTVVKSDKKRLALLEE 169
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAG--LLPPAAGTIKLDGGDIDDPDvAEACHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 170 E-----AKLMSEIEEGKTEAAERMKevadelrdigadsaeprarriLAGLGfskemqEKPCTDFSGGWRMRISLARALFL 244
Cdd:PRK13539 92 EnlefwAAFLGGEELDIAAALEAVG---------------------LAPLA------HLPFGYLSAGQKRRVALARLLVS 144
|
170
....*....|....*....
gi 17559834 245 EPTLLMLDEPTNHLDLNAV 263
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAV 163
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
98-283 |
7.38e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 48.49 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 98 ASLTIVYGRRYGLVGPNGMGKTTLLKHIGarKLAIPSHIDLLYCEQEIQVDSTSAIDTVvksDKKRLALLEEEAKLMSEI 177
Cdd:PRK10070 47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLN--RLIEPTRGQVLIDGVDIAKISDAELREV---RRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 178 ----------EEGKTEAAERMKEVADELRDIGADSAeprarrilaGLGFSKEMqekpctdfSGGWRMRISLARALFLEPT 247
Cdd:PRK10070 122 tvldntafgmELAGINAEERREKALDALRQVGLENY---------AHSYPDEL--------SGGMRQRVGLARALAINPD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17559834 248 LLMLDEPTNHLDLNAVIWLDNYL----QTWKKTLLIVSHD 283
Cdd:PRK10070 185 ILLMDEAFSALDPLIRTEMQDELvklqAKHQRTIVFISHD 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
433-579 |
7.82e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 47.58 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIG---------KIDPNDGELR--KHRTLR-IGWFDQHAN------------------EALNG 482
Cdd:PRK10895 32 VGLLGPNGAGKTTTFYMVVGivprdagniIIDDEDISLLplHARARRgIGYLPQEASifrrlsvydnlmavlqirDDLSA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 483 EQTP--VEFLCTKFNIDYqeARKQLGttglaahahtvkiKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLD-IESID- 558
Cdd:PRK10895 112 EQREdrANELMEEFHIEH--LRDSMG-------------QSLSGGERRRVEIARALAANPKFILLDEPFAGVDpISVIDi 176
|
170 180
....*....|....*....|..
gi 17559834 559 -ALAEAIRDFNGGVVMVTHDER 579
Cdd:PRK10895 177 kRIIEHLRDSGLGVLITDHNVR 198
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
194-283 |
7.96e-06 |
|
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: 48.02 E-value: 7.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 194 ELRDIGADSAEPRARRILAGLGFSKEMQEKPcTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDlnAVIWLDnyLQT- 272
Cdd:cd03294 128 EVQGVPRAEREERAAEALELVGLEGWEHKYP-DELSGGMQQRVGLARALAVDPDILLMDEAFSALD--PLIRRE--MQDe 202
|
90
....*....|....*...
gi 17559834 273 -------WKKTLLIVSHD 283
Cdd:cd03294 203 llrlqaeLQKTIVFITHD 220
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
404-579 |
7.96e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 7.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 404 VLGLHDVNFGYGKDVLFK-KLNFgvdMDSRIAIV-GPNGVGKSTLLKLLIGKIDPNDGELRKHrtlrigwfdqhaNEALN 481
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFDlSITF---LPSAITYIkGANGCGKSSLLRMIAGIMQPSSGNIYYK------------NCNIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 482 GEQTPvefLCT--------KFNIDYQEARKQLG-----TTGLAAHAHTVKIKD--------LSGGQKSRVALCNLALGGP 540
Cdd:PRK13541 66 NIAKP---YCTyighnlglKLEMTVFENLKFWSeiynsAETLYAAIHYFKLHDlldekcysLSSGMQKIVAIARLIACQS 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17559834 541 DIIILDEPTNNLDIESIDALAE--AIRDFNGGVVMV-THDER 579
Cdd:PRK13541 143 DLWLLDEVETNLSKENRDLLNNliVMKANSGGIVLLsSHLES 184
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
109-294 |
8.88e-06 |
|
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: 47.11 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 109 GLVGPNGMGKTTLLKHI-GARKlaiPSHIDLLYCEQEIQVDSTSAidtvvksdKKRL-------ALLE-----EEAKLMS 175
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLtGELR---PTSGTAYINGYSIRTDRKAA--------RQSLgycpqfdALFDeltvrEHLRFYA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 176 EIEeGKTEAaERMKEVADELRDIGadsaeprarrilaglgfSKEMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPT 255
Cdd:cd03263 101 RLK-GLPKS-EIKEEVELLLRVLG-----------------LTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17559834 256 NHLDLNA--VIWldNYLQTWKK--TLLIVSHDQGFLDSVCTDI 294
Cdd:cd03263 162 SGLDPASrrAIW--DLILEVRKgrSIILTTHSMDEAEALCDRI 202
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
99-254 |
1.04e-05 |
|
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: 47.15 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLKHI-GarkLAIPSHIDLLYCEQEIqvdSTSAIDTvvksdKKRLAL--LEEEAKLMS 175
Cdd:cd03218 20 SLSVKQGEIVGLLGPNGAGKTTTFYMIvG---LVKPDSGKILLDGQDI---TKLPMHK-----RARLGIgyLPQEASIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 176 E--IEEGKTEAAERMKEVADELRDigadsaepRARRILAGLGFSKeMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDE 253
Cdd:cd03218 89 KltVEENILAVLEIRGLSKKEREE--------KLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
.
gi 17559834 254 P 254
Cdd:cd03218 160 P 160
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
96-259 |
1.07e-05 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 48.56 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 96 DKASLTIVYGRRYGLVGPNGMGKTTLLKhigarklAIPS--HIDllycEQEIQVDSTSAIDTVVKSDKKRLALLEEEAKL 173
Cdd:TIGR02203 349 DSISLVIEPGETVALVGRSGSGKSTLVN-------LIPRfyEPD----SGQILLDGHDLADYTLASLRRQVALVSQDVVL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 174 MSE-----IEEGKTEAAERmKEVADELRDIGADS---AEPrarrilagLGFSKEMQEKPcTDFSGGWRMRISLARALFLE 245
Cdd:TIGR02203 418 FNDtiannIAYGRTEQADR-AEIERALAAAYAQDfvdKLP--------LGLDTPIGENG-VLLSGGQRQRLAIARALLKD 487
|
170
....*....|....
gi 17559834 246 PTLLMLDEPTNHLD 259
Cdd:TIGR02203 488 APILILDEATSALD 501
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
109-255 |
1.18e-05 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 46.90 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 109 GLVGPNGMGKTTLLK----HIGARKLAIpshidlLYCEQEIQVDSTSAIdtvVKsdkKRLALLEEEAKL---MSeIEE-- 179
Cdd:COG0410 33 ALLGRNGAGKTTLLKaisgLLPPRSGSI------RFDGEDITGLPPHRI---AR---LGIGYVPEGRRIfpsLT-VEEnl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 180 --------GKTEAAERMKEVADELrdigadsaePRarrilagLgfsKEMQEKPCTDFSGGWRMRISLARALFLEPTLLML 251
Cdd:COG0410 100 llgayarrDRAEVRADLERVYELF---------PR-------L---KERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
....
gi 17559834 252 DEPT 255
Cdd:COG0410 161 DEPS 164
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
195-283 |
1.25e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 46.70 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 195 LRDIGADSAEPRARRILAGLGFSKEMQEKPcTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYL---- 270
Cdd:PRK10584 115 LRGESSRQSRNGAKALLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfsln 193
|
90
....*....|...
gi 17559834 271 QTWKKTLLIVSHD 283
Cdd:PRK10584 194 REHGTTLILVTHD 206
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
409-612 |
1.33e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.49 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 409 DVNFGYG--KDV-LFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGEL-----RKHRTLRIGWFDQHANEAl 480
Cdd:PTZ00265 387 NVRFHYDtrKDVeIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindsHNLKDINLKWWRSKIGVV- 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 481 ngEQTPVEFLCT-KFNIDYQ----------------------------------------------------EARKQLGT 507
Cdd:PTZ00265 466 --SQDPLLFSNSiKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliEMRKNYQT 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 508 ---TGLAAHAHTVKIKD-------------------LSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIR 565
Cdd:PTZ00265 544 ikdSEVVDVSKKVLIHDfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN 623
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 566 DFNGG----VVMVTHdeRL-VVRTDCNLWVV---ENQGIDEIDGDFEDYKKEVLD 612
Cdd:PTZ00265 624 NLKGNenriTIIIAH--RLsTIRYANTIFVLsnrERGSTVDVDIIGEDPTKDNKE 676
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
203-299 |
1.35e-05 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 46.91 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 203 AEPRARRILAGLGFSKEMQEKPCTdFSGGWRMRISLARALFLEPTLLMLDEPTNHLD---LNAViwldnyLQTWKK---- 275
Cdd:COG1126 113 AEERAMELLERVGLADKADAYPAQ-LSGGQQQRVAIARALAMEPKVMLFDEPTSALDpelVGEV------LDVMRDlake 185
|
90 100
....*....|....*....|....*.
gi 17559834 276 --TLLIVSHDQGFLDSVCTDIIHLDN 299
Cdd:COG1126 186 gmTMVVVTHEMGFAREVADRVVFMDG 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
96-259 |
1.39e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 47.41 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 96 DKASLTIVYGRRYGLVGPNGMGKTTLLKHIgarklaipshIDLLYCEQ-EIQVDStSAIDtvvKSDKKRLALLEEEAKLM 174
Cdd:COG4152 18 DDVSFTVPKGEIFGLLGPNGAGKTTTIRII----------LGILAPDSgEVLWDG-EPLD---PEDRRRIGYLPEERGLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 175 SeieegkteaaeRMKeVAD------ELRDIGADSAEPRARRILAGLGFsKEMQEKPCTDFSGGWRMRISLARALFLEPTL 248
Cdd:COG4152 84 P-----------KMK-VGEqlvylaRLKGLSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170
....*....|.
gi 17559834 249 LMLDEPTNHLD 259
Cdd:COG4152 151 LILDEPFSGLD 161
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
435-547 |
1.39e-05 |
|
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: 47.87 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 435 IVGPNGVGKSTLLKLLIGKIDPNDGELR------------KHRTLrigwF-----DQHANEALNGEQTP-----VEFLCT 492
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILldgqpvtadnreAYRQL----FsavfsDFHLFDRLLGLDGEadparARELLE 438
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559834 493 KFNIDyqearkqlgttglaahaHTVKIKD-------LSGGQKSRVALCNLALGGPDIIILDE 547
Cdd:COG4615 439 RLELD-----------------HKVSVEDgrfsttdLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
105-283 |
1.50e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 46.99 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 105 GRRYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIqvdstsaidtvvKSDKKRLALLEEEAKLMSEIEEGKTEA 184
Cdd:PRK13639 28 GEMVALLGPNGAGKSTLFLHFNG--ILKPTSGEVLIKGEPI------------KYDKKSLLEVRKTVGIVFQNPDDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 185 AERMKEVADELRDIG--ADSAEPRARRILAGLGFSKeMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNA 262
Cdd:PRK13639 94 PTVEEDVAFGPLNLGlsKEEVEKRVKEALKAVGMEG-FENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180
....*....|....*....|....
gi 17559834 263 VIWLDNYLQTWKK---TLLIVSHD 283
Cdd:PRK13639 173 ASQIMKLLYDLNKegiTIIISTHD 196
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
419-583 |
1.51e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 46.96 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 419 LFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR--------KHRTLRIGWFDQHANEALNGEQ-TPVEF 489
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKvdgkvlyfGKDIFQIDAIKLRKEVGMVFQQpNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 490 LCTKFNIDY----------QEARK----QLGTTGLAAHAH---TVKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNL 552
Cdd:PRK14246 105 LSIYDNIAYplkshgikekREIKKiveeCLRKVGLWKEVYdrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190
....*....|....*....|....*....|...
gi 17559834 553 DIESIDALAEAIRDFNG--GVVMVTHDERLVVR 583
Cdd:PRK14246 185 DIVNSQAIEKLITELKNeiAIVIVSHNPQQVAR 217
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
522-577 |
1.62e-05 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 45.89 E-value: 1.62e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 17559834 522 LSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDF---NGGVVMVTHD 577
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELadaGKAVLLISSE 163
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
198-284 |
1.65e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 198 IGADSAEPRARRILAG-----LGFSKEMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLD-LNAVI---WLDN 268
Cdd:PRK10938 367 IGIYQAVSDRQQKLAQqwldiLGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDpLNRQLvrrFVDV 446
|
90
....*....|....*.
gi 17559834 269 YLQTWKKTLLIVSHDQ 284
Cdd:PRK10938 447 LISEGETQLLFVSHHA 462
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
418-577 |
1.74e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 46.62 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 418 VLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELR----------------------------------- 462
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILidgkdvtklpeykrakyigrvfqdpmmgtapsmti 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 463 -----------KHRTLRIGwfdqhaneaLNGEQTpvEFlctkfnidYQEARKQLGtTGLAAHAHTvKIKDLSGGQksRVA 531
Cdd:COG1101 100 eenlalayrrgKRRGLRRG---------LTKKRR--EL--------FRELLATLG-LGLENRLDT-KVGLLSGGQ--RQA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17559834 532 LCNL--ALGGPDIIILDEPTNNLDIES----IDALAEAIRDFNGGVVMVTHD 577
Cdd:COG1101 157 LSLLmaTLTKPKLLLLDEHTAALDPKTaalvLELTEKIVEENNLTTLMVTHN 208
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
92-259 |
1.79e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 47.00 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 92 KLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArkLAIPShidllycEQEIQVDStsaIDTvvkSDKKRLALLEEEA 171
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNA--LLIPS-------EGKVYVDG---LDT---SDEENLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 172 KLMSEIEEGKTEAAERMKEVADELRDIGADSAEPRAR--RILAGLGFSKEMQEKPCTdFSGGWRMRISLARALFLEPTLL 249
Cdd:PRK13633 88 GMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERvdESLKKVGMYEYRRHAPHL-LSGGQKQRVAIAGILAMRPECI 166
|
170
....*....|
gi 17559834 250 MLDEPTNHLD 259
Cdd:PRK13633 167 IFDEPTAMLD 176
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
79-262 |
1.80e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 47.88 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 79 DIKIENFDI-SAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHI------GARKLAIPSHIDLLYCEQEI------ 145
Cdd:COG4178 362 ALALEDLTLrTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpyGSGRIARPAGARVLFLPQRPylplgt 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 146 ---QVDSTSAIDTVvkSDKKRLALLEEeAKLmseieegkTEAAERMKEVADelrdigadsaeprARRILaglgfskemqe 222
Cdd:COG4178 442 lreALLYPATAEAF--SDAELREALEA-VGL--------GHLAERLDEEAD-------------WDQVL----------- 486
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17559834 223 kpctdfSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNA 262
Cdd:COG4178 487 ------SLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN 520
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
95-283 |
1.94e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.46 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 95 FDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARkLAiPSHIDLLYCEQEIQVDSTSAIdtvvkSDKKRLALLEEE---- 170
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSAR-LA-PDAGEVHYRMRDGQLRDLYAL-----SEAERRRLLRTEwgfv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 171 -----AKLMSEIEEGkTEAAERMKEVAD----ELRDIGADSAE----PRARrilaglgfskeMQEKPCTdFSGGWRMRIS 237
Cdd:PRK11701 95 hqhprDGLRMQVSAG-GNIGERLMAVGArhygDIRATAGDWLErveiDAAR-----------IDDLPTT-FSGGMQQRLQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17559834 238 LARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTL----LIVSHD 283
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglavVIVTHD 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
96-258 |
2.49e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.13 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 96 DKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARKLAIPSHIDLLYCEQEIQVDSTSaiDTvvksDKKRLALLEEEAKLMS 175
Cdd:TIGR02633 18 DGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIR--DT----ERAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 176 EIEegkteAAERMKeVADELRDIGADSAEP----RARRILAGLGFSKEMQEKPCTDFSGGWRMRISLARALFLEPTLLML 251
Cdd:TIGR02633 92 ELS-----VAENIF-LGNEITLPGGRMAYNamylRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLIL 165
|
....*..
gi 17559834 252 DEPTNHL 258
Cdd:TIGR02633 166 DEPSSSL 172
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
434-576 |
2.58e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 434 AIVGPNGVGKSTLLKLLIGKIDPNDGELR---KHRTLR---------IGWFDQHANeaLNGEQTPVE--FLCTKF----- 494
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILylgKEVTFNgpkssqeagIGIIHQELN--LIPQLTIAEniFLGREFvnrfg 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 495 NID----YQEARKQLGTTGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNL-DIESiDALAEAIRDF-- 567
Cdd:PRK10762 112 RIDwkkmYAEADKLLARLNLRFSSDK-LVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTET-ESLFRVIRELks 189
|
170
....*....|
gi 17559834 568 -NGGVVMVTH 576
Cdd:PRK10762 190 qGRGIVYISH 199
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
414-554 |
2.96e-05 |
|
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: 46.39 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 414 YGKDVLfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRkhRTLRIGWFDQHAnEALNGeqTPVEFLCtk 493
Cdd:cd03291 48 VGAPVL-KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK--HSGRISFSSQFS-WIMPG--TIKENII-- 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 494 FNIDYQEARK-------QL--GTTGLAAHAHTVKIK---DLSGGQKSRVALCNLALGGPDIIILDEPTNNLDI 554
Cdd:cd03291 120 FGVSYDEYRYksvvkacQLeeDITKFPEKDNTVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
99-284 |
3.06e-05 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 46.60 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLKHIgarklaipshidllyceqeiqvdstsaidtvvksdkkrlALLEEeaklmseIE 178
Cdd:COG3839 23 DLDIEDGEFLVLLGPSGCGKSTLLRMI---------------------------------------AGLED-------PT 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 179 EGK----------TEAAER--------------MKeVAD------ELRDIGADSAEPRARRILAGLGFSKEMQEKPcTDF 228
Cdd:COG3839 57 SGEiliggrdvtdLPPKDRniamvfqsyalyphMT-VYEniafplKLRKVPKAEIDRRVREAAELLGLEDLLDRKP-KQL 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEPTNHLD----LNAVIWLDNYLQTWKKTLLIVSHDQ 284
Cdd:COG3839 135 SGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHDQ 194
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
227-297 |
3.13e-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: 44.87 E-value: 3.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 227 DFSGGWRMRISLARALFLEPTLLMLDEPTNHLD----LNAVIWLDNYLQTWKKTLLIVSHDQGFLDSVcTDIIHL 297
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNAARAIRRLSEEGKKTALVVEHDLAVLDYL-SDRIHV 144
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
434-583 |
3.55e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.97 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 434 AIVGPNGVGKSTLLKLLIGKIdPNDGELRKHRTlrigwfdqHANEALNGEQ----TPVEFLCTK------------FNID 497
Cdd:PRK13547 31 ALLGRNGAGKSTLLKALAGDL-TGGGAPRGARV--------TGDVTLNGEPlaaiDAPRLARLRavlpqaaqpafaFSAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 498 -------YQEARKQLGTT----GLA------AHAHTVKIKD---LSGGQKSRV----ALCNL-----ALGGPDIIILDEP 548
Cdd:PRK13547 102 eivllgrYPHARRAGALThrdgEIAwqalalAGATALVGRDvttLSGGELARVqfarVLAQLwpphdAAQPPRYLLLDEP 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 17559834 549 TNNLDIESIDALAEAI----RDFNGGVVMVTHDERLVVR 583
Cdd:PRK13547 182 TAALDLAHQHRLLDTVrrlaRDWNLGVLAIVHDPNLAAR 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
229-259 |
3.55e-05 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 44.85 E-value: 3.55e-05
10 20 30
....*....|....*....|....*....|.
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEPTNHLD 259
Cdd:cd03213 113 SGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
82-288 |
3.71e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 45.33 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 82 IENFDIS--AQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIgarklaipshIDLLYCEQEiqvdsTSAIDTVVKS 159
Cdd:COG2401 31 LEAFGVElrVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL----------AGALKGTPV-----AGCVDVPDNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 DKKRLALLEeeaklmseieegkteaaermkevadelrDIGADSAEPRARRILAGLGFS---------KEMqekpctdfSG 230
Cdd:COG2401 96 FGREASLID----------------------------AIGRKGDFKDAVELLNAVGLSdavlwlrrfKEL--------ST 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559834 231 GWRMRISLARALFLEPTLLMLDEPTNHLD-LNAVIWLDNYLQTWKK---TLLIVSHDQGFLD 288
Cdd:COG2401 140 GQKFRFRLALLLAERPKLLVIDEFCSHLDrQTAKRVARNLQKLARRagiTLVVATHHYDVID 201
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
522-593 |
3.88e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.62 E-value: 3.88e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17559834 522 LSGGQKSRVALCNLALGGPDIIILDEPTNNLDIeSIDA-----LAEAIRDFNGGVVMVTHDERLVVRTDCNLWVVEN 593
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDV-SVQAqilqlLRELQQELNMGLLFITHNLSIVRKLADRVAVMQN 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
110-303 |
4.51e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 45.25 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 110 LVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQVDSTSAIDTVvksdKKRLALLEEEAKLMSEieegkteaAERMK 189
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICG--IERPSAGKIWFSGHDITRLKNREVPFL----RRQIGMIFQDHHLLMD--------RTVYD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 190 EVADELRDIGADSAEPRaRRILAGL---GFSKEMQEKPcTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLD---LNAV 263
Cdd:PRK10908 99 NVAIPLIIAGASGDDIR-RRVSAALdkvGLLDKAKNFP-IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17559834 264 IWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKLH 303
Cdd:PRK10908 177 LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
409-576 |
4.64e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.22 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 409 DVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDgELRKHRTLRIGWFDQHANEALNGE----- 483
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNE-EARVEGEVRLFGRNIYSPDVDPIEvrrev 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 484 ----QTPVEF----------LCTKFNiDYQEARKQLGTT---GLAAHAHTVKIKD--------LSGGQKSRVALCNLALG 538
Cdd:PRK14267 88 gmvfQYPNPFphltiydnvaIGVKLN-GLVKSKKELDERvewALKKAALWDEVKDrlndypsnLSGGQRQRLVIARALAM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17559834 539 GPDIIILDEPTNNLDIESIDALAEAIRDFNG--GVVMVTH 576
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
99-323 |
4.99e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.85 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLK-----------HI---G----ARKLAIPSHI------------DLlyceqeiqvd 148
Cdd:COG4586 42 SFTIEPGEIVGFIGPNGAGKSTTIKmltgilvptsgEVrvlGyvpfKRRKEFARRIgvvfgqrsqlwwDL---------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 149 stSAIDTvvksdkkrLALLeeeaKLMSEIEEgkTEAAERMKEVADELrDIGadsaeprarRILaglgfskemqEKPCTDF 228
Cdd:COG4586 112 --PAIDS--------FRLL----KAIYRIPD--AEYKKRLDELVELL-DLG---------ELL----------DTPVRQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEPTNHLDLNA--VIW--LDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKLhT 304
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSkeAIRefLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI-I 234
|
250
....*....|....*....
gi 17559834 305 YRGNYTLFKKQYAQDMQVH 323
Cdd:COG4586 235 YDGSLEELKERFGPYKTIV 253
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
228-282 |
5.22e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 5.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 17559834 228 FSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWK----KTLLIVSH 282
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdkadKTIITIAH 1417
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
228-299 |
5.26e-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: 44.07 E-value: 5.26e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559834 228 FSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTLLIVSHDQGfLDSVCTDIIHLDN 299
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGHRPS-LWKFHDRVLDLDG 162
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
110-282 |
5.63e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 45.15 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 110 LVGPNGMGKTTLLKHIGARKLAIPS-----HIDL----LYCEQEIQVDSTSAIDTVVKSDKK-------------RLALL 167
Cdd:PRK14239 36 LIGPSGSGKSTLLRSINRMNDLNPEvtitgSIVYnghnIYSPRTDTVDLRKEIGMVFQQPNPfpmsiyenvvyglRLKGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 168 EEEAKLMSEIEEGKTEAAermkeVADELRDIGADSAeprarrilagLGFSkemqekpctdfsGGWRMRISLARALFLEPT 247
Cdd:PRK14239 116 KDKQVLDEAVEKSLKGAS-----IWDEVKDRLHDSA----------LGLS------------GGQQQRVCIARVLATSPK 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 17559834 248 LLMLDEPTNHLDLNAVIWLDNYLQTWKK--TLLIVSH 282
Cdd:PRK14239 169 IILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTR 205
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
215-349 |
5.70e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 46.48 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 215 GFSKEMQEKPcTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLD-------LNAVIWLDNYLQTwkKTLLIVSHDQGFL 287
Cdd:TIGR00957 749 GDRTEIGEKG-VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkhiFEHVIGPEGVLKN--KTRILVTHGISYL 825
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 288 DSVCTDIIHLDN--------QKLHTYRGNYTLFKKQYAQDmqvhEKNFDQQQKQLKAMKKEGKSAKQAEE 349
Cdd:TIGR00957 826 PQVDVIIVMSGGkisemgsyQELLQRDGAFAEFLRTYAPD----EQQGHLEDSWTALVSGEGKEAKLIEN 891
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
395-553 |
5.77e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 45.71 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 395 PETTKLNPPVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELrkhrtlrigwfdq 474
Cdd:PRK09452 5 NKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 475 haneALNG--------EQTPVEflcTKF-------------NIDY----------------QEARKQLGTTGLAAHahtv 517
Cdd:PRK09452 72 ----MLDGqdithvpaENRHVN---TVFqsyalfphmtvfeNVAFglrmqktpaaeitprvMEALRMVQLEEFAQR---- 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 17559834 518 KIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLD 553
Cdd:PRK09452 141 KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
74-315 |
6.16e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 45.38 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 74 MENSMDIKIENFDISAQGKLLF-----DKASLTIVYGRRYGLVGPNGMGKTTLLKHIGArklaipshidLLYCEQEIQVD 148
Cdd:PRK13645 1 FDFSKDIILDNVSYTYAKKTPFefkalNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNG----------LIISETGQTIV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 149 STSAIDTVVKSDKKrLALLEEEAKLMSEIEEGKTEAAERMKEVADELRDIGADSAE--PRARRILAGLGFSKEMQEKPCT 226
Cdd:PRK13645 71 GDYAIPANLKKIKE-VKRLRKEIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEayKKVPELLKLVQLPEDYVKRSPF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 227 DFSGGWRMRISLARALFLEPTLLMLDEPTNHLD-------LNAVIWLDnylQTWKKTLLIVSHDQGFLDSVCTDIIHLDN 299
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDpkgeedfINLFERLN---KEYKKRIIMVTHNMDQVLRIADEVIVMHE 226
|
250
....*....|....*.
gi 17559834 300 QKLHTYRGNYTLFKKQ 315
Cdd:PRK13645 227 GKVISIGSPFEIFSNQ 242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
523-583 |
6.28e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 6.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 523 SGGQKS------RVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDF--------NGGVVMVTHDERLVVR 583
Cdd:TIGR00606 1201 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIiksrsqqrNFQLLVITHDEDFVEL 1275
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
94-259 |
6.80e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 94 LFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIgaRKLAIP---------SH----IDLLYCEQEIQVDS------TSAID 154
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLI--ERLYDPtegdiiindSHnlkdINLKWWRSKIGVVSqdpllfSNSIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 155 TVVK----SDKKRLALLEEEAKLMSEIEEGKTEAAERMKEVADELRDIGAD----------------------------- 201
Cdd:PTZ00265 478 NNIKyslySLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTtdsneliemrknyqtikdsevvdvskkvl 557
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 202 -----SAEPRARRILAGLGFSKemqekpctdFSGGWRMRISLARALFLEPTLLMLDEPTNHLD 259
Cdd:PTZ00265 558 ihdfvSALPDKYETLVGSNASK---------LSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
434-565 |
7.47e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 44.16 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 434 AIVGPNGVGKSTLLKLL-----IGKIDPN---DG-ELRKHRTLRIGWFDQhaNEALNGEQTPVEFLctKFnidyqearkq 504
Cdd:cd03232 37 ALMGESGAGKTTLLDVLagrktAGVITGEiliNGrPLDKNFQRSTGYVEQ--QDVHSPNLTVREAL--RF---------- 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559834 505 lgttglaaHAhtvKIKDLSGGQKSRVAL-CNLAlGGPDIIILDEPTNNLDIESIDALAEAIR 565
Cdd:cd03232 103 --------SA---LLRGLSVEQRKRLTIgVELA-AKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
433-577 |
9.31e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.85 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLK----LLIGKIDpNDGELRKH-------------------RTLRIGWFDQHANEALNGEQTPV-E 488
Cdd:COG0419 26 NLIVGPNGAGKSTILEairyALYGKAR-SRSKLRSDlinvgseeasvelefehggKRYRIERRQGEFAEFLEAKPSERkE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 489 FLCTKFNID-YQEARKQLG--TTGLAAHAHTVK------------------IKDLSGGQKSRVALCNLALggpdiIILDe 547
Cdd:COG0419 105 ALKRLLGLEiYEELKERLKelEEALESALEELAelqklkqeilaqlsgldpIETLSGGERLRLALADLLS-----LILD- 178
|
170 180 190
....*....|....*....|....*....|
gi 17559834 548 pTNNLDIESIDALAEAIRDfnggVVMVTHD 577
Cdd:COG0419 179 -FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
227-287 |
9.38e-05 |
|
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: 44.24 E-value: 9.38e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 227 DFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDN-----YLQTWKKTLLIVSHDQGFL 287
Cdd:cd03290 140 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegilkFLQDDKRTLVLVTHKLQYL 205
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
99-282 |
9.41e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 44.19 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 99 SLTIVYGRRYGLVGPNGMGKTTLLKHIgARKLAiPSHIDLLYCEQeiqvDSTSAidtvvKSDKKRLALLEEEAKLMSE-- 176
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLI-AGFLT-PASGSLTLNGQ----DHTTT-----PPSRRPVSMLFQENNLFSHlt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 177 IEEG---------KTEAAERmkevaDELRDIgadsaeprARRIlaglGFSKEMQEKPcTDFSGGWRMRISLARALFLEPT 247
Cdd:PRK10771 88 VAQNiglglnpglKLNAAQR-----EKLHAI--------ARQM----GIEDLLARLP-GQLSGGQRQRVALARCLVREQP 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 17559834 248 LLMLDEPTNHLD--LNAVI--WLDNYLQTWKKTLLIVSH 282
Cdd:PRK10771 150 ILLLDEPFSALDpaLRQEMltLVSQVCQERQLTLLMVSH 188
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
522-592 |
9.76e-05 |
|
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: 43.47 E-value: 9.76e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 522 LSGGQKSRVALCN-LALG-GPDIIILDEPTNNLDIESIDALAEAIR---DFNGGVVMVTHDERLVVRTDcnlWVVE 592
Cdd:cd03238 88 LSGGELQRVKLASeLFSEpPGTLFILDEPSTGLHQQDINQLLEVIKgliDLGNTVILIEHNLDVLSSAD---WIID 160
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
80-302 |
1.12e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 44.31 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLfDKASLTIVYGRRYGLVGPNGMGKTtlLKHIGARKLAIPShidllyceqeiqVDSTSAidtVVKS 159
Cdd:PRK10418 5 IELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAG------------VRQTAG---RVLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 DKKRLALLEEEAKLMSEIEEGKTEAAERMKEVADELRDIGADSAEPRARRIL------AGLGFSKEMQEKPCTDFSGGWR 233
Cdd:PRK10418 67 DGKPVAPCALRGRKIATIMQNPRSAFNPLHTMHTHARETCLALGKPADDATLtaaleaVGLENAARVLKLYPFEMSGGML 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 234 MRISLARALFLEPTLLMLDEPTNHLDLNA----VIWLDNYLQTWKKTLLIVSHDQGFLDSVCTDIIHLDNQKL 302
Cdd:PRK10418 147 QRMMIALALLCEAPFIIADEPTTDLDVVAqariLDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
36-282 |
1.40e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 45.12 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 36 LPEVEGDQEEHGGIGSGAELGAHFTVSQLSKTGTQLAQMENSmdIKIENFD-ISAQGKLLFDKASLTIVYGRRYGLVGPN 114
Cdd:TIGR00954 410 LDDVKSGNFKRPRVEEIESGREGGRNSNLVPGRGIVEYQDNG--IKFENIPlVTPNGDVLIESLSFEVPSGNNLLICGPN 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 115 GMGKTTLLKHIG------ARKLAIPSHIDLLYCEQEIQVDSTSAIDTVV----KSDKKRLALLEEEAKLMSEI------- 177
Cdd:TIGR00954 488 GCGKSSLFRILGelwpvyGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIIypdsSEDMKRRGLSDKDLEQILDNvqlthil 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 178 -EEGKTEAAERMKEVadelrdigadsaeprarrilaglgfskemqekpctdFSGGWRMRISLARALFLEPTLLMLDEPTN 256
Cdd:TIGR00954 568 eREGGWSAVQDWMDV------------------------------------LSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
250 260
....*....|....*....|....*.
gi 17559834 257 HLDLNAVIWLDNYLQTWKKTLLIVSH 282
Cdd:TIGR00954 612 AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
229-321 |
1.59e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 44.82 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEPTNHLDlnAV----IwLDNYLQTWK-KTLLIVSHDQGFLDSVctDIIHL-DNQKL 302
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLD--AEterqI-LELLAEHAQnKTVLMITHRLTGLEQF--DRICVmDNGQI 551
|
90 100
....*....|....*....|..
gi 17559834 303 HTYrGNY-TLFKKQ--YAQDMQ 321
Cdd:PRK11160 552 IEQ-GTHqELLAQQgrYYQLKQ 572
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
226-282 |
1.75e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 43.68 E-value: 1.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 17559834 226 TDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKK--TLLIVSH 282
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
80-283 |
1.97e-04 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 43.53 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLkHIGARKLAIPShidllyceQEIQVDSTSAIDTvvKS 159
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLL-SMISRLLPPDS--------GEVLVDGLDVATT--PS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 160 DK--KRLALLEEEAKLMSEI--EE-----------GK-TEAAERMKEVADELRDIGadsaeprarrilaglgfskEMQEK 223
Cdd:COG4604 71 RElaKRLAILRQENHINSRLtvRElvafgrfpyskGRlTAEDREIIDEAIAYLDLE-------------------DLADR 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559834 224 PCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQ----TWKKTLLIVSHD 283
Cdd:COG4604 132 YLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRrladELGKTVVIVLHD 195
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
421-593 |
1.99e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 44.25 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 421 KKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDP---------------NDGELRKHRTLRIGWFDQhaNEALNGEQT 485
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPtrgqvlidgvdiakiSDAELREVRRKKIAMVFQ--SFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 486 PVEflCTKFNIDY---------QEARKQLGTTGLAAHAHTVKiKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLD--- 553
Cdd:PRK10070 123 VLD--NTAFGMELaginaeerrEKALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEAFSALDpli 199
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17559834 554 -IESIDALAEAIRDFNGGVVMVTHDERLVVRTDCNLWVVEN 593
Cdd:PRK10070 200 rTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
520-585 |
2.02e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 2.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 520 KDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDF----NGGVVMVTHDERLVVRTD 585
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdkaDKTIITIAHRIASIKRSD 1426
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
201-283 |
2.64e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.08 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 201 DSAEPRARRILAGLGFSKEMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTL--- 277
Cdd:PRK10261 437 KAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFgia 516
|
....*..
gi 17559834 278 -LIVSHD 283
Cdd:PRK10261 517 yLFISHD 523
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
189-583 |
2.86e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.08 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 189 KEVADELR---DIGADSAEPRARRILAGLGF--SKEMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLN-- 261
Cdd:PRK10261 125 EQIAESIRlhqGASREEAMVEAKRMLDQVRIpeAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiq 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 262 -AVIWLDNYLQT-WKKTLLIVSHDQGfldsVCTDIIhldNQKLHTYRGNytlfkkqyAQDMQVHEKNFDQQQK------- 332
Cdd:PRK10261 205 aQILQLIKVLQKeMSMGVIFITHDMG----VVAEIA---DRVLVMYQGE--------AVETGSVEQIFHAPQHpytrall 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 333 ----QLKAMKKEG----------KSAKQAEEQVKQqmankakkggkknagkvnDDDDAGAPeLLQRRKEYSvkfQFP-ET 397
Cdd:PRK10261 270 aavpQLGAMKGLDyprrfplislEHPAKQEPPIEQ------------------DTVVDGEP-ILQVRNLVT---RFPlRS 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 398 TKLNPPVLGLHDVnfgygkdvlfKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGEL------------RKHR 465
Cdd:PRK10261 328 GLLNRVTREVHAV----------EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIifngqridtlspGKLQ 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 466 TLR--IGWFDQHANEALNGEQTP----VEFLCTKFNIDYQEARKQ----LGTTGLAAHAHTVKIKDLSGGQKSRVALCN- 534
Cdd:PRK10261 398 ALRrdIQFIFQDPYASLDPRQTVgdsiMEPLRVHGLLPGKAAAARvawlLERVGLLPEHAWRYPHEFSGGQRQRICIARa 477
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 17559834 535 LALgGPDIIILDEPTNNLDI----ESIDALAEAIRDFNGGVVMVTHDERLVVR 583
Cdd:PRK10261 478 LAL-NPKVIIADEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHDMAVVER 529
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
434-497 |
2.96e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 43.15 E-value: 2.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 434 AIVGPNGVGKSTLLKLL--IGKIDPNDGELRKHRTLRIGWFDQHANEALNGEQTPVEFLCTKFNID 497
Cdd:pfam13304 3 VLIGPNGSGKSNLLEALrfLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLED 68
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
229-266 |
3.04e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 43.71 E-value: 3.04e-04
10 20 30
....*....|....*....|....*....|....*...
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWL 266
Cdd:PLN03211 208 SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
107-259 |
3.23e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 42.87 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 107 RYGLVGPNGMGKTTLLKHIGArkLAIPSHIDLLYCEQEIQVDSTSAIDTVVKsdkkrLALLEEEAKLMSEIEEgkteaae 186
Cdd:PRK13652 32 RIAVIGPNGAGKSTLFRHFNG--ILKPTSGSVLIRGEPITKENIREVRKFVG-----LVFQNPDDQIFSPTVE------- 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559834 187 rmKEVADELRDIGADSA--EPRARRILAGLGFSkEMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLD 259
Cdd:PRK13652 98 --QDIAFGPINLGLDEEtvAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
398-464 |
3.23e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 41.76 E-value: 3.23e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17559834 398 TKLNPPVLGLhDVNFGYGKDVLFKKLNfgvdmDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKH 464
Cdd:pfam03193 80 RAIGYPVLFV-SAKTGEGIEALKELLK-----GKTTVLAGQSGVGKSTLLNALLPELDLRTGEISEK 140
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
521-598 |
3.65e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 42.76 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 521 DLSGG--QKSRVALCNLAlGGPdIIILDEPTNNLDIES----IDALAEAIRDFNGGVVMVTHDERLVVRTDCNLWVVENQ 594
Cdd:PRK10418 140 EMSGGmlQRMMIALALLC-EAP-FIIADEPTTDLDVVAqariLDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHG 217
|
....
gi 17559834 595 GIDE 598
Cdd:PRK10418 218 RIVE 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
109-283 |
3.82e-04 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 43.17 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 109 GLVGPNGMGKTTLLKHI-GarkLAIPS--HIDLlycEQEIQVDSTSAIDtvVKSDKKRLALLEEEAKL---MSeieegkt 182
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIaG---LERPDsgRIRL---GGEVLQDSARGIF--LPPHRRRIGYVFQEARLfphLS------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 183 eaaermkeVADEL----RDIGADSAEPRARRILAGLGFSKEMQEKPcTDFSGGWRMRISLARALFLEPTLLMLDEPtnhl 258
Cdd:COG4148 94 --------VRGNLlygrKRAPRAERRISFDEVVELLGIGHLLDRRP-ATLSGGERQRVAIGRALLSSPRLLLMDEP---- 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 17559834 259 dLNAviwLDN--------YLQTWKKTL----LIVSHD 283
Cdd:COG4148 161 -LAA---LDLarkaeilpYLERLRDELdipiLYVSHS 193
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
105-296 |
3.88e-04 |
|
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: 42.74 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 105 GRRYGLVGPNGMGKTTLLKhIGARKLaIPShidllYCEQEIQVDSTSAID-----------TVVKSDKKRLALLEEEAKL 173
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALK-ILAGKL-KPN-----LGKFDDPPDWDEILDefrgselqnyfTKLLEGDVKVIVKPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 174 MSEIEEGKTEAAERMKEVADELRDIgADSAEPRarrilaglgfskEMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDE 253
Cdd:cd03236 99 IPKAVKGKVGELLKKKDERGKLDEL-VDQLELR------------HVLDRNIDQLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17559834 254 PTNHLD----LNAVIwLDNYLQTWKKTLLIVSHDQGFLDSVcTDIIH 296
Cdd:cd03236 166 PSSYLDikqrLNAAR-LIRELAEDDNYVLVVEHDLAVLDYL-SDYIH 210
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
229-297 |
4.12e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 42.94 E-value: 4.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKKTL----LIVSHDqgfLDsvctDIIHL 297
Cdd:PRK11144 130 SGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREInipiLYVSHS---LD----EILRL 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
402-464 |
4.21e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.12 E-value: 4.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 402 PPVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKH 464
Cdd:PRK15439 9 PPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG 71
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
80-283 |
4.48e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.46 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARKLAIPS---------HIDLLYCEQEIQVDST 150
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGfrvegkvtfHGKNLYAPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 151 SAIDTVV-------KSDKKRLALleeEAKL------MSEIEEGKTEAAERMKEVADELRDIGadsaeprarrilaglgfs 217
Cdd:PRK14243 91 RRIGMVFqkpnpfpKSIYDNIAY---GARIngykgdMDELVERSLRQAALWDEVKDKLKQSG------------------ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17559834 218 kemqekpcTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKK--TLLIVSHD 283
Cdd:PRK14243 150 --------LSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTHN 209
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
228-260 |
5.38e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 43.36 E-value: 5.38e-04
10 20 30
....*....|....*....|....*....|...
gi 17559834 228 FSGGWRMRISLARALFLEPTLLMLDEPTNHLDL 260
Cdd:TIGR01271 549 LSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
423-595 |
5.75e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.04 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 423 LNFGVDMDSRIAIVGPNGVGKSTLLKLLI-------GKIDPNDGELRK------HRTLRIGwfdqhanealngEQTPVEF 489
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFrivelekGRIMIDDCDVAKfgltdlRRVLSII------------PQSPVLF 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 490 LCT-KFNID-YQEARKqlgtTGLAAHAHTVKIKD-------------------LSGGQKSRVALCNLALGGPDIIILDEP 548
Cdd:PLN03232 1323 SGTvRFNIDpFSEHND----ADLWEALERAHIKDvidrnpfgldaevseggenFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17559834 549 TNNLDIESIDALAEAIRDFNGGVVMVTHDERLVVRTDCNLWVVENQG 595
Cdd:PLN03232 1399 TASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSG 1445
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
84-283 |
5.75e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 42.39 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 84 NFDISAQGKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKHIGARKLAIPSHidllYCEQEIQVDSTSAIDTV-VKSDKK 162
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY----RYSGDVLLGGRSIFNYRdVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 163 RLALLEEEAKLMSEIEEGKTEAAERMKEVA--DELRDIGadsaepRARRILAGL--GFSKEMQEKPCTdFSGGWRMRISL 238
Cdd:PRK14271 102 RVGMLFQRPNPFPMSIMDNVLAGVRAHKLVprKEFRGVA------QARLTEVGLwdAVKDRLSDSPFR-LSGGQQQLLCL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17559834 239 ARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTW--KKTLLIVSHD 283
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHN 221
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
91-259 |
6.11e-04 |
|
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: 41.83 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 91 GKLLFDKASLTIVYGRRYGLVGPNGMGKTTLLKhigarklaipshidLLY-----CEQEIQVDSTSAIDTVVKSDKKRLA 165
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILR--------------LLFrfydvSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 166 LLEEEAKL-----MSEIEEGKTEAAERMKEVADELRDIgadsaeprARRILA-GLGFSKEMQEKPcTDFSGGWRMRISLA 239
Cdd:cd03253 79 VVPQDTVLfndtiGYNIRYGRPDATDEEVIEAAKAAQI--------HDKIMRfPDGYDTIVGERG-LKLSGGEKQRVAIA 149
|
170 180
....*....|....*....|
gi 17559834 240 RALFLEPTLLMLDEPTNHLD 259
Cdd:cd03253 150 RAILKNPPILLLDEATSALD 169
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
403-577 |
6.29e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 42.01 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 403 PVLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDG---------------------EL 461
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggrsifnyrdvlEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 462 RKhrtlRIGWFDQHAN--------EALNGEQTPVEFLCTKFNIDYQEARKQLGTTGLAAHAHTVKIKDLSGGQKSRVALC 533
Cdd:PRK14271 100 RR----RVGMLFQRPNpfpmsimdNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17559834 534 NLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNG--GVVMVTHD 577
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
98-291 |
6.55e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 42.18 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 98 ASLTIVYGRRYGLVGPNGMGKTTLLK------HIGARKLAI---PSHIDL-----LYCEQEIQVDSTSAI---DTVVKSD 160
Cdd:PRK15056 26 ASFTVPGGSIAALVGVNGSGKSTLFKalmgfvRLASGKISIlgqPTRQALqknlvAYVPQSEEVDWSFPVlveDVVMMGR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 161 KKRLALLEEEAKLMSEIeegKTEAAERMkevadelrdigaDSAEPRARRIlaglgfskemqekpcTDFSGGWRMRISLAR 240
Cdd:PRK15056 106 YGHMGWLRRAKKRDRQI---VTAALARV------------DMVEFRHRQI---------------GELSGGQKKRVFLAR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17559834 241 ALFLEPTLLMLDEPTNHLDLNA---VIWLDNYLQTWKKTLLIVSHDQGFLDSVC 291
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTearIISLLRELRDEGKTMLVSTHNLGSVTEFC 209
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
521-591 |
7.36e-04 |
|
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: 41.55 E-value: 7.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 521 DLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEA-----IRDFNGGVVMVTHDERLVVRTDcnlWVV 591
Cdd:cd03290 140 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgilkfLQDDKRTLVLVTHKLQYLPHAD---WII 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
202-283 |
9.34e-04 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 41.28 E-value: 9.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 202 SAEPRAR--RILAGLGFSKEMQEKPcTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLD--LNA--VIWLDNYLQTWKK 275
Cdd:COG3840 103 TAEQRAQveQALERVGLAGLLDRLP-GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpaLRQemLDLVDELCRERGL 181
|
....*...
gi 17559834 276 TLLIVSHD 283
Cdd:COG3840 182 TVLMVTHD 189
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
79-282 |
1.01e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 41.93 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 79 DIKIENFDISAQGK--LLFDKASLTIVYGRRYGLVGPNGMGKTTllkhigarklaIPSHIDLLY--CEQEIQVDSTSAID 154
Cdd:PRK11176 341 DIEFRNVTFTYPGKevPALRNINFKIPAGKTVALVGRSGSGKST-----------IANLLTRFYdiDEGEILLDGHDLRD 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 155 TVVKSDKKRLALLEEEAKLMSE-----IEEGKTEAAERmkevadelRDIgadsaePRARRILAGLGFSKEMQEKPCT--- 226
Cdd:PRK11176 410 YTLASLRNQVALVSQNVHLFNDtiannIAYARTEQYSR--------EQI------EEAARMAYAMDFINKMDNGLDTvig 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559834 227 ----DFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKK--TLLIVSH 282
Cdd:PRK11176 476 engvLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH 537
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
404-576 |
1.06e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 41.05 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 404 VLGLHDVNFGYGKDVLFKKLNFGVDMDSRIAIVGPNGVGKSTLLKLLIGKID--PN---------DG---------ELRK 463
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvsgevylDGqdifkmdviELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 464 hrtlRIGWFDQHANEALNGEQTPVEFLCTKFNiDYQEARKQLGTT---GLAAHAHTVKIKD--------LSGGQKSRVAL 532
Cdd:PRK14247 83 ----RVQMVFQIPNPIPNLSIFENVALGLKLN-RLVKSKKELQERvrwALEKAQLWDEVKDrldapagkLSGGQQQRLCI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17559834 533 CNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNG--GVVMVTH 576
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
80-301 |
1.06e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.53 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENF----DISaqgkLLFDKaSLTIvygrrygLVGPNGMGKTTLLK-------HIGARKLAI---PSHIDLLYCEQEI 145
Cdd:COG3593 6 IKIKNFrsikDLS----IELSD-DLTV-------LVGENNSGKSSILEalrlllgPSSSRKFDEedfYLGDDPDLPEIEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 146 QVDSTSAIDTVVKS---DKKRLALLEEEAKLMSEIEEGKTEAAERMKEVADEL---RDIGADSAEPRARRILAGLGFS-K 218
Cdd:COG3593 74 ELTFGSLLSRLLRLllkEEDKEELEEALEELNEELKEALKALNELLSEYLKELldgLDLELELSLDELEDLLKSLSLRiE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 219 EMQEKPCTDFSGG--WRMRISLARALFL-----EPTLLMLDEPTNHLDLNAVIWLDNYLQ---TWKKTLLIVSHDQGFLD 288
Cdd:COG3593 154 DGKELPLDRLGSGfqRLILLALLSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKelsEKPNQVIITTHSPHLLS 233
|
250
....*....|....
gi 17559834 289 SVCTD-IIHLDNQK 301
Cdd:COG3593 234 EVPLEnIRRLRRDS 247
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
229-282 |
1.08e-03 |
|
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: 40.10 E-value: 1.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWKK---TLLIVSH 282
Cdd:cd03216 84 SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
522-581 |
1.13e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 41.65 E-value: 1.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559834 522 LSGGQKSRVALCNLALGGPDIIILDEPTNNLDI----ESIDALAEAIRDFNGGVVMVTHDERLV 581
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLITHDLALV 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
398-567 |
1.29e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 398 TKLNPPVLGLHDVNFgygkdvlfkKLNFGvdmdsRI-AIVGPNGVGKSTLLKLLIGkIDPN---------DGELRKHRTL 467
Cdd:NF040905 8 TKTFPGVKALDDVNL---------SVREG-----EIhALCGENGAGKSTLMKVLSG-VYPHgsyegeilfDGEVCRFKDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 468 R----IGWFDQHANEALNGEQTPVE--FL---CTKFN-IDYQEARKQ----LGTTGLAAHAHTvKIKDLSGGQKSRV--- 530
Cdd:NF040905 73 RdseaLGIVIIHQELALIPYLSIAEniFLgneRAKRGvIDWNETNRRarelLAKVGLDESPDT-LVTDIGVGKQQLVeia 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 17559834 531 -ALC-NLALggpdiIILDEPTNNLDIESIDALAEAIRDF 567
Cdd:NF040905 152 kALSkDVKL-----LILDEPTAALNEEDSAALLDLLLEL 185
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
203-315 |
1.42e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 40.99 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 203 AEPRARRILAGLGFSKEMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLDNYLQTWK---KTLLI 279
Cdd:PRK13631 152 AKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKannKTVFV 231
|
90 100 110
....*....|....*....|....*....|....*.
gi 17559834 280 VSHDQGFLDSVCTDIIHLDNQKLHTYRGNYTLFKKQ 315
Cdd:PRK13631 232 ITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
197-259 |
1.63e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.26 E-value: 1.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559834 197 DIGADSAEPRARRILAGLGFSkEMQEKPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLD 259
Cdd:NF000106 115 DLSRKDARARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
96-255 |
1.79e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 96 DKASLTIVYGRRYGLVGPNGMGKTTLLKHI-GARKLaipshidllyceQEIQVdstsaidTVVKSDkkrlalleeeaklM 174
Cdd:NF033858 18 DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIaGARKI------------QQGRV-------EVLGGD-------------M 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 175 SeieegktEAAER---------MKE-----------VADEL----RDIGADSAEpRARRI---LAGLGFSkEMQEKPCTD 227
Cdd:NF033858 66 A-------DARHRravcpriayMPQglgknlyptlsVFENLdffgRLFGQDAAE-RRRRIdelLRATGLA-PFADRPAGK 136
|
170 180
....*....|....*....|....*...
gi 17559834 228 FSGGWRMRISLARALFLEPTLLMLDEPT 255
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
392-595 |
2.11e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 41.24 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 392 FQFPETTKlnpPVLglHDVNFgygkdvlfkKLNFGvDMdsrIAIVGPNGVGKSTLLKLLIGKIDPNDGELRKHR----TL 467
Cdd:PRK10789 321 FTYPQTDH---PAL--ENVNF---------TLKPG-QM---LGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDipltKL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 468 RI-GWFDQHA---------------NEAL---NGEQTPVEFLCTKFNID---------YQearKQLGTTGLAahahtvki 519
Cdd:PRK10789 383 QLdSWRSRLAvvsqtpflfsdtvanNIALgrpDATQQEIEHVARLASVHddilrlpqgYD---TEVGERGVM-------- 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17559834 520 kdLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDFNGGVVMVTHDERLVVRTDCNLWVVENQG 595
Cdd:PRK10789 452 --LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHG 525
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
388-547 |
2.27e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.03 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 388 YSVKFQfpETTK----LNPPVLGLHDVNFGYGKDVLFKKLN---FGVDMDSRIAIVGPNGVGKSTLLKLLIGKIDPNDG- 459
Cdd:PRK13545 3 YKVKFE--HVTKkykmYNKPFDKLKDLFFRSKDGEYHYALNnisFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 460 -ELRKHRTL-RIGwfdqhanEALNGEQTPVEFLCTK-FNIDYQEARKQLGTTGLAAHAHTVK-----IKDLSGGQKSRVA 531
Cdd:PRK13545 81 vDIKGSAALiAIS-------SGLNGQLTGIENIELKgLMMGLTKEKIKEIIPEIIEFADIGKfiyqpVKTYSSGMKSRLG 153
|
170
....*....|....*.
gi 17559834 532 LCNLALGGPDIIILDE 547
Cdd:PRK13545 154 FAISVHINPDILVIDE 169
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
433-581 |
2.31e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.18 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 433 IAIVGPNGVGKSTLLKLLIGKIDPNDGELRKHRTLRIgwfdQHANEALNGEQTPVE-----FLCTKFNidyqeaRKQLGT 507
Cdd:PRK13546 53 IGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSV----IAISAGLSGQLTGIEniefkMLCMGFK------RKEIKA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 508 --------TGLAAHAHTvKIKDLSGGQKSRVALCNLALGGPDIIILDEPTNNLDIESIDALAEAIRDF---NGGVVMVTH 576
Cdd:PRK13546 123 mtpkiiefSELGEFIYQ-PVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFkeqNKTIFFVSH 201
|
....*
gi 17559834 577 DERLV 581
Cdd:PRK13546 202 NLGQV 206
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
229-260 |
2.50e-03 |
|
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: 40.23 E-value: 2.50e-03
10 20 30
....*....|....*....|....*....|..
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEPTNHLDL 260
Cdd:cd03291 161 SGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
229-254 |
2.65e-03 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 40.01 E-value: 2.65e-03
10 20
....*....|....*....|....*.
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEP 254
Cdd:COG1137 138 SGGERRRVEIARALATNPKFILLDEP 163
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
223-259 |
3.11e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 39.63 E-value: 3.11e-03
10 20 30
....*....|....*....|....*....|....*..
gi 17559834 223 KPCTDFSGGWRMRISLARALFLEPTLLMLDEPTNHLD 259
Cdd:COG1117 150 KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
518-575 |
3.26e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 40.39 E-value: 3.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17559834 518 KIKDLSGG--QKsrVALCNLALGGPDIIILDEPTNNLDIES-------IDALAEAirdfNGGVVMVT 575
Cdd:COG1129 391 PVGNLSGGnqQK--VVLAKWLATDPKVLILDEPTRGIDVGAkaeiyrlIRELAAE----GKAVIVIS 451
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
228-296 |
3.75e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 39.63 E-value: 3.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559834 228 FSGGWRMRISLARALFLEPTLLMLDEPTNHLDLNAVIWLD---NYLQTWKKTLLIVSHDQGFLDSVCTDIIH 296
Cdd:CHL00131 152 FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAegiNKLMTSENSIILITHYQRLLDYIKPDYVH 223
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
110-289 |
4.08e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 110 LVGPNGMGKTTLLKHIgarKLAipshidlLYCEQEIQVDSTSAIDTVVKSDKKRLalleeEAKLMSEIEEGKTEAAERMK 189
Cdd:cd03240 27 IVGQNGAGKTTIIEAL---KYA-------LTGELPPNSKGGAHDPKLIREGEVRA-----QVKLAFENANGKKYTITRSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 190 EVAD--------ELRDIGADsaePRAR-----RILAGLGFskemqekpctdfsggwrmRISLARALFLEPTLLMLDEPTN 256
Cdd:cd03240 92 AILEnvifchqgESNWPLLD---MRGRcsggeKVLASLII------------------RLALAETFGSNCGILALDEPTT 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17559834 257 HLD-------LNAVIwlDNYLQTWKKTLLIVSHDQGFLDS 289
Cdd:cd03240 151 NLDeenieesLAEII--EERKSQKNFQLIVITHDEELVDA 188
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
202-282 |
6.20e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 202 SAEPRARRIL-----AGLGFSKEMQekPCTDFSGGWRMRISLARALFLE---PTLLMLDEPTNHLDLNAVIWLDNYLQTW 273
Cdd:TIGR00630 801 EAVPSISRKLqtlcdVGLGYIRLGQ--PATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRL 878
|
90
....*....|..
gi 17559834 274 KK---TLLIVSH 282
Cdd:TIGR00630 879 VDkgnTVVVIEH 890
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
432-464 |
6.49e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 36.83 E-value: 6.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 17559834 432 RIAIVG-PNgVGKSTLLKLLIGKI-----------DPNDGELRKH 464
Cdd:pfam01926 1 RVALVGrPN-VGKSTLINALTGAKaivsdypgttrDPNEGRLELK 44
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
519-600 |
7.17e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.50 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 519 IKDLSGGQKS------RVALCNLALGGPDIIILDEPTNNLDIESIDALAEAI----RDFNG--GVVMVTHDERLVVRTDC 586
Cdd:PRK01156 799 IDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIeyslKDSSDipQVIMISHHRELLSVADV 878
|
90
....*....|....
gi 17559834 587 NLWVVENQGIDEID 600
Cdd:PRK01156 879 AYEVKKSSGSSKVI 892
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
420-450 |
7.63e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.83 E-value: 7.63e-03
10 20 30
....*....|....*....|....*....|..
gi 17559834 420 FKKLNFGVDMDSRI-AIVGPNGVGKSTLLKLL 450
Cdd:COG3950 14 FEDLEIDFDNPPRLtVLVGENGSGKTTLLEAI 45
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
80-200 |
8.14e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 39.33 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559834 80 IKIENFDISAQGKLLFDKASLTIVYGRryglvgpNGMGKTTL---LKHIGARKLAIPSHIDLLY------CEQEIQVDST 150
Cdd:COG4694 6 KKLKNVGAFKDFGWLAFFKKLNLIYGE-------NGSGKSTLsriLRSLELGDTSSEVIAEFEIeaggsaPNPSVRVFNR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 17559834 151 SAIDTVVKSDKK---RLALLEEEAKLMSEIEEGKTEAAERMKEVADELRDIGA 200
Cdd:COG4694 79 DFVEENLRSGEEikgIFTLGEENIELEEEIEELEKEIEDLKKELDKLEKELKE 131
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
229-259 |
8.54e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 38.91 E-value: 8.54e-03
10 20 30
....*....|....*....|....*....|.
gi 17559834 229 SGGWRMRISLARALFLEPTLLMLDEPTNHLD 259
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
228-259 |
9.83e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 38.90 E-value: 9.83e-03
10 20 30
....*....|....*....|....*....|..
gi 17559834 228 FSGGWRMRISLARALFLEPTLLMLDEPTNHLD 259
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| |
