|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-511 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 530.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 6 VEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGTHYGYLDQHTVLTPGRTIRD 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 86 VLADAFLPLFEKEKALNEVTEKMGTATPEELeelleQMAEIQDALEAGGFYLLDMKIEEAARGLGIDAIGLDRDVSALSG 165
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEPDEDLE-----RLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 166 GQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAFLLISHDTEFMNKCVDVIFHLEFTKMTRYTATYE 245
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 246 KFLELAEINKNQHINAYEKQREFIKKQEDFIAKNKARYSTTGRAKSRQKQLDRMELIDRPETAIKPEFSFKESRASSRFV 325
Cdd:COG0488 236 AYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLGKKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 326 FEGENVEIGYT-HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPAYFEQEVKA--DNIT 402
Cdd:COG0488 316 LELEGLSKSYGdKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEEldPDKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 403 PIDDVWNTFPGLDQHQIRAMLAKCGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAM 482
Cdd:COG0488 396 VLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEAL 475
|
490 500
....*....|....*....|....*....
gi 445977555 483 KAYKGTILLVCHEPDFYEDWITKVWDVEE 511
Cdd:COG0488 476 DDFPGTVLLVSHDRYFLDRVATRILEFED 504
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-495 |
7.53e-80 |
|
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: 259.48 E-value: 7.53e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 14 GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGTHYGYLDQHTVLTPGRTIRDVLADAFLP 93
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 94 LFEKEKALNEVTEKMGTAtPEELEELLEQMAEIQDALEAGGFYLLDMKIEEAArglgiDAIGL---DRDVSALSGGQRTK 170
Cdd:TIGR03719 96 IKDALDRFNEISAKYAEP-DADFDKLAAEQAELQEIIDAADAWDLDSQLEIAM-----DALRCppwDADVTKLSGGERRR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 171 VLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAFLLISHDTEFMNKCVDVIFHLEFTKMTRYTATYEKFLEL 250
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 251 AEINKNQHINAYEKQREFIKKQEDFI--------AKNKARYSTTGR--AKSRQKQLDRMELIdrpetaIKPefsfkesra 320
Cdd:TIGR03719 250 KQKRLEQEEKEESARQKTLKRELEWVrqspkgrqAKSKARLARYEEllSQEFQKRNETAEIY------IPP--------- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 321 SSRF---VFEGENVEIGYTHPLLPK-LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPAYFEQEv 396
Cdd:TIGR03719 315 GPRLgdkVIEAENLTKAFGDKLLIDdLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQS- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 397 kADNITPIDDVWNTFP-GLDQHQI-------RAMLAKCGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTN 468
Cdd:TIGR03719 394 -RDALDPNKTVWEEISgGLDIIKLgkreipsRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTN 472
|
490 500
....*....|....*....|....*..
gi 445977555 469 HLDVTAKAELKKAMKAYKGTILLVCHE 495
Cdd:TIGR03719 473 DLDVETLRALEEALLNFAGCAVVISHD 499
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-509 |
3.92e-77 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 251.73 E-value: 3.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 13 FGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGTHYGYLDQ-------HTVLtpgrtirD 85
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQdqfafeeFTVL-------D 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 86 VLADAFLPLFE--KEK----ALNEVTEKMGTAtpeeleelleqMAEIQDAL-EAGGfYLLDMKIEEAARGLGIDA---IG 155
Cdd:PRK15064 84 TVIMGHTELWEvkQERdriyALPEMSEEDGMK-----------VADLEVKFaEMDG-YTAEARAGELLLGVGIPEeqhYG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 156 LdrdVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAFLLISHDTEFMNKcvdVIFH---L 232
Cdd:PRK15064 152 L---MSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNS---VCTHmadL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 233 EFTKMTRYTATYEKFLELAEINKNQHINAYEKQREFIKKQEDFIAKNKARYSTTGRAKSRQKQLDRMELID-RPETAIKP 311
Cdd:PRK15064 226 DYGELRVYPGNYDEYMTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKLEEvKPSSRQNP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 312 EFSFKESRASSRFVFEGENVEIGY-THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPA 390
Cdd:PRK15064 306 FIRFEQDKKLHRNALEVENLTKGFdNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 391 YFEQEVKAD---NITPID--DVWNTfPGLDQHQIRAMLAKCGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDE 465
Cdd:PRK15064 386 YYAQDHAYDfenDLTLFDwmSQWRQ-EGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDE 464
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 445977555 466 PTNHLDVTAKAELKKAMKAYKGTILLVCHEPDFYEDWITKVWDV 509
Cdd:PRK15064 465 PTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEI 508
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-507 |
2.08e-76 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 252.56 E-value: 2.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGTHYGYLDQhtvlTPG 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQ----DPP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 81 R----TIRDVLADAFLPLFEKEKALNEVTEKMGTatpEELEELLEQMAEIQDALEAGGFYLLDMKIEEAARGLGIDAigl 156
Cdd:PRK11147 77 RnvegTVYDFVAEGIEEQAEYLKRYHDISHLVET---DPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDP--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 157 DRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAFLLISHDTEFMNKCVDVIFHLEFTK 236
Cdd:PRK11147 151 DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 237 MTRYTATYEKFLELAEinKNQHINAyEKQREFIKK--QED-FIAKN-KARYS-TTGRAKSrQKQLdRMELIDRPETAIKP 311
Cdd:PRK11147 231 LVSYPGNYDQYLLEKE--EALRVEE-LQNAEFDRKlaQEEvWIRQGiKARRTrNEGRVRA-LKAL-RRERSERREVMGTA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 312 EFSFKESRASSRFVFEGENVEigYTHP---LLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLE 388
Cdd:PRK11147 306 KMQVEEASRSGKIVFEMENVN--YQIDgkqLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 389 PAYFEQ---EVKADNiTPIDDVWN-----TFPGLDQHQI-----------RAMlakcglknehisRPLSQLSGGEQAKVR 449
Cdd:PRK11147 384 VAYFDQhraELDPEK-TVMDNLAEgkqevMVNGRPRHVLgylqdflfhpkRAM------------TPVKALSGGERNRLL 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 450 LCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAYKGTILLVCHEPDFYEDWITKVW 507
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECW 508
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-494 |
1.85e-74 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 245.41 E-value: 1.85e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 14 GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGqLIHD-QGRVEWTPGTHYGYLDQHTVLTPGRTIRDVLADAFL 92
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKEfEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 93 PLFEKEKALNEVTEKMgtATPEELE-ELLEQMAEIQDALEAGGFYLLDMKIEEAArglgiDAIGL---DRDVSALSGGQR 168
Cdd:PRK11819 97 EVKAALDRFNEIYAAY--AEPDADFdALAAEQGELQEIIDAADAWDLDSQLEIAM-----DALRCppwDAKVTKLSGGER 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 169 TKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAFLLISHDTEFMNKCVDVIFHLEFTKMTRYTATYEKFL 248
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 249 E-----LAEINKNQ--HINAYEKQREFIK-----KQedfiAKNKARYSttgR-----AKSRQKQLDRMELIdrpetaIKP 311
Cdd:PRK11819 250 EqkakrLAQEEKQEaaRQKALKRELEWVRqspkaRQ----AKSKARLA---RyeellSEEYQKRNETNEIF------IPP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 312 efsfkesraSSRF---VFEGENVEIGYTHPLLPK-LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFL 387
Cdd:PRK11819 317 ---------GPRLgdkVIEAENLSKSFGDRLLIDdLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 388 EPAYFEQEvkADNITPIDDVWNTFP-GLDQHQI-------RAMLAKCGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESN 459
Cdd:PRK11819 388 KLAYVDQS--RDALDPNKTVWEEISgGLDIIKVgnreipsRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGN 465
|
490 500 510
....*....|....*....|....*....|....*
gi 445977555 460 WLLFDEPTNHLDVTAKAELKKAMKAYKGTILLVCH 494
Cdd:PRK11819 466 VLLLDEPTNDLDVETLRALEEALLEFPGCAVVISH 500
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-495 |
1.48e-68 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 231.98 E-value: 1.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 14 GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGTHYGYLDQHTVLTPGRTIRDVLaDAFLP 93
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVI-DGDRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 94 LFEKEKALNEVTEKM-GTAtpeeleelleqMAEIQDALEAGGFYLLDMKIEEAARGLGIDAIGLDRDVSALSGGQRTKVL 172
Cdd:PRK10636 91 YRQLEAQLHDANERNdGHA-----------IATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 173 LAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAFLLISHDTEFMNKCVDVIFHLEFTKMTRYTATYEKFlELAE 252
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSF-EVQR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 253 INK-NQHINAYEKQREFIKKQEDFIAKNKARYSTTGRAKSRQKQLDRMELIdRPETAIKP-EFSFKESRASSRFVFEGEN 330
Cdd:PRK10636 239 ATRlAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELI-APAHVDNPfHFSFRAPESLPNPLLKMEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 331 VEIGYTHPL-LPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPAYFEQE----VKADNiTPID 405
Cdd:PRK10636 318 VSAGYGDRIiLDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHqlefLRADE-SPLQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 406 DVWNTFPGLDQHQIRAMLAKCGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAY 485
Cdd:PRK10636 397 HLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF 476
|
490
....*....|
gi 445977555 486 KGTILLVCHE 495
Cdd:PRK10636 477 EGALVVVSHD 486
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-511 |
7.54e-59 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 207.02 E-value: 7.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 6 VEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTF-----MNIITG-----QLIHDQGRVewtpgthygYLDQHT 75
Cdd:PLN03073 180 MENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFlrymaMHAIDGipkncQILHVEQEV---------VGDDTT 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 76 VLT---PGRTIRDVLADAFLPLFEKEKALNEVTE----KMGTATPEELEELLEQMAEIQDALEAGGFYLLDMKIEEAARG 148
Cdd:PLN03073 251 ALQcvlNTDIERTQLLEEEAQLVAQQRELEFETEtgkgKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILAG 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 149 LGIDAIGLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAFLLISHDTEFMNKCVDV 228
Cdd:PLN03073 331 LSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTD 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 229 IFHLEFTKMTRYTATYEKFLEL-AEINKNQH--INAYEKQREFIKKqedFIakNKARYSTTgRA---KSRQKQLDRMELI 302
Cdd:PLN03073 411 ILHLHGQKLVTYKGDYDTFERTrEEQLKNQQkaFESNERSRSHMQA---FI--DKFRYNAK-RAslvQSRIKALDRLGHV 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 303 DR--PETAIKPEFSFKESRASSRfVFEGENVEIGYT-HPLLPK-LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLS 378
Cdd:PLN03073 485 DAvvNDPDYKFEFPTPDDRPGPP-IISFSDASFGYPgGPLLFKnLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSS 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 379 GKTSLGDFLEPAYFEQEvKADNI----TPIDDVWNTFPGLDQHQIRAMLAKCGLKNEHISRPLSQLSGGEQAKVRLCKLM 454
Cdd:PLN03073 564 GTVFRSAKVRMAVFSQH-HVDGLdlssNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKIT 642
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 445977555 455 GEESNWLLFDEPTNHLDVTAKAELKKAMKAYKGTILLVCHEPDFYEDWITKVWDVEE 511
Cdd:PLN03073 643 FKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSE 699
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-249 |
3.21e-55 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 193.36 E-value: 3.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGTHYGYLDQH-TVLTPGR 81
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHqEELDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 82 TIRDVLADAFlplfekekalNEVTEKmgtatpeeleelleqmaEIQDALEAGGFYlldmkieeaarglGIDAiglDRDVS 161
Cdd:COG0488 395 TVLDELRDGA----------PGGTEQ-----------------EVRGYLGRFLFS-------------GDDA---FKPVG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 162 ALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAFLLISHDTEFMNKCVDVIFHLEFTKMTRYT 241
Cdd:COG0488 432 VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYP 511
|
....*...
gi 445977555 242 ATYEKFLE 249
Cdd:COG0488 512 GGYDDYLE 519
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-233 |
1.93e-50 |
|
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: 169.17 E-value: 1.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGTHYGYLDQhtvltpgrti 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 84 rdvladaflplfekekalnevtekmgtatpeeleelleqmaeiqdaleaggfylldmkieeaarglgidaigldrdvsaL 163
Cdd:cd03221 71 -------------------------------------------------------------------------------L 71
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 164 SGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAFLLISHDTEFMNKCVDVIFHLE 233
Cdd:cd03221 72 SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELE 141
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
327-511 |
1.73e-44 |
|
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: 153.37 E-value: 1.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 327 EGENVEIGYT-HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPAYFEQevkadnitpid 405
Cdd:cd03221 2 ELENLSKTYGgKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 406 dvwntfpgldqhqiramlakcglknehisrplsqLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAY 485
Cdd:cd03221 71 ----------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEY 116
|
170 180
....*....|....*....|....*.
gi 445977555 486 KGTILLVCHEPDFYEDWITKVWDVEE 511
Cdd:cd03221 117 PGTVILVSHDRYFLDQVATKIIELED 142
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-494 |
3.21e-38 |
|
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: 146.59 E-value: 3.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MS-LLTVEKLGHTF--GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGqLIHDQGRVEWTPGTHYGYLDQHTVL 77
Cdd:COG1123 1 MTpLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRISGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 78 TPGRTIRDVLADAflplfekEKALNEVTekmgtatpeeleelleQMAEIQDALEAGGFYLLDMK--IEEAARGLGIDAIg 155
Cdd:COG1123 80 LRGRRIGMVFQDP-------MTQLNPVT----------------VGDQIAEALENLGLSRAEARarVLELLEAVGLERR- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 156 LDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV----EHIHWLTNYLKEYPHAFLLISHDTEFMNKCVDVIFH 231
Cdd:COG1123 136 LDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVttqaEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 232 LEFTKMTRYTATYEKFlelaeinknqhinayekqrefikkqedfiaknkarysttgrakSRQKQLDRMELIDRPETAIKP 311
Cdd:COG1123 216 MDDGRIVEDGPPEEIL-------------------------------------------AAPQALAAVPRLGAARGRAAP 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 312 EfsfkesRASSRFVFEGENVEIGY------THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD 385
Cdd:COG1123 253 A------AAAAEPLLEVRNLSKRYpvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDG 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 386 FLEPAYFEQEVKA----------------DNITPIDDV----WNTFPGLDQHQIRA----MLAKCGLKNEHISRPLSQLS 441
Cdd:COG1123 327 KDLTKLSRRSLRElrrrvqmvfqdpysslNPRMTVGDIiaepLRLHGLLSRAERRErvaeLLERVGLPPDLADRYPHELS 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445977555 442 GGEQAkvRLC---------KLmgeesnwLLFDEPTNHLDVTAKAE----LKKAMKAYKGTILLVCH 494
Cdd:COG1123 407 GGQRQ--RVAiaralalepKL-------LILDEPTSALDVSVQAQilnlLRDLQRELGLTYLFISH 463
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-248 |
2.67e-33 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 132.71 E-value: 2.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGTHYGYLDQhtvltpgrti 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQ---------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 84 rDVLADaflplFEKEKALnevTEKMGtatpeeleelleQMAEIQDAleaggfylldmkiEEAARG-LG-----IDAIGld 157
Cdd:PRK15064 390 -DHAYD-----FENDLTL---FDWMS------------QWRQEGDD-------------EQAVRGtLGrllfsQDDIK-- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 158 RDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAFLLISHDTEFMNKCVDVIFHLEFTKM 237
Cdd:PRK15064 434 KSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGV 513
|
250
....*....|.
gi 445977555 238 TRYTATYEKFL 248
Cdd:PRK15064 514 VDFSGTYEEYL 524
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-218 |
6.45e-33 |
|
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: 125.93 E-value: 6.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW--TPGTHY---------GYL 71
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdgRDLASLsrrelarriAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 72 DQHTVLTPGRTIRDVLA---DAFLPLFEKEKALNEvtekmgtatpeeleelleqmAEIQDALEAggfylldmkieeaarg 148
Cdd:COG1120 81 PQEPPAPFGLTVRELVAlgrYPHLGLFGRPSAEDR--------------------EAVEEALER---------------- 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445977555 149 LGIDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLK----EYPHAFLLISHD 218
Cdd:COG1120 125 TGLEHL-ADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRrlarERGRTVVMVLHD 197
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-232 |
2.88e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 123.66 E-value: 2.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW--TPGTHY----GYLDQH 74
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgKPPRRArrriGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 75 TVLTPGR--TIRDVLAdaflplfekekalnevtekMGT--ATPEELEELLEQMAEIQDALEAggfylldmkieeaargLG 150
Cdd:COG1121 84 AEVDWDFpiTVRDVVL-------------------MGRygRRGLFRRPSRADREAVDEALER----------------VG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 151 IDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKE---YPHAFLLISHDTEFMNKCVD 227
Cdd:COG1121 129 LEDL-ADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElrrEGKTILVVTHDLGAVREYFD 207
|
....*
gi 445977555 228 VIFHL 232
Cdd:COG1121 208 RVLLL 212
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-233 |
1.16e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 121.08 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW-------TPGTHY----GYLD 72
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdgkplsaMPPPEWrrqvAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 73 QHTVLTPGrTIRDVLADAFLplFEKEKAlnevtekmgtatpeeleelleQMAEIQDALEAggfylldmkieeaargLGID 152
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQ--LRERKF---------------------DRERALELLER----------------LGLP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 153 AIGLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEH----IHWLTNYLKEYPHAFLLISHDTEFMNKCVDV 228
Cdd:COG4619 121 PDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADR 200
|
....*
gi 445977555 229 IFHLE 233
Cdd:COG4619 201 VLTLE 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-218 |
4.01e-30 |
|
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: 116.81 E-value: 4.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW------TPGTHY----GYLD 72
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWngepirDAREDYrrrlAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 73 QHTVLTPGRTIRDVLadAFLplfekekalnevtekmgtatpeeleelleqmaeiqdaLEAGGFYLLDMKIEEAARGLGID 152
Cdd:COG4133 82 HADGLKPELTVRENL--RFW-------------------------------------AALYGLRADREAIDEALEAVGLA 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445977555 153 AIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPH---AFLLISHD 218
Cdd:COG4133 123 GL-ADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLArggAVLLTTHQ 190
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-236 |
4.91e-30 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 115.03 E-value: 4.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 5 TVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWtpgthygyldqhtvltpgrtir 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 85 dvladaflplfekekalnevtekmgtatpeeleelleqmaeiqdaleaGGFYLLDMKIEEAARGLGIdaigldrdVSALS 164
Cdd:cd00267 59 ------------------------------------------------DGKDIAKLPLEELRRRIGY--------VPQLS 82
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 165 GGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYP---HAFLLISHDTEFMNKCVDVIFHLEFTK 236
Cdd:cd00267 83 GGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAeegRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-229 |
5.12e-30 |
|
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: 117.65 E-value: 5.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW--TPGTHY--------GYLD 72
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdgEDVRKEprearrqiGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 73 QHTVLTPGRTIRDVLA--DAFLPLFEKEKALnevtekmgtatpeeleelleqmaeiqdaleaggfylldmKIEEAARGLG 150
Cdd:COG4555 81 DERGLYDRLTVRENIRyfAELYGLFDEELKK---------------------------------------RIEELIELLG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 151 IDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEY---PHAFLLISHDTEFMNKCVD 227
Cdd:COG4555 122 LEEF-LDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCD 200
|
..
gi 445977555 228 VI 229
Cdd:COG4555 201 RV 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-220 |
3.41e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 115.16 E-value: 3.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW---TPGTHY-------GYLDQ 73
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgeDVARDPaevrrriGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 74 HTVLTPGRTIRDVL---ADAF-LPLFEKEKALNEVTEKMGtatpeeleelleqmaeiqdaleaggfylldmkIEEAArgl 149
Cdd:COG1131 81 EPALYPDLTVRENLrffARLYgLPRKEARERIDELLELFG--------------------------------LTDAA--- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445977555 150 gidaiglDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEY---PHAFLLISHDTE 220
Cdd:COG1131 126 -------DRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaeGKTVLLSTHYLE 192
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-191 |
5.08e-29 |
|
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: 111.97 E-value: 5.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 19 FKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW-----------TPGTHYGYLDQHTVLTPGRTIRDVL 87
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdltdderkSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 88 ADAFLPLFEKEKAlnevtekmgtatpeeleelleqmaeiqdaleaggfylLDMKIEEAARGLGIDAI---GLDRDVSALS 164
Cdd:pfam00005 81 RLGLLLKGLSKRE-------------------------------------KDARAEEALEKLGLGDLadrPVGERPGTLS 123
|
170 180
....*....|....*....|....*..
gi 445977555 165 GGQRTKVLLAKLLLEQPEVLLLDEPTN 191
Cdd:pfam00005 124 GGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
325-497 |
1.21e-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: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 325 VFEGENVEIGY-THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDflEP-------------A 390
Cdd:COG1120 1 MLEAENLSVGYgGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG--RDlaslsrrelarriA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 391 YFEQEVKAD-NITPIDDV----------WNTFPGLDQHQIRAMLAKCGLknEHIS-RPLSQLSGGEQAKVRLCKLMGEES 458
Cdd:COG1120 79 YVPQEPPAPfGLTVRELValgryphlglFGRPSAEDREAVEEALERTGL--EHLAdRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 445977555 459 NWLLFDEPTNHLDVTAKAE---LKKAMKAYKG-TILLVCHEPD 497
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEvleLLRRLARERGrTVVMVLHDLN 199
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-233 |
1.37e-28 |
|
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: 112.56 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 6 VEKLGHTFGD--RTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWtPGTHYGYLDQHTVltpGRTI 83
Cdd:cd03225 2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV-DGKDLTKLSLKEL---RRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 84 RDVLADAFLPLFEkekalNEVTEkmgtatpeeleelleqmaEIQDALEAGGFYLLDM--KIEEAARGLGIDAIgLDRDVS 161
Cdd:cd03225 78 GLVFQNPDDQFFG-----PTVEE------------------EVAFGLENLGLPEEEIeeRVEEALELVGLEGL-RDRSPF 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 162 ALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYP---HAFLLISHDTEFMNKCVDVIFHLE 233
Cdd:cd03225 134 TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaegKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
327-497 |
3.01e-28 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 110.60 E-value: 3.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 327 EGENVEIGYT-HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDflepayfeqevkadniTPId 405
Cdd:cd03214 1 EVENLSVGYGgRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG----------------KDL- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 406 dvwNTFPGLDQHQIRA----MLAKCGLknEHIS-RPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAE--- 477
Cdd:cd03214 64 ---ASLSPKELARKIAyvpqALELLGL--AHLAdRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIElle 138
|
170 180
....*....|....*....|.
gi 445977555 478 -LKKAMKAYKGTILLVCHEPD 497
Cdd:cd03214 139 lLRRLARERGKTVVMVLHDLN 159
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-218 |
6.11e-28 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 109.83 E-value: 6.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 5 TVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLDQHTVLTPGRtir 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI---------LLDGKDLASLSP--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 85 dvladaflplfeKEKAlnevtekmgtatpeeleellEQMAEIQDALEAggfylldmkieeaargLGIDAIgLDRDVSALS 164
Cdd:cd03214 69 ------------KELA--------------------RKIAYVPQALEL----------------LGLAHL-ADRPFNELS 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 165 GGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAF----LLISHD 218
Cdd:cd03214 100 GGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERgktvVMVLHD 157
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-224 |
1.12e-27 |
|
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: 116.57 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 6 VEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGTHYGYLDQ-HTVLTPGRTIR 84
Cdd:TIGR03719 325 AENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQsRDALDPNKTVW 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 85 DVLADAflplfekekalnevtekmgtatpeeleelleqmaeiQDALEAGGFylldmkiEEAARGL-------GIDAiglD 157
Cdd:TIGR03719 405 EEISGG------------------------------------LDIIKLGKR-------EIPSRAYvgrfnfkGSDQ---Q 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445977555 158 RDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAFLLISHDTEFMNK 224
Cdd:TIGR03719 439 KKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDR 505
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-232 |
1.24e-27 |
|
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: 109.93 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 6 VEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwTPGTHY-------GYLDQHTVLT 78
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIR-VFGKPLekerkriGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 79 PGR--TIRDVLAdafLPLFEKEKALNEVTEKmgtatpeeleelleQMAEIQDALEAGGfyLLDMKieeaarglgidaigl 156
Cdd:cd03235 81 RDFpiSVRDVVL---MGLYGHKGLFRRLSKA--------------DKAKVDEALERVG--LSELA--------------- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445977555 157 DRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLT---NYLKEYPHAFLLISHDTEFMNKCVDVIFHL 232
Cdd:cd03235 127 DRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYellRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-233 |
3.47e-27 |
|
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: 109.34 E-value: 3.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTF-GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWtpgthygyLDQHTVLTPGRT 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLV--------DGKDITKKNLRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 IRD----VLADAFLPLFEkEKALNEVT---EKMGTATpeeleelleqmAEIQDaleaggfylldmKIEEAARGLGIDAIg 155
Cdd:COG1122 73 LRRkvglVFQNPDDQLFA-PTVEEDVAfgpENLGLPR-----------EEIRE------------RVEEALELVGLEHL- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 156 LDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHA---FLLISHDTEFMNKCVDVIFHL 232
Cdd:COG1122 128 ADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHDLDLVAELADRVIVL 207
|
.
gi 445977555 233 E 233
Cdd:COG1122 208 D 208
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
329-496 |
4.37e-27 |
|
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: 108.39 E-value: 4.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGYT-HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSL-GDFLEP-----AYFEQEVKADNI 401
Cdd:cd03235 3 EDLTVSYGgHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLEKerkriGYVPQRRSIDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 402 TPID--DV--------WNTFPGL---DQHQIRAMLAKCGLKnEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTN 468
Cdd:cd03235 83 FPISvrDVvlmglyghKGLFRRLskaDKAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190
....*....|....*....|....*....|.
gi 445977555 469 HLDVTAKAELK---KAMKAYKGTILLVCHEP 496
Cdd:cd03235 162 GVDPKTQEDIYellRELRREGMTILVVTHDL 192
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-233 |
1.58e-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: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGD-RTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW--TPGTHY---------GYL 71
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIngVDLSDLdpaswrrqiAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 72 DQHTVLTPGrTIRDVLA----DAflplfeKEKALNEVTEKMGtatpeeleelleqMAEIQDALEAGgfylLDMKIEEAAR 147
Cdd:COG4988 417 PQNPYLFAG-TIRENLRlgrpDA------SDEELEAALEAAG-------------LDEFVAALPDG----LDTPLGEGGR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 148 GLgidaigldrdvsalSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYP--HAFLLISHDTEFMNKC 225
Cdd:COG4988 473 GL--------------SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAkgRTVILITHRLALLAQA 538
|
....*...
gi 445977555 226 vDVIFHLE 233
Cdd:COG4988 539 -DRILVLD 545
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-232 |
1.96e-26 |
|
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: 107.58 E-value: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFG----DRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW--TPGTHY-------- 68
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgRPVTRRrrkafrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 69 -GYLDQH--TVLTPGRTIRDVLAdaflplfekekalnevtekmgtaTPEELEELLEQMAEIQDALEAggfylldmkieea 145
Cdd:COG1124 81 vQMVFQDpyASLHPRHTVDRILA-----------------------EPLRIHGLPDREERIAELLEQ------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 146 argLGIDAIGLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV----EHIHWLTNYLKEYPHAFLLISHDtef 221
Cdd:COG1124 125 ---VGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHD--- 198
|
250
....*....|.
gi 445977555 222 mnkcVDVIFHL 232
Cdd:COG1124 199 ----LAVVAHL 205
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
230-315 |
2.09e-25 |
|
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: 99.57 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 230 FHLEFTKMTRYTATYEKFLELAEINKNQHINAYEKQREFIKKQEDFIAKNKARYSTTGRAKSRQKQLDRMELIDRPEtAI 309
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEKPE-RD 79
|
....*.
gi 445977555 310 KPEFSF 315
Cdd:pfam12848 80 KPKLRF 85
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-220 |
4.81e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.93 E-value: 4.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 13 FGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGTHYGYLDQHTVLTPG--RTIRDVLAda 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSlpLTVRDLVA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 91 fLPLFEKEKALNEVTekmgtatpeeleelLEQMAEIQDALEAggfylldmkieeaargLGIDAIgLDRDVSALSGGQRTK 170
Cdd:NF040873 80 -MGRWARRGLWRRLT--------------RDDRAAVDDALER----------------VGLADL-AGRQLGELSGGQRQR 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 445977555 171 VLLAKLLLEQPEVLLLDEPTNYLD---VEHIHWLTNYLKEYPHAFLLISHDTE 220
Cdd:NF040873 128 ALLAQGLAQEADLLLLDEPTTGLDaesRERIIALLAEEHARGATVVVVTHDLE 180
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-220 |
6.36e-25 |
|
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: 101.32 E-value: 6.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwtpgthygYLDQHTVLTPGRTI 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK--------VLGKDIKKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 84 RDVladAFLPlfekekalnevtekmgtatpeeleelleqmaeiqdalEAGGFYlLDMKIEEAARglgidaigldrdvsaL 163
Cdd:cd03230 73 RRI---GYLP-------------------------------------EEPSLY-ENLTVRENLK---------------L 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 164 SGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEY---PHAFLLISHDTE 220
Cdd:cd03230 97 SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILE 156
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
325-501 |
1.57e-24 |
|
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: 101.02 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 325 VFEGENVEIGY-THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLG----DFLEPAYFEQ----- 394
Cdd:COG4133 2 MLEAENLSCRRgERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgepiRDAREDYRRRlaylg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 395 ---EVKADnITPID--DVWNTFPGL--DQHQIRAMLAKCGLKnEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPT 467
Cdd:COG4133 82 hadGLKPE-LTVREnlRFWAALYGLraDREAIDEALEAVGLA-GLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 445977555 468 NHLDVTAKAELKKAMKAYK---GTILLVCHEPDFYED 501
Cdd:COG4133 160 TALDAAGVALLAELIAAHLargGAVLLTTHQPLELAA 196
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-233 |
2.20e-24 |
|
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: 107.23 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 14 GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV--------EWTPGT---HYGYLDQHTVLTPGrT 82
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrQIDPASlrrQIGVVLQDVFLFSG-T 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 IRD--VLADAFLPLFEKEKALnevtekmgtatpeeleelleQMAEIQDALEA--GGfylLDMKIEEAARGLgidaigldr 158
Cdd:COG2274 565 IREniTLGDPDATDEEIIEAA--------------------RLAGLHDFIEAlpMG---YDTVVGEGGSNL--------- 612
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445977555 159 dvsalSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV--EHIhwLTNYLKEY--PHAFLLISHDTEFMNKCvDVIFHLE 233
Cdd:COG2274 613 -----SGGQRQRLAIARALLRNPRILILDEATSALDAetEAI--ILENLRRLlkGRTVIIIAHRLSTIRLA-DRIIVLD 683
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-218 |
4.25e-24 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 105.59 E-value: 4.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 6 VEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGTHYGYLDQHtvltpgrtiRD 85
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQS---------RD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 86 VLADaflplfekEKALNEVtekmgtatpeeleelleqMAEIQDALEAGGFylldmkiEEAARGL-------GIDAiglDR 158
Cdd:PRK11819 398 ALDP--------NKTVWEE------------------ISGGLDIIKVGNR-------EIPSRAYvgrfnfkGGDQ---QK 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 159 DVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAFLLISHD 218
Cdd:PRK11819 442 KVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHD 501
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-218 |
4.60e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 101.32 E-value: 4.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTF----GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWT------PGTHYGY 70
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDgkpvtgPGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 71 LDQHTVLTPGRTIRD-VLadafLPLfekekalnevtekmgtatpeeleelleqmaEIQDALEAggfylldmKIEEAARGL 149
Cdd:COG1116 85 VFQEPALLPWLTVLDnVA----LGL------------------------------ELRGVPKA--------ERRERAREL 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445977555 150 gIDAIGL----DRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV---EHIH-WLTNYLKEYPHAFLLISHD 218
Cdd:COG1116 123 -LELVGLagfeDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltrERLQdELLRLWQETGKTVLFVTHD 198
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
327-507 |
4.72e-24 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 99.85 E-value: 4.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 327 EGENVEIGYTH---PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSlgdflepaYFEQEVKADNI-- 401
Cdd:cd03225 1 ELKNLSFSYPDgarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVL--------VDGKDLTKLSLke 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 402 -------------------TPIDDVwnTFP----GLDQHQIRA----MLAKCGLKnEHISRPLSQLSGGEQAKVRLCKLM 454
Cdd:cd03225 73 lrrkvglvfqnpddqffgpTVEEEV--AFGlenlGLPEEEIEErveeALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 445977555 455 GEESNWLLFDEPTNHLDVTAKAELKKAMKAYKG---TILLVCHEPDFYEDWITKVW 507
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVI 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-218 |
6.62e-24 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 99.89 E-value: 6.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLF----KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW--------------TP 64
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdgkdllklsrrlrkIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 65 GTHYGYL--DQHTVLTPGRTIRDVLADAFLPLF--EKEKALNEvtekmgtatpeeleelleqmaeiqdaleaggfylldm 140
Cdd:cd03257 81 RKEIQMVfqDPMSSLNPRMTIGEQIAEPLRIHGklSKKEARKE------------------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 141 KIEEAARGLGIDAIGLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV----EHIHWLTNYLKEYPHAFLLIS 216
Cdd:cd03257 124 AVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVsvqaQILDLLKKLQEELGLTLLFIT 203
|
..
gi 445977555 217 HD 218
Cdd:cd03257 204 HD 205
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
335-511 |
8.97e-24 |
|
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: 97.32 E-value: 8.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 335 YTHPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKtslgdflepayfeqevkadnitpIddvwnTFPGL 414
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGE-----------------------I-----LIDGK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 415 DQHQIRAMLAKcglknEHISRpLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAYKG---TILL 491
Cdd:cd00267 62 DIAKLPLEELR-----RRIGY-VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVII 135
|
170 180
....*....|....*....|
gi 445977555 492 VCHEPDFYEDWITKVWDVEE 511
Cdd:cd00267 136 VTHDPELAELAADRVIVLKD 155
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-499 |
1.16e-23 |
|
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: 104.48 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 29 GEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPgthygylDQHTVLTPGR-TIrdvLADAFLPLFEKEKalnEVTEK 107
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEP-------SWDEVLKRFRgTE---LQDYFKKLANGEI---KVAHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 108 mgtatpeeleellEQMAE-IQDALEAGGFYLLD-----MKIEEAARGLGIDAIgLDRDVSALSGGQRTKVLLAKLLLEQP 181
Cdd:COG1245 166 -------------PQYVDlIPKVFKGTVRELLEkvderGKLDELAEKLGLENI-LDRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 182 EVLLLDEPTNYLDV-------EHIHWLTNYLKeyphAFLLISHDTEFMNKCVDVIfHLE---------FTKM--TRytat 243
Cdd:COG1245 232 DFYFFDEPSSYLDIyqrlnvaRLIRELAEEGK----YVLVVEHDLAILDYLADYV-HILygepgvygvVSKPksVR---- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 244 yekflelaeINKNQHINAY---EKQReFIKKQEDFiaknkarysttgRAKSRQKQLDRMELIDRPETAIK-PEFSFKesr 319
Cdd:COG1245 303 ---------VGINQYLDGYlpeENVR-IRDEPIEF------------EVHAPRREKEEETLVEYPDLTKSyGGFSLE--- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 320 assrfvfegenVEIGythpllpklsmTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGdfLEPAYFEQEVKAD 399
Cdd:COG1245 358 -----------VEGG-----------EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED--LKISYKPQYISPD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 400 NITPIDDV---WNTfPGLDQHQIRAMLAKcGLKNEHI-SRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDV--- 472
Cdd:COG1245 414 YDGTVEEFlrsANT-DDFGSSYYKTEIIK-PLGLEKLlDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqr 491
|
490 500
....*....|....*....|....*....
gi 445977555 473 --TAKAeLKKAMKAYKGTILLVCHepDFY 499
Cdd:COG1245 492 laVAKA-IRRFAENRGKTAMVVDH--DIY 517
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-499 |
2.23e-23 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 103.73 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 29 GEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTP----------GTH-YGYLDQhtvLTPG--RTIR-----DVLADA 90
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswdevlkrfrGTElQNYFKK---LYNGeiKVVHkpqyvDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 91 FlplfeKEKAlNEVTEKmgtatpeeleelleqmaeiqdALEAGgfylldmKIEEAARGLGIDAIgLDRDVSALSGGQRTK 170
Cdd:PRK13409 176 F-----KGKV-RELLKK---------------------VDERG-------KLDEVVERLGLENI-LDRDISELSGGELQR 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 171 VLLAKLLLEQPEVLLLDEPTNYLDV-EHIHwLTNYLKEYP--HAFLLISHDTEFMNKCVDVIfHLEFTKmtryTATYEKF 247
Cdd:PRK13409 221 VAIAAALLRDADFYFFDEPTSYLDIrQRLN-VARLIRELAegKYVLVVEHDLAVLDYLADNV-HIAYGE----PGAYGVV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 248 LELAEINK--NQHINAYEKQrEFIKkqedfIAKNKARYSTtgRAKSRQKQLDRmeLIDRPETAIK-PEFSFkesrassrf 324
Cdd:PRK13409 295 SKPKGVRVgiNEYLKGYLPE-ENMR-----IRPEPIEFEE--RPPRDESERET--LVEYPDLTKKlGDFSL--------- 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 325 vfegeNVEIGYthpllpklsmtIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGdfLEPAYFEQEVKADNITPI 404
Cdd:PRK13409 356 -----EVEGGE-----------IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--LKISYKPQYIKPDYDGTV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 405 DDVW-NTFPGLDQHQIRAMLAKcGLKNEHI-SRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDV-----TAKAe 477
Cdd:PRK13409 418 EDLLrSITDDLGSSYYKSEIIK-PLQLERLlDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlaVAKA- 495
|
490 500
....*....|....*....|..
gi 445977555 478 LKKAMKAYKGTILLVCHepDFY 499
Cdd:PRK13409 496 IRRIAEEREATALVVDH--DIY 515
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-218 |
6.34e-23 |
|
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: 96.77 E-value: 6.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDR----TLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVE------WTPGTHYGYLDQ 73
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 74 HTVLTPGRTIRDVLAdafLPLfekekalnevtekmgtatpeeleelleqmaEIQDALEAggfylldmKIEEAARGLgIDA 153
Cdd:cd03293 81 QDALLPWLTVLDNVA---LGL------------------------------ELQGVPKA--------EARERAEEL-LEL 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445977555 154 IGL----DRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV---EHIH-WLTNYLKEYPHAFLLISHD 218
Cdd:cd03293 119 VGLsgfeNAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltrEQLQeELLDIWRETGKTVLLVTHD 191
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-229 |
8.88e-23 |
|
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: 96.50 E-value: 8.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV--------EWTPGT---HYGYLDQHTVLTPGrTIRDVLA 88
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdirQLDPADlrrNIGYVPQDVTLFYG-TLRDNIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 89 daflplfekekalnevtekmgtatpeeleelleqmaeiqdaleAGGFYLLDMKIEEAARGLGIDAI------GLDRDVS- 161
Cdd:cd03245 100 -------------------------------------------LGAPLADDERILRAAELAGVTDFvnkhpnGLDLQIGe 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 162 ---ALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD----VEHIHWLTNYLKeyPHAFLLISHDTEFMNKCVDVI 229
Cdd:cd03245 137 rgrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDmnseERLKERLRQLLG--DKTLIIITHRPSLLDLVDRII 209
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-218 |
1.36e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.15 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVE--------WTPG---THYGYL 71
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngrpladWSPAelaRRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 72 DQHTVLTPGRTIRDVLAdaflplfekekalnevtekMGtATPEELEELLEQmAEIQDALEAggfylldmkieeaarglgI 151
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVA-------------------MG-RAPHGLSRAEDD-ALVAAALAQ------------------V 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 152 DAIGL-DRDVSALSGGQRTKVLLAKLLL------EQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPH----AFLLISHD 218
Cdd:PRK13548 123 DLAHLaGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHerglAVIVVLHD 200
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-232 |
1.38e-22 |
|
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: 100.82 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRT-LFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV--------EWTPGTHY---GYL 71
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvplaDADADSWRdqiAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 72 DQHTVLTPGrTIRDVLAdaflplfekeKALNEVTEkmgtatpeeleelleqmAEIQDALEAGGfyLLDMkieEAARGLGI 151
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIR----------LARPDASD-----------------AEIREALERAG--LDEF---VAALPQGL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 152 DAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYP--HAFLLISHDTEFMNKCvDVI 229
Cdd:TIGR02857 449 DTP-IGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAqgRTVLLVTHRLALAALA-DRI 526
|
...
gi 445977555 230 FHL 232
Cdd:TIGR02857 527 VVL 529
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-233 |
2.52e-22 |
|
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: 95.25 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTF--GDRTLF--KDVSMRLLAGEHVGLVGANGVGKSTFMNIIT-------------GQLIHDQGRVEWTP-- 64
Cdd:cd03255 1 IELKNLSKTYggGGEKVQalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGgldrptsgevrvdGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 65 GTHYGYLDQHTVLTPGRTIRD-VLadafLPLFEKEKALNEvtekmgtatpeeleelleqmaeiqdaleaggfylLDMKIE 143
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALEnVE----LPLLLAGVPKKE----------------------------------RRERAE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 144 EAARGLGIDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEH----IHWLTNYLKEYPHAFLLISHDT 219
Cdd:cd03255 123 ELLERVGLGDR-LNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP 201
|
250
....*....|....
gi 445977555 220 EFMNKCvDVIFHLE 233
Cdd:cd03255 202 ELAEYA-DRIIELR 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-233 |
5.18e-22 |
|
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: 99.46 E-value: 5.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTF--GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV--------EWTPGT---HYGY 70
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvdlrDLDEDDlrrRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 71 LDQHTVLTPGrTIRDVLadaflpLFekekALNEVTEkmgtatpeeleelleqmAEIQDALEAGGfyLLDMkIEEAARGLg 150
Cdd:COG4987 414 VPQRPHLFDT-TLRENL------RL----ARPDATD-----------------EELWAALERVG--LGDW-LAALPDGL- 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 151 iDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEY--PHAFLLISHDTEFMNKcVDV 228
Cdd:COG4987 462 -DTW-LGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHRLAGLER-MDR 538
|
....*
gi 445977555 229 IFHLE 233
Cdd:COG4987 539 ILVLE 543
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-477 |
9.30e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.17 E-value: 9.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW--------TPG--THYG--- 69
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdgepvrfrSPRdaQAAGiai 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 70 -YldQHTVLTPGRTIRDVLadaFLplfekekalnevtekmgtatpeeleelleqmaeiqdALEAGGFYLLDMK--IEEAA 146
Cdd:COG1129 84 iH--QELNLVPNLSVAENI---FL------------------------------------GREPRRGGLIDWRamRRRAR 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 147 R---GLGIDaIGLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYL---DVEHIHWLTNYLKEYPHAFLLISHdte 220
Cdd:COG1129 123 EllaRLGLD-IDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLterEVERLFRIIRRLKAQGVAIIYISH--- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 221 FMNKcvdvIFHL--EFTKMT--RYTATYekflELAEINKNQHINAyekqrefikkqedfiaknkarysTTGRAKSrqkql 296
Cdd:COG1129 199 RLDE----VFEIadRVTVLRdgRLVGTG----PVAELTEDELVRL-----------------------MVGRELE----- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 297 drmELIDRPETAIKPEfsfkesrassrfVFEGENVEIGythPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKP 376
Cdd:COG1129 243 ---DLFPKRAAAPGEV------------VLEVEGLSVG---GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPA 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 377 LSGKTSLG----DFLEP--------AYF-----------EQEVkADNIT-PIDDVWNTFPGLDQHQIRA----MLAKCGL 428
Cdd:COG1129 305 DSGEIRLDgkpvRIRSPrdairagiAYVpedrkgeglvlDLSI-RENITlASLDRLSRGGLLDRRRERAlaeeYIKRLRI 383
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 445977555 429 KNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAE 477
Cdd:COG1129 384 KTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAE 432
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
343-468 |
1.02e-21 |
|
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: 91.56 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEP-----------AYFEQEV-------KADNITPI 404
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdderkslrkeiGYVFQDPqlfprltVRENLRLG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445977555 405 DDVWNTFPGLDQHQIRAMLAKCGLK---NEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTN 468
Cdd:pfam00005 84 LLLKGLSKREKDARAEEALEKLGLGdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
337-497 |
1.62e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.30 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 337 HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPAYFEQEVKADN---ITPIDDV------ 407
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDslpLTVRDLVamgrwa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 408 ----WNTFPGLDQHQIRAMLAKCGLKnEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMK 483
Cdd:NF040873 85 rrglWRRLTRDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLA 163
|
170
....*....|....*..
gi 445977555 484 AYKG---TILLVCHEPD 497
Cdd:NF040873 164 EEHArgaTVVVVTHDLE 180
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-484 |
1.82e-21 |
|
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: 97.20 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHD--QGRVEW------------TPGTHY 68
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWsgsplkasnirdTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 69 GYLDQHTVLTPGRTirdVLADAFLPlfekekalNEVTEKMGtatpeeleelleQMAeiqdaleaggFYLLDMKIEEAARG 148
Cdd:TIGR02633 81 VIIHQELTLVPELS---VAENIFLG--------NEITLPGG------------RMA----------YNAMYLRAKNLLRE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 149 LGIDAIGLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNY---LKEYPHAFLLISHDTEFMNKC 225
Cdd:TIGR02633 128 LQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIirdLKAHGVACVYISHKLNEVKAV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 226 VDVIfhleftkmtrytatyekflelAEINKNQHInayekqrefikkqedfiaknkarySTTGRAKSRQKQLDRMeLIDRP 305
Cdd:TIGR02633 208 CDTI---------------------CVIRDGQHV------------------------ATKDMSTMSEDDIITM-MVGRE 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 306 ETAIKPefsfKESRASSRFVFEGENVEIgyTHPLLPK------LSMTIERGEKIAIVGCNGVGKSTLLKTILGKI----- 374
Cdd:TIGR02633 242 ITSLYP----HEPHEIGDVILEARNLTC--WDVINPHrkrvddVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpgkfe 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 375 -------KPLSGKTSLGDFLEP-AYFEQEVKADNITPIDDV--------WNTFPGL-------DQHQIRAMLAKCGLKNE 431
Cdd:TIGR02633 316 gnvfingKPVDIRNPAQAIRAGiAMVPEDRKRHGIVPILGVgknitlsvLKSFCFKmridaaaELQIIGSAIQRLKVKTA 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 445977555 432 HISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKA 484
Cdd:TIGR02633 396 SPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQ 448
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-220 |
1.98e-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: 93.61 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLI-----------HDQGRVE-WTPGTHY 68
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPptygndvrlfgERRGGEDvWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 69 GYL--DQHTVLTPGRTIRDVLADAF---LPLFekekalNEVTEkmgtatpeeleelleqmAEIQDALEaggfyLLDMkie 143
Cdd:COG1119 81 GLVspALQLRFPRDETVLDVVLSGFfdsIGLY------REPTD-----------------EQRERARE-----LLEL--- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 144 eaargLGIDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYL----KEYPHAFLLISHDT 219
Cdd:COG1119 130 -----LGLAHL-ADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLdklaAEGAPTLVLVTHHV 203
|
.
gi 445977555 220 E 220
Cdd:COG1119 204 E 204
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-220 |
6.46e-21 |
|
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: 91.10 E-value: 6.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHvGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGT----------HYGYLDQ 73
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDvlkqpqklrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 74 HTVLTPGRTIRDVLADAflplfekeKALNEVTEKmgtatpeeleellEQMAEIQDALEAGGfyLLDMKieeaarglgida 153
Cdd:cd03264 80 EFGVYPNFTVREFLDYI--------AWLKGIPSK-------------EVKARVDEVLELVN--LGDRA------------ 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445977555 154 iglDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYP--HAFLLISHDTE 220
Cdd:cd03264 125 ---KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGedRIVILSTHIVE 190
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-220 |
6.85e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 94.06 E-value: 6.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLlTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW---------TPGT-HYGY 70
Cdd:COG1118 1 MSI-EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLngrdlftnlPPRErRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 71 LDQHTVLTPGRTIRD-VladAF----LPLFEKEKAlnevtekmgtatpeeleelleqmaeiQDALEaggfyLLDMkieea 145
Cdd:COG1118 80 VFQHYALFPHMTVAEnI---AFglrvRPPSKAEIR--------------------------ARVEE-----LLEL----- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 146 arglgIDAIGL-DRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVeHIH-----WLTNYLKEYPHAFLLISHDT 219
Cdd:COG1118 121 -----VQLEGLaDRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDA-KVRkelrrWLRRLHDELGGTTVFVTHDQ 194
|
.
gi 445977555 220 E 220
Cdd:COG1118 195 E 195
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-229 |
1.37e-20 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 89.97 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGqLIH-DQGRVEwtpgthygyldqhtvltpgrt 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILG-LIKpDSGEIT--------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 irdvladaflpLFEKEKALN-EVTEKMGTAtpeeleelleqmaeiqdaLEAGGFY-----------------LLDMKIEE 144
Cdd:cd03268 59 -----------FDGKSYQKNiEALRRIGAL------------------IEAPGFYpnltarenlrllarllgIRKKRIDE 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 145 AARGLGIDAIGlDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNY---LKEYPHAFLLISHDTEF 221
Cdd:cd03268 110 VLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELilsLRDQGITVLISSHLLSE 188
|
....*...
gi 445977555 222 MNKCVDVI 229
Cdd:cd03268 189 IQKVADRI 196
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-220 |
3.82e-20 |
|
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: 88.73 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV--------EWTPG-THYGYLDQH 74
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrdvtGVPPErRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 75 TVLTPGRTIRDVLAdafLPLfeKEKALNEvtekmgtatpeeleelleqmAEIQDaleaggfylldmKIEEAARGLGIDAI 154
Cdd:cd03259 81 YALFPHLTVAENIA---FGL--KLRGVPK--------------------AEIRA------------RVRELLELVGLEGL 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 155 gLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAF----LLISHDTE 220
Cdd:cd03259 124 -LNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELgittIYVTHDQE 192
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-218 |
5.63e-20 |
|
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: 93.04 E-value: 5.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTF-----GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTpGTHYGYLDQHTVL 77
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD-GKDLTKLSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 78 TPGRTIRDVLADAFLPLFEKEKALNEVTE---KMGTATPeeleelleqmAEIQDALEAggfyLLDMkieeaargLGIDAI 154
Cdd:COG1123 339 ELRRRVQMVFQDPYSSLNPRMTVGDIIAEplrLHGLLSR----------AERRERVAE----LLER--------VGLPPD 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 155 GLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLK----EYPHAFLLISHD 218
Cdd:COG1123 397 LADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlqrELGLTYLFISHD 464
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-229 |
7.20e-20 |
|
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: 88.65 E-value: 7.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLD----------- 72
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV---------LFDgeditglpphe 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 73 ----------QHTVLTPGRTIRDVLAdaflplfekekalneVTEKMGTATPEELEELLEQMAEIQDaleaggfylldmKI 142
Cdd:cd03219 72 iarlgigrtfQIPRLFPELTVLENVM---------------VAAQARTGSGLLLARARREEREARE------------RA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 143 EEAARGLGIDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYP---HAFLLISHDT 219
Cdd:cd03219 125 EELLERVGLADL-ADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRergITVLLVEHDM 203
|
250
....*....|
gi 445977555 220 EFMNKCVDVI 229
Cdd:cd03219 204 DVVMSLADRV 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-232 |
1.13e-19 |
|
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: 88.56 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLD-------- 72
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRI---------LFDgrditglp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 73 -------------QHTVLTPGRTIRDVLADAflplfekekalneVTEKMGTATPEELEELLEQMAEIQDALEaggfylld 139
Cdd:COG0411 73 phriarlgiartfQNPRLFPELTVLENVLVA-------------AHARLGRGLLAALLRLPRARREEREARE-------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 140 mKIEEAARGLGIDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEP--------TNYLdVEHIHWLTnylKEYPHA 211
Cdd:COG0411 132 -RAEELLERVGLADR-ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPaaglnpeeTEEL-AELIRRLR---DERGIT 205
|
250 260
....*....|....*....|.
gi 445977555 212 FLLISHDtefmnkcVDVIFHL 232
Cdd:COG0411 206 ILLIEHD-------MDLVMGL 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
300-509 |
1.51e-19 |
|
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: 91.58 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 300 ELIDRPEtaiKPEFSFKESRASSRFVFEGENVEIGY--THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPL 377
Cdd:TIGR02857 299 AVLDAAP---RPLAGKAPVTAAPASSLEFSGVSVAYpgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 378 SGKTSLG-----DFLE-------------PAYFEQEVkADNITPIDdvwntfPGLDQHQIRAMLAKCGLKNEHISRPL-- 437
Cdd:TIGR02857 376 EGSIAVNgvplaDADAdswrdqiawvpqhPFLFAGTI-AENIRLAR------PDASDAEIREALERAGLDEFVAALPQgl 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 438 --------SQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAYKG--TILLVCHEPDFYEdWITKVW 507
Cdd:TIGR02857 449 dtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALAA-LADRIV 527
|
..
gi 445977555 508 DV 509
Cdd:TIGR02857 528 VL 529
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-197 |
1.88e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.29 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgtHYGYLDQHTV--LT 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTV------LVAGDDVEALsaRA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 79 PGRTIRDVLADAFLPLfekEKALNEVTEkMGTaTPeeleelleQMAEIQDALEAGgfyllDMKIEEAARGLGIDAIGlDR 158
Cdd:PRK09536 75 ASRRVASVPQDTSLSF---EFDVRQVVE-MGR-TP--------HRSRFDTWTETD-----RAAVERAMERTGVAQFA-DR 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 445977555 159 DVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEH 197
Cdd:PRK09536 136 PVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINH 174
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
336-501 |
1.97e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 86.94 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 336 THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKtSLGDFLEPAYFEQEVKADNITPIDDVwntfpgld 415
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA-GCVDVPDNQFGREASLIDAIGRKGDF-------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 416 qHQIRAMLAKCGLkNEHIS--RPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD-VTAK---AELKKAMKAYKGTI 489
Cdd:COG2401 113 -KDAVELLNAVGL-SDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrQTAKrvaRNLQKLARRAGITL 190
|
170
....*....|..
gi 445977555 490 LLVCHEPDFYED 501
Cdd:COG2401 191 VVATHHYDVIDD 202
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
299-510 |
2.44e-19 |
|
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: 90.97 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 299 MELIDRPETAIKPEFSFKESRASSRFVFEgeNVEIGY--THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKP 376
Cdd:COG4988 312 FALLDAPEPAAPAGTAPLPAAGPPSIELE--DVSFSYpgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 377 LSGK-----TSLGDFLEPAYFEQEVK------------ADNITpiddvwntF--PGLDQHQIRAMLAKCGLkNEHISR-- 435
Cdd:COG4988 390 YSGSilingVDLSDLDPASWRRQIAWvpqnpylfagtiRENLR--------LgrPDASDEELEAALEAAGL-DEFVAAlp 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 436 -----PL----SQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAYKG--TILLVCHEPDFYEDWiT 504
Cdd:COG4988 461 dgldtPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALLAQA-D 539
|
....*.
gi 445977555 505 KVWDVE 510
Cdd:COG4988 540 RILVLD 545
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
329-494 |
2.58e-19 |
|
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: 85.13 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGY---THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDflepayfeqevkadniTPID 405
Cdd:cd03228 4 KNVSFSYpgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG----------------VDLR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 406 DvwntfpgLDQHQIRAMLA----KCGLKN----EHIsrplsqLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAE 477
Cdd:cd03228 68 D-------LDLESLRKNIAyvpqDPFLFSgtirENI------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170
....*....|....*....
gi 445977555 478 LKKAMKAYKG--TILLVCH 494
Cdd:cd03228 135 ILEALRALAKgkTVIVIAH 153
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
339-515 |
3.15e-19 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 91.00 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 339 LLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPAYFEQEVKADNITPIDDVWN---TFPGL- 414
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIDgdrEYRQLe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 415 ----------DQHQI-----------------RA--MLAKCGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDE 465
Cdd:PRK10636 96 aqlhdanernDGHAIatihgkldaidawtirsRAasLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 445977555 466 PTNHLDVTAKAELKKAMKAYKGTILLVCHEPDFYEDWITKVWDVEEWSQN 515
Cdd:PRK10636 176 PTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLF 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-217 |
4.17e-19 |
|
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: 84.40 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLDqhtvltpGRTI 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI---------LVD-------GKEV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 84 RdvladaflplfekekalnevtekmgTATPeeleelleqmaeiQDALEAGgfylldmkieeaarglgidaIGLdrdVSAL 163
Cdd:cd03216 65 S-------------------------FASP-------------RDARRAG--------------------IAM---VYQL 83
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 445977555 164 SGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNY---LKEYPHAFLLISH 217
Cdd:cd03216 84 SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVirrLRAQGVAVIFISH 140
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-233 |
4.47e-19 |
|
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: 85.39 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 5 TVEKLGHTFGDRT-LFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTpGTHYGYLDQHtvltpgRTI 83
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLN-GKPIKAKERR------KSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 84 RDVLADAFLPLFEkEKALNEVTEKMgtatpeeleelleqmaeiqDALEAGGfylldMKIEEAARGLGIDAIGlDRDVSAL 163
Cdd:cd03226 74 GYVMQDVDYQLFT-DSVREELLLGL-------------------KELDAGN-----EQAETVLKDLDLYALK-ERHPLSL 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445977555 164 SGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYP---HAFLLISHDTEFMNKCVDVIFHLE 233
Cdd:cd03226 128 SGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAaqgKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
299-496 |
5.72e-19 |
|
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: 89.83 E-value: 5.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 299 MELIDRPETAIKPEfsfKESRASSRFVFEGENVEIGY---THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIK 375
Cdd:COG4987 310 NELLDAPPAVTEPA---EPAPAPGGPSLELEDVSFRYpgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 376 PLSGKTSLG-----DFLEP------AYFEQEVK------ADNITPIDdvwntfPGLDQHQIRAMLAKCGLKNEHISRPL- 437
Cdd:COG4987 387 PQSGSITLGgvdlrDLDEDdlrrriAVVPQRPHlfdttlRENLRLAR------PDATDEELWAALERVGLGDWLAALPDg 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445977555 438 ---------SQLSGGEQAkvRLC--KLMGEESNWLLFDEPTNHLD-VTAKAELKKAMKAYKG-TILLVCHEP 496
Cdd:COG4987 461 ldtwlgeggRRLSGGERR--RLAlaRALLRDAPILLLDEPTEGLDaATEQALLADLLEALAGrTVLLITHRL 530
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
326-498 |
5.95e-19 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 85.72 E-value: 5.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 326 FEGENVEIGY---THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDF----LEPA-------Y 391
Cdd:cd03245 3 IEFRNVSFSYpnqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqLDPAdlrrnigY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 392 FEQEVK------ADNIT----PIDDV----WNTFPGLDQhqiramlakcgLKNEH-------ISRPLSQLSGGEQAKVRL 450
Cdd:cd03245 83 VPQDVTlfygtlRDNITlgapLADDErilrAAELAGVTD-----------FVNKHpngldlqIGERGRGLSGGQRQAVAL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 445977555 451 CKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAYKG--TILLVCHEPDF 498
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSL 201
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
343-506 |
1.30e-18 |
|
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: 85.29 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLgDFLEPAYFEQEVKA------------DNITPIDDVW-- 408
Cdd:COG4555 20 VSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI-DGEDVRKEPREARRqigvlpderglyDRLTVRENIRyf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 409 NTFPGLDQHQIRA---MLAKC-GLkNEHISRPLSQLSGGEQAKVRL-CKLMGEESNwLLFDEPTNHLDVTAKAELKKAMK 483
Cdd:COG4555 99 AELYGLFDEELKKrieELIELlGL-EEFLDRRVGELSTGMKKKVALaRALVHDPKV-LLLDEPTNGLDVMARRLLREILR 176
|
170 180
....*....|....*....|....*.
gi 445977555 484 AYKG---TILLVCHEPDFYEDWITKV 506
Cdd:COG4555 177 ALKKegkTVLFSSHIMQEVEALCDRV 202
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
329-495 |
1.47e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.45 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGY-THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD----------------FLePay 391
Cdd:PRK11231 6 ENLTVGYgTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarrlaLL-P-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 392 fEQEVKADNIT----------PIDDVWNTFPGLDQHQIRAMLAKCGLkNEHISRPLSQLSGGEQAKVRLCKLMGEESNWL 461
Cdd:PRK11231 83 -QHHLTPEGITvrelvaygrsPWLSLWGRLSAEDNARVNQAMEQTRI-NHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 445977555 462 LFDEPTNHLDVTAKAELKKAMKAYKG---TILLVCHE 495
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTqgkTVVTVLHD 197
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-194 |
1.54e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.07 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHD---QGRVewtpgthygYLDqHTVLTPG 80
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEV---------LLN-GRRLTAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 81 ----RTIRDVLADAflPLFEKekaLNeVTEKMGTATPEELEELLEQmAEIQDALEA---GGFYlldmkieeaarglgida 153
Cdd:COG4136 72 paeqRRIGILFQDD--LLFPH---LS-VGENLAFALPPTIGRAQRR-ARVEQALEEaglAGFA----------------- 127
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 445977555 154 iglDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:COG4136 128 ---DRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
296-494 |
2.52e-18 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 88.35 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 296 LDRM-ELIDRPetaikPEFSFKESRASsRFVFEG----ENVEIGY---THPLLPKLSMTIERGEKIAIVGCNGVGKSTLL 367
Cdd:COG2274 445 LERLdDILDLP-----PEREEGRSKLS-LPRLKGdielENVSFRYpgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLL 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 368 KTILGKIKPLSGKTSLGDF----LEP-------AYFEQEVK------ADNITpiddVWNtfPGLDQHQIRAMLAKCGLKN 430
Cdd:COG2274 519 KLLLGLYEPTSGRILIDGIdlrqIDPaslrrqiGVVLQDVFlfsgtiRENIT----LGD--PDATDEEIIEAARLAGLHD 592
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445977555 431 EHISRPL----------SQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAYKG--TILLVCH 494
Cdd:COG2274 593 FIEALPMgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAH 668
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-501 |
4.07e-18 |
|
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: 87.17 E-value: 4.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITG--QLIHDQGRVEWTPG--THYGYLD-QHTVLT 78
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVAlcEKCGYVErPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 79 P----GRTIRDVLADaFLPLFEKEKAlnEVTEKMGTATPEELEELLEQ--MAEIQDALEAGGfYLLDMKIEEAARGLGID 152
Cdd:TIGR03269 81 PcpvcGGTLEPEEVD-FWNLSDKLRR--RIRKRIAIMLQRTFALYGDDtvLDNVLEALEEIG-YEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 153 AIG-----LDRDvsaLSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD---VEHIH-WLTNYLKEYPHAFLLISHDTEFMN 223
Cdd:TIGR03269 157 QLShrithIARD---LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKLVHnALEEAVKASGISMVLTSHWPEVIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 224 KCVDVIFHLE---FTKMTRYTATYEKFLELAEinknqhinAYEKQREFIKKQEDFIAKN-KARYSTTGRAKSRqkqldrm 299
Cdd:TIGR03269 234 DLSDKAIWLEngeIKEEGTPDEVVAVFMEGVS--------EVEKECEVEVGEPIIKVRNvSKRYISVDRGVVK------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 300 elidrpetAIkpefsfkesrassrfvfegENVeigythpllpklSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSG 379
Cdd:TIGR03269 299 --------AV-------------------DNV------------SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 380 KTS--LGD-----------------------FLEPAYFEQEVKADNITpiDDVWNTFPG-LDQHQIRAMLAKCGLKNEHI 433
Cdd:TIGR03269 340 EVNvrVGDewvdmtkpgpdgrgrakryigilHQEYDLYPHRTVLDNLT--EAIGLELPDeLARMKAVITLKMVGFDEEKA 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445977555 434 SRPL----SQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD----VTAKAELKKAMKAYKGTILLVCHEPDFYED 501
Cdd:TIGR03269 418 EEILdkypDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFVLD 493
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
20-194 |
5.06e-18 |
|
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: 87.23 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV--------EWTPGT---HYGYLDQHTVLTPGrTIRDVLA 88
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVlldgvdirQIDPADlrrNIGYVPQDPRLFYG-TLRDNIA 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 89 daflplfekekalnevtekMGTATPEEleelleqmAEIQDALEAGGfylldmkIEEAARGlgiDAIGLDRDVS----ALS 164
Cdd:TIGR03375 561 -------------------LGAPYADD--------EEILRAAELAG-------VTEFVRR---HPDGLDMQIGergrSLS 603
|
170 180 190
....*....|....*....|....*....|
gi 445977555 165 GGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:TIGR03375 604 GGQRQAVALARALLRDPPILLLDEPTSAMD 633
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-233 |
7.75e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 82.40 E-value: 7.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MS-LLTVEKLGHTFGD----RTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW--TP--------- 64
Cdd:COG1136 1 MSpLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIdgQDisslserel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 65 ----GTHYGYLDQHTVLTPGRTIRD-VLadafLPLFEKEKALNEVTEKmgtatpeeleelleqmaeIQDALEAggfylld 139
Cdd:COG1136 81 arlrRRHIGFVFQFFNLLPELTALEnVA----LPLLLAGVSRKERRER------------------ARELLER------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 140 mkieeaargLGIDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEH----IHWLTNYLKEYPHAFLLI 215
Cdd:COG1136 132 ---------VGLGDR-LDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMV 201
|
250
....*....|....*...
gi 445977555 216 SHDTEFMNKCvDVIFHLE 233
Cdd:COG1136 202 THDPELAARA-DRVIRLR 218
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-227 |
8.23e-18 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 86.76 E-value: 8.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGTHYGYLDQHTVltpgrt 82
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQL------ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 irDVLADAFLPLFEKEKALNEVTEKmgtatpeeleelleqmaEIQDALeaGGFYLLDMKIEEAARglgidaigldrdvsA 162
Cdd:PRK10636 386 --EFLRADESPLQHLARLAPQELEQ-----------------KLRDYL--GGFGFQGDKVTEETR--------------R 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 163 LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAFLLISHDTEFMNKCVD 227
Cdd:PRK10636 431 FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTD 495
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-495 |
8.73e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.99 E-value: 8.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwTPGTHYGYLDQHTVLTPGRT 82
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTIT-INNINYNKLDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 IrdvladaflpLFEKEKALNEVTekmgtatpeeleelleqmaeIQDALEAG--------GFYLLDMKIEEAARGLGIDAI 154
Cdd:PRK09700 84 I----------IYQELSVIDELT--------------------VLENLYIGrhltkkvcGVNIIDWREMRVRAAMMLLRV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 155 GLDRD----VSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYL---DVEHIHWLTNYLKEYPHAFLLISHDTEFMNKCVD 227
Cdd:PRK09700 134 GLKVDldekVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 228 vifhleftkmtRYT----ATYEKFLELAEINkNQHINAYEKQREFikkqedfiaknKARYSTTgraksrqkqldrmelid 303
Cdd:PRK09700 214 -----------RYTvmkdGSSVCSGMVSDVS-NDDIVRLMVGREL-----------QNRFNAM----------------- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 304 RPETaikpefsfkeSRASSRFVFEGENVeIGYTHPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSL 383
Cdd:PRK09700 254 KENV----------SNLAHETVFEVRNV-TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRL 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 384 -GDFLEP-----------AYFEQEVKADNITPIDDV------------------WNTFPGLDQHQI----RAMLA-KCGL 428
Cdd:PRK09700 323 nGKDISPrspldavkkgmAYITESRRDNGFFPNFSIaqnmaisrslkdggykgaMGLFHEVDEQRTaenqRELLAlKCHS 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 429 KNEHISrplsQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMK--AYKG-TILLVCHE 495
Cdd:PRK09700 403 VNQNIT----ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRqlADDGkVILMVSSE 468
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-197 |
9.40e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.75 E-value: 9.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW--TPGTHYG---------YLD 72
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLgdKPISMLSsrqlarrlaLLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 73 QHTVLTPGRTIRDVLA---DAFLPLFEKekaLNEVTEKMgtatpeeleelleqmaeIQDALEaggfyllDMKIEEAArgl 149
Cdd:PRK11231 83 QHHLTPEGITVRELVAygrSPWLSLWGR---LSAEDNAR-----------------VNQAME-------QTRINHLA--- 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 445977555 150 gidaiglDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEH 197
Cdd:PRK11231 133 -------DRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH 173
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
338-495 |
1.11e-17 |
|
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: 82.94 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 338 PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLG--DF---------LEPAYFEQEVKAD-NITPID 405
Cdd:TIGR03873 15 LIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAgvDLhglsrraraRRVALVEQDSDTAvPLTVRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 406 DV----------WNTFPGLDQHQIRAMLAKCGLknEHI-SRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTA 474
Cdd:TIGR03873 95 VValgriphrslWAGDSPHDAAVVDRALARTEL--SHLaDRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRA 172
|
170 180
....*....|....*....|....
gi 445977555 475 KAELKKAMKAYKG---TILLVCHE 495
Cdd:TIGR03873 173 QLETLALVRELAAtgvTVVAALHD 196
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-229 |
1.97e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 80.79 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW-------TPGTHYGYLDQHTV 76
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkpldiAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 77 LTPGRTIRDVLAD-AFLPLFEKEKALNEVTEkmgtatpeeleelleqmaeiqdaleaggfYLLDMKIEEAArglgidaig 155
Cdd:cd03269 81 LYPKMKVIDQLVYlAQLKGLKKEEARRRIDE-----------------------------WLERLELSEYA--------- 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 156 lDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD---VEHIHWLTNYLKEYPHAFLLISHDTEFMNK-CVDVI 229
Cdd:cd03269 123 -NKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDpvnVELLKDVIRELARAGKTVILSTHQMELVEElCDRVL 199
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-218 |
2.51e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 81.70 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGTHYGYLDQHTVLtpg 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 81 rtirdvlaDAFLPLfekekalnevtekmgTATPEELEELLEQMAEIQDALE---AGgfYLLDMKIEEaarglgidaigld 157
Cdd:PRK09544 79 --------DTTLPL---------------TVNRFLRLRPGTKKEDILPALKrvqAG--HLIDAPMQK------------- 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 158 rdvsaLSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE---HIHWLTNYLK-EYPHAFLLISHD 218
Cdd:PRK09544 121 -----LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNgqvALYDLIDQLRrELDCAVLMVSHD 180
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-233 |
6.10e-17 |
|
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: 78.58 E-value: 6.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 14 GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW--TPGTHY---------GYLDQHTVLTPGrT 82
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIdgVDLRDLdleslrkniAYVPQDPFLFSG-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 IRDVLadaflplfekekalnevtekmgtatpeeleelleqmaeiqdaleaggfylldmkieeaarglgidaigldrdvsa 162
Cdd:cd03228 92 IRENI--------------------------------------------------------------------------- 96
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445977555 163 LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYP--HAFLLISHDTEFMNKCvDVIFHLE 233
Cdd:cd03228 97 LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAkgKTVIVIAHRLSTIRDA-DRIIVLD 168
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
337-508 |
6.37e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 83.85 E-value: 6.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 337 HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKtILGKIKPL---------------------------------SGKTSL 383
Cdd:PRK11147 16 APLLDNAELHIEDNERVCLVGRNGAGKSTLMK-ILNGEVLLddgriiyeqdlivarlqqdpprnvegtvydfvaEGIEEQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 384 GDFLEpAY------FEQEVKADNITPIDDVWNTfpgLDQH-------QIRAMLAKCGLKNEhisRPLSQLSGGEQAKVRL 450
Cdd:PRK11147 95 AEYLK-RYhdishlVETDPSEKNLNELAKLQEQ---LDHHnlwqlenRINEVLAQLGLDPD---AALSSLSGGWLRKAAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 451 CKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAYKGTILLVCHEPDFYEDWITKVWD 508
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVD 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-189 |
6.38e-17 |
|
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: 79.89 E-value: 6.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVeWTPG---THY----------GY 70
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKI-LLDGqdiTKLpmhkrarlgiGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 71 LDQHTVLTPGRTIRDVLaDAFLPLFEKEKalnevtekmgtatpeeleelleqmAEIQDALEaggfYLLDMkieeaargLG 150
Cdd:cd03218 80 LPQEASIFRKLTVEENI-LAVLEIRGLSK------------------------KEREEKLE----ELLEE--------FH 122
|
170 180 190
....*....|....*....|....*....|....*....
gi 445977555 151 IDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEP 189
Cdd:cd03218 123 ITHL-RKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
343-501 |
6.96e-17 |
|
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: 78.21 E-value: 6.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGktslgdflepayfeqEVKADNITPIDDVwntfpgldqhqiRAM 422
Cdd:cd03230 19 ISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSG---------------EIKVLGKDIKKEP------------EEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 423 LAKCGLKNEHISRP--LS-----QLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAYK---GTILLV 492
Cdd:cd03230 72 KRRIGYLPEEPSLYenLTvrenlKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLS 151
|
....*....
gi 445977555 493 CHEPDFYED 501
Cdd:cd03230 152 SHILEEAER 160
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-229 |
7.14e-17 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 79.85 E-value: 7.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 6 VEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV-----EWTPGT---------HYGYL 71
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgeDISGLSeaelyrlrrRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 72 DQHTVLTPGRTIRDVLAdafLPLFEKEKaLNEvtekmgtatpeeleelleqmAEIQDaleaggfyLLDMKIEEAarGLGI 151
Cdd:cd03261 83 FQSGALFDSLTVFENVA---FPLREHTR-LSE--------------------EEIRE--------IVLEKLEAV--GLRG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 152 DAiglDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD-------VEHIHWLTnylKEYPHAFLLISHDTEFMNK 224
Cdd:cd03261 129 AE---DLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLK---KELGLTSIMVTHDLDTAFA 202
|
....*
gi 445977555 225 CVDVI 229
Cdd:cd03261 203 IADRI 207
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-194 |
8.73e-17 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 80.10 E-value: 8.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 2 SLLTVEKLGHTF-GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW--TPGTHY---------- 68
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVdgQDVTALrgralrrlrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 69 --GYLDQHTVLTPGRT-IRDVLA---------DAFLPLFEKEkalnevtekmgtatpeeleelleqmaEIQDALEAggfy 136
Cdd:COG3638 81 riGMIFQQFNLVPRLSvLTNVLAgrlgrtstwRSLLGLFPPE--------------------------DRERALEA---- 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 137 lLDMkieeaargLGIDAIGLDRdVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:COG3638 131 -LER--------VGLADKAYQR-ADQLSGGQQQRVAIARALVQEPKLILADEPVASLD 178
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
337-472 |
1.08e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 79.77 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 337 HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDflEP-------------AYFEQ--------- 394
Cdd:COG4559 14 RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNG--RPlaawspwelarrrAVLPQhsslafpft 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 395 --EVKADNITPiddvWNTFPGLDQHQIRAMLAKCGLkNEHISRPLSQLSGGEQAKVR----LCKL---MGEESNWLLFDE 465
Cdd:COG4559 92 veEVVALGRAP----HGSSAAQDRQIVREALALVGL-AHLAGRSYQTLSGGEQQRVQlarvLAQLwepVDGGPRWLFLDE 166
|
....*..
gi 445977555 466 PTNHLDV 472
Cdd:COG4559 167 PTSALDL 173
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
343-497 |
1.28e-16 |
|
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: 78.69 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD----FLEPAyfEQEV----KADNITPIDDVWNTF--- 411
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtAAPPA--DRPVsmlfQENNLFAHLTVEQNVglg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 412 --PGL-----DQHQIRAMLAKCGLKNEHISRPlSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELK----K 480
Cdd:cd03298 95 lsPGLkltaeDRQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLdlvlD 173
|
170
....*....|....*..
gi 445977555 481 AMKAYKGTILLVCHEPD 497
Cdd:cd03298 174 LHAETKMTVLMVTHQPE 190
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-207 |
1.32e-16 |
|
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: 79.15 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGD-RTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWtpgthYGYlDQHTVltPGRT 82
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLI-----DGT-DINKL--KGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 IRDVLAD-AFL----PLFEKEKAL-NEVTEKMGTATPEELEELLEQMAEIQDALEAggfylldmkieeaarglgIDAIGL 156
Cdd:cd03256 73 LRQLRRQiGMIfqqfNLIERLSVLeNVLSGRLGRRSTWRSLFGLFPKEEKQRALAA------------------LERVGL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 157 D----RDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKE 207
Cdd:cd03256 135 LdkayQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKR 189
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
343-496 |
1.37e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.38 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSL--GDFLEPAYFEQEVKA-------DNITPIDDV--WNTF 411
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdgGDIDDPDVAEACHYLghrnamkPALTVAENLefWAAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 412 PGLDQHQIRAMLAKCGLKN-EHIsrPLSQLSGGEQAKVRLCKLMGEESN-WLLfDEPTNHLDVTAKAELKKAMKAYK--- 486
Cdd:PRK13539 101 LGGEELDIAAALEAVGLAPlAHL--PFGYLSAGQKRRVALARLLVSNRPiWIL-DEPTAALDAAAVALFAELIRAHLaqg 177
|
170
....*....|
gi 445977555 487 GTILLVCHEP 496
Cdd:PRK13539 178 GIVIAATHIP 187
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
330-494 |
1.51e-16 |
|
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: 77.35 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 330 NVEIGYTH---PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPAYfeQEVKADNITpidd 406
Cdd:cd03247 5 NVSFSYPEqeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL--EKALSSLIS---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 407 VWNTFPGLDQHQIRAMLAKcglknehisrplsQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD-VTAKAELKKAMKAY 485
Cdd:cd03247 79 VLNQRPYLFDTTLRNNLGR-------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDpITERQLLSLIFEVL 145
|
170
....*....|
gi 445977555 486 KG-TILLVCH 494
Cdd:cd03247 146 KDkTLIWITH 155
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
350-503 |
1.54e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 82.47 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 350 GEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPAYFEQEVKAD-------NI--------------------- 401
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDpektvreNVeegvaevkaaldrfneiyaay 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 402 -TPIDDV-------------------WNtfpgLDqHQI-RAMLA-KCGLKNEhisrPLSQLSGGEQAKVRLCKLMGEESN 459
Cdd:PRK11819 113 aEPDADFdalaaeqgelqeiidaadaWD----LD-SQLeIAMDAlRCPPWDA----KVTKLSGGERRRVALCRLLLEKPD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 445977555 460 WLLFDEPTNHLDVTAKAELKKAMKAYKGTILLVCHEPDFYED---WI 503
Cdd:PRK11819 184 MLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNvagWI 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-195 |
1.67e-16 |
|
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: 77.92 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGthygyldqhtvltPGRTI 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-------------PLDFQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 84 RDVLADAFLPLFEKE--KALNEVTEKMGTATPEELeelleqmaeiqdaleaggfyllDMKIEEAARGLGIDAIGlDRDVS 161
Cdd:cd03231 68 RDSIARGLLYLGHAPgiKTTLSVLENLRFWHADHS----------------------DEQVEEALARVGLNGFE-DRPVA 124
|
170 180 190
....*....|....*....|....*....|....
gi 445977555 162 ALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV 195
Cdd:cd03231 125 QLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-196 |
1.94e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 82.13 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 14 GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV--------EWTPGT---HYGYLDQHTVLTPGrT 82
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirDLTLESlrrQIGVVPQDTFLFSG-T 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 IRDVLAdaflplfekekalnevtekMG--TATpeeleelleqMAEIQDALEAGGfylldmkIEEAARGL--GIDA-IGlD 157
Cdd:COG1132 430 IRENIR-------------------YGrpDAT----------DEEVEEAAKAAQ-------AHEFIEALpdGYDTvVG-E 472
|
170 180 190
....*....|....*....|....*....|....*....
gi 445977555 158 RDVSaLSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE 196
Cdd:COG1132 473 RGVN-LSGGQRQRIAIARALLKDPPILILDEATSALDTE 510
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-218 |
2.68e-16 |
|
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: 78.14 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwtpgthygyldqhtvltpgrtirdVLAdaFLPLFEKEK 99
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR------------------------VAG--LVPWKRRKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 100 ALNEVTEKMGTATpeeleelleQMaeIQDALEAGGFYLL----DMKIEEAARG-------LGIDAIgLDRDVSALSGGQR 168
Cdd:cd03267 92 FLRRIGVVFGQKT---------QL--WWDLPVIDSFYLLaaiyDLPPARFKKRldelselLDLEEL-LDTPVRQLSLGQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 445977555 169 TKVLLAKLLLEQPEVLLLDEPTNYLDV---EHIH-WLTNYLKEYPHAFLLISHD 218
Cdd:cd03267 160 MRAEIAAALLHEPEILFLDEPTIGLDVvaqENIRnFLKEYNRERGTTVLLTSHY 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
326-496 |
3.05e-16 |
|
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: 76.49 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 326 FEGENVEIGY---THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGK-------------TSLGDFLep 389
Cdd:cd03246 1 LEVENVSFRYpgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRvrldgadisqwdpNELGDHV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 390 AYFEQEVK------ADNItpiddvwntfpgldqhqiramlakcglknehisrplsqLSGGEQAKVRLCKLMGEESNWLLF 463
Cdd:cd03246 79 GYLPQDDElfsgsiAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190
....*....|....*....|....*....|....*.
gi 445977555 464 DEPTNHLDVTAKAELK---KAMKAYKGTILLVCHEP 496
Cdd:cd03246 121 DEPNSHLDVEGERALNqaiAALKAAGATRIVIAHRP 156
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-217 |
5.77e-16 |
|
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: 76.24 E-value: 5.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPgthygyldqhtvlTPGRTI 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG-------------TPLAEQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 84 RDVLADAFLPLFEKEKALNEVTekmgtatpeeleelleqmaeiqdALEAGGFY-----LLDMKIEEAARGLGIDAIGlDR 158
Cdd:TIGR01189 68 RDEPHENILYLGHLPGLKPELS-----------------------ALENLHFWaaihgGAQRTIEDALAAVGLTGFE-DL 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445977555 159 DVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPH---AFLLISH 217
Cdd:TIGR01189 124 PAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLArggIVLLTTH 185
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
329-497 |
7.24e-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: 76.40 E-value: 7.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGY-THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD----------------FLEPAY 391
Cdd:cd03259 4 KGLSKTYgSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvpperrnigmvFQDYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 392 FEQEVKADNItpiddvwnTFP----GLDQHQIRA----MLAKCGLKNeHISRPLSQLSGGEQAKVRLCKLMGEESNWLLF 463
Cdd:cd03259 84 FPHLTVAENI--------AFGlklrGVPKAEIRArvreLLELVGLEG-LLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 445977555 464 DEPTNHLDVTAKAELKKAMKAY----KGTILLVCHEPD 497
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqrelGITTIYVTHDQE 192
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
346-499 |
7.43e-16 |
|
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: 77.06 E-value: 7.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 346 TIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLgDFLEPAYFEQEVKADNITPIDD-VWNTFPGLDQH-QIRAML 423
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIKADYEGTVRDlLSSITKDFYTHpYFKTEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 424 AKcGLKNEHI-SRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAY----KGTILLVCHepDF 498
Cdd:cd03237 100 AK-PLQIEQIlDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEH--DI 176
|
.
gi 445977555 499 Y 499
Cdd:cd03237 177 I 177
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-218 |
7.71e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.42 E-value: 7.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTF---------GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTpGTHYGYL 71
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR-GEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 72 DQHTVLTPGRTIRDVLADAFlplfekekalnevtekmGTATPEELEElleqmAEIQDALEaggfYLLDM-------KIEE 144
Cdd:PRK10419 80 NRAQRKAFRRDIQMVFQDSI-----------------SAVNPRKTVR-----EIIREPLR----HLLSLdkaerlaRASE 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 145 AARGLGIDAIGLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV----EHIHWLTNYLKEYPHAFLLISHD 218
Cdd:PRK10419 134 MLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHD 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-484 |
8.14e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.97 E-value: 8.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHdqgrvewtpGTHYG--YLDQHTVltPG 80
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPH---------GTYEGeiIFEGEEL--QA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 81 RTIRDvladaflplfekekalnevTEKMGTATPEELEELLEQM--AE---IQDALEAGGFYLLDMKIEEAA---RGLGID 152
Cdd:PRK13549 74 SNIRD-------------------TERAGIAIIHQELALVKELsvLEnifLGNEITPGGIMDYDAMYLRAQkllAQLKLD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 153 aIGLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYL---DVEHIHWLTNYLKEYPHAFLLISHDTEFMNKCVDVI 229
Cdd:PRK13549 135 -INPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLtesETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 230 fhleftkmtrytatyekflelAEINKNQHInAYEKQREFikKQEDFIAKnkarysTTGRaksrqkqldrmELidrpeTAI 309
Cdd:PRK13549 214 ---------------------CVIRDGRHI-GTRPAAGM--TEDDIITM------MVGR-----------EL-----TAL 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 310 KPefsfKESRASSRFVFEGENVEIgyTHPLLPK------LSMTIERGEKIAIVGCNGVGKSTLLKTILG--------KI- 374
Cdd:PRK13549 248 YP----REPHTIGEVILEVRNLTA--WDPVNPHikrvddVSFSLRRGEILGIAGLVGAGRTELVQCLFGaypgrwegEIf 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 375 ---KPLSGKTSLgDFLEP--AYFEQEVKADNITPIDDVWN--TFPGLDQ-------------HQIRAMLAKCGLKNEHIS 434
Cdd:PRK13549 322 idgKPVKIRNPQ-QAIAQgiAMVPEDRKRDGIVPVMGVGKniTLAALDRftggsriddaaelKTILESIQRLKVKTASPE 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 445977555 435 RPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKA 484
Cdd:PRK13549 401 LAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQ 450
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-194 |
1.08e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 78.58 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLDQHTV--LT 78
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI---------LIGGRDVtdLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 79 PGRtiRDV--------------LAD--AFlPL-FEKEKAlnevtekmgtatpeeleelleqmAEIQDaleaggfylldmK 141
Cdd:COG3839 72 PKD--RNIamvfqsyalyphmtVYEniAF-PLkLRKVPK-----------------------AEIDR------------R 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 445977555 142 IEEAARGLGIDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:COG3839 114 VREAAELLGLEDL-LDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-218 |
1.25e-15 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 76.00 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLF--KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVeWTPGT-----------HYGY 70
Cdd:cd03263 1 LQIRNLTKTYKKGTKPavDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTA-YINGYsirtdrkaarqSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 71 LDQHTVLTPGRTIRDVLAdaflpLFEKEKALNEVTEKmgtatpeeleelleqmaeiqdaleaggfylldMKIEEAARGLG 150
Cdd:cd03263 80 CPQFDALFDELTVREHLR-----FYARLKGLPKSEIK--------------------------------EEVELLLRVLG 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 151 IDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPH--AFLLISHD 218
Cdd:cd03263 123 LTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
321-494 |
1.45e-15 |
|
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: 76.22 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 321 SSRFVFEGENVEIgythPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLepAYFEQEVKADN 400
Cdd:cd03267 22 SLKSLFKRKYREV----EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV--PWKRRKKFLRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 401 ITPI----DDVWNTFP------------GLDQHQIRAMLAKCG--LKNEHI-SRPLSQLSGGEQAKVRLCKLMGEESNWL 461
Cdd:cd03267 96 IGVVfgqkTQLWWDLPvidsfyllaaiyDLPPARFKKRLDELSelLDLEELlDTPVRQLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 445977555 462 LFDEPTNHLDVTAKAELKKAMKAY----KGTILLVCH 494
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSH 212
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
338-471 |
1.80e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.35 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 338 PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDflepayfeqevkadniTPIDDvWN-------- 409
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG----------------RPLAD-WSpaelarrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 410 ---------TFP---------GL---------DQHQIRAMLAKCGLknEHIS-RPLSQLSGGEQAKVR----LCKL--MG 455
Cdd:PRK13548 79 avlpqhsslSFPftveevvamGRaphglsraeDDALVAAALAQVDL--AHLAgRDYPQLSGGEQQRVQlarvLAQLwePD 156
|
170
....*....|....*.
gi 445977555 456 EESNWLLFDEPTNHLD 471
Cdd:PRK13548 157 GPPRWLLLDEPTSALD 172
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
339-478 |
2.44e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.74 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 339 LLPkLSMTIERGEKIAIVGCNGVGKSTLLKTILGkIKPLSGK-----TSLGDFLEP------AYFEQEVKAdniTPIDDV 407
Cdd:PRK03695 12 LGP-LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSiqfagQPLEAWSAAelarhrAYLSQQQTP---PFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 408 W---------NTFPGLDQHQIRAMLAKCGLKNEhISRPLSQLSGGEQAKVRLC-------KLMGEESNWLLFDEPTNHLD 471
Cdd:PRK03695 87 FqyltlhqpdKTRTEAVASALNEVAEALGLDDK-LGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLD 165
|
....*..
gi 445977555 472 VTAKAEL 478
Cdd:PRK03695 166 VAQQAAL 172
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-189 |
2.51e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.45 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVeWTPG---THY--------- 68
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI-FLDGediTHLpmhkrarlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 69 -GYLDQHTVLTPGRTIRDVLAdAFLPLFEKEKalnevtekmgtatpeeleelleqmAEIQDALEAggfyLLdmkiEEaar 147
Cdd:COG1137 80 iGYLPQEASIFRKLTVEDNIL-AVLELRKLSK------------------------KEREERLEE----LL----EE--- 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 445977555 148 gLGIDAIgldRDV--SALSGGQRTKVLLAKLLLEQPEVLLLDEP 189
Cdd:COG1137 124 -FGITHL---RKSkaYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-220 |
2.51e-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 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: 76.34 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLF-----KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTpgthygyldqhtvlt 78
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFekkalDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTID--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 79 pGRTIRDvladaflplfEKEKALNEVTEKMGTAtpeeleellEQMAEIQ--------DAleAGG---FYLLDMKIEEAAR 147
Cdd:TIGR04521 66 -GRDITA----------KKKKKLKDLRKKVGLV---------FQFPEHQlfeetvykDI--AFGpknLGLSEEEAEERVK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 148 GLgIDAIGLDRDVS-----ALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD---VEHIHWLTNYL-KEYPHAFLLISHD 218
Cdd:TIGR04521 124 EA-LELVGLDEEYLerspfELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDpkgRKEILDLFKRLhKEKGLTVILVTHS 202
|
..
gi 445977555 219 TE 220
Cdd:TIGR04521 203 ME 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
334-498 |
2.52e-15 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 74.83 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 334 GYTHPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPAYFEQE---VKADNI--------- 401
Cdd:cd03255 14 GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaaFRRRHIgfvfqsfnl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 402 ----TPIDDV-----WNTFPGLDQHQ-IRAMLAKCGLKnEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD 471
Cdd:cd03255 94 lpdlTALENVelpllLAGVPKKERRErAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLD 172
|
170 180 190
....*....|....*....|....*....|.
gi 445977555 472 -VTAKA--ELKKAMKAYKG-TILLVCHEPDF 498
Cdd:cd03255 173 sETGKEvmELLRELNKEAGtTIVVVTHDPEL 203
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-223 |
2.84e-15 |
|
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: 74.60 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVeWTPGTHYGYLD----------Q 73
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI-YIGGRDVTDLPpkdrdiamvfQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 74 HTVLTPGRTIRDVLAdafLPLfekekalnevteKMGTATPeeleelleqmAEIqdaleaggfyllDMKIEEAARGLGIDA 153
Cdd:cd03301 80 NYALYPHMTVYDNIA---FGL------------KLRKVPK----------DEI------------DERVREVAELLQIEH 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 154 IgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD----VEHIHWLTNYLKEYPHAFLLISHD-TEFMN 223
Cdd:cd03301 123 L-LDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDqVEAMT 196
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-196 |
3.38e-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: 78.17 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 14 GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwTPGTHYGYLDQHTVltpGRTIRDVLADAFLp 93
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT-LDGVPVSSLDQDEV---RRRVSVCAQDAHL- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 94 lFEKEkALNEVTEKMGTATPeeleelleqmAEIQDALEAGGfyLLDMkIEEAARGLGIDaigLDRDVSALSGGQRTKVLL 173
Cdd:TIGR02868 421 -FDTT-VRENLRLARPDATD----------EELWAALERVG--LADW-LRALPDGLDTV---LGEGGARLSGGERQRLAL 482
|
170 180
....*....|....*....|...
gi 445977555 174 AKLLLEQPEVLLLDEPTNYLDVE 196
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAE 505
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-225 |
3.90e-15 |
|
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: 77.87 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKL--GHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV--------EWTP---GTHYGY 70
Cdd:COG4618 331 LSVENLtvVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsQWDReelGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 71 LDQHTVLTPGrTIRDVLAdaflplfekekalnevteKMGTATPEeleelleqmaeiqdaleaggfylldmKIEEAARGLG 150
Cdd:COG4618 411 LPQDVELFDG-TIAENIA------------------RFGDADPE--------------------------KVVAAAKLAG 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 151 I-DAI-----GLDRDV----SALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTN---YLKEYPHAFLLISH 217
Cdd:COG4618 446 VhEMIlrlpdGYDTRIgeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAairALKARGATVVVITH 525
|
....*...
gi 445977555 218 DTEFMNKC 225
Cdd:COG4618 526 RPSLLAAV 533
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-217 |
4.21e-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: 4.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTL----FKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwtpgthygyLDQHTVLT 78
Cdd:cd03266 1 MITADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT---------VDGFDVVK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 79 PGRTIR---DVLADAFlPLFEKEKALNEVtekmgtatpeeleelleqmaeiqdaLEAGGFYLLD-----MKIEEAARGLG 150
Cdd:cd03266 72 EPAEARrrlGFVSDST-GLYDRLTARENL-------------------------EYFAGLYGLKgdeltARLEELADRLG 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 151 IDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYP---HAFLLISH 217
Cdd:cd03266 126 MEEL-LDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRalgKCILFSTH 194
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
329-495 |
4.64e-15 |
|
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: 74.46 E-value: 4.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGY-THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGK--------TSLGD-------------F 386
Cdd:cd03261 4 RGLTKSFgGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEvlidgediSGLSEaelyrlrrrmgmlF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 387 LEPAYFeqevkaDNITPIDDVwnTFP-----GLDQHQIRAMLAKC----GLKNEHISRPlSQLSGGEQAKVRLCKLMGEE 457
Cdd:cd03261 84 QSGALF------DSLTVFENV--AFPlrehtRLSEEEIREIVLEKleavGLRGAEDLYP-AELSGGMKKRVALARALALD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 445977555 458 SNWLLFDEPTNHLD-VTAKA------ELKKAMKAykgTILLVCHE 495
Cdd:cd03261 155 PELLLYDEPTAGLDpIASGViddlirSLKKELGL---TSIMVTHD 196
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
329-498 |
4.91e-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: 72.99 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGYTHPLLPK-LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDflEPAYFEQEVKADNITPIDDV 407
Cdd:cd03229 4 KNVSKRYGQKTVLNdVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDG--EDLTDLEDELPPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 408 ---WNTFPGLDQHQIRAMLakcglknehisrplsqLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKA 484
Cdd:cd03229 82 fqdFALFPHLTVLENIALG----------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKS 145
|
170
....*....|....*...
gi 445977555 485 YKG----TILLVCHEPDF 498
Cdd:cd03229 146 LQAqlgiTVVLVTHDLDE 163
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
329-498 |
5.49e-15 |
|
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: 74.53 E-value: 5.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGY--THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPAYFEQEVKA-------- 398
Cdd:cd03256 4 ENLSKTYpnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrqigmi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 399 -------DNITPIDDV--------------WNTFPGLDQHQIRAMLAKCGLKnEHISRPLSQLSGGEQAKVRLCKLMGEE 457
Cdd:cd03256 84 fqqfnliERLSVLENVlsgrlgrrstwrslFGLFPKEEKQRALAALERVGLL-DKAYQRADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 445977555 458 SNWLLFDEPTNHLDVTAKAE----LKKAMKAYKGTILLVCHEPDF 498
Cdd:cd03256 163 PKLILADEPVASLDPASSRQvmdlLKRINREEGITVIVSLHQVDL 207
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-194 |
6.32e-15 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 74.14 E-value: 6.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIItgQLIHDQGRVEWTPGThygyldqhtVLTPGRTI 83
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLL--NRLNDLIPGAPDEGE---------VLLDGKDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 84 RDVLADaflplfekekaLNEVTEKMG----TATPEEleelleqmAEIQDALEAG-------GFYLLDMKIEEAARGLGID 152
Cdd:cd03260 70 YDLDVD-----------VLELRRRVGmvfqKPNPFP--------GSIYDNVAYGlrlhgikLKEELDERVEEALRKAALW 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 445977555 153 AIGLDR-DVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:cd03260 131 DEVKDRlHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALD 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
327-494 |
6.52e-15 |
|
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: 74.08 E-value: 6.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 327 EGENVEIGYT-----HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTslgdflepayfeqEVKADNI 401
Cdd:cd03257 3 EVKNLSVSFPtgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSI-------------IFDGKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 402 TPIDDVWNTFPG-------------LD-----QHQIR-------------AMLAKCGLKNEHISRPLS-------QLSGG 443
Cdd:cd03257 70 LKLSRRLRKIRRkeiqmvfqdpmssLNprmtiGEQIAeplrihgklskkeARKEAVLLLLVGVGLPEEvlnryphELSGG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445977555 444 EQAKVRLC-------KLmgeesnwLLFDEPTNHLDVTAKAE----LKKAMKAYKGTILLVCH 494
Cdd:cd03257 150 QRQRVAIAralalnpKL-------LIADEPTSALDVSVQAQildlLKKLQEELGLTLLFITH 204
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-218 |
6.85e-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: 6.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGqLIH-DQGRVewtpgthygYLDQHTV--L 77
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG-FETpDSGRI---------LLDGRDVtgL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 78 TPGRtiRDV--------L------AD--AFlPLfeKEKALNEvtekmgtatpeeleelleqmAEIQDaleaggfylldmK 141
Cdd:COG3842 73 PPEK--RNVgmvfqdyaLfphltvAEnvAF-GL--RMRGVPK--------------------AEIRA------------R 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 142 IEEAARGLGIDAIGlDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV---EHI-HWLTNYLKEYPHAFLLISH 217
Cdd:COG3842 116 VAELLELVGLEGLA-DRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAklrEEMrEELRRLQRELGITFIYVTH 194
|
.
gi 445977555 218 D 218
Cdd:COG3842 195 D 195
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
325-506 |
7.38e-15 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 74.35 E-value: 7.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 325 VFEGENVEIGY-THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSG------------------KTSLGd 385
Cdd:COG1119 3 LLELRNVTVRRgGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvrlfgerrggedvwelRKRIG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 386 FLEPA---YFEQEVKA---------DNItpidDVWNTFPGLDQHQIRAMLAKCGLKnEHISRPLSQLSGGEQAKVRLCK- 452
Cdd:COG1119 82 LVSPAlqlRFPRDETVldvvlsgffDSI----GLYREPTDEQRERARELLELLGLA-HLADRPFGTLSQGEQRRVLIARa 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445977555 453 LMGE-ESnwLLFDEPTNHLDVTAKAELKKAMK--AYKG--TILLVCHEPdfyED---WITKV 506
Cdd:COG1119 157 LVKDpEL--LILDEPTAGLDLGARELLLALLDklAAEGapTLVLVTHHV---EEippGITHV 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
342-497 |
8.56e-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: 73.48 E-value: 8.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 342 KLSMTIErGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLepaYFEQEVKAdNITP----IDDVWNT---FPGL 414
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV---LFDSRKKI-NLPPqqrkIGLVFQQyalFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 415 -----------------DQHQIRAMLAKCGLknEHI-SRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAK- 475
Cdd:cd03297 91 nvrenlafglkrkrnreDRISVDELLDLLGL--DHLlNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRl 168
|
170 180
....*....|....*....|....*
gi 445977555 476 ---AELKKAMKAYKGTILLVCHEPD 497
Cdd:cd03297 169 qllPELKQIKKNLNIPVIFVTHDLS 193
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
325-506 |
9.21e-15 |
|
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: 76.87 E-value: 9.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 325 VFEGENVEIGYTH---PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKP---LSGKTSLG--DFLEP------- 389
Cdd:COG1123 4 LLEVRDLSVRYPGgdvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDgrDLLELsealrgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 390 --AYFEQEVKA--DNITPIDDVWNTF--PGLDQHQIRA----MLAKCGLKnEHISRPLSQLSGGEQAKVRLCKLMGEESN 459
Cdd:COG1123 84 riGMVFQDPMTqlNPVTVGDQIAEALenLGLSRAEARArvleLLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 445977555 460 WLLFDEPTNHLDVTAKAE----LKKAMKAYKGTILLVCHEPDFYEDWITKV 506
Cdd:COG1123 163 LLIADEPTTALDVTTQAEildlLRELQRERGTTVLLITHDLGVVAEIADRV 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
15-227 |
1.15e-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: 76.38 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 15 DRTLFK---DVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV------EWT----PG-------THY-GYLDQ 73
Cdd:TIGR03269 293 DRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdEWVdmtkPGpdgrgraKRYiGILHQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 74 HTVLTPGRTIRDVLADAFLPLFEKEKAlnevtekmgtatpeeleelleQMAEIQdALEAGGFYlldmkiEEAARGLgida 153
Cdd:TIGR03269 373 EYDLYPHRTVLDNLTEAIGLELPDELA---------------------RMKAVI-TLKMVGFD------EEKAEEI---- 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 154 igLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD----VEHIHWLTNYLKEYPHAFLLISHDTEFMNKCVD 227
Cdd:TIGR03269 421 --LDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCD 496
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-220 |
1.17e-14 |
|
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: 73.17 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 6 VEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRvewtpGTHYGYldqhtvltpgrtirD 85
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGR-----ATVAGH--------------D 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 86 VLADAflplfekekalNEVTEKMGtatpeeleeLLEQMAEIQDALEA-------GGFY-----LLDMKIEEAarglgIDA 153
Cdd:cd03265 64 VVREP-----------REVRRRIG---------IVFQDLSVDDELTGwenlyihARLYgvpgaERRERIDEL-----LDF 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 154 IGL----DRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV---EHIhWltNYLKEYPHAF----LLISHDTE 220
Cdd:cd03265 119 VGLleaaDRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPqtrAHV-W--EYIEKLKEEFgmtiLLTTHYME 193
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
329-478 |
1.47e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 73.34 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGytHPLLPkLSMTIERGEKIAIVGCNGVGKSTLLKTILGkIKPLSGK-----TSLGDFLEP------AYFEQEVK 397
Cdd:COG4138 4 NDVAVA--GRLGP-ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEillngRPLSDWSAAelarhrAYLSQQQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 398 ADNITPiddVWNTfpgLDQHQ---------IRAMLAKCG-LK-NEHISRPLSQLSGGEQAKVRLCKLM-------GEESN 459
Cdd:COG4138 80 PPFAMP---VFQY---LALHQpagasseavEQLLAQLAEaLGlEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptiNPEGQ 153
|
170
....*....|....*....
gi 445977555 460 WLLFDEPTNHLDVTAKAEL 478
Cdd:COG4138 154 LLLLDEPMNSLDVAQQAAL 172
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-220 |
1.81e-14 |
|
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: 73.14 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLlTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVeWTPG---THY-------GY 70
Cdd:cd03296 1 MSI-EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI-LFGGedaTDVpvqernvGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 71 LDQHTVLTPGRTIRDVLADAFlplfeKEKALNEVTEKmgtatpeeleelleqmAEIQDALEAggfyLLDMkieeaargLG 150
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGL-----RVKPRSERPPE----------------AEIRAKVHE----LLKL--------VQ 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445977555 151 IDAIGlDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV----EHIHWLTNYLKEYPHAFLLISHDTE 220
Cdd:cd03296 126 LDWLA-DRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQE 198
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-220 |
1.97e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 72.87 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRllAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWtpgthygyLDQ-HTVLTPGR- 81
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFDLTIA--AGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW--------NGQdLTALPPAEr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 82 ---------------TIRDVLADAFLP---LFEKEKAlnevtekmgtatpeeleelleqmaeiqdaleaggfylldmKIE 143
Cdd:COG3840 72 pvsmlfqennlfphlTVAQNIGLGLRPglkLTAEQRA----------------------------------------QVE 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 144 EAARGLGIDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD----VEHIHWLTNYLKEYPHAFLLISHDT 219
Cdd:COG3840 112 QALERVGLAGL-LDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHDP 190
|
.
gi 445977555 220 E 220
Cdd:COG3840 191 E 191
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
327-501 |
1.97e-14 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 72.44 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 327 EGENVEIGYTH--PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGK-----TSLGDFLEPA--YFEQEVK 397
Cdd:cd03292 2 EFINVTKTYPNgtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTirvngQDVSDLRGRAipYLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 398 --------------ADNITPIDDVWNTFPGLDQHQIRAMLAKCGLKNEHISRPlSQLSGGEQAKVRLCKLMGEESNWLLF 463
Cdd:cd03292 82 vvfqdfrllpdrnvYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 445977555 464 DEPTNHLDVTAKAELKKAMKAYK---GTILLVCHEPDFYED 501
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDT 201
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-220 |
2.03e-14 |
|
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: 72.75 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLfKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV--------EWTPGTH-YGYLDQH 74
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIllngkditNLPPEKRdISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 75 TVLTPGRTIRDVLAdaflplFEKEKALNEVTEKmgtatpeeleelleqmaeiqdaleaggfyllDMKIEEAARGLGIDAI 154
Cdd:cd03299 80 YALFPHMTVYKNIA------YGLKKRKVDKKEI-------------------------------ERKVLEIAEMLGIDHL 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 155 gLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEH----IHWLTNYLKEYPHAFLLISHDTE 220
Cdd:cd03299 123 -LNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHDFE 191
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
338-496 |
2.49e-14 |
|
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: 75.47 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 338 PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPAYFEQEVKAD-----------NITPIDD 406
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRvsvcaqdahlfDTTVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 407 VWNTFPGLDQHQIRAMLAKCGLKNEHISRPL----------SQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKA 476
Cdd:TIGR02868 429 LRLARPDATDEELWAALERVGLADWLRALPDgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETAD 508
|
170 180
....*....|....*....|..
gi 445977555 477 ELKKAM-KAYKG-TILLVCHEP 496
Cdd:TIGR02868 509 ELLEDLlAALSGrTVVLITHHL 530
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-218 |
3.77e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.74 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTF-----------GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTfmniiTG----QLIHDQGRVeWTPGTH 67
Cdd:PRK15134 275 LLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKST-----TGlallRLINSQGEI-WFDGQP 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 68 YGYLDQHTVLTPGRTIRDVLADAFLPLFEKEKALNEVTEKMGTATPEELEELLEQmaeiqdaleaggfylldmKIEEAAR 147
Cdd:PRK15134 349 LHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQ------------------QVIAVME 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 148 GLGIDAIGLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD--VE-HIHWLTNYLKE-YPHAFLLISHD 218
Cdd:PRK15134 411 EVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktVQaQILALLKSLQQkHQLAYLFISHD 485
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
4-240 |
4.17e-14 |
|
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: 74.69 E-value: 4.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKL--GHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVE--------WTP---GTHYGY 70
Cdd:TIGR01842 317 LSVENVtiVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRldgadlkqWDRetfGKHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 71 LDQHTVLTPGrTIRDVLAdaflplfekekalnevtekmgtatpeeleelleQMAEIQDAleaggfylldMKIEEAARGLG 150
Cdd:TIGR01842 397 LPQDVELFPG-TVAENIA---------------------------------RFGENADP----------EKIIEAAKLAG 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 151 I-DAI-----GLDRDV----SALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHA---FLLISH 217
Cdd:TIGR01842 433 VhELIlrlpdGYDTVIgpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARgitVVVITH 512
|
250 260
....*....|....*....|...
gi 445977555 218 DTEFMNkCVDVIFHLEFTKMTRY 240
Cdd:TIGR01842 513 RPSLLG-CVDKILVLQDGRIARF 534
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-217 |
4.20e-14 |
|
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: 70.32 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 14 GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVE--------WTP---GTHYGYLDQHTVLTPGrT 82
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRldgadisqWDPnelGDHVGYLPQDDELFSG-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 IRdvladaflplfekekalnevtekmgtatpeeleelleqmaeiqdaleaggfylldmkieeaarglgiDAIgldrdvsa 162
Cdd:cd03246 92 IA-------------------------------------------------------------------ENI-------- 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 163 LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTN---YLKEYPHAFLLISH 217
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQaiaALKAAGATRIVIAH 154
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
336-495 |
5.06e-14 |
|
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: 71.13 E-value: 5.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 336 THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD----FLEP------------AYFEQEVKAD 399
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtDLPPkdrdiamvfqnyALYPHMTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 400 NITpiddvwntFP----GLDQHQIRAMLAKCG--LKNEH-ISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD- 471
Cdd:cd03301 92 NIA--------FGlklrKVPKDEIDERVREVAelLQIEHlLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDa 163
|
170 180
....*....|....*....|....*..
gi 445977555 472 ---VTAKAELKKAMKAYKGTILLVCHE 495
Cdd:cd03301 164 klrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
336-498 |
5.11e-14 |
|
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: 71.02 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 336 THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFlepAYFEQEVKADNI-TPIDDV---WNTF 411
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGL---KLTDDKKNINELrQKVGMVfqqFNLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 412 PGL------------------DQHQIRAM--LAKCGLKNEHISRPlSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD 471
Cdd:cd03262 89 PHLtvlenitlapikvkgmskAEAEERALelLEKVGLADKADAYP-AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
170 180 190
....*....|....*....|....*....|
gi 445977555 472 VTAKAELKKAMK--AYKG-TILLVCHEPDF 498
Cdd:cd03262 168 PELVGEVLDVMKdlAEEGmTMVVVTHEMGF 197
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-218 |
7.15e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.41 E-value: 7.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 22 VSMRLLAGEHVGLVGANGVGKSTFMNIITGqLIHDQGRV--------EWTPGT---HYGYLDQHTVLTPGRTIRDVLA-- 88
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEIllngrplsDWSAAElarHRAYLSQQQSPPFAMPVFQYLAlh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 89 -DAFLPLFEKEKALNEVTEKMGtatpeeleelleqmaeiqdaleaggfylLDMKieeaarglgidaigLDRDVSALSGG- 166
Cdd:COG4138 94 qPAGASSEAVEQLLAQLAEALG----------------------------LEDK--------------LSRPLTQLSGGe 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445977555 167 -QRtkVLLAKLLLE-------QPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAFLLI---SHD 218
Cdd:COG4138 132 wQR--VRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVvmsSHD 192
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-229 |
8.33e-14 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 70.65 E-value: 8.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 24 MRLLAGEHVGLVGANGVGKSTFMNIITGQL------IHDQGRVEWTPGTHYGYLDQhtvltpgrtiRDVLADAFlPLFEK 97
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIppakgtVKVAGASPGKGWRHIGYVPQ----------RHEFAWDF-PISVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 98 EKALNEVTEKMGtatpEELEELLEQMAEIQDALEAGGFYLLdmkieeaarglgidaigLDRDVSALSGGQRTKVLLAKLL 177
Cdd:TIGR03771 70 HTVMSGRTGHIG----WLRRPCVADFAAVRDALRRVGLTEL-----------------ADRPVGELSGGQRQRVLVARAL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 445977555 178 LEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYP---HAFLLISHD-TEFMNKCVDVI 229
Cdd:TIGR03771 129 ATRPSVLLLDEPFTGLDMPTQELLTELFIELAgagTAILMTTHDlAQAMATCDRVV 184
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
329-497 |
8.59e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 70.94 E-value: 8.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGYTHPLLpKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD----FLEPA------YFeQEvka 398
Cdd:COG3840 5 DDLTYRYGDFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltALPPAerpvsmLF-QE--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 399 DNITPIDDVWNTF-----PGL-----DQHQIRAMLAKCGLkNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTN 468
Cdd:COG3840 80 NNLFPHLTVAQNIglglrPGLkltaeQRAQVEQALERVGL-AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190
....*....|....*....|....*....|...
gi 445977555 469 HLDVTAKAE----LKKAMKAYKGTILLVCHEPD 497
Cdd:COG3840 159 ALDPALRQEmldlVDELCRERGLTVLMVTHDPE 191
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-229 |
1.36e-13 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 69.14 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW-------------TPGTHYGY 70
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdgedltdledelpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 71 LDQHTVLTPGRTIRDvladaflplfekekalNevtekmgtatpeeleelleqmaeiqdaleaggfylldmkieeaarglg 150
Cdd:cd03229 81 VFQDFALFPHLTVLE----------------N------------------------------------------------ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 151 idaIGLdrdvsALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLK----EYPHAFLLISHDTEFMNKCV 226
Cdd:cd03229 97 ---IAL-----GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKslqaQLGITVVLVTHDLDEAARLA 168
|
...
gi 445977555 227 DVI 229
Cdd:cd03229 169 DRV 171
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
336-498 |
1.38e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.51 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 336 THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTIlGKIKPLSGKTSLGDFLE---PAYFEQEVKADnITPIDDVWNTFP 412
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEEITSGDLIVDGLKvndPKVDERLIRQE-AGMVFQQFYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 413 GLD--------------------QHQIRAMLAKCGLKnEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDV 472
Cdd:PRK09493 91 HLTalenvmfgplrvrgaskeeaEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP 169
|
170 180
....*....|....*....|....*....
gi 445977555 473 TAKAELKKAMK--AYKG-TILLVCHEPDF 498
Cdd:PRK09493 170 ELRHEVLKVMQdlAEEGmTMVIVTHEIGF 198
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
339-496 |
1.68e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 69.44 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 339 LLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLG----DFLEPAYFEQ--------EVKAdNITPIDD 406
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNggplDFQRDSIARGllylghapGIKT-TLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 407 V--WNTFPGLDqhQIRAMLAKCGLKN-EHisRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMK 483
Cdd:cd03231 94 LrfWHADHSDE--QVEEALARVGLNGfED--RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
170
....*....|....*.
gi 445977555 484 AY---KGTILLVCHEP 496
Cdd:cd03231 170 GHcarGGMVVLTTHQD 185
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
334-494 |
1.71e-13 |
|
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: 69.81 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 334 GYTHPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD-------------FLEPAYFEQEVKADN 400
Cdd:cd03293 14 GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpdrgyvFQQDALLPWLTVLDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 401 IT-PIDDVWNTfPGLDQHQIRAMLAKCGLKN-EHiSRPlSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKA-- 476
Cdd:cd03293 94 VAlGLELQGVP-KAEARERAEELLELVGLSGfEN-AYP-HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREql 170
|
170 180
....*....|....*....|
gi 445977555 477 --ELKKAMKAYKGTILLVCH 494
Cdd:cd03293 171 qeELLDIWRETGKTVLLVTH 190
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-217 |
2.02e-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: 69.81 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 15 DRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV--EWTPGTHYG--YL-------DQHTVLTpGRTI 83
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVllDGKPISQYEhkYLhskvslvGQEPVLF-ARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 84 RDVLADAFlplfeKEKALNEVTekmgtatpeeleelleqmaEIQDALEAGGFylldmkIEEAARGLGIDAiglDRDVSAL 163
Cdd:cd03248 105 QDNIAYGL-----QSCSFECVK-------------------EAAQKAHAHSF------ISELASGYDTEV---GEKGSQL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 445977555 164 SGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYP--HAFLLISH 217
Cdd:cd03248 152 SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPerRTVLVIAH 207
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-196 |
2.15e-13 |
|
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: 69.57 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwtpgthygyLDqhtvltpGRTIRD------------VL 87
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIL---------ID-------GHDVRDytlaslrrqiglVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 88 ADAFLplFEkekalNEVTEKMGTATPEELeelleqMAEIQDALEAGGFYLLDMKIEEaarglGIDAIGLDRDVSaLSGGQ 167
Cdd:cd03251 83 QDVFL--FN-----DTVAENIAYGRPGAT------REEVEEAARAANAHEFIMELPE-----GYDTVIGERGVK-LSGGQ 143
|
170 180
....*....|....*....|....*....
gi 445977555 168 RTKVLLAKLLLEQPEVLLLDEPTNYLDVE 196
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTE 172
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-231 |
2.15e-13 |
|
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: 68.61 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLghTFGDRtlFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLDQHTVltPGRT 82
Cdd:cd03215 4 VLEVRGL--SVKGA--VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEI---------TLDGKPV--TRRS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 IRDVLAD--AFLPlfekekalnevtekmgtatpeeleelleqmaeiQDALEAGGFylLDMKIEEAArglgidAIGldrdv 160
Cdd:cd03215 69 PRDAIRAgiAYVP---------------------------------EDRKREGLV--LDLSVAENI------ALS----- 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445977555 161 SALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV---EHIHWLTNYLKEYPHAFLLISHDT-EFMNKC--VDVIFH 231
Cdd:cd03215 103 SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVgakAEIYRLIRELADAGKAVLLISSELdELLGLCdrILVMYE 179
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-230 |
2.35e-13 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 69.62 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTpGTHYGYLDQHTvLTPGR- 81
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-GQDITGLSEKE-LYELRr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 82 ---------------TIRDVLAdafLPLFEKEKaLNEvtekmgtatpeeleelleqmAEIQDaleaggfyLLDMKIEEAa 146
Cdd:COG1127 83 rigmlfqggalfdslTVFENVA---FPLREHTD-LSE--------------------AEIRE--------LVLEKLELV- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 147 rGLGiDAIglDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD-------VEHIHWLTnylKEYPHAFLLISHDT 219
Cdd:COG1127 130 -GLP-GAA--DKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDpitsaviDELIRELR---DELGLTSVVVTHDL 202
|
250
....*....|..
gi 445977555 220 EFMNKCVD-VIF 230
Cdd:COG1127 203 DSAFAIADrVAV 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
329-503 |
2.90e-13 |
|
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: 69.29 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGYTHPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSL-GDFLEPAYFEQEvkadNITPIDDV 407
Cdd:cd03299 4 ENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDITNLPPEKR----DISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 408 WNTFPGLD-------------------QHQIRAMLAKCGLknEHI-SRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPT 467
Cdd:cd03299 80 YALFPHMTvykniayglkkrkvdkkeiERKVLEIAEMLGI--DHLlNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 445977555 468 NHLDVTAKA----ELKKAMKAYKGTILLVCHepDFYEDWI 503
Cdd:cd03299 158 SALDVRTKEklreELKKIRKEFGVTVLHVTH--DFEEAWA 195
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-249 |
2.96e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 72.20 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 14 GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGTHYGYLDQHTVltpgrtirDVLADAFLP 93
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHV--------DGLDLSSNP 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 94 LFEKEKALNEVTEKmgtatpeeleelleqmaeiqdaleaggfylldmKIEEAARGLGIDAIGLDRDVSALSGGQRTKVLL 173
Cdd:PLN03073 592 LLYMMRCFPGVPEQ---------------------------------KLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAF 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445977555 174 AKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAFLLISHDTEFMNKCVDVIFHLEFTKMTRYTAT---YEKFLE 249
Cdd:PLN03073 639 AKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTfhdYKKTLQ 717
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-233 |
3.01e-13 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 68.86 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 27 LAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVE-----W--------TPGT--HYGYLDQHTVLTPGRTIRDVLADAF 91
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvLfdsrkkinLPPQqrKIGLVFQQYALFPHLNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 92 lplfeKEKALNEVTekmgtatpeeleellEQMAEIQDALeaggfylldmkieeaarglGIDAIgLDRDVSALSGGQRTKV 171
Cdd:cd03297 101 -----KRKRNREDR---------------ISVDELLDLL-------------------GLDHL-LNRYPAQLSGGEKQRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445977555 172 LLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAF----LLISHDTEFMNKCVDVIFHLE 233
Cdd:cd03297 141 ALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLnipvIFVTHDLSEAEYLADRIVVME 206
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-218 |
3.34e-13 |
|
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: 69.83 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 2 SLLTVEKLGHTF---------GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTpGTHYGYLD 72
Cdd:TIGR02769 1 SLLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFR-GQDLYQLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 73 QHTVLTPGRTIRDVLAD---AFLPLFEKEKALNEVTEKMgtatpeELEELLEQMAEIQDALEAggfylldmkieeaargL 149
Cdd:TIGR02769 80 RKQRRAFRRDVQLVFQDspsAVNPRMTVRQIIGEPLRHL------TSLDESEQKARIAELLDM----------------V 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445977555 150 GIDAIGLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV----EHIHWLTNYLKEYPHAFLLISHD 218
Cdd:TIGR02769 138 GLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHD 210
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-196 |
4.08e-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: 68.97 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 29 GEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWtPGTHYGYLDQHTVLTPGRTIRDVLAdaflplfekekalnEVTEKM 108
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIKADYEGTVRDLLS--------------SITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 109 GTATpeeleelleqmaeiqdaleaggFYlldmkIEEAARGLGIDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDE 188
Cdd:cd03237 90 YTHP----------------------YF-----KTEIAKPLQIEQI-LDREVPELSGGELQRVAIAACLSKDADIYLLDE 141
|
....*...
gi 445977555 189 PTNYLDVE 196
Cdd:cd03237 142 PSAYLDVE 149
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-218 |
4.14e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 69.32 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGqlihdqgrvewtpgthygyLDQ--HTVLTPGR 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-------------------LETpsAGELLAGT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 82 TirdVLADAflplfekekalNEVTEKMgtatpeeleelleqmaeIQDAleaggfYLLDMK--IEEAARGLG--------- 150
Cdd:PRK11247 74 A---PLAEA-----------REDTRLM-----------------FQDA------RLLPWKkvIDNVGLGLKgqwrdaalq 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445977555 151 -IDAIGL-DRDV---SALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD----VEHIHWLTNYLKEYPHAFLLISHD 218
Cdd:PRK11247 117 aLAAVGLaDRANewpAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-194 |
4.59e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 69.75 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTpGTHYGYLDQHTV------- 76
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD-GEPLDPEDRRRIgylpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 77 -LTPGRTIRDVLadAFL------PLFEKEKALNEVTEKMGtatpeeleelleqmaeIQDAleaggfylLDMKIEEaargl 149
Cdd:COG4152 81 gLYPKMKVGEQL--VYLarlkglSKAEAKRRADEWLERLG----------------LGDR--------ANKKVEE----- 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 445977555 150 gidaigldrdvsaLSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:COG4152 130 -------------LSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-220 |
6.43e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 68.74 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTFG----DRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwtpgthygyLDQHTV 76
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEIT---------LDGVPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 77 LTPGRTiRDVL--ADAFLPLfekekalnevtekmgtatpeeleelleqmaeiQDALE--AGGFYLLDM-KIEEAARGLGI 151
Cdd:COG4525 72 TGPGAD-RGVVfqKDALLPW--------------------------------LNVLDnvAFGLRLRGVpKAERRARAEEL 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 152 DA-IGL----DRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV---EHIHWLTNYLKEYPHA-FLLISHDTE 220
Cdd:COG4525 119 LAlVGLadfaRRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAltrEQMQELLLDVWQRTGKgVFLITHSVE 196
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
344-494 |
7.72e-13 |
|
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: 66.30 E-value: 7.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 344 SMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDflepayfeQEVKADNitPIDdvwntfpgldqhqirAML 423
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------KEVSFAS--PRD---------------ARR 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445977555 424 AKCGLknehisrpLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAYKG---TILLVCH 494
Cdd:cd03216 75 AGIAM--------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-372 |
8.97e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.43 E-value: 8.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVE----KLGHTfgdRTLFKDvSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwtpgTHYgyldQHTV 76
Cdd:PRK10938 1 MSSLQISqgtfRLSDT---KTLQLP-SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ----SQF----SHIT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 77 LTPGRTIRDVLADAFLPlfEKEKALNEVTEKMGTATpeeleelleqmAE-IQDALEAggfyllDMKIEEAARGLGIDAIg 155
Cdd:PRK10938 69 RLSFEQLQKLVSDEWQR--NNTDMLSPGEDDTGRTT-----------AEiIQDEVKD------PARCEQLAQQFGITAL- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 156 LDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPH---AFLLISHDTEFMNKCVDVIFHL 232
Cdd:PRK10938 129 LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLVLNRFDEIPDFVQFAGVL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 233 EFTKMTRyTATYEKFLelaeinknqhinayekqrefikkQEDFIAKNKarYSttgraksrqKQLDRMELIDRPETAIKPE 312
Cdd:PRK10938 209 ADCTLAE-TGEREEIL-----------------------QQALVAQLA--HS---------EQLEGVQLPEPDEPSARHA 253
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445977555 313 FSFKESRassrfvFEGENVEIGYT-HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILG 372
Cdd:PRK10938 254 LPANEPR------IVLNNGVVSYNdRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-195 |
1.03e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.03 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwtpgthygYLDQHTVLtpgrt 82
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH--------YRMRDGQL----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 iRDVLAdaflpLFEKEKALNEVTE------------KMG-TATpeeleelleqmAEIQDALEAGG--FYlldMKI-EEAA 146
Cdd:PRK11701 73 -RDLYA-----LSEAERRRLLRTEwgfvhqhprdglRMQvSAG-----------GNIGERLMAVGarHY---GDIrATAG 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 445977555 147 RGLG---IDAIGLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV 195
Cdd:PRK11701 133 DWLErveIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV 184
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-194 |
1.09e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 68.19 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFG-----DRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLDQhtvlt 78
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSI---------LIDG----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 79 pgrtiRDVladAFLPLFEKEKALNEVTE--KMGTATpeeleelleqmaeiqdaleaggfyllDMKIEE---------AAR 147
Cdd:COG1101 68 -----KDV---TKLPEYKRAKYIGRVFQdpMMGTAP--------------------------SMTIEEnlalayrrgKRR 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 148 GLGIdaiGLDRD-----------------------VSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:COG1101 114 GLRR---GLTKKrrelfrellatlglglenrldtkVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
329-492 |
1.13e-12 |
|
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: 67.46 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGYTH-PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD---------------------- 385
Cdd:cd03224 4 ENLNAGYGKsQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditglppheraragigyvpeg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 386 ------------FLEPAYFEQEVKADniTPIDDVWNTFPGLDQHQiramlakcglknehiSRPLSQLSGGEQAKVRLCK- 452
Cdd:cd03224 84 rrifpeltveenLLLGAYARRRAKRK--ARLERVYELFPRLKERR---------------KQLAGTLSGGEQQMLAIARa 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 445977555 453 LMGEESnWLLFDEPTNHLDVTAKAELKKAMKAYKG---TILLV 492
Cdd:cd03224 147 LMSRPK-LLLLDEPSEGLAPKIVEEIFEAIRELRDegvTILLV 188
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-199 |
1.26e-12 |
|
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: 67.51 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 16 RTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV------------EWTPgTHYGYLDQHTVLTpGRTI 83
Cdd:cd03252 15 PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladpAWLR-RQVGVVLQENVLF-NRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 84 RD--VLADAFLPLFEKEKAlnevtekmgtatpeeleelleqmAEIQDALEaggfYLLDMKieeaargLGIDAIGLDRDVS 161
Cdd:cd03252 93 RDniALADPGMSMERVIEA-----------------------AKLAGAHD----FISELP-------EGYDTIVGEQGAG 138
|
170 180 190
....*....|....*....|....*....|....*...
gi 445977555 162 aLSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIH 199
Cdd:cd03252 139 -LSGGQRQRIAIARALIHNPRILIFDEATSALDYESEH 175
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-220 |
1.30e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.96 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLlTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTpGT----------HYGY 70
Cdd:PRK10851 1 MSI-EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH-GTdvsrlhardrKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 71 LDQHTVLTPGRTIRDVLADAFLPLFEKEKALNEVTEKMGTAtpeeleelleqmaeiqdaleaggfyLLDM-KIEEAArgl 149
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTQ-------------------------LLEMvQLAHLA--- 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 150 gidaiglDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV----EHIHWLTNYLKEYPHAFLLISHDTE 220
Cdd:PRK10851 131 -------DRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQE 198
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-196 |
1.32e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.12 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 2 SLLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQgrvewTPGTHYGYLDqHTVLTPGR 81
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDK-----SAGSHIELLG-RTVQREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 82 TIRDVLADAFLP--LFEKEKALNEVT-------EKMGTATPEELEELLEQMAEIQDALeaggfylldmkieEAARGLGID 152
Cdd:PRK09984 77 LARDIRKSRANTgyIFQQFNLVNRLSvlenvliGALGSTPFWRTCFSWFTREQKQRAL-------------QALTRVGMV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 445977555 153 AIGLDRdVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE 196
Cdd:PRK09984 144 HFAHQR-VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPE 186
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-195 |
1.52e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.82 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPG----THYG----YLDQHT 75
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddPDVAeachYLGHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 76 VLTPGRTIRDVLadAFlplfekekalnevtekmgtatpeeleelleqMAEIQDALEAGgfylldmkIEEAARGLGIDAIg 155
Cdd:PRK13539 83 AMKPALTVAENL--EF-------------------------------WAAFLGGEELD--------IAAALEAVGLAPL- 120
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 445977555 156 LDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV 195
Cdd:PRK13539 121 AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
331-472 |
1.78e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.10 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 331 VEIGYThPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDflEPAY------------------- 391
Cdd:PRK09536 11 VEFGDT-TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG--DDVEalsaraasrrvasvpqdts 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 392 --FEQEVKAD---NITPIDDVWNTFPGLDQHQIRAMLAKCGLkNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEP 466
Cdd:PRK09536 88 lsFEFDVRQVvemGRTPHRSRFDTWTETDRAAVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
....*.
gi 445977555 467 TNHLDV 472
Cdd:PRK09536 167 TASLDI 172
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-211 |
1.93e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.37 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTpgthygyldqhtvltpGRT 82
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ----------------GEP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 I---RDVLADAFLPLfekekalnevtekmGTAtpeeleelleqmAEIQD---ALEAGGFYL-LDMKIEEAARGLGIDAIG 155
Cdd:PRK13538 65 IrrqRDEYHQDLLYL--------------GHQ------------PGIKTeltALENLRFYQrLHGPGDDEALWEALAQVG 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 156 LDR--DVSA--LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEypHA 211
Cdd:PRK13538 119 LAGfeDVPVrqLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ--HA 176
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-477 |
1.93e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.17 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTF-GDRTLfKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVeWTPGTHYGYldqhtvltp 79
Cdd:PRK11288 2 SPYLSFDGIGKTFpGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI-LIDGQEMRF--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 80 gRTIRDVLaDAFLPLFEKEkaLNEVTEkMGTAT-------PeeleelleqmaeiqdalEAGGFylLDMK--IEEAARGLg 150
Cdd:PRK11288 71 -ASTTAAL-AAGVAIIYQE--LHLVPE-MTVAEnlylgqlP-----------------HKGGI--VNRRllNYEAREQL- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 151 iDAIGLDRD----VSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYL---DVEHIHWLTNYLKEYPHAFLLISHDtefmn 223
Cdd:PRK11288 126 -EHLGVDIDpdtpLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLsarEIEQLFRVIRELRAEGRVILYVSHR----- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 224 kcVDVIFHL--EFT--KMTRYTATyekFLELAEINKNQHINAyekqrefikkqedfiaknkarysTTGRaksrqkqldrm 299
Cdd:PRK11288 200 --MEEIFALcdAITvfKDGRYVAT---FDDMAQVDRDQLVQA-----------------------MVGR----------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 300 ELID----RPETAikpefsfKESRassrfvFEGENVE-IGYTHPLlpklSMTIERGEKIAIVGCNGVGKSTLLKTILGKI 374
Cdd:PRK11288 241 EIGDiygyRPRPL-------GEVR------LRLDGLKgPGLREPI----SFSVRAGEIVGLFGLVGAGRSELMKLLYGAT 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 375 KPLSGKTSL----------------GDFLEPayfeQEVKADNITP----------------------IDDVWNTfpGLDQ 416
Cdd:PRK11288 304 RRTAGQVYLdgkpidirsprdairaGIMLCP----EDRKAEGIIPvhsvadninisarrhhlragclINNRWEA--ENAD 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445977555 417 HQIRAMlakcGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAE 477
Cdd:PRK11288 378 RFIRSL----NIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHE 434
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
329-471 |
2.11e-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: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGY--THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDF----LE----PAY------- 391
Cdd:COG2884 5 ENVSKRYpgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrLKrreiPYLrrrigvv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 392 FeQEVK-------ADNItpiddvwnTFP----GLDQHQIR----AMLAKCGLKNEHISRPlSQLSGGEQAKV-------- 448
Cdd:COG2884 85 F-QDFRllpdrtvYENV--------ALPlrvtGKSRKEIRrrvrEVLDLVGLSDKAKALP-HELSGGEQQRVaiaralvn 154
|
170 180
....*....|....*....|....*
gi 445977555 449 --RLcklmgeesnwLLFDEPTNHLD 471
Cdd:COG2884 155 rpEL----------LLADEPTGNLD 169
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-233 |
2.47e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 66.23 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 14 GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTpGTHYGYLDQHTV---------------LT 78
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN-GQDLSRLKRREIpylrrrigvvfqdfrLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 79 PGRTIRDVLAdafLPLfekekalnEVTEKmgtatpeeleelleQMAEIQDALEAggfyLLDMkieeaargLGIDAIGlDR 158
Cdd:COG2884 92 PDRTVYENVA---LPL--------RVTGK--------------SRKEIRRRVRE----VLDL--------VGLSDKA-KA 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 159 DVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPH---AFLLISHDTEFMNKCVDVIFHLE 233
Cdd:COG2884 134 LPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRrgtTVLIATHDLELVDRMPKRVLELE 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-230 |
2.75e-12 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 66.01 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwtpgthygyLDQHTVLTPGRTI 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTII---------IDGLKLTDDKKNI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 84 RDVLADA---F--LPLFEKEKALNEVTEkmgtatpeeleelleqmAEIQdaleaggfyLLDMKIEEA-ARGLGI-DAIGL 156
Cdd:cd03262 72 NELRQKVgmvFqqFNLFPHLTVLENITL-----------------APIK---------VKGMSKAEAeERALELlEKVGL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 157 DRDVSA----LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPH---AFLLISHDTEFMNKCVD-V 228
Cdd:cd03262 126 ADKADAypaqLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEegmTMVVVTHEMGFAREVADrV 205
|
..
gi 445977555 229 IF 230
Cdd:cd03262 206 IF 207
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-222 |
3.07e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 66.65 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWT------PGTHYGYLDQHTV 76
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 77 LTPGRTIRDVLAdaflplFEKEKALNEVTEKMGTAtpeeleellEQMAEIQDALEAGgfylldmkieeaarglgidaigl 156
Cdd:PRK11248 81 LLPWRNVQDNVA------FGLQLAGVEKMQRLEIA---------HQMLKKVGLEGAE----------------------- 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445977555 157 DRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV---EHIHWLTNYL-KEYPHAFLLISHDTE---FM 222
Cdd:PRK11248 123 KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAftrEQMQTLLLKLwQETGKQVLLITHDIEeavFM 195
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-233 |
3.30e-12 |
|
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: 65.92 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTF-----GDRTL--FKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTpgTHYGYLD--- 72
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR--HDGGWVDlaq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 73 --QHTVL-----TPG------RTI-----RDVLADaflPLFEkekalnevtekMGTatpeeleelleqmaeiqDALEAgg 134
Cdd:COG4778 82 asPREILalrrrTIGyvsqflRVIprvsaLDVVAE---PLLE-----------RGV-----------------DREEA-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 135 fylldmkIEEAARGLgiDAIGLDRDVSAL-----SGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD-------VEHIHwlt 202
Cdd:COG4778 129 -------RARARELL--ARLNLPERLWDLppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDaanravvVELIE--- 196
|
250 260 270
....*....|....*....|....*....|.
gi 445977555 203 nYLKEYPHAFLLISHDTEFMNKCVDVIFHLE 233
Cdd:COG4778 197 -EAKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
343-501 |
3.92e-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: 3.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTS-LGDFLEPA------YFEQEVKADNITPIDDVWNTFPGLD 415
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfDGKPLDIAarnrigYLPEERGLYPKMKVIDQLVYLAQLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 416 -------QHQIRAMLAKCGLKnEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAYKG- 487
Cdd:cd03269 99 glkkeeaRRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARa 177
|
170
....*....|....*.
gi 445977555 488 --TILLVCHEPDFYED 501
Cdd:cd03269 178 gkTVILSTHQMELVEE 193
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
325-497 |
4.07e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.55 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 325 VFEGENVEIGYTH---PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLgdflepayFEQEVKADNI 401
Cdd:PRK13632 7 MIKVENVSFSYPNsenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI--------DGITISKENL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 402 TPI-----------DdvwNTFPG---------------LDQHQIRAML----AKCGLKNeHISRPLSQLSGGEQAKVRLC 451
Cdd:PRK13632 79 KEIrkkigiifqnpD---NQFIGatveddiafglenkkVPPKKMKDIIddlaKKVGMED-YLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 445977555 452 KLMGEESNWLLFDEPTNHLDVTAKAELKKAM----KAYKGTILLVCHEPD 497
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMvdlrKTRKKTLISITHDMD 204
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
334-494 |
4.25e-12 |
|
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: 68.61 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 334 GYTHPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFL------------------EPAYFEQE 395
Cdd:TIGR01193 484 GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqfinylpqEPYIFSGS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 396 VkADNI-------TPIDDVWNTfpgLDQHQIRAMLAKC--GLKNEhISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEP 466
Cdd:TIGR01193 564 I-LENLllgakenVSQDEIWAA---CEIAEIKDDIENMplGYQTE-LSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
170 180
....*....|....*....|....*....
gi 445977555 467 TNHLDV-TAKAELKKAMKAYKGTILLVCH 494
Cdd:TIGR01193 639 TSNLDTiTEKKIVNNLLNLQDKTIIFVAH 667
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-196 |
4.25e-12 |
|
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: 68.59 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFG--DRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLDQH-----T 75
Cdd:TIGR02203 330 DVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI---------LLDGHdladyT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 76 VLTPGRTIRDVLADAFLplFEKEKALNEVTEKMGTATpeeleelleqMAEIQDALEAGgfYLLDMkieeaarglgIDAI- 154
Cdd:TIGR02203 401 LASLRRQVALVSQDVVL--FNDTIANNIAYGRTEQAD----------RAEIERALAAA--YAQDF----------VDKLp 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 445977555 155 -GLDRDV----SALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE 196
Cdd:TIGR02203 457 lGLDTPIgengVLLSGGQRQRLAIARALLKDAPILILDEATSALDNE 503
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
326-494 |
4.25e-12 |
|
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: 65.66 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 326 FEGENVEIGY-THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLepaYFEQEVKADNITPI 404
Cdd:cd03260 1 IELRDLNVYYgDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVL---LDGKDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 405 ddvW------------NTFP---------GLDQHQIRAM----------LAKCGLKNEhISRPLS--QLSGGEQAKVRLC 451
Cdd:cd03260 78 ---ElrrrvgmvfqkpNPFPgsiydnvayGLRLHGIKLKeelderveeaLRKAALWDE-VKDRLHalGLSGGQQQRLCLA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 445977555 452 KLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAYKG--TILLVCH 494
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTH 198
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
343-493 |
4.51e-12 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 65.47 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLgDFLEPAYFEQEVKA------------DNITPIDDV--W 408
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV-DGFDVVKEPAEARRrlgfvsdstglyDRLTARENLeyF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 409 NTFPGLDQHQIRAMLAKCGLK---NEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAY 485
Cdd:cd03266 103 AGLYGLKGDELTARLEELADRlgmEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL 182
|
170
....*....|
gi 445977555 486 K--GTILLVC 493
Cdd:cd03266 183 RalGKCILFS 192
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
329-495 |
5.17e-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: 5.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGY-THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGK-----TSLGDFLEPAYFEQEVK----- 397
Cdd:COG1127 9 RNLTKSFgDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEilvdgQDITGLSEKELYELRRRigmlf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 398 -----------ADNItpiddvwnTFP-----GLDQHQIRAM----LAKCGLKNEHISRPlSQLSGGEQAKVRL------- 450
Cdd:COG1127 89 qggalfdsltvFENV--------AFPlrehtDLSEAEIRELvlekLELVGLPGAADKMP-SELSGGMRKRVALaralald 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 445977555 451 CKLmgeesnwLLFDEPTNHLD-VTAKA------ELKKAMKAykgTILLVCHE 495
Cdd:COG1127 160 PEI-------LLYDEPTAGLDpITSAVidelirELRDELGL---TSVVVTHD 201
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
12-220 |
6.38e-12 |
|
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: 64.88 E-value: 6.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 12 TFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVeWTPGThygyldQHTVLTPGRTirdvladAF 91
Cdd:TIGR01277 7 RYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSI-KVNDQ------SHTGLAPYQR-------PV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 92 LPLFEKEKALNEVT--EKMGTATPEELEELLEQMAeiqdaleaggfylldmKIEEAARGLGIDAIgLDRDVSALSGGQRT 169
Cdd:TIGR01277 73 SMLFQENNLFAHLTvrQNIGLGLHPGLKLNAEQQE----------------KVVDAAQQVGIADY-LDRLPEQLSGGQRQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 170 KVLLAKLLLEQPEVLLLDEPTNYLD----VEHIHWLTNYLKEYPHAFLLISHDTE 220
Cdd:TIGR01277 136 RVALARCLVRPNPILLLDEPFSALDpllrEEMLALVKQLCSERQRTLLMVTHHLS 190
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-495 |
6.95e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.81 E-value: 6.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTF----GDRTLFKDVSMRLLAGEHVGLVGANGVGKS-TFMNII----TGQLIHDQGRVEWTpGTHYGYL 71
Cdd:PRK15134 3 QPLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpSPPVVYPSGDIRFH-GESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 72 DQHTVltpgRTIR-DVLADAFL-------PLFEKEKALNEVT---EKMGTATPEeleelleqmAEIQDALEAGGfylldm 140
Cdd:PRK15134 82 SEQTL----RGVRgNKIAMIFQepmvslnPLHTLEKQLYEVLslhRGMRREAAR---------GEILNCLDRVG------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 141 kIEEAARGLgidaigldRDVS-ALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE---HIHWLTNYLK-EYPHAFLLI 215
Cdd:PRK15134 143 -IRQAAKRL--------TDYPhQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSvqaQILQLLRELQqELNMGLLFI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 216 SHDTEFMNKCVDVIFHLEFTKMTRYTATYEKFlelaeiNKNQHinAYEKQrefIKKQEdfiaknkarysTTGRAKSRQKQ 295
Cdd:PRK15134 214 THNLSIVRKLADRVAVMQNGRCVEQNRAATLF------SAPTH--PYTQK---LLNSE-----------PSGDPVPLPEP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 296 LDRMELIDRPETAikpefsFKESRASSRFVfegenveIGYtHPLLPKLSMTIERGEKIAIVGCNGVGKST----LLKTIL 371
Cdd:PRK15134 272 ASPLLDVEQLQVA------FPIRKGILKRT-------VDH-NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 372 --GKI----KPLSGKTSlGDFLEPAYFEQEVKAD---NITPIDDVWNTFP-GLDQHQ------------IRAMlAKCGLK 429
Cdd:PRK15134 338 sqGEIwfdgQPLHNLNR-RQLLPVRHRIQVVFQDpnsSLNPRLNVLQIIEeGLRVHQptlsaaqreqqvIAVM-EEVGLD 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 430 NEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAE----LKKAMKAYKGTILLVCHE 495
Cdd:PRK15134 416 PETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQilalLKSLQQKHQLAYLFISHD 485
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-220 |
7.62e-12 |
|
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: 64.95 E-value: 7.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW---------TPGTHYGYLDQH 74
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLdgkditnlpPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 75 TVLTPGRTIRDVLAdafLPLFEKEKALNEVTEKmgtatpeeleelleqmaeIQDALEAggfylldMKIEEAARglgidai 154
Cdd:cd03300 81 YALFPHLTVFENIA---FGLRLKKLPKAEIKER------------------VAEALDL-------VQLEGYAN------- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 155 gldRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPH----AFLLISHDTE 220
Cdd:cd03300 126 ---RKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQE 192
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
11-218 |
7.65e-12 |
|
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: 66.67 E-value: 7.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 11 HTFGDRTLfkDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTpGTHYGYLDQHTVLTP-GRTIRDVLAD 89
Cdd:TIGR02142 7 KRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLN-GRTLFDSRKGIFLPPeKRRIGYVFQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 90 AflPLFEKEKALNEVTEKMGTATPEELEELLEQMAEIqdaleaggfylldmkieeaargLGIDAIgLDRDVSALSGGQRT 169
Cdd:TIGR02142 84 A--RLFPHLSVRGNLRYGMKRARPSERRISFERVIEL----------------------LGIGHL-LGRLPGRLSGGEKQ 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 445977555 170 KVLLAKLLLEQPEVLLLDEPTNYLDV----EHIHWLTNYLKEYPHAFLLISHD 218
Cdd:TIGR02142 139 RVAIGRALLSSPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHS 191
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-229 |
7.70e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.12 E-value: 7.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV--EWTPGTHYG---YLDQ--HT 75
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfEGEDISTLKpeiYRQQvsYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 76 VLTP---GRTIRDVLadaflpLFekekalnevtekmgtatPEELEELLEQMAEIQDALEAGGfylLDMKIeeaarglgid 152
Cdd:PRK10247 87 AQTPtlfGDTVYDNL------IF-----------------PWQIRNQQPDPAIFLDDLERFA---LPDTI---------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 153 aigLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDvEH--------IHwltNYLKEYPHAFLLISHDTEFMNK 224
Cdd:PRK10247 131 ---LTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD-ESnkhnvneiIH---RYVREQNIAVLWVTHDKDEINH 203
|
....*
gi 445977555 225 CVDVI 229
Cdd:PRK10247 204 ADKVI 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
329-494 |
8.79e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.99 E-value: 8.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGYTHplLP-KLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD----------------FLEPAY 391
Cdd:PRK10771 5 TDITWLYHH--LPmRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtttppsrrpvsmlFQENNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 392 FEQEVKADNITpiddvWNTFPGL-----DQHQIRAMLAKCGLKNeHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEP 466
Cdd:PRK10771 83 FSHLTVAQNIG-----LGLNPGLklnaaQREKLHAIARQMGIED-LLARLPGQLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190
....*....|....*....|....*....|..
gi 445977555 467 TNHLDVTAKAE----LKKAMKAYKGTILLVCH 494
Cdd:PRK10771 157 FSALDPALRQEmltlVSQVCQERQLTLLMVSH 188
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-218 |
1.22e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.49 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTpgthygYLDQHTvLTPGRTIRDVLADAFL--PLFEK 97
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWI------FKDEKN-KKKTKEKEKVLEKLVIqkTRFKK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 98 EKALNEVTEKMGTAtpeeleellEQMAEIQdaleaggfyLLDMKIEE----AARGLG-------------IDAIGLD--- 157
Cdd:PRK13651 97 IKKIKEIRRRVGVV---------FQFAEYQ---------LFEQTIEKdiifGPVSMGvskeeakkraakyIELVGLDesy 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445977555 158 --RDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD---VEHIHWLTNYLKEYPHAFLLISHD 218
Cdd:PRK13651 159 lqRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-197 |
1.65e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 64.33 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 5 TVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW-------TPG----THYGYLDQ 73
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVdgldvatTPSrelaKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 74 HTVLTPGRTIRDVLAdaflplF-----EKEKaLNEVTEKMgtatpeeleelleqmaeIQDALEAggFYLLDMKieeaarg 148
Cdd:COG4604 83 ENHINSRLTVRELVA------FgrfpySKGR-LTAEDREI-----------------IDEAIAY--LDLEDLA------- 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 445977555 149 lgidaiglDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEH 197
Cdd:COG4604 130 --------DRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKH 170
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-194 |
1.72e-11 |
|
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: 63.34 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTF-GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLI--HDQGRV--------EWTPGTHYGYLD 72
Cdd:cd03213 9 LTVTVKSSPSkSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVlingrpldKRSFRKIIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 73 QHTVLTPGRTIRDVLADAflplfekekalnevtekmgtatpeeleelleqmAEIqdaleaggfylldmkieeaaRGlgid 152
Cdd:cd03213 89 QDDILHPTLTVRETLMFA---------------------------------AKL--------------------RG---- 111
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 445977555 153 aigldrdvsaLSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:cd03213 112 ----------LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-194 |
1.79e-11 |
|
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: 63.83 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 15 DRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHD---QGRV-----EWTPGT---HYGYLDQHTVLTPGRTI 83
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQIlfngqPRKPDQfqkCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 84 RDVLAdaFLPLFekekalnevtekmgtATPEELEELLEQMAEIQDALeaggfylldmkieeaaRGLGIDAIGLDRdVSAL 163
Cdd:cd03234 99 RETLT--YTAIL---------------RLPRKSSDAIRKKRVEDVLL----------------RDLALTRIGGNL-VKGI 144
|
170 180 190
....*....|....*....|....*....|.
gi 445977555 164 SGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:cd03234 145 SGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
329-496 |
2.10e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 65.48 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGY-THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD----FLEP-----AY-FEQ--- 394
Cdd:COG3839 7 ENVSKSYgGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvtDLPPkdrniAMvFQSyal 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 395 ----EVkADNItpiddvwnTFP----GLDQHQIRA----MLAKCGLknEHI--SRPlSQLSGGEQ-------AKVRLCKL 453
Cdd:COG3839 87 yphmTV-YENI--------AFPlklrKVPKAEIDRrvreAAELLGL--EDLldRKP-KQLSGGQRqrvalgrALVREPKV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 445977555 454 mgeesnwLLFDEPTNHLD----VTAKAELKKAMKAYKGTILLVCHEP 496
Cdd:COG3839 155 -------FLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHDQ 194
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-207 |
2.16e-11 |
|
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: 63.86 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFG-DRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTpGTHYGYLDQHTVltpgR 81
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLE-GTDITKLRGKKL----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 82 TIRDVLADAF--LPLFEKEKAL-NEVTEKMGTATPEELEELLEQMAEIQDALEAggfylLDMkieeaargLGIDAIGLDR 158
Cdd:TIGR02315 76 KLRRRIGMIFqhYNLIERLTVLeNVLHGRLGYKPTWRSLLGRFSEEDKERALSA-----LER--------VGLADKAYQR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 445977555 159 dVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKE 207
Cdd:TIGR02315 143 -ADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKR 190
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-194 |
2.27e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.44 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNII-------TGQLIHDQGRVEWTPGTH--YGYL 71
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIagleditSGDLFIGEKRMNDVPPAErgVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 72 DQHTVLTPGRTIRDVLAdaF-LPLFEKEKAlnevtekmgtatpeeleelleqmaEIqdaleaggfyllDMKIEEAARGLG 150
Cdd:PRK11000 81 FQSYALYPHLSVAENMS--FgLKLAGAKKE------------------------EI------------NQRVNQVAEVLQ 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 445977555 151 IDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PRK11000 123 LAHL-LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-221 |
2.31e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.22 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLDQHTVltpgRTI 83
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSI---------VVNGQTI----NLV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 84 RDvlADAFLPLFEKEK------ALNEVTEKMGTATPEELEELLEQmAEIQ-------DALEAGGFYLLDMKIEEAARGlg 150
Cdd:PRK10619 73 RD--KDGQLKVADKNQlrllrtRLTMVFQHFNLWSHMTVLENVME-APIQvlglskqEARERAVKYLAKVGIDERAQG-- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445977555 151 idaigldRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE---HIHWLTNYLKEYPHAFLLISHDTEF 221
Cdd:PRK10619 148 -------KYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGF 214
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-218 |
2.35e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.13 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTF----GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGqLIHDQGRVEwtpgthygyldqHTV 76
Cdd:PRK09473 10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMG-LLAANGRIG------------GSA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 77 LTPGRTIRDvladafLPlfekEKALNEV---------TEKMGTATPEELEELleQMAEI---------QDALEAGGFYLL 138
Cdd:PRK09473 77 TFNGREILN------LP----EKELNKLraeqismifQDPMTSLNPYMRVGE--QLMEVlmlhkgmskAEAFEESVRMLD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 139 DMKIEEAARGLGIDAigldrdvSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV---EHIHWLTNYLK-EYPHAFLL 214
Cdd:PRK09473 145 AVKMPEARKRMKMYP-------HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvqAQIMTLLNELKrEFNTAIIM 217
|
....
gi 445977555 215 ISHD 218
Cdd:PRK09473 218 ITHD 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
329-494 |
2.47e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 65.12 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGY-THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD----FLEPayfEQ-EVK----- 397
Cdd:COG3842 9 ENVSKRYgDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvtGLPP---EKrNVGmvfqd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 398 ---------ADNItpiddvwnTFP----GLDQHQIRA----MLAKCGLKnEHISRPLSQLSGGEQAKVRLC-------KL 453
Cdd:COG3842 86 yalfphltvAENV--------AFGlrmrGVPKAEIRArvaeLLELVGLE-GLADRYPHQLSGGQQQRVALAralapepRV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 445977555 454 mgeesnwLLFDEPTNHLDVTAK----AELKKAMKAYKGTILLVCH 494
Cdd:COG3842 157 -------LLLDEPLSALDAKLReemrEELRRLQRELGITFIYVTH 194
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
339-478 |
3.05e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 339 LLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPAYFEQEVKADNITP--IDDVWNTFPGLDQ 416
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPltVNRFLRLRPGTKK 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445977555 417 HQIRAMLAKcgLKNEH-ISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAEL 478
Cdd:PRK09544 99 EDILPALKR--VQAGHlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-197 |
3.50e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.85 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 7 EKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVeWTPGTHY------------GYLDQH 74
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIqhyaskevarriGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 75 TVlTPGR-TIRDVLADA---FLPLFEKEKAlnevtekmgtatpeeleelleqmaEIQDAleaggfylldmkIEEAARGLG 150
Cdd:PRK10253 90 AT-TPGDiTVQELVARGrypHQPLFTRWRK------------------------EDEEA------------VTKAMQATG 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 445977555 151 IDAIGlDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEH 197
Cdd:PRK10253 133 ITHLA-DQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-196 |
4.17e-11 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 63.01 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV-----------EWTPGTHYGYLDQHTVLTPGrTIRDVLa 88
Cdd:cd03254 20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisRKSLRSMIGVVLQDTFLFSG-TIMENI- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 89 daflplfekekalnevteKMGTATPeeleelleQMAEIQDALEAGGFYLLDMKIEEaarglgidaiGLDRDV----SALS 164
Cdd:cd03254 98 ------------------RLGRPNA--------TDEEVIEAAKEAGAHDFIMKLPN----------GYDTVLgengGNLS 141
|
170 180 190
....*....|....*....|....*....|..
gi 445977555 165 GGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE 196
Cdd:cd03254 142 QGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-190 |
4.20e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.05 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWtpgthygylDQHTVltpgrTIRD-------------- 85
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI---------DGKPV-----RIRSprdaialgigmvhq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 86 --VLADAFlplfekekalnevtekmgTAtpeeleelleqmAE-IQDALEAGGFYLLDMK-----IEEAAR--GLGIDaig 155
Cdd:COG3845 88 hfMLVPNL------------------TV------------AEnIVLGLEPTKGGRLDRKaararIRELSEryGLDVD--- 134
|
170 180 190
....*....|....*....|....*....|....*
gi 445977555 156 LDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPT 190
Cdd:COG3845 135 PDAKVEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-229 |
4.23e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.52 E-value: 4.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTFMNIItgqlihdqgrvewtpgthyGYLDQHTVLT---PGRTIRDVLADAFLPL-- 94
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNIL-------------------GCLDKPTSGTyrvAGQDVATLDADALAQLrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 95 ------FEKEKALNEVTEKMGTATPeeleelleqmaeiqdALEAGgfyLLDMKIEEAARGLgIDAIGLDRDV----SALS 164
Cdd:PRK10535 86 ehfgfiFQRYHLLSHLTAAQNVEVP---------------AVYAG---LERKQRLLRAQEL-LQRLGLEDRVeyqpSQLS 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 165 GGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV---EHIHWLTNYLKEYPHAFLLISHDTEFMNKCVDVI 229
Cdd:PRK10535 147 GGQQQRVSIARALMNGGQVILADEPTGALDShsgEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVI 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
335-478 |
4.29e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 65.70 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 335 YTHPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEpayFEQEVKAdnITP--IDDvwNTFP 412
Cdd:TIGR01271 437 YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRIS---FSPQTSW--IMPgtIKD--NIIF 509
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445977555 413 GL--DQHQIRAMLAKCGLKnEHISR-------PLSQ----LSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAEL 478
Cdd:TIGR01271 510 GLsyDEYRYTSVIKACQLE-EDIALfpekdktVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
329-495 |
4.45e-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: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGYTH-PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD----------------FLEPAY 391
Cdd:cd03300 4 ENVSKFYGGfVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkditnlpphkrpvntvFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 392 FEQEVKADNItpiddvwnTFP----GLDQHQIRA----MLAKCGLKnEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLF 463
Cdd:cd03300 84 FPHLTVFENI--------AFGlrlkKLPKAEIKErvaeALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 445977555 464 DEPTNHLDV----TAKAELKKAMKAYKGTILLVCHE 495
Cdd:cd03300 155 DEPLGALDLklrkDMQLELKRLQKELGITFVFVTHD 190
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
333-471 |
4.78e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 62.81 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 333 IGY---THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD----FLEPAYFEQEVKADNITPI- 404
Cdd:PRK10247 13 VGYlagDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedisTLKPEIYRQQVSYCAQTPTl 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445977555 405 --DDVWNT--FPGLDQHQ------IRAMLAKCGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD 471
Cdd:PRK10247 93 fgDTVYDNliFPWQIRNQqpdpaiFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
339-495 |
5.11e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.27 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 339 LLPKLSMTIERGEKIAIVGCNGVGKSTLLKtILGKIKPLSGktslGDFL----------------EPAYFEQEV-KADNI 401
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPPSE----GEILldaqpleswsskafarKVAYLPQQLpAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 402 T----------PIDDVWNTFPGLDQHQIRAMLAKCGLKnEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD 471
Cdd:PRK10575 101 TvrelvaigryPWHGALGRFGAADREKVEEAISLVGLK-PLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180
....*....|....*....|....*...
gi 445977555 472 VTAKAE---LKKAMKAYKG-TILLVCHE 495
Cdd:PRK10575 180 IAHQVDvlaLVHRLSQERGlTVIAVLHD 207
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
344-498 |
6.00e-11 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 62.70 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 344 SMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDflepayfeQEVKADNiTPIDDV----------WNTFP- 412
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDG--------EDLTDSK-KDINKLrrkvgmvfqqFNLFPh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 413 ---------------GLDQHQIRA----MLAKCGLKNEHISRPlSQLSGGEQAKV---R-LC---KLMgeesnwlLFDEP 466
Cdd:COG1126 92 ltvlenvtlapikvkKMSKAEAEErameLLERVGLADKADAYP-AQLSGGQQQRVaiaRaLAmepKVM-------LFDEP 163
|
170 180 190
....*....|....*....|....*....|....*
gi 445977555 467 TNHLDVTAKAELKKAMK--AYKG-TILLVCHEPDF 498
Cdd:COG1126 164 TSALDPELVGEVLDVMRdlAKEGmTMVVVTHEMGF 198
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
334-495 |
6.03e-11 |
|
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: 62.60 E-value: 6.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 334 GYTHPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGK-----TSLGDFLEPA----------------YF 392
Cdd:cd03258 15 GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSvlvdgTDLTLLSGKElrkarrrigmifqhfnLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 393 EQEVKADNITPIDDVWNTfPGLDQH-QIRAMLAKCGLKNEHISRPlSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD 471
Cdd:cd03258 95 SSRTVFENVALPLEIAGV-PKAEIEeRVLELLELVGLEDKADAYP-AQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
170 180
....*....|....*....|....*...
gi 445977555 472 VTAKAE----LKKAMKAYKGTILLVCHE 495
Cdd:cd03258 173 PETTQSilalLRDINRELGLTIVLITHE 200
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
337-498 |
6.75e-11 |
|
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: 61.02 E-value: 6.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 337 HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTI--L-----GKIKPLSGKTSLgdFL--EPaYFEQevkadnitpiddv 407
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALagLwpwgsGRIGMPEGEDLL--FLpqRP-YLPL------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 408 wntfpgldqhqiramlakcGLKNEHISRPLSQ-LSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAYK 486
Cdd:cd03223 78 -------------------GTLREQLIYPWDDvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG 138
|
170
....*....|..
gi 445977555 487 GTILLVCHEPDF 498
Cdd:cd03223 139 ITVISVGHRPSL 150
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-218 |
6.90e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.57 E-value: 6.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVE---WTPgthygYLDQHTVLtpgRTIRDVLA-------D 89
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgYVP-----FKRRKEFA---RRIGVVFGqrsqlwwD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 90 afLPL---FEKEKALNEVTEkmgtatpeeleelleqmAEIQDALEaggfYLLDMkieeaargLGIDAIgLDRDVSALSGG 166
Cdd:COG4586 111 --LPAidsFRLLKAIYRIPD-----------------AEYKKRLD----ELVEL--------LDLGEL-LDTPVRQLSLG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 445977555 167 QRTKVLLAKLLLEQPEVLLLDEPTNYLDV---EHIHwltNYLKEYPHAF----LLISHD 218
Cdd:COG4586 159 QRMRCELAAALLHRPKILFLDEPTIGLDVvskEAIR---EFLKEYNRERgttiLLTSHD 214
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-197 |
7.33e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.88 E-value: 7.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 5 TVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNII-------TGQ-LIHDQGRVEWTP---GTHYGYLDQ 73
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLgrhqppsEGEiLLDAQPLESWSSkafARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 74 HTVLTPGRTIRDVLADAFLPLfekekalnevtekmgtatpeeleelleqmaeiQDALeaGGFYLLDM-KIEEAarglgID 152
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGRYPW--------------------------------HGAL--GRFGAADReKVEEA-----IS 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 445977555 153 AIGL----DRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEH 197
Cdd:PRK10575 134 LVGLkplaHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-225 |
7.52e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.22 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTpgthygylDQHTVLTP- 79
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID--------DEDISLLPl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 80 -GRTIRDVladAFLP----------LFEKEKALNEVTEKMGTatpeeleellEQMAEIQDALeaggfyLLDMKIEEAARG 148
Cdd:PRK10895 73 hARARRGI---GYLPqeasifrrlsVYDNLMAVLQIRDDLSA----------EQREDRANEL------MEEFHIEHLRDS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 149 LGidaigldrdvSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD---VEHIHWLTNYLKEYPHAFLLISHDT-EFMNK 224
Cdd:PRK10895 134 MG----------QSLSGGERRRVEIARALAANPKFILLDEPFAGVDpisVIDIKRIIEHLRDSGLGVLITDHNVrETLAV 203
|
.
gi 445977555 225 C 225
Cdd:PRK10895 204 C 204
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
300-471 |
7.72e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.46 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 300 ELID-RPETaikpEFSFKESRASSRFVFEGENVEIGY---THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIK 375
Cdd:PRK11160 316 EITEqKPEV----TFPTTSTAAADQVSLTLNNVSFTYpdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 376 PLSGKTSLGDFLEPAYFEQEVKAdNITPID---DVWNT---------FPGLDQHQIRAMLAKCGLKNeHIS--RPLS--- 438
Cdd:PRK11160 392 PQQGEILLNGQPIADYSEAALRQ-AISVVSqrvHLFSAtlrdnlllaAPNASDEALIEVLQQVGLEK-LLEddKGLNawl 469
|
170 180 190
....*....|....*....|....*....|....*...
gi 445977555 439 -----QLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD 471
Cdd:PRK11160 470 geggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-194 |
8.80e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 62.73 E-value: 8.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 2 SLLTVEKLGHTFGD--RTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTpgthygyldqHTVLTP 79
Cdd:PRK13635 4 EIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG----------GMVLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 80 gRTIRDVLADAFLpLFEkekalNEVTEKMGTAtpeeleelleqmaeIQD----ALEAGGFYLLDM--KIEEAARGLGIDA 153
Cdd:PRK13635 74 -ETVWDVRRQVGM-VFQ-----NPDNQFVGAT--------------VQDdvafGLENIGVPREEMveRVDQALRQVGMED 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 445977555 154 IgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PRK13635 133 F-LNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
329-497 |
9.82e-11 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 61.93 E-value: 9.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGY--THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDF----LEP-------AYFEQE 395
Cdd:cd03295 4 ENVTKRYggGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdireQDPvelrrkiGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 396 VK-------ADNITpiddvwnTFPGL---DQHQIRA----MLAKCGLKNEHIS-RPLSQLSGGEQAKVRLCKLMGEESNW 460
Cdd:cd03295 84 IGlfphmtvEENIA-------LVPKLlkwPKEKIREradeLLALVGLDPAEFAdRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 445977555 461 LLFDEPTNHLDVTAKAELKKAMKAYK----GTILLVCHEPD 497
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQqelgKTIVFVTHDID 197
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-196 |
9.85e-11 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 61.93 E-value: 9.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLDQHTVLTPGRT 82
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI---------TVDGEDLTDSKKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 IRDVLAD------AFlPLFEKEKALNEVTE------KMGTAtpeeleelleqmaeiqdalEAggfylldmkiEEAARGLg 150
Cdd:COG1126 72 INKLRRKvgmvfqQF-NLFPHLTVLENVTLapikvkKMSKA-------------------EA----------EERAMEL- 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 445977555 151 IDAIGL----DRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE 196
Cdd:COG1126 121 LERVGLadkaDAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE 170
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
329-497 |
1.02e-10 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 62.03 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGY-----THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKP------LSGKTSLGDFLEPAY-FeQE- 395
Cdd:COG1116 11 RGVSKRFptgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPtsgevlVDGKPVTGPGPDRGVvF-QEp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 396 -------VkADNItpiddvwnTFP----GLD----QHQIRAMLAKCGLKN-EHiSRPlSQLSGGEQAKVRLCKLMGEESN 459
Cdd:COG1116 90 allpwltV-LDNV--------ALGlelrGVPkaerRERARELLELVGLAGfED-AYP-HQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 445977555 460 WLLFDEPTNHLDVTAKA----ELKKAMKAYKGTILLVCHEPD 497
Cdd:COG1116 159 VLLMDEPFGALDALTRErlqdELLRLWQETGKTVLFVTHDVD 200
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
343-497 |
1.05e-10 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 61.60 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLkTILGKI-KPLSGKTSLGDflepayfeQEVKADNITPIDDVWNT----------- 410
Cdd:COG1136 27 VSLSIEAGEFVAIVGPSGSGKSTLL-NILGGLdRPTSGEVLIDG--------QDISSLSERELARLRRRhigfvfqffnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 411 FPGL-------------------DQHQIRAMLAKCGLKNEHISRPlSQLSGGEQAKVRLCK-LMGEESnwLLF-DEPTNH 469
Cdd:COG1136 98 LPELtalenvalplllagvsrkeRRERARELLERVGLGDRLDHRP-SQLSGGQQQRVAIARaLVNRPK--LILaDEPTGN 174
|
170 180 190
....*....|....*....|....*....|..
gi 445977555 470 LD-VTAK---AELKKAMKAYKGTILLVCHEPD 497
Cdd:COG1136 175 LDsKTGEevlELLRELNRELGTTIVMVTHDPE 206
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
340-503 |
1.11e-10 |
|
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: 60.41 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 340 LPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKikplSGKTSLGDFLePAYFEQEVKAdnitpiddvwntfpgLDQHQi 419
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFL-PKFSRNKLIF---------------IDQLQ- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 420 raMLAKCGLKNEHISRPLSQLSGGEQAKVRLCKLMGEES--NWLLFDEPTNHLDVTAKAELKKAMKAY---KGTILLVCH 494
Cdd:cd03238 70 --FLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVILIEH 147
|
170
....*....|.
gi 445977555 495 EPDF--YEDWI 503
Cdd:cd03238 148 NLDVlsSADWI 158
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-230 |
1.26e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 62.37 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLlTVEKLGHTFGDRTLF-----KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLDqht 75
Cdd:PRK13637 1 MSI-KIENLTHIYMEGTPFekkalDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKI---------IID--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 76 vltpGRTIRDvladaflplfeKEKALNEVTEKMGTAtpeeleellEQMAEIQDALEAggfylLDMKIEEAARGLG----- 150
Cdd:PRK13637 68 ----GVDITD-----------KKVKLSDIRKKVGLV---------FQYPEYQLFEET-----IEKDIAFGPINLGlseee 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 151 --------IDAIGLDRDVSA------LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD----------VEHIHwltnylK 206
Cdd:PRK13637 119 ienrvkraMNIVGLDYEDYKdkspfeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgrdeilnkIKELH------K 192
|
250 260
....*....|....*....|....
gi 445977555 207 EYPHAFLLISHDTEFMNKCVDVIF 230
Cdd:PRK13637 193 EYNMTIILVSHSMEDVAKLADRII 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-196 |
1.43e-10 |
|
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: 61.40 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 15 DRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIItgQLIHD--QGRVewtpgthygYLDQHTV--LTPgRTIRDVLAda 90
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL--ERFYDptSGEI---------LLDGVDIrdLNL-RWLRSQIG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 91 flpLFEKEKALNEVTekmgtatpeeleelleqmaeIQDALEAGGFYLLDMKIEEAARGLGIDAI------GLDRDV---- 160
Cdd:cd03249 81 ---LVSQEPVLFDGT--------------------IAENIRYGKPDATDEEVEEAAKKANIHDFimslpdGYDTLVgerg 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 445977555 161 SALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE 196
Cdd:cd03249 138 SQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-196 |
2.14e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 62.90 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLG-HTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGqlI--HDQGRVEWTPGTHYGYLDQHTVLTPG 80
Cdd:COG4178 363 LALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG--LwpYGSGRIARPAGARVLFLPQRPYLPLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 81 rTIRDVLAdafLPlfekeKALNEVTEkmgtatpeeleelleqmAEIQDALEAGGF-YLLDMkieeaarglgidaigLDRD 159
Cdd:COG4178 441 -TLREALL---YP-----ATAEAFSD-----------------AELREALEAVGLgHLAER---------------LDEE 479
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 445977555 160 VS---ALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE 196
Cdd:COG4178 480 ADwdqVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-194 |
2.26e-10 |
|
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: 60.20 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 28 AGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwTPGTHYGYLD----------QHTVLTPGRTIRDVLADAFLPLFEk 97
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVL-INGVDVTAAPpadrpvsmlfQENNLFAHLTVEQNVGLGLSPGLK- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 98 ekaLNEVTEKmgtatpeeleelleqmaeiqdaleaggfylldmKIEEAARGLGIDaiGLD-RDVSALSGGQRTKVLLAKL 176
Cdd:cd03298 101 ---LTAEDRQ---------------------------------AIEVALARVGLA--GLEkRLPGELSGGERQRVALARV 142
|
170
....*....|....*...
gi 445977555 177 LLEQPEVLLLDEPTNYLD 194
Cdd:cd03298 143 LVRDKPVLLLDEPFAALD 160
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
335-478 |
2.29e-10 |
|
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: 61.41 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 335 YTHPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEpayFEQEVKAdnITPIDDVWNTFPGL 414
Cdd:cd03291 48 VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRIS---FSSQFSW--IMPGTIKENIIFGV 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445977555 415 --DQHQIRAMLAKCGLKnEHISR-------PLSQ----LSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAEL 478
Cdd:cd03291 123 syDEYRYKSVVKACQLE-EDITKfpekdntVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-194 |
2.34e-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: 60.53 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 2 SLLTVEKLGHTFGDR----TLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW-----TP-------- 64
Cdd:COG4181 7 PIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLagqdlFAldedarar 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 65 --GTHYGYLDQHTVLTPGRTirdvladaflplfekekALNEVtekmgtATPeeleelleqmAEIQDALEAGgfylldmki 142
Cdd:COG4181 87 lrARHVGFVFQSFQLLPTLT-----------------ALENV------MLP----------LELAGRRDAR--------- 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 445977555 143 EEAARGLgiDAIGLDRDVSA----LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:COG4181 125 ARARALL--ERVGLGHRLDHypaqLSGGEQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-230 |
2.39e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 63.20 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 15 DRTLFKDVSMRLLAGEHVGLVGANGVGKST-------FMNIITGQLIHDQgrvewTPGTHYG--YLDQHTVLTP------ 79
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTvaallqnLYQPTGGQVLLDG-----VPLVQYDhhYLHRQVALVGqepvlf 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 80 GRTIRDVLADAFlplfekekalnevtekmgTATPeeleelleqMAEIQDALEAGGFYLLDMKIEEaarglgidaiGLDRD 159
Cdd:TIGR00958 568 SGSVRENIAYGL------------------TDTP---------DEEIMAAAKAANAHDFIMEFPN----------GYDTE 610
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 160 V----SALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAFLLISHDTEFMNKCVDVIF 230
Cdd:TIGR00958 611 VgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQILV 685
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
337-501 |
2.66e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 60.92 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 337 HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDflepayfeqeVKADNITPIDDVWNTFPGLDQ 416
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGD----------ITIDTARSLSQQKGLIRQLRQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 417 H-------------------------------------QIRAMLAKCGLKNEHISRPlSQLSGGEQAKVRLCKLMGEESN 459
Cdd:PRK11264 86 HvgfvfqnfnlfphrtvleniiegpvivkgepkeeataRARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 445977555 460 WLLFDEPTNHLDVTAKAELKKAMKAY---KGTILLVCHEPDFYED 501
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHEMSFARD 209
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
339-492 |
2.67e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.60 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 339 LLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGK-----TSLGDFLEPAyfeqevKAD-------------- 399
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDvifngQPMSKLSSAA------KAElrnqklgfiyqfhh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 400 ---NITPIDDV------WNTFPGLDQHQIRAMLAKCGLKNEHISRPlSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHL 470
Cdd:PRK11629 98 llpDFTALENVamplliGKKKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180
....*....|....*....|....*
gi 445977555 471 DV-TAKA--ELKKAMKAYKGTILLV 492
Cdd:PRK11629 177 DArNADSifQLLGELNRLQGTAFLV 201
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
336-471 |
2.82e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 61.03 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 336 THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGdflepayfEQEVKA-----------DNITP- 403
Cdd:COG4525 19 PQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLD--------GVPVTGpgadrgvvfqkDALLPw 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445977555 404 ---IDDVwnTFP----GLDQHQIRA----MLAKCGLKnEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD 471
Cdd:COG4525 91 lnvLDNV--AFGlrlrGVPKAERRAraeeLLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
11-220 |
3.14e-10 |
|
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: 61.66 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 11 HTFGDRTLfkDVSMRLLAGEHVGLVGANGVGKSTFMNIITGqLIH-DQGRVE-------------WTPgTH---YGYLDQ 73
Cdd:COG4148 9 LRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAG-LERpDSGRIRlggevlqdsargiFLP-PHrrrIGYVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 74 HTVLTPGRTIRDVLADA--FLPLFEKEKALNEVTEkmgtatpeeleelleqmaeiqdaleaggfylLdmkieeaargLGI 151
Cdd:COG4148 85 EARLFPHLSVRGNLLYGrkRAPRAERRISFDEVVE-------------------------------L----------LGI 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445977555 152 DAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAF----LLISHDTE 220
Cdd:COG4148 124 GHL-LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELdipiLYVSHSLD 195
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-233 |
3.79e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 62.17 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 17 TLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHdQGRV--------EWTPGT---HYGYLDQHTVLTPGrTIRD 85
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLkingielrELDPESwrkHLSWVGQNPQLPHG-TLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 86 --VLADAFLPlfekEKALNEVTEKmgtatpeeleellEQMAEIQDALEAGgfylLDMKIEEAARGLgidaigldrdvsal 163
Cdd:PRK11174 442 nvLLGNPDAS----DEQLQQALEN-------------AWVSEFLPLLPQG----LDTPIGDQAAGL-------------- 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445977555 164 SGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHA--FLLISHDTEFMnKCVDVIFHLE 233
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRqtTLMVTHQLEDL-AQWDQIWVMQ 557
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
336-503 |
4.04e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 59.41 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 336 THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLepAYFEQE-------VKaDNIT---PID 405
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--AYVSQEpwiqngtIR-ENILfgkPFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 406 DVW--------------NTFPGLDQHQIramlakcGLKNehISrplsqLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD 471
Cdd:cd03250 94 EERyekvikacalepdlEILPDGDLTEI-------GEKG--IN-----LSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 445977555 472 V-TAKA--E--LKKAMKAYKgTILLVCHEPDF--YEDWI 503
Cdd:cd03250 160 AhVGRHifEncILGLLLNNK-TRILVTHQLQLlpHADQI 197
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
340-494 |
4.07e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 60.83 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 340 LPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD--------------------FLEPAY--FEQEVK 397
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkkvglvFQYPEYqlFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 398 AD-NITPIDdvwntfPGLDQHQI-----RAMlAKCGLKNEHIS-RPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHL 470
Cdd:PRK13637 103 KDiAFGPIN------LGLSEEEIenrvkRAM-NIVGLDYEDYKdKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180
....*....|....*....|....*...
gi 445977555 471 DVTAK----AELKKAMKAYKGTILLVCH 494
Cdd:PRK13637 176 DPKGRdeilNKIKELHKEYNMTIILVSH 203
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
340-497 |
4.25e-10 |
|
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: 59.79 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 340 LPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLG--DFLEP-----------AYFEQEVKADNIT-PID 405
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEgkQITEPgpdrmvvfqnySLLPWLTVRENIAlAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 406 DVWNTFPGLDQHQI-RAMLAKCGLKNEHISRPlSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAM-- 482
Cdd:TIGR01184 81 RVLPDLSKSERRAIvEEHIALVGLTEAADKRP-GQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmq 159
|
170
....*....|....*..
gi 445977555 483 --KAYKGTILLVCHEPD 497
Cdd:TIGR01184 160 iwEEHRVTVLMVTHDVD 176
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-218 |
4.36e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwtpgthygyLDQHTVLTpgRTIRDVLADAFLPLFEKEK 99
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVT---------LDGHEVVT--RSPQDGLANGIVYISEDRK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 100 A----LN-EVTEKMGTATPEELEELLEQMAEIQDALEAGGFYLLdMKIEEAARGlgiDAIGLdrdvsaLSGGQRTKVLLA 174
Cdd:PRK10762 338 RdglvLGmSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRL-FNIKTPSME---QAIGL------LSGGNQQKVAIA 407
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 445977555 175 KLLLEQPEVLLLDEPTNYLDV---EHIHWLTNYLKEYPHAFLLISHD 218
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVgakKEIYQLINQFKAEGLSIILVSSE 454
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-190 |
4.46e-10 |
|
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: 59.76 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLgHTF-GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW-------TPgTHY------G 69
Cdd:cd03224 1 LEVENL-NAGyGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrditgLP-PHEraragiG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 70 YLDQHTVLTPGRTIRDVLadaflplfekekalnevteKMGtATPEELEELLEQMAEIQDALEAggfyLLDMkieeaargl 149
Cdd:cd03224 79 YVPEGRRIFPELTVEENL-------------------LLG-AYARRRAKRKARLERVYELFPR----LKER--------- 125
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 445977555 150 gidaigLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPT 190
Cdd:cd03224 126 ------RKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-194 |
4.50e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.80 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLF-----KDVSMRLLAGEHVGLVGANGVGKSTFmniitgqLIHDQGRVEWTPGT-HYGyldqHTVL 77
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerralYDVNVSIPSGSYVAIIGHTGSGKSTL-------LQHLNGLLQPTSGTvTIG----ERVI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 78 TPGRtirdvladaflplfeKEKALNEVTEKMGTAtpeeleellEQMAEIQDALE------AGGFYLLDMKIEEA---ARG 148
Cdd:PRK13634 72 TAGK---------------KNKKLKPLRKKVGIV---------FQFPEHQLFEEtvekdiCFGPMNFGVSEEDAkqkARE 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 445977555 149 LgIDAIGLDRDVSA-----LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PRK13634 128 M-IELVGLPEELLArspfeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
337-494 |
4.72e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.28 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 337 HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTS-LGDFLEP-------AYFEQEVKADNITP--IDD 406
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISiLGQPTRQalqknlvAYVPQSEEVDWSFPvlVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 407 V----------WNTFPGLDQHQI-RAMLAKCGLKnEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAK 475
Cdd:PRK15056 100 VvmmgryghmgWLRRAKKRDRQIvTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180
....*....|....*....|..
gi 445977555 476 AE---LKKAMKAYKGTILLVCH 494
Cdd:PRK15056 179 ARiisLLRELRDEGKTMLVSTH 200
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-200 |
4.90e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.59 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV----EWTPG------THYGYLDQ 73
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIslcgEPVPSrarharQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 74 HTVLTPGRTIRDVLAdaflpLFEKEKALNEVTEKmgtatpeeleelleqmAEIQDALEAGgfylldmKIEEAArglgida 153
Cdd:PRK13537 88 FDNLDPDFTVRENLL-----VFGRYFGLSAAAAR----------------ALVPPLLEFA-------KLENKA------- 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 445977555 154 iglDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD--VEHIHW 200
Cdd:PRK13537 133 ---DAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDpqARHLMW 178
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
343-511 |
5.13e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.52 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPAYFEQEvkadNITPIDD---VWNTFP------- 412
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQK----EIKPVRKkvgVVFQFPesqlfee 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 413 -------------GLDQHQIRAMLAK----CGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAK 475
Cdd:PRK13643 101 tvlkdvafgpqnfGIPKEKAEKIAAEklemVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 445977555 476 AELKKAMKAYK---GTILLVCHEPDFYEDWITKVWDVEE 511
Cdd:PRK13643 181 IEMMQLFESIHqsgQTVVLVTHLMDDVADYADYVYLLEK 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-200 |
5.59e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 61.00 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLG--HTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV----EWTPG------THY 68
Cdd:PRK13536 37 MSTVAIDLAGvsKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvlgVPVPArarlarARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 69 GYLDQHTVLTPGRTIRDVLAdaflpLFEKEKALNevTEKMGTATPEeleelleqmaeiqdaleaggfyLLDM-KIEEAAr 147
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLL-----VFGRYFGMS--TREIEAVIPS----------------------LLEFaRLESKA- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 148 glgidaiglDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD--VEHIHW 200
Cdd:PRK13536 167 ---------DARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDphARHLIW 212
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-247 |
7.07e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 60.23 E-value: 7.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 21 DVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwtpgthygyldqhtvltpgrtirdvLADAFLPLFEKEKA 100
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTIT-------------------------IAGYHITPETGNKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 101 LNEVTEKMGTAtpeeleellEQMAEIQ-------DALEAG--GFYLLDMKIEEAARGLgIDAIGLDRDVSA-----LSGG 166
Cdd:PRK13641 80 LKKLRKKVSLV---------FQFPEAQlfentvlKDVEFGpkNFGFSEDEAKEKALKW-LKKVGLSEDLISkspfeLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 167 QRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYP---HAFLLISHDTEFMNKCVDVIFHLEFTKMTRYTAT 243
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQkagHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASP 229
|
....
gi 445977555 244 YEKF 247
Cdd:PRK13641 230 KEIF 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
338-494 |
7.20e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 60.61 E-value: 7.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 338 PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPAYFEQEVKADNITPIDD----------- 406
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDnldleftvren 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 407 --VWNTFPGLDQHQIRA----MLAKCGLKNEHISRpLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKA---E 477
Cdd:PRK13536 135 llVFGRYFGMSTREIEAvipsLLEFARLESKADAR-VSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHliwE 213
|
170
....*....|....*..
gi 445977555 478 LKKAMKAYKGTILLVCH 494
Cdd:PRK13536 214 RLRSLLARGKTILLTTH 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-196 |
7.50e-10 |
|
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: 59.17 E-value: 7.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 12 TFG---DRTLFKDVSMRLLAGEHVGLVGANGVGKST-------FMNIITGQ-LIHDQGRVEWTPGT---HYGYLDQHTVL 77
Cdd:cd03253 7 TFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTilrllfrFYDVSSGSiLIDGQDIREVTLDSlrrAIGVVPQDTVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 78 ---TPGRTIRdvladaflplFEKEKALNEVTEKMGTAtpeeleelleqmAEIQDALEAGGF-YllDMKIEEaaRGLgida 153
Cdd:cd03253 87 fndTIGYNIR----------YGRPDATDEEVIEAAKA------------AQIHDKIMRFPDgY--DTIVGE--RGL---- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 445977555 154 igldrdvsALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE 196
Cdd:cd03253 137 --------KLSGGEKQRVAIARAILKNPPILLLDEATSALDTH 171
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-199 |
8.44e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 59.34 E-value: 8.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 13 FGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNII-------TGQLIhdqgrvewtpgthygyLDQHTVLTPGRTIRD 85
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLI----------------VDGLKVNDPKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 86 VLADA---F--LPLFEKEKALNEVTekMGtatPEELEELLEQMAEIQdALEaggfyLLDmKIEEAARglgidaigLDRDV 160
Cdd:PRK09493 75 IRQEAgmvFqqFYLFPHLTALENVM--FG---PLRVRGASKEEAEKQ-ARE-----LLA-KVGLAER--------AHHYP 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 445977555 161 SALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIH 199
Cdd:PRK09493 135 SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRH 173
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
344-498 |
8.54e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 8.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 344 SMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSlGDFLEPAY--FEQEVKAdnitpIDDVW---NT---FPGLD 415
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ-SQFSHITRlsFEQLQKL-----VSDEWqrnNTdmlSPGED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 416 ----------QHQIR-----AMLAKcGLKNEH-ISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELK 479
Cdd:PRK10938 97 dtgrttaeiiQDEVKdparcEQLAQ-QFGITAlLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA 175
|
170 180
....*....|....*....|....*.
gi 445977555 480 K---AMKAYKGTILLVCHE----PDF 498
Cdd:PRK10938 176 EllaSLHQSGITLVLVLNRfdeiPDF 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
346-472 |
8.61e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 8.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 346 TIERGEKIAIVGCNGVGKSTLLKTILGKIKPlsgktSLGDFLEPA----------------YFEqEVKADNITP------ 403
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIP-----NLGDYEEEPswdevlkrfrgtelqnYFK-KLYNGEIKVvhkpqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 404 IDDVWNTFPGldqhQIRAMLAK---CGLKNEHIS---------RPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD 471
Cdd:PRK13409 169 VDLIPKVFKG----KVRELLKKvdeRGKLDEVVErlglenildRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
.
gi 445977555 472 V 472
Cdd:PRK13409 245 I 245
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-196 |
8.93e-10 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 58.66 E-value: 8.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTFMN-------------IITGQLIHDQGRVEWTpgTHYGYLDQHTVLTPGrTIRDV 86
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLalfrlvelssgsiLIDGVDISKIGLHDLR--SRISIIPQDPVLFSG-TIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 87 LAdaflPLFEK-EKALNEVTEKMgtatpeeleelleQMAEIQDALEAGgfylLDMKIEEaaRGLGidaigldrdvsaLSG 165
Cdd:cd03244 98 LD----PFGEYsDEELWQALERV-------------GLKEFVESLPGG----LDTVVEE--GGEN------------LSV 142
|
170 180 190
....*....|....*....|....*....|.
gi 445977555 166 GQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE 196
Cdd:cd03244 143 GQRQLLCLARALLRKSKILVLDEATASVDPE 173
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
329-494 |
9.12e-10 |
|
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: 59.17 E-value: 9.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGY--THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD--------------------- 385
Cdd:cd03253 4 ENVTFAYdpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrraigvvpqd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 386 ---FLEPAYF-----------EQEVKADNITPIDDVWNTFP-GLDqhqirAMLAKCGLKnehisrplsqLSGGEQAKVRL 450
Cdd:cd03253 84 tvlFNDTIGYnirygrpdatdEEVIEAAKAAQIHDKIMRFPdGYD-----TIVGERGLK----------LSGGEKQRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 445977555 451 CKLMGEESNWLLFDEPTNHLDVTAKAELKKAM-KAYKG-TILLVCH 494
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALrDVSKGrTTIVIAH 194
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
340-497 |
9.56e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 59.84 E-value: 9.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 340 LPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD------------------------FLEPAYFEQE 395
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkkvslvfqFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 396 VKAD-NITPIddvwNTFPGLDQHQIRAM--LAKCGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDV 472
Cdd:PRK13641 103 VLKDvEFGPK----NFGFSEDEAKEKALkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180
....*....|....*....|....*...
gi 445977555 473 TAKAELKKAMKAYKG---TILLVCHEPD 497
Cdd:PRK13641 179 EGRKEMMQLFKDYQKaghTVILVTHNMD 206
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
343-494 |
1.03e-09 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 58.99 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD-------------------FLEPAYFEqevkadNITP 403
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditglppheiarlgigrtFQIPRLFP------ELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 404 IDDV--------------WNTFPGLDQHQIRAM--LAKCGLKnEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPT 467
Cdd:cd03219 93 LENVmvaaqartgsglllARARREEREARERAEelLERVGLA-DLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190
....*....|....*....|....*....|
gi 445977555 468 ---NHLDVTAKAELKKAMKAYKGTILLVCH 494
Cdd:cd03219 172 aglNPEETEELAELIRELRERGITVLLVEH 201
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-220 |
1.29e-09 |
|
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: 58.63 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTFMNIITG------QLIHDQGRVEWTPGTHYGYLDQHTVLTPGRTIRDVLAdaflp 93
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlaqptsGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 94 lfekeKALNEVTEKMGTAtpeeleellEQMAEIQDALEAGGfylldmkIEEAArglgidaiglDRDVSALSGGQRTKVLL 173
Cdd:TIGR01184 77 -----LAVDRVLPDLSKS---------ERRAIVEEHIALVG-------LTEAA----------DKRPGQLSGGMKQRVAI 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 445977555 174 AKLLLEQPEVLLLDEPTNYLDV----EHIHWLTNYLKEYPHAFLLISHDTE 220
Cdd:TIGR01184 126 ARALSIRPKVLLLDEPFGALDAltrgNLQEELMQIWEEHRVTVLMVTHDVD 176
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-230 |
1.31e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.61 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwtpgthygyldqhtvltpg 80
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIR------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 81 rtIRDVLADAFLPLFEKEKALNEVTEKMGTAtpeeleELLEQMAEIQDALE---AGGFYLLDMKIEEA-ARGLGIDA-IG 155
Cdd:PRK11264 62 --VGDITIDTARSLSQQKGLIRQLRQHVGFV------FQNFNLFPHRTVLEniiEGPVIVKGEPKEEAtARARELLAkVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 156 LDRDVSA----LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNY---LKEYPHAFLLISHDTEFMNKCVD- 227
Cdd:PRK11264 134 LAGKETSyprrLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTirqLAQEKRTMVIVTHEMSFARDVADr 213
|
...
gi 445977555 228 VIF 230
Cdd:PRK11264 214 AIF 216
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-229 |
1.40e-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: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 29 GEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPgthygylDQHTVLTPGRTIRdvLADAFLPLFEKE-KALneVTEK 107
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPP-------DWDEILDEFRGSE--LQNYFTKLLEGDvKVI--VKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 108 MGTATPEELEELLEQMAEIQDALEaggfylldmKIEEAARGLGIDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLD 187
Cdd:cd03236 95 YVDLIPKAVKGKVGELLKKKDERG---------KLDELVDQLELRHV-LDRNIDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 445977555 188 EPTNYLDVEH---IHWLTNYLKEYPHAFLLISHDTEFMNKCVDVI 229
Cdd:cd03236 165 EPSSYLDIKQrlnAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-218 |
1.40e-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: 60.47 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTfmniiTGQ----LIHDQGRVEWTpGTHYGYLDQHTvLTPGRtiRD---VLADAFl 92
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKST-----LGLallrLIPSEGEIRFD-GQDLDGLSRRA-LRPLR--RRmqvVFQDPF- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 93 plfekeKALNE-------VTEKMGTATPEELEELLEQMaeIQDALEAggfylldmkieeaargLGIDAIGLDRDVSALSG 165
Cdd:COG4172 373 ------GSLSPrmtvgqiIAEGLRVHGPGLSAAERRAR--VAEALEE----------------VGLDPAARHRYPHEFSG 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 445977555 166 GQRTKVLLAKLLLEQPEVLLLDEPTNYLDV----EHIHWLTNYLKEYPHAFLLISHD 218
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDVsvqaQILDLLRDLQREHGLAYLFISHD 485
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-61 |
1.46e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.55 E-value: 1.46e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 445977555 19 FKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVE 61
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-194 |
1.49e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.44 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 28 AGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVeWTPGthygylDQHTVLTPGRtiRDVLAdaflpLFEKEKALNEVT-- 105
Cdd:PRK10771 24 RGERVAILGPSGAGKSTLLNLIAGFLTPASGSL-TLNG------QDHTTTPPSR--RPVSM-----LFQENNLFSHLTva 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 106 EKMGTATPEELEELLEQMAEIQDAleaggfylldmkieeaARGLGIDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLL 185
Cdd:PRK10771 90 QNIGLGLNPGLKLNAAQREKLHAI----------------ARQMGIEDL-LARLPGQLSGGQRQRVALARCLVREQPILL 152
|
....*....
gi 445977555 186 LDEPTNYLD 194
Cdd:PRK10771 153 LDEPFSALD 161
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-194 |
1.54e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.05 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 16 RTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLihdqgrvewtpgthygyldqhtVLTPGRTIRDVLADAFlplf 95
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL----------------------KGTPVAGCVDVPDNQF---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 96 EKEKALNEvtekmgtatpeeleelleQMAEIQDALEAggFYLLdmkieeAARGLGiDAIGLDRDVSALSGGQRTKVLLAK 175
Cdd:COG2401 97 GREASLID------------------AIGRKGDFKDA--VELL------NAVGLS-DAVLWLRRFKELSTGQKFRFRLAL 149
|
170
....*....|....*....
gi 445977555 176 LLLEQPEVLLLDEPTNYLD 194
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLD 168
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-478 |
1.68e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.06 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVE--------WTPG-TH-YG-YL 71
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEiggnpcarLTPAkAHqLGiYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 72 -DQHTVLTPGRTIRDVLAdafLPLFEKEKALNEVTEKmgtatpeeleelleqMAEIQDALE----AGGFYLLDMKIEEAA 146
Cdd:PRK15439 91 vPQEPLLFPNLSVKENIL---FGLPKRQASMQKMKQL---------------LAALGCQLDldssAGSLEVADRQIVEIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 147 RGLGIDAigldrdvsalsggqrtkvllakllleqpEVLLLDEPTNYL---DVEHIHWLTNYLKEYPHAFLLISHDTEFMN 223
Cdd:PRK15439 153 RGLMRDS----------------------------RILILDEPTASLtpaETERLFSRIRELLAQGVGIVFISHKLPEIR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 224 KCVDVIfhlefTKMTR-YTATYEKfleLAEINKNQHINAYEKQrefikkqedfiAKNKarysttGRAKSRQKQLD----- 297
Cdd:PRK15439 205 QLADRI-----SVMRDgTIALSGK---TADLSTDDIIQAITPA-----------AREK------SLSASQKLWLElpgnr 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 298 RMELIDRPETAIKPefsfkesrassrfvFEGEnveiGYTHpllpkLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPL 377
Cdd:PRK15439 260 RQQAAGAPVLTVED--------------LTGE----GFRN-----ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPAR 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 378 SGKTSLGdflepayfEQEVKADNIT----------PIDD-----------VWNTFpGLDQHQI---------RAML---- 423
Cdd:PRK15439 317 GGRIMLN--------GKEINALSTAqrlarglvylPEDRqssglyldaplAWNVC-ALTHNRRgfwikpareNAVLeryr 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 424 AKCGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAEL 478
Cdd:PRK15439 388 RALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDI 442
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
350-509 |
1.76e-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: 58.53 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 350 GEKIAIVGCNGVGKSTLLKTILGKIKPlsgktSLGDFLEPA----------------YFEQeVKADNITPI------DDV 407
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKP-----NLGKFDDPPdwdeildefrgselqnYFTK-LLEGDVKVIvkpqyvDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 408 WNTFPG-----LDQHQIRAMLAKC--GLKNEHI-SRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAK---A 476
Cdd:cd03236 100 PKAVKGkvgelLKKKDERGKLDELvdQLELRHVlDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRlnaA 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 445977555 477 ELKKAMKAYKGTILLVCHE---PDFYEDWITKVWDV 509
Cdd:cd03236 180 RLIRELAEDDNYVLVVEHDlavLDYLSDYIHCLYGE 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
327-494 |
1.76e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.05 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 327 EGENVEIGY-THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDflEPA-----YFEQEV---- 396
Cdd:PRK13537 9 DFRNVEKRYgDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG--EPVpsrarHARQRVgvvp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 397 KADNITP----IDD--VWNTFPGLDQHQIRAMLAK----CGLKNEhISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEP 466
Cdd:PRK13537 87 QFDNLDPdftvRENllVFGRYFGLSAAAARALVPPllefAKLENK-ADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190
....*....|....*....|....*....|.
gi 445977555 467 TNHLDVTAKA---ELKKAMKAYKGTILLVCH 494
Cdd:PRK13537 166 TTGLDPQARHlmwERLRSLLARGKTILLTTH 196
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-218 |
1.78e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.41 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSM--RLL-------AGEHVGLVGANGVGKSTFMNIITGQL-----IHDQGRV--EWTPGT---HYGYLDQHTVLTPG 80
Cdd:PRK03695 4 NDVAVstRLGplsaevrAGEILHLVGPNGAGKSTLLARMAGLLpgsgsIQFAGQPleAWSAAElarHRAYLSQQQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 81 RTIRDVLA---DAFLPLFEKEKALNEVTEKMGtatpeeleelleqmaeiqdaleaggfylLDMKieeaarglgidaigLD 157
Cdd:PRK03695 84 MPVFQYLTlhqPDKTRTEAVASALNEVAEALG----------------------------LDDK--------------LG 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445977555 158 RDVSALSGGQRTKVLLAKLLLE-----QPE--VLLLDEPTNYLDVEHIHWLTNYLKEYPH---AFLLISHD 218
Cdd:PRK03695 122 RSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSLDVAQQAALDRLLSELCQqgiAVVMSSHD 192
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-217 |
1.87e-09 |
|
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: 56.78 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLG-HTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGTHYGYLDQHTVLTPGrT 82
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLG-T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 IRDVLAdaflplfekekalnevtekmgtatpeeleelleqmaeiqdaleaggfYLLDMkieeaarglgidaigldrdvsA 162
Cdd:cd03223 80 LREQLI-----------------------------------------------YPWDD---------------------V 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 163 LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAFLLISH 217
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH 146
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
338-495 |
2.10e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.17 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 338 PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSL-GDFLEPAYFEQEV--KADNITPIDDVW-NTFPG 413
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdGKPVEGPGAERGVvfQNEGLLPWRNVQdNVAFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 414 LD---------QHQIRAMLAKCGLKNEHiSRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKK-AMK 483
Cdd:PRK11248 95 LQlagvekmqrLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTlLLK 173
|
170
....*....|....*
gi 445977555 484 AYKGT---ILLVCHE 495
Cdd:PRK11248 174 LWQETgkqVLLITHD 188
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-194 |
2.14e-09 |
|
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: 58.08 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 14 GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV--------EWTP---GTHYGYLDQHTVLTPGRT 82
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedirEQDPvelRRKIGYVIQQIGLFPHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 IRDVLAdaFLPLFEKEKAlnevtekmgtatpeeleelleqmAEIQDaleaggfylldmKIEEAARGLGIDAIGL-DRDVS 161
Cdd:cd03295 92 VEENIA--LVPKLLKWPK-----------------------EKIRE------------RADELLALVGLDPAEFaDRYPH 134
|
170 180 190
....*....|....*....|....*....|...
gi 445977555 162 ALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:cd03295 135 ELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
340-497 |
2.23e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 58.71 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 340 LPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD--------------------FLEP--AYFEQEVK 397
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysrkglmklresvgmvFQDPdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 398 AD------NIT-PIDDVwntfpgldQHQIRAMLAKCGLknEHI-SRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNH 469
Cdd:PRK13636 102 QDvsfgavNLKlPEDEV--------RKRVDNALKRTGI--EHLkDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190
....*....|....*....|....*....|..
gi 445977555 470 LDVTAKAE----LKKAMKAYKGTILLVCHEPD 497
Cdd:PRK13636 172 LDPMGVSEimklLVEMQKELGLTIIIATHDID 203
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-190 |
2.24e-09 |
|
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: 57.68 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLgHTF-GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWtpgthygylDqhtvltp 79
Cdd:COG0410 1 MPMLEVENL-HAGyGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRF---------D------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 80 GRTIRDVLAD-------AFLP----LFekeKALNeVTE--KMGTATPEELEELLEQMAEIqdaleaggfylLDM--KIEE 144
Cdd:COG0410 64 GEDITGLPPHriarlgiGYVPegrrIF---PSLT-VEEnlLLGAYARRDRAEVRADLERV-----------YELfpRLKE 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 445977555 145 aaRglgidaigLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPT 190
Cdd:COG0410 129 --R--------RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
299-502 |
2.24e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.86 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 299 MELIDRPETAikPEFSFKESRASSRFVFEGENVEIgYTH---PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILG--- 372
Cdd:PRK11174 325 VTFLETPLAH--PQQGEKELASNDPVTIEAEDLEI-LSPdgkTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflp 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 373 -----KI--KPLSgKTSLGDFL--------EPAYFEQEVKaDNITPIDdvwntfPGLDQHQIRAMLAKCGLkNEHISRpL 437
Cdd:PRK11174 402 yqgslKIngIELR-ELDPESWRkhlswvgqNPQLPHGTLR-DNVLLGN------PDASDEQLQQALENAWV-SEFLPL-L 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 438 SQ------------LSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDvtAKAE------LKKAMKAYkgTILLVCHEPDFY 499
Cdd:PRK11174 472 PQgldtpigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLD--AHSEqlvmqaLNAASRRQ--TTLMVTHQLEDL 547
|
...
gi 445977555 500 EDW 502
Cdd:PRK11174 548 AQW 550
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-229 |
2.32e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.30 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIhdqgrvewTPGTHYGYLDQHTVLTPGRT 82
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLT--------GGGAPRGARVTGDVTLNGEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 I-----------RDVLADAFLPLFEKekALNEVTekmgtatpeeleelleQMAEIQDALEAGGFYLLDMKIEEAARGLGi 151
Cdd:PRK13547 73 LaaidaprlarlRAVLPQAAQPAFAF--SAREIV----------------LLGRYPHARRAGALTHRDGEIAWQALALA- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 152 DAIGLD-RDVSALSGGQRTKVLLAKLLLE---------QPEVLLLDEPTNYLDVEHIHWLTNYL----KEYPHAFLLISH 217
Cdd:PRK13547 134 GATALVgRDVTTLSGGELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVrrlaRDWNLGVLAIVH 213
|
250
....*....|..
gi 445977555 218 DTEFMNKCVDVI 229
Cdd:PRK13547 214 DPNLAARHADRI 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
21-223 |
2.52e-09 |
|
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: 57.42 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 21 DVSMRLLAGEHVGLVGANGVGKSTFMNII-------TGQLIHDQGRVEWTPGTHYGYLDQH--TVLTPGRTI--RDVLAD 89
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIykeelptSGTIRVNGQDVSDLRGRAIPYLRRKigVVFQDFRLLpdRNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 90 AFLPLfekekalnEVTEKMGTATPEeleelleqmaEIQDALEAGGfylLDMKIEEAARGlgidaigldrdvsaLSGGQRT 169
Cdd:cd03292 99 VAFAL--------EVTGVPPREIRK----------RVPAALELVG---LSHKHRALPAE--------------LSGGEQQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 445977555 170 KVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHA---FLLISHDTEFMN 223
Cdd:cd03292 144 RVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAgttVVVATHAKELVD 200
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
340-497 |
2.52e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 59.74 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 340 LPKLSMTIERGEKIAIVGCNGVGKSTLLkTILGKI-KPLSGK---------TSLGDFLepAYFEQE-------------- 395
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLM-NILGCLdKPTSGTyrvagqdvaTLDADAL--AQLRREhfgfifqryhllsh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 396 -VKADNItpidDVWNTFPGLDQHQ----IRAMLAKCGLkNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHL 470
Cdd:PRK10535 101 lTAAQNV----EVPAVYAGLERKQrllrAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190
....*....|....*....|....*....|
gi 445977555 471 DVTAKAELKKAMKAYKG---TILLVCHEPD 497
Cdd:PRK10535 176 DSHSGEEVMAILHQLRDrghTVIIVTHDPQ 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
343-492 |
2.59e-09 |
|
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: 56.67 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDflepayfeqevKADNITPIDDVwntfpgldqhqIRAM 422
Cdd:cd03215 19 VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG-----------KPVTRRSPRDA-----------IRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 423 LA-------KCGLK-----NEHISRPlSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAYK---G 487
Cdd:cd03215 77 IAyvpedrkREGLVldlsvAENIALS-SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdagK 155
|
....*
gi 445977555 488 TILLV 492
Cdd:cd03215 156 AVLLI 160
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
347-495 |
2.81e-09 |
|
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: 56.43 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 347 IERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLgDFLEPAYFEQEVKadnitpiddvwntfpgldqhqiramlakc 426
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVYKPQYID----------------------------- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445977555 427 glknehisrplsqLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAY----KGTILLVCHE 495
Cdd:cd03222 72 -------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHD 131
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
340-506 |
3.36e-09 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 57.16 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 340 LPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGK-TSLGD---FLEPAY-FEQEVKA-DNITPIDDVWntfpG 413
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTvTVRGRvssLLGLGGgFNPELTGrENIYLNGRLL----G 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 414 LDQHQIRAMLAK----CGLKnEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAYK--- 486
Cdd:cd03220 114 LSRKEIDEKIDEiiefSELG-DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLkqg 192
|
170 180
....*....|....*....|
gi 445977555 487 GTILLVCHEPDFYEDWITKV 506
Cdd:cd03220 193 KTVILVSHDPSSIKRLCDRA 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
335-495 |
3.65e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.87 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 335 YTHPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD------------------------FLEPA 390
Cdd:PRK13646 18 YEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkrigmvfqFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 391 YFEQEVKADNI-------TPIDDVWNtfpglDQHQiraMLAKCGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLF 463
Cdd:PRK13646 98 LFEDTVEREIIfgpknfkMNLDEVKN-----YAHR---LLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 445977555 464 DEPTNHLDVTAKAELKKAMKAYK----GTILLVCHE 495
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHD 205
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
337-498 |
4.15e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 57.29 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 337 HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSlgdflepayfeqeVKADNITPIDDVWNTFPGLDQ 416
Cdd:PRK10619 18 HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIV-------------VNGQTINLVRDKDGQLKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 417 HQIRAM---------------------------------------------LAKCGLKNEHISRPLSQLSGGEQAKVRLC 451
Cdd:PRK10619 85 NQLRLLrtrltmvfqhfnlwshmtvlenvmeapiqvlglskqeareravkyLAKVGIDERAQGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 445977555 452 KLMGEESNWLLFDEPTNHLDVTAKAELKKAMK--AYKG-TILLVCHEPDF 498
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQqlAEEGkTMVVVTHEMGF 214
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
337-496 |
4.15e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.05 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 337 HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTI--L-----GKIKPLSGKTSLgdFLeP--AYFEQEVKADNIT---PI 404
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIagLwpygsGRIARPAGARVL--FL-PqrPYLPLGTLREALLypaTA 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 405 DDVwntfpglDQHQIRAMLAKCGLknEHI------SRPLSQ-LSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAE 477
Cdd:COG4178 453 EAF-------SDAELREALEAVGL--GHLaerldeEADWDQvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAA 523
|
170 180
....*....|....*....|.
gi 445977555 478 LKKAMKA--YKGTILLVCHEP 496
Cdd:COG4178 524 LYQLLREelPGTTVISVGHRS 544
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-220 |
4.35e-09 |
|
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: 56.82 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDR----TLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVeWTPGT------------ 66
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSV-LVDGTdltllsgkelrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 67 ---HYGYLDQHTVLTPGRTIRDVLAdafLPLfekekalnevtekmgtatpeeleelleQMAEIQDAleaggfylldmKIE 143
Cdd:cd03258 80 arrRIGMIFQHFNLLSSRTVFENVA---LPL---------------------------EIAGVPKA-----------EIE 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 144 EAARGLgIDAIGL----DRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAF----LLI 215
Cdd:cd03258 119 ERVLEL-LELVGLedkaDAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELgltiVLI 197
|
....*
gi 445977555 216 SHDTE 220
Cdd:cd03258 198 THEME 202
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
340-497 |
4.67e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.51 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 340 LPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSL-GDFLEPAYFEQEVKADNI---TPIDDVWNTFP--- 412
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIREVRKFVGLvfqNPDDQIFSPTVeqd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 413 --------GLDQ----HQIRAMLAKCGLKnEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKK 480
Cdd:PRK13652 100 iafgpinlGLDEetvaHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELID 178
|
170 180
....*....|....*....|.
gi 445977555 481 AMKA----YKGTILLVCHEPD 497
Cdd:PRK13652 179 FLNDlpetYGMTVIFSTHQLD 199
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
339-498 |
4.71e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 56.38 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 339 LLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILG--KIKPLSGKTSLgdflepayfeqevKADNIT--PIDDvwntfpgl 414
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILF-------------KGEDITdlPPEE-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 415 dqhqiRAML----------AKCGLKNEHISRPLSQ-LSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMK 483
Cdd:cd03217 74 -----RARLgiflafqyppEIPGVKNADFLRYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVIN 148
|
170 180
....*....|....*....|....*.
gi 445977555 484 AYKG---TILLVCH--------EPDF 498
Cdd:cd03217 149 KLREegkSVLIITHyqrlldyiKPDR 174
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
328-478 |
5.04e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 57.30 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 328 GENVEIGYTHPLLPK-LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPAYFEQEVK------ADN 400
Cdd:PRK10253 10 GEQLTLGYGKYTVAEnLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVArrigllAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 401 ITPIDDV----------------WNTFPGLDQHQIRAMLAKCGLkNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFD 464
Cdd:PRK10253 90 ATTPGDItvqelvargryphqplFTRWRKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170
....*....|....
gi 445977555 465 EPTNHLDVTAKAEL 478
Cdd:PRK10253 169 EPTTWLDISHQIDL 182
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-194 |
5.06e-09 |
|
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: 55.78 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 15 DRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLDQHTVLTPGRTIRDvladaflpl 94
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGVPVSDLEKALSS--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 95 fekekalnevtekmgtatpeeleelleQMAEIQDALeaggfYLLDMKIEEaarGLGIdaigldrdvsALSGGQRTKVLLA 174
Cdd:cd03247 76 ---------------------------LISVLNQRP-----YLFDTTLRN---NLGR----------RFSGGERQRLALA 110
|
170 180
....*....|....*....|
gi 445977555 175 KLLLEQPEVLLLDEPTNYLD 194
Cdd:cd03247 111 RILLQDAPIVLLDEPTVGLD 130
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
343-380 |
5.82e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 56.63 E-value: 5.82e-09
10 20 30
....*....|....*....|....*....|....*...
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGK 380
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-218 |
6.38e-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: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTFGD----RTLFKDVSMRLLAGEHVGLVGANGVGKS-TFMNII---TGQLIHDQGRVEwtpgthygYLD 72
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllPDPAAHPSGSIL--------FDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 73 QHTVLTPGRTIRDVLAD-----------AFLPLFEKEKALNEVTEKMGTATPeeleelleqmAEIQD-ALEaggfyLLDM 140
Cdd:COG4172 76 QDLLGLSERELRRIRGNriamifqepmtSLNPLHTIGKQIAEVLRLHRGLSG----------AAARArALE-----LLER 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 141 -KIEEAARGLGidaigldrdvsA----LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV---EHIHWLTNYLK-EYPHA 211
Cdd:COG4172 141 vGIPDPERRLD-----------AyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVtvqAQILDLLKDLQrELGMA 209
|
....*..
gi 445977555 212 FLLISHD 218
Cdd:COG4172 210 LLLITHD 216
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
329-494 |
6.94e-09 |
|
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: 55.96 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGY---THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFL------------------ 387
Cdd:cd03244 6 KNVSLRYrpnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskiglhdlrsrisiipq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 388 EPAYFEQEVKaDNITPiddvwntfpgLDQH---QIRAMLAKCGLKNEHISRPL----------SQLSGGEQAKVRLCKLM 454
Cdd:cd03244 86 DPVLFSGTIR-SNLDP----------FGEYsdeELWQALERVGLKEFVESLPGgldtvveeggENLSVGQRQLLCLARAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 445977555 455 GEESNWLLFDEPTNHLDVTAKAELKKA-MKAYKG-TILLVCH 494
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTiREAFKDcTVLTIAH 196
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
343-494 |
7.38e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.40 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFlEPayFEQEVK-ADNIT--------------PIDdv 407
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY-VP--FKRRKEfARRIGvvfgqrsqlwwdlpAID-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 408 wnTFP------GLDQHQIRAMLAKC----GLKnEHISRPLSQLSGGEQAKVRLC-------KLmgeesnwLLFDEPTNHL 470
Cdd:COG4586 116 --SFRllkaiyRIPDAEYKKRLDELvellDLG-ELLDTPVRQLSLGQRMRCELAaallhrpKI-------LFLDEPTIGL 185
|
170 180
....*....|....*....|....*...
gi 445977555 471 DVTAKAELKKAMKAY----KGTILLVCH 494
Cdd:COG4586 186 DVVSKEAIREFLKEYnrerGTTILLTSH 213
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
296-494 |
7.72e-09 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 58.25 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 296 LDRM-ELIDRPETAIKPEFSFKESRASSRFVFEgeNVEIGY--THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILG 372
Cdd:COG1132 311 AERIfELLDEPPEIPDPPGAVPLPPVRGEIEFE--NVSFSYpgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 373 KIKPLSGK-------------TSLGDFLepAYFEQEVK------ADNItpiddvwnTF--PGLDQHQIRAMLAKCGLKnE 431
Cdd:COG1132 389 FYDPTSGRilidgvdirdltlESLRRQI--GVVPQDTFlfsgtiRENI--------RYgrPDATDEEVEEAAKAAQAH-E 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 432 HISRpLSQ------------LSGGE------------QAKVrlcklmgeesnwLLFDEPTNHLDVTAKAELKKAMKAY-K 486
Cdd:COG1132 458 FIEA-LPDgydtvvgergvnLSGGQrqriaiarallkDPPI------------LILDEATSALDTETEALIQEALERLmK 524
|
....*....
gi 445977555 487 G-TILLVCH 494
Cdd:COG1132 525 GrTTIVIAH 533
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-496 |
7.77e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.59 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 339 LLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSL-GDFLepaYFEQEV-KADNITPIDDVW------NT 410
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdGKVL---YFGKDIfQIDAIKLRKEVGmvfqqpNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 411 FPGL----------------DQHQIRAMLAKC----GLKNE---HISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPT 467
Cdd:PRK14246 102 FPHLsiydniayplkshgikEKREIKKIVEEClrkvGLWKEvydRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190
....*....|....*....|....*....|.
gi 445977555 468 NHLDVTAKAELKKAMKAYKG--TILLVCHEP 496
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNeiAIVIVSHNP 212
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
338-508 |
8.12e-09 |
|
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: 55.80 E-value: 8.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 338 PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPAYFEQEVKADNITPI----DDVW----- 408
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVayaaQKPWllnat 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 409 ----NTFPG-LDQHQIRAMLAKCGLKNE----------HISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVT 473
Cdd:cd03290 95 veenITFGSpFNKQRYKAVTDACSLQPDidllpfgdqtEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 445977555 474 AKAELKKA-----MKAYKGTILLVCHEPDF--YEDWITKVWD 508
Cdd:cd03290 175 LSDHLMQEgilkfLQDDKRTLVLVTHKLQYlpHADWIIAMKD 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
338-480 |
8.17e-09 |
|
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: 56.19 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 338 PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD----------------FLEPAYFEQEVKADNI 401
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqernvgfvFQHYALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 402 TPIDDVWNTFPGLDQHQIRA----MLAKCGLKNEHISRPlSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAE 477
Cdd:cd03296 96 AFGLRVKPRSERPPEAEIRAkvheLLKLVQLDWLADRYP-AQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKE 174
|
...
gi 445977555 478 LKK 480
Cdd:cd03296 175 LRR 177
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-217 |
9.21e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 55.23 E-value: 9.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGqlihdqgrvewtpgtHYGYLdqhtvLTPGRTi 83
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG---------------HPKYE-----VTEGEI- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 84 rdvladaflpLFEKEKalnevtekmgtatpeeleelleqmaeiqdaleaggfyLLDMKIEEAAR-GL-----------GI 151
Cdd:cd03217 60 ----------LFKGED-------------------------------------ITDLPPEERARlGIflafqyppeipGV 92
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 152 DAIGLDRDVSA-LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLT---NYLKEYPHAFLLISH 217
Cdd:cd03217 93 KNADFLRYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAeviNKLREEGKSVLIITH 162
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-220 |
9.71e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGhtfGDRtlFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLDQHTVltPGRT 82
Cdd:PRK15439 268 VLTVEDLT---GEG--FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI---------MLNGKEI--NALS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 IRDVLADA--FLP-------LF-EKEKALNEVTEKMGTatpeeleelleQMAEIQDALEAGGFylldmkiEEAARGLGID 152
Cdd:PRK15439 332 TAQRLARGlvYLPedrqssgLYlDAPLAWNVCALTHNR-----------RGFWIKPARENAVL-------ERYRRALNIK 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445977555 153 AIGLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV---EHIHWLTNYLKEYPHAFLLISHDTE 220
Cdd:PRK15439 394 FNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVsarNDIYQLIRSIAAQNVAVLFISSDLE 464
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
16-194 |
1.06e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 57.75 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 16 RTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLihdqgrvewTPGTHYgyldQHTVLTPGRTI-----RDVLA-- 88
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRS---------PKGVKG----SGSVLLNGMPIdakemRAISAyv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 89 ---DAFLPLFEKEKALNEVTE-KMGTATPEELeelleQMAEIQDALEaggfyllDMKIEEAARGLgidaIGLDRDVSALS 164
Cdd:TIGR00955 105 qqdDLFIPTLTVREHLMFQAHlRMPRRVTKKE-----KRERVDEVLQ-------ALGLRKCANTR----IGVPGRVKGLS 168
|
170 180 190
....*....|....*....|....*....|
gi 445977555 165 GGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:TIGR00955 169 GGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-233 |
1.18e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 56.28 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHT------FGDRTLFkDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwtpgthygyldqhtv 76
Cdd:PRK13643 1 MIKFEKVNYTyqpnspFASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVT--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 77 ltpgrtirdvLADAFLPLFEKEKALNEVTEKMGTATPEELEELLEQMAEIQDALEAGGFYLLDMKIEEAArGLGIDAIGL 156
Cdd:PRK13643 65 ----------VGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIA-AEKLEMVGL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 157 DRDV-----SALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE---HIHWLTNYLKEYPHAFLLISHDTEFMNKCVDV 228
Cdd:PRK13643 134 ADEFwekspFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKariEMMQLFESIHQSGQTVVLVTHLMDDVADYADY 213
|
....*
gi 445977555 229 IFHLE 233
Cdd:PRK13643 214 VYLLE 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
343-497 |
1.40e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.40 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPAYFEQEVKADNITP------------IDDVWNt 410
Cdd:PRK13631 45 ISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSkkiknfkelrrrVSMVFQ- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 411 FP------------------GLDQHQIRA------MLAKCGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEP 466
Cdd:PRK13631 124 FPeyqlfkdtiekdimfgpvALGVKKSEAkklakfYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEP 203
|
170 180 190
....*....|....*....|....*....|....
gi 445977555 467 TNHLDVTAKAE---LKKAMKAYKGTILLVCHEPD 497
Cdd:PRK13631 204 TAGLDPKGEHEmmqLILDAKANNKTVFVITHTME 237
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
300-494 |
1.88e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 57.04 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 300 ELIDRpetaiKPEFSFKESRASSRF--VFEGENVEIGY-THPLLP---KLSMTIERGEKIAIVGCNGVGKSTLLKTILGK 373
Cdd:TIGR00958 456 EYLDR-----KPNIPLTGTLAPLNLegLIEFQDVSFSYpNRPDVPvlkGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 374 IKPLSGKTSLGD---------FL---------EPAYFEQEVKaDNITpiddvwntfPGLDQ---HQIRAMLAKCGLK--- 429
Cdd:TIGR00958 531 YQPTGGQVLLDGvplvqydhhYLhrqvalvgqEPVLFSGSVR-ENIA---------YGLTDtpdEEIMAAAKAANAHdfi 600
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445977555 430 -------NEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAYKGTILLVCH 494
Cdd:TIGR00958 601 mefpngyDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
340-497 |
1.97e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.78 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 340 LPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLEPAYFEQ--EVKaDNITPIDDVWNtFP----- 412
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVK-RLRKEIGLVFQ-FPeyqlf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 413 ---------------GLDQHQ----IRAMLAKCGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVT 473
Cdd:PRK13645 105 qetiekdiafgpvnlGENKQEaykkVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180
....*....|....*....|....*...
gi 445977555 474 AKAE----LKKAMKAYKGTILLVCHEPD 497
Cdd:PRK13645 185 GEEDfinlFERLNKEYKKRIIMVTHNMD 212
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-190 |
1.99e-08 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 54.84 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW--TPGTHY----------GYL 71
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLdgEDITKLppheraragiAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 72 DQhtvltpGRTIrdvladafLPLFEKEKALnevteKMG-TATPEELeelleqmAEIQDALEAGGFYLLDMkieeaarglg 150
Cdd:TIGR03410 81 PQ------GREI--------FPRLTVEENL-----LTGlAALPRRS-------RKIPDEIYELFPVLKEM---------- 124
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 445977555 151 idaigLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPT 190
Cdd:TIGR03410 125 -----LGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-196 |
2.04e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 56.76 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTL--FKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV--------EWTPGThygyLD 72
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIllngqpiaDYSEAA----LR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 73 QHTVLTPGR------TIRDVLADAfLPLFEKEKaLNEVTEKMGtatpeeleelleqmaeIQDALEAG-GfylLDMKIEEA 145
Cdd:PRK11160 414 QAISVVSQRvhlfsaTLRDNLLLA-APNASDEA-LIEVLQQVG----------------LEKLLEDDkG---LNAWLGEG 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 445977555 146 ARglgidaigldrdvsALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE 196
Cdd:PRK11160 473 GR--------------QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAE 509
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
339-496 |
2.11e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.79 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 339 LLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSL-GDFLEPAYFEQ--EVKADNITPIDDVWNTFPGLD 415
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvGQPLHQMDEEAraKLRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 416 -------------------QHQIRAMLAKCGLKNEHISRPlSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAK- 475
Cdd:PRK10584 105 alenvelpallrgessrqsRNGAKALLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGd 183
|
170 180
....*....|....*....|....
gi 445977555 476 --AELKKAM-KAYKGTILLVCHEP 496
Cdd:PRK10584 184 kiADLLFSLnREHGTTLILVTHDL 207
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
340-506 |
2.12e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.51 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 340 LPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLgdflepayFEQEVKADNITPI-----------DD-- 406
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKV--------MGREVNAENEKWVrskvglvfqdpDDqv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 407 ----VWN--TF-P---GLDQHQI----RAMLAKCGLKnEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDV 472
Cdd:PRK13647 93 fsstVWDdvAFgPvnmGLDKDEVerrvEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 445977555 473 TAKAELKKAMKAYKG---TILLVCHEPDFYEDWITKV 506
Cdd:PRK13647 172 RGQETLMEILDRLHNqgkTVIVATHDVDLAAEWADQV 208
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
344-483 |
2.26e-08 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 54.97 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 344 SMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDF-------------------LEPAYFEQEVKADNITPi 404
Cdd:TIGR04406 21 SLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQdithlpmherarlgigylpQEASIFRKLTVEENIMA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 405 ddVWNTFPGLDQHQIRAMLAKCgLKNEHISRPLSQ----LSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKK 480
Cdd:TIGR04406 100 --VLEIRKDLDRAEREERLEAL-LEEFQISHLRDNkamsLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVGDIKK 176
|
...
gi 445977555 481 AMK 483
Cdd:TIGR04406 177 IIK 179
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
337-478 |
2.33e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.42 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 337 HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDflEP------AYFEQ--------EVKADnIT 402
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG--EPirrqrdEYHQDllylghqpGIKTE-LT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 403 PIDDV-WNT--FPGLDQHQIRAMLAKCGLKN-EHIsrPLSQLSGGEQAKVRLCKL-MGEESNWLLfDEPTNHLDVTAKAE 477
Cdd:PRK13538 91 ALENLrFYQrlHGPGDDEALWEALAQVGLAGfEDV--PVRQLSAGQQRRVALARLwLTRAPLWIL-DEPFTAIDKQGVAR 167
|
.
gi 445977555 478 L 478
Cdd:PRK13538 168 L 168
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
10-194 |
2.49e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.14 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 10 GHTFGDRTLFkDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygyldqhtvltpgrtirdVLAD 89
Cdd:PRK13649 15 GTPFEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSV-------------------------RVDD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 90 AFLPLFEKEKALNEVTEKMGTAtpeeleellEQMAEIQDALE------AGGFYLLDMKIEEA---ARG----LGIDAIGL 156
Cdd:PRK13649 69 TLITSTSKNKDIKQIRKKVGLV---------FQFPESQLFEEtvlkdvAFGPQNFGVSQEEAealAREklalVGISESLF 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 445977555 157 DRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PRK13649 140 EKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-217 |
2.56e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 54.69 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGE-HVgLVGANGVGKSTFMNIITGqliHD-----QGRV--------EWTP----- 64
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEvHA-IMGPNGSGKSTLAKVLMG---HPkyevtSGSIlldgedilELSPderar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 65 -GTHYGYldQHTVLTPGRTIRDvladaFLPLfekekALNEVTEkmgtatpeeleelleqmaEIQDALEaggfylLDMKIE 143
Cdd:COG0396 77 aGIFLAF--QYPVEIPGVSVSN-----FLRT-----ALNARRG------------------EELSARE------FLKLLK 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 144 EAARGLGIDAIGLDRDVSA-LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEY--PH-AFLLISH 217
Cdd:COG0396 121 EKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLrsPDrGILIITH 198
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
343-496 |
2.59e-08 |
|
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: 54.75 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGktslgdflepayfeqEVKAD--NITPIDD-------------V 407
Cdd:COG4181 31 ISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSG---------------TVRLAgqDLFALDEdararlrarhvgfV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 408 WNTF---PGL-----------------DQHQIRAMLAKCGLKN--EHisRPlSQLSGGEQAKVRLCK-LMGEESnwLLF- 463
Cdd:COG4181 96 FQSFqllPTLtalenvmlplelagrrdARARARALLERVGLGHrlDH--YP-AQLSGGEQQRVALARaFATEPA--ILFa 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 445977555 464 DEPTNHLD-VTAKA--ELKKAMKAYKGTIL-LVCHEP 496
Cdd:COG4181 171 DEPTGNLDaATGEQiiDLLFELNRERGTTLvLVTHDP 207
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
329-494 |
2.61e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 55.38 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGYTH--PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSL-----GDFL-------------- 387
Cdd:PRK13644 5 ENVSYSYPDgtPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidtGDFSklqgirklvgivfq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 388 --EPAYFEQEVKADNITPIDDVwnTFPGLD-QHQIRAMLAKCGLKNEHISRPLSqLSGGEQAKVRLCKLMGEESNWLLFD 464
Cdd:PRK13644 85 npETQFVGRTVEEDLAFGPENL--CLPPIEiRKRVDRALAEIGLEKYRHRSPKT-LSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190
....*....|....*....|....*....|...
gi 445977555 465 EPTNHLDV-TAKAELKKAMKAY-KG-TILLVCH 494
Cdd:PRK13644 162 EVTSMLDPdSGIAVLERIKKLHeKGkTIVYITH 194
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-61 |
2.82e-08 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 54.46 E-value: 2.82e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 445977555 14 GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVE 61
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-216 |
2.94e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.99 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 21 DVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLihdqgrvewtPGTHYG--YLDQHTV--LTPGRTIRDVLAdaFLPLFE 96
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAY----------PGKFEGnvFINGKPVdiRNPAQAIRAGIA--MVPEDR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 97 KEKALNEVTeKMGTATPEELEELLEQMAEIQDALEAGGfylldmkIEEAARGLGIDAIGLDRDVSALSGGQRTKVLLAKL 176
Cdd:TIGR02633 346 KRHGIVPIL-GVGKNITLSVLKSFCFKMRIDAAAELQI-------IGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKM 417
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 445977555 177 LLEQPEVLLLDEPTNYLDV---EHIHWLTNYLKEYPHAFLLIS 216
Cdd:TIGR02633 418 LLTNPRVLILDEPTRGVDVgakYEIYKLINQLAQEGVAIIVVS 460
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
339-496 |
2.99e-08 |
|
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: 54.20 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 339 LLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIkpLSGKTSLGDFLepaYFEQEVKADNIT------PIDDVWntFP 412
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGTTSGQIL---FNGQPRKPDQFQkcvayvRQDDIL--LP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 413 GL------------------DQHQIRAMLAKCGLKNEHISRP----LSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHL 470
Cdd:cd03234 95 GLtvretltytailrlprksSDAIRKKRVEDVLLRDLALTRIggnlVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180
....*....|....*....|....*....
gi 445977555 471 DVTAKAELKKAMKAY---KGTILLVCHEP 496
Cdd:cd03234 175 DSFTALNLVSTLSQLarrNRIVILTIHQP 203
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
336-498 |
3.07e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 54.63 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 336 THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTI-LGKIkPLSGKTSLGDflEPAYFEQEVKADNITPI-DDV------ 407
Cdd:COG4161 14 SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLET-PDSGQLNIAG--HQFDFSQKPSEKAIRLLrQKVgmvfqq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 408 WNTFPGL------------------DQHQIRAM--LAKCGLKNEHISRPLsQLSGGEQAKVRLCKLMGEESNWLLFDEPT 467
Cdd:COG4161 91 YNLWPHLtvmenlieapckvlglskEQAREKAMklLARLRLTDKADRFPL-HLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190
....*....|....*....|....*....|....
gi 445977555 468 NHLD--VTAK-AELKKAMKAYKGTILLVCHEPDF 498
Cdd:COG4161 170 AALDpeITAQvVEIIRELSQTGITQVIVTHEVEF 203
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
14-196 |
3.09e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 56.12 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 14 GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNiitgqLIHdqgRVeWTPgthygylDQHTVLTPGRTIRDV----LAD 89
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLIN-----LLQ---RV-FDP-------QSGRILIDGTDIRTVtrasLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 90 AFLPLFEKEKALNEVTE---KMG--TATPeeleelleqmAEIQDALEAGGfyLLDMkIEeaARGLGIDAIGLDRDvSALS 164
Cdd:PRK13657 410 NIAVVFQDAGLFNRSIEdniRVGrpDATD----------EEMRAAAERAQ--AHDF-IE--RKPDGYDTVVGERG-RQLS 473
|
170 180 190
....*....|....*....|....*....|..
gi 445977555 165 GGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE 196
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVE 505
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
325-494 |
3.46e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 54.71 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 325 VFEGENVEIGYTHPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDF---LEPAYFEQEVKA--- 398
Cdd:PRK13633 11 SYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdtsDEENLWDIRNKAgmv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 399 ----DN--ITPI--DDVwnTF-P---GLDQHQIRAMLAKCgLKN----EHISRPLSQLSGGEQAKVRLCKLMGEESNWLL 462
Cdd:PRK13633 91 fqnpDNqiVATIveEDV--AFgPenlGIPPEEIRERVDES-LKKvgmyEYRRHAPHLLSGGQKQRVAIAGILAMRPECII 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 445977555 463 FDEPTNHLDVTAKAE----LKKAMKAYKGTILLVCH 494
Cdd:PRK13633 168 FDEPTAMLDPSGRREvvntIKELNKKYGITIILITH 203
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-249 |
3.71e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.81 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTF-GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVeWTPGTHYGYLDQHTVL-T 78
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV-LIRGEPITKENIREVRkF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 79 PGRTIRDVLADAFLPLFEKEKALNEVTEKMGTATpeeleelleqmaeiqdaleaggfylLDMKIEEAARGLGIDAIgLDR 158
Cdd:PRK13652 80 VGLVFQNPDDQIFSPTVEQDIAFGPINLGLDEET-------------------------VAHRVSSALHMLGLEEL-RDR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 159 DVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD----VEHIHWLTNYLKEYPHAFLLISHDTEFMNKCVDVIFHLEF 234
Cdd:PRK13652 134 VPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDK 213
|
250
....*....|....*
gi 445977555 235 TKMTRYTATYEKFLE 249
Cdd:PRK13652 214 GRIVAYGTVEEIFLQ 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
340-495 |
4.49e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 54.31 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 340 LPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGK-----TSLGDF--LEPAYFEQEVKA---DNITP------ 403
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNvswrgEPLAKLnrAQRKAFRRDIQMvfqDSISAvnprkt 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 404 ----IDDVWNTFPGLD----QHQIRAMLAKCGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAK 475
Cdd:PRK10419 108 vreiIREPLRHLLSLDkaerLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180
....*....|....*....|....
gi 445977555 476 AE---LKKAMKAYKGT-ILLVCHE 495
Cdd:PRK10419 188 AGvirLLKKLQQQFGTaCLFITHD 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
346-494 |
5.40e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 54.26 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 346 TIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD------------------------FLEPAYFEQEVKAD-- 399
Cdd:PRK13634 29 SIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitagkknkklkplrkkvgivfqFPEHQLFEETVEKDic 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 400 ----NI-TPIDDVwntfpgldQHQIRAMLAKCGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTA 474
Cdd:PRK13634 109 fgpmNFgVSEEDA--------KQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180
....*....|....*....|....*..
gi 445977555 475 KAELkkaMKAY------KG-TILLVCH 494
Cdd:PRK13634 181 RKEM---MEMFyklhkeKGlTTVLVTH 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
346-472 |
5.71e-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: 55.18 E-value: 5.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 346 TIERGEKIAIVGCNGVGKSTLLKTILGKIKPlsgktSLGDFLEPA----------------YFeQEVKADNITP------ 403
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKP-----NLGDYDEEPswdevlkrfrgtelqdYF-KKLANGEIKVahkpqy 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 404 IDDVWNTFPG--------LDQHQIRAMLA-KCGLKNEhISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDV 472
Cdd:COG1245 169 VDLIPKVFKGtvrellekVDERGKLDELAeKLGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
20-194 |
9.05e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 53.46 E-value: 9.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLDqhtvltpGRTIrdvladaflplfeKEK 99
Cdd:PRK13632 26 KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEI---------KID-------GITI-------------SKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 100 ALNEVTEKMGT--ATPEELEELLEQMAEIQDALEAGGFYLLDMK--IEEAARGLGIDAIgLDRDVSALSGGQRTKVLLAK 175
Cdd:PRK13632 77 NLKEIRKKIGIifQNPDNQFIGATVEDDIAFGLENKKVPPKKMKdiIDDLAKKVGMEDY-LDKEPQNLSGGQKQRVAIAS 155
|
170
....*....|....*....
gi 445977555 176 LLLEQPEVLLLDEPTNYLD 194
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLD 174
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-247 |
9.17e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.47 E-value: 9.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKST-FMNiITGQLIHDQGRVEWTpgthygyldqhtvltpGR 81
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTlFMN-LSGLLRPQKGAVLWQ----------------GK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 82 tirdvladaflPLFEKEKALNEVTEKMGTAtpeeleelleqmaeIQDALEAGGFYLLDMKIEEAARGLGI---------- 151
Cdd:PRK13638 64 -----------PLDYSKRGLLALRQQVATV--------------FQDPEQQIFYTDIDSDIAFSLRNLGVpeaeitrrvd 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 152 DAIGL-------DRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD----VEHIHWLTNYLKEYPHAfLLISHDTE 220
Cdd:PRK13638 119 EALTLvdaqhfrHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpagrTQMIAIIRRIVAQGNHV-IISSHDID 197
|
250 260
....*....|....*....|....*..
gi 445977555 221 FMNKCVDVIFHLEFTKMTRYTATYEKF 247
Cdd:PRK13638 198 LIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-225 |
9.35e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.41 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 15 DRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV-----EWTPGTHYGYLDQHTVL-TPGRtiRDvla 88
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIrlngkDISPRSPLDAVKKGMAYiTESR--RD--- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 89 DAFLPLFEkekalneVTEKMGTATPEELEELLEQMAEIQDALEAggfylldmKIEEAARG-LGIDAIGLDRDVSALSGGQ 167
Cdd:PRK09700 350 NGFFPNFS-------IAQNMAISRSLKDGGYKGAMGLFHEVDEQ--------RTAENQRElLALKCHSVNQNITELSGGN 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445977555 168 RTKVLLAKLLLEQPEVLLLDEPTNYLDV---EHIHWLTNYLKEYPHAFLLISHD-TEFMNKC 225
Cdd:PRK09700 415 QQKVLISKWLCCCPEVIIFDEPTRGIDVgakAEIYKVMRQLADDGKVILMVSSElPEIITVC 476
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-194 |
1.09e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 13 FGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQliHDQ---------------GRVEWTPGTHYGY------L 71
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD--HPQgysndltlfgrrrgsGETIWDIKKHIGYvssslhL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 72 DqHTVLTpgrTIRDVLADAFlplFEKEKALNEVTEKmgtatpeeleelleQMAEIQDALEAggfylldmkieeaargLGI 151
Cdd:PRK10938 348 D-YRVST---SVRNVILSGF---FDSIGIYQAVSDR--------------QQKLAQQWLDI----------------LGI 390
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 445977555 152 DAIGLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PRK10938 391 DKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
339-494 |
1.15e-07 |
|
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: 52.87 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 339 LLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTsLGD-----FLEPAYFEQE---VKADNI----TPIDD 406
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-LVDghdlaLADPAWLRRQvgvVLQENVlfnrSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 407 VWNTFPGLDQHQIRAMlAKCGLKNEHISR-PL----------SQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAK 475
Cdd:cd03252 96 IALADPGMSMERVIEA-AKLAGAHDFISElPEgydtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180
....*....|....*....|.
gi 445977555 476 AELKKAMKAY-KG-TILLVCH 494
Cdd:cd03252 175 HAIMRNMHDIcAGrTVIIIAH 195
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
329-494 |
1.16e-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: 52.93 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGY----THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD---------FL-------- 387
Cdd:cd03249 4 KNVSFRYpsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdirdlnlrWLrsqiglvs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 388 -EPAYFEQEVkADNITpiddvWNTFPGLDQHQIRAmlakCGLKNEH---ISRPL----------SQLSGGEQAKVRLCKL 453
Cdd:cd03249 84 qEPVLFDGTI-AENIR-----YGKPDATDEEVEEA----AKKANIHdfiMSLPDgydtlvgergSQLSGGQKQRIAIARA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 445977555 454 MGEESNWLLFDEPTNHLDVTAKAELKKAM-KAYKG-TILLVCH 494
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALdRAMKGrTTIVIAH 196
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
128-255 |
1.17e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 53.70 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 128 DALEAGGFYLldmkieeaaRGLGIDAIGLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKE 207
Cdd:PRK13631 151 EAKKLAKFYL---------NKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD 221
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 445977555 208 YP---HAFLLISHDTEFMNKCVDVIFHLEFTKMTRYTATYEKFLELAEINK 255
Cdd:PRK13631 222 AKannKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHIINS 272
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
336-506 |
1.36e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 52.71 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 336 THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTI-LGKIkPLSGKTSL-GDFLEpayFEQEVKADNITPI-DDV----- 407
Cdd:PRK11124 14 AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEM-PRSGTLNIaGNHFD---FSKTPSDKAIRELrRNVgmvfq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 408 -WNTFP----------------GLDQHQI--RAM--LAKCGLkNEHISR-PLsQLSGGEQAKVRLCKLMGEESNWLLFDE 465
Cdd:PRK11124 90 qYNLWPhltvqqnlieapcrvlGLSKDQAlaRAEklLERLRL-KPYADRfPL-HLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 445977555 466 PTNHLDVTAKAELKKAMKAYKGT-I--LLVCHEPDFYEDWITKV 506
Cdd:PRK11124 168 PTAALDPEITAQIVSIIRELAETgItqVIVTHEVEVARKTASRV 211
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-218 |
1.64e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 53.20 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTF-GDRTLFK----------DVSMRLLAGEHVGLVGANGVGKSTFMNIITGqLIH-DQGRVEW--TPGTHY 68
Cdd:COG4608 7 LLEVRDLKKHFpVRGGLFGrtvgvvkavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLR-LEEpTSGEILFdgQDITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 69 G--------------YLDQHTVLTPGRTIRDVLADAFLplfekekaLNEVTEKmgtatpeeleelleqmAEIQDaleagg 134
Cdd:COG4608 86 SgrelrplrrrmqmvFQDPYASLNPRMTVGDIIAEPLR--------IHGLASK----------------AERRE------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 135 fylldmKIEEAarglgIDAIGLDRDVS-----ALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV----EHIHWLTNYL 205
Cdd:COG4608 136 ------RVAEL-----LELVGLRPEHAdryphEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVsiqaQVLNLLEDLQ 204
|
250
....*....|...
gi 445977555 206 KEYPHAFLLISHD 218
Cdd:COG4608 205 DELGLTYLFISHD 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
338-477 |
1.74e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 52.71 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 338 PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFL--EPAYFEQEVKA-------DN----ITPI 404
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlsEETVWDVRRQVgmvfqnpDNqfvgATVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 405 DDVwnTFpGLDQHQI---------RAMLAKCGLKnEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAK 475
Cdd:PRK13635 101 DDV--AF-GLENIGVpreemvervDQALRQVGME-DFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGR 176
|
..
gi 445977555 476 AE 477
Cdd:PRK13635 177 RE 178
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
339-495 |
2.03e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 53.16 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 339 LLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD----------------FLEPAYFEQEVKADNIT 402
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlhardrkvgfvFQHYALFRHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 403 piddvwntFpGL---------DQHQIRAMLAKC--GLKNEHIS-RPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHL 470
Cdd:PRK10851 97 --------F-GLtvlprrerpNAAAIKAKVTQLleMVQLAHLAdRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180
....*....|....*....|....*....
gi 445977555 471 DVTAKAELKKAMK----AYKGTILLVCHE 495
Cdd:PRK10851 168 DAQVRKELRRWLRqlheELKFTSVFVTHD 196
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
343-471 |
2.03e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 53.30 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSL-GDFLE--PAYFEqevkadnitPIDDVWNT---FP---- 412
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLdGVDLShvPPYQR---------PINMMFQSyalFPhmtv 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445977555 413 ------GLDQHQ---------IRAMLAKCGLKnEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD 471
Cdd:PRK11607 109 eqniafGLKQDKlpkaeiasrVNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-218 |
2.06e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.79 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGTHYG----------------YLDQHTVLTPGRTI 83
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmkddewravrsdiqmiFQDPLASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 84 RDVLAD---AFLPLFEKEKALNEVTEKMgtatpeeleelleqmaeiqdaleaggfylldMKIeeaarGLGIDAIglDRDV 160
Cdd:PRK15079 118 GEIIAEplrTYHPKLSRQEVKDRVKAMM-------------------------------LKV-----GLLPNLI--NRYP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445977555 161 SALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPH----AFLLISHD 218
Cdd:PRK15079 160 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemglSLIFIAHD 221
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
338-494 |
2.17e-07 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 51.64 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 338 PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTS----------LGDF--------LEPAYFEQEVKAd 399
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgidistipLEDLrssltiipQDPTLFSGTIRS- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 400 NITPIDDvwntfpgLDQHQIRAMLAkcglknehISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELK 479
Cdd:cd03369 101 NLDPFDE-------YSDEEIYGALR--------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ 165
|
170
....*....|....*..
gi 445977555 480 KAMKA--YKGTILLVCH 494
Cdd:cd03369 166 KTIREefTNSTILTIAH 182
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
338-471 |
2.46e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.80 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 338 PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFLepAYFEQEVKADNITPIDDVWNTFPgLDQH 417
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV--AYVPQQAWIQNDSLRENILFGKA-LNEK 728
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445977555 418 QIRAMLAKCGL----------KNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD 471
Cdd:TIGR00957 729 YYQQVLEACALlpdleilpsgDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-194 |
2.49e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 52.92 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLD-QHTVLTP-- 79
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI---------MLDgVDLSHVPpy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 80 GRTIRDVLAD-AFLP--LFEKEKALNEVTEKMGTAtpeeleelleqmaEIQDALEAggfYLLDMKIEEAARglgidaigl 156
Cdd:PRK11607 90 QRPINMMFQSyALFPhmTVEQNIAFGLKQDKLPKA-------------EIASRVNE---MLGLVHMQEFAK--------- 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 445977555 157 dRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PRK11607 145 -RKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
343-480 |
3.62e-07 |
|
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: 51.00 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD-----------------FL--EPAYFEQEVKADNITP 403
Cdd:cd03218 19 VSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlgigYLpqEASIFRKLTVEENILA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 404 IDDVWNTFPGLDQHQIRAMLAKCGLknEHIS-RPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKK 480
Cdd:cd03218 99 VLEIRGLSKKEREEKLEELLEEFHI--THLRkSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQK 174
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
141-194 |
3.91e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.15 E-value: 3.91e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 445977555 141 KIEEAARGLGIDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PRK11650 114 RVAEAARILELEPL-LDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-196 |
3.93e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 52.71 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwtpgthygyLDqhtvltpGRTIRD----------VLAD 89
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIL---------LD-------GHDLRDytlaslrnqvALVS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 90 AFLPLFEKEKALNEVTEKMGTATpeeleelleqMAEIQDALEAGgfYLLDMkIEEAARGLgiDAIGLDRDVSaLSGGQRT 169
Cdd:PRK11176 424 QNVHLFNDTIANNIAYARTEQYS----------REQIEEAARMA--YAMDF-INKMDNGL--DTVIGENGVL-LSGGQRQ 487
|
170 180
....*....|....*....|....*..
gi 445977555 170 KVLLAKLLLEQPEVLLLDEPTNYLDVE 196
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTE 514
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
340-495 |
4.28e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.22 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 340 LPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKP-----LSGKTSLGDFLEPA--YFeQEVKadnITP----IDDVW 408
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPsagelLAGTAPLAEAREDTrlMF-QDAR---LLPwkkvIDNVG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 409 NTFPGLDQHQIRAMLAKCGLKNEHISRPlSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKA---- 484
Cdd:PRK11247 104 LGLKGQWRDAALQALAAVGLADRANEWP-AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESlwqq 182
|
170
....*....|.
gi 445977555 485 YKGTILLVCHE 495
Cdd:PRK11247 183 HGFTVLLVTHD 193
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
343-494 |
4.97e-07 |
|
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: 50.45 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDF---LEPA-------YFEQEVKADNI-TPIDDVW--- 408
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHdvvREPRevrrrigIVFQDLSVDDElTGWENLYiha 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 409 --NTFPGLDQHQ-IRAMLAKCGLkNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKA---ELKKAM 482
Cdd:cd03265 99 rlYGVPGAERRErIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAhvwEYIEKL 177
|
170
....*....|...
gi 445977555 483 KAYKG-TILLVCH 494
Cdd:cd03265 178 KEEFGmTILLTTH 190
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
143-195 |
5.10e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.10 E-value: 5.10e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 445977555 143 EEAARGLGIDAIGLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV 195
Cdd:NF040905 385 EEYRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-194 |
5.14e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.93 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIIT--GQLIHDqgrVEWTPGTHYgylDQHTVLTPg 80
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPE---VTITGSIVY---NGHNIYSP- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 81 RT----IRDVLADAF-----LPLFEKEKA-----LNEVTEKmgtatpeeleelleqmaeiqdaleaggfYLLDMKIEEAA 146
Cdd:PRK14239 78 RTdtvdLRKEIGMVFqqpnpFPMSIYENVvyglrLKGIKDK----------------------------QVLDEAVEKSL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 445977555 147 RGLGI-DAIG--LDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PRK14239 130 KGASIwDEVKdrLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
337-498 |
5.66e-07 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 50.95 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 337 HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDflEPAYFEQEvKADNITPIDD---------- 406
Cdd:COG4598 21 LEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGG--EEIRLKPD-RDGELVPADRrqlqrirtrl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 407 --VWNTFpGLDQH------------------------QIRAMLAKCGLKNEHISRPlSQLSGGEQAKVRLCKLMGEESNW 460
Cdd:COG4598 98 gmVFQSF-NLWSHmtvlenvieapvhvlgrpkaeaieRAEALLAKVGLADKRDAYP-AHLSGGQQQRAAIARALAMEPEV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 445977555 461 LLFDEPTNHLDVTAKAELKKAMK--AYKG-TILLVCHEPDF 498
Cdd:COG4598 176 MLFDEPTSALDPELVGEVLKVMRdlAEEGrTMLVVTHEMGF 216
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-218 |
6.53e-07 |
|
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: 51.21 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFG-DRTLFK---DVSMRLLAGEHVGLVGANGVGKSTFMNIITGqLIHDQGRVEwtpgthygyldqhtvlt 78
Cdd:COG0444 1 LLEVRNLKVYFPtRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILG-LLPPPGITS----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 79 pGRTI---RDVLAdafLPlfekEKALNEVTEKmgtatpeeleelleQMAEI-QDALEAggfylLD--MKIEE-------- 144
Cdd:COG0444 63 -GEILfdgEDLLK---LS----EKELRKIRGR--------------EIQMIfQDPMTS-----LNpvMTVGDqiaeplri 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 145 -------AARGLGIDAI---GLDRDVSA-------LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV-------EHIHW 200
Cdd:COG0444 116 hgglskaEARERAIELLervGLPDPERRldrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVtiqaqilNLLKD 195
|
250
....*....|....*...
gi 445977555 201 LTnylKEYPHAFLLISHD 218
Cdd:COG0444 196 LQ---RELGLAILFITHD 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
344-497 |
7.10e-07 |
|
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: 50.72 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 344 SMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTslgdflepayfeqEVKADNITPIDD-------------VWNT 410
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKV-------------LIDGQDIAAMSRkelrelrrkkismVFQS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 411 FpGLDQH---------------------QIRAM--LAKCGLKNEHISRPlSQLSGGEQAKVRLCKLMGEESNWLLFDEPT 467
Cdd:cd03294 111 F-ALLPHrtvlenvafglevqgvpraerEERAAeaLELVGLEGWEHKYP-DELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190
....*....|....*....|....*....|....
gi 445977555 468 NHLDVTAKAELK----KAMKAYKGTILLVCHEPD 497
Cdd:cd03294 189 SALDPLIRREMQdellRLQAELQKTIVFITHDLD 222
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
344-477 |
7.23e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.12 E-value: 7.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 344 SMTIERGEKIAIVGCNGVGKSTLLKtILGKI-KPLSGKTSLG--DFLEPAyfeQEVKADNITPIDDVW-NTFPGLD---- 415
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLAR-LLTMIeTPTGGELYYQgqDLLKAD---PEAQKLLRQKIQIVFqNPYGSLNprkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 416 --------------------QHQIRAMLAKCGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAK 475
Cdd:PRK11308 111 vgqileepllintslsaaerREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
..
gi 445977555 476 AE 477
Cdd:PRK11308 191 AQ 192
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-218 |
7.56e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.20 E-value: 7.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 18 LFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGqlihdqgrvewtpgthygyLDQHT---VLTPGRTIRDVLADAFLPL 94
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGG-------------------LDTPTsgdVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 95 FEKE--------KALNEVTEKMGTATPEELEELLEQMAEiQDALEAggfylldmkieeaarglgIDAIGLDRDV----SA 162
Cdd:PRK11629 85 RNQKlgfiyqfhHLLPDFTALENVAMPLLIGKKKPAEIN-SRALEM------------------LAAVGLEHRAnhrpSE 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 163 LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPH----AFLLISHD 218
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRlqgtAFLVVTHD 205
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-196 |
7.58e-07 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 50.57 E-value: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLDQHTV-LTPGRT 82
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEI---------RVGGEEIrLKPDRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 IRDVLADAflplfekeKALNEVTEKMGTAtpeeleellEQ-------MAEIQDALEAGgFYLLDMKIEEA---ARGLgID 152
Cdd:COG4598 80 GELVPADR--------RQLQRIRTRLGMV---------FQsfnlwshMTVLENVIEAP-VHVLGRPKAEAierAEAL-LA 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 445977555 153 AIGLD--RDV--SALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE 196
Cdd:COG4598 141 KVGLAdkRDAypAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPE 188
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
349-501 |
7.70e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.91 E-value: 7.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 349 RGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDfLEPAYFEQEVKADNITPIDDVWNTFPGLDQHQIRAMLAKCGL 428
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 429 KnehisrplsqlsggeqakvrlcklmgeesnWLLFDEPTNHLDVTAKAEL---------KKAMKAYKGTILLVCHEPDFY 499
Cdd:smart00382 80 D------------------------------VLILDEITSLLDAEQEALLllleelrllLLLKSEKNLTVILTTNDEKDL 129
|
..
gi 445977555 500 ED 501
Cdd:smart00382 130 GP 131
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-233 |
8.51e-07 |
|
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: 49.78 E-value: 8.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 18 LFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWtpGTHYGYLDQHTVLTPGrTIRDVLadAFLPLFEK 97
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV--PGSIAYVSQEPWIQNG-TIRENI--LFGKPFDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 98 EKaLNEVTEKMgtatpeeleelleqmaeiqdALEAggfyllDMKIEEAarglGIDA-IGlDRDVSaLSGGQRTKVLLAKL 176
Cdd:cd03250 95 ER-YEKVIKAC--------------------ALEP------DLEILPD----GDLTeIG-EKGIN-LSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445977555 177 LLEQPEVLLLDEPTNYLDVE---HI--HWLTNYLKEyPHAFLLISHDTEFMNKCvDVIFHLE 233
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHvgrHIfeNCILGLLLN-NKTRILVTHQLQLLPHA-DQIVVLD 201
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
337-495 |
9.72e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.56 E-value: 9.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 337 HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGktslgdflEPAYFEQEVKADNITPIDDVwnTFPG--- 413
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKG--------EILFERQSIKKDLCTYQKQL--CFVGhrs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 414 -------------LDQHQIRAMLAKCGL----KNEH-ISRPLSQLSGGEQAKVRLCKL-MGEESNWLLfDEPTNHLDVTA 474
Cdd:PRK13540 84 ginpyltlrenclYDIHFSPGAVGITELcrlfSLEHlIDYPCGLLSSGQKRQVALLRLwMSKAKLWLL-DEPLVALDELS 162
|
170 180
....*....|....*....|....
gi 445977555 475 KAELKKAMKAYK---GTILLVCHE 495
Cdd:PRK13540 163 LLTIITKIQEHRakgGAVLLTSHQ 186
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
5-111 |
9.93e-07 |
|
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: 49.11 E-value: 9.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 5 TVEKLGHTFGDRTL------FKDvsmrllaGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWtPGTHYGYLDQHTVLT 78
Cdd:cd03222 2 LYPDCVKRYGVFFLlvelgvVKE-------GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVYKPQYIDLS 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 445977555 79 PGRTIRDVLA-----DAFLPLFEKEKALNEVTEKMGTA 111
Cdd:cd03222 74 GGELQRVAIAaallrNATFYLFDEPSAYLDIEQRLNAA 111
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
343-471 |
1.15e-06 |
|
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: 49.50 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGeKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSL--GDFLEP--------AYFEQEVKA-DNITPID--DVWN 409
Cdd:cd03264 19 VSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgQDVLKQpqklrrriGYLPQEFGVyPNFTVREflDYIA 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445977555 410 TFPGLDQ----HQIRAMLAKCGLkNEHISRPLSQLSGGEQAKVRL-CKLMGEESnWLLFDEPTNHLD 471
Cdd:cd03264 98 WLKGIPSkevkARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIaQALVGDPS-ILIVDEPTAGLD 162
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
322-496 |
1.22e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 49.18 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 322 SRFVFEGENveigyTHPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKP---LSGKTSLGDfLEPAYFEQEVKA 398
Cdd:cd03233 10 SFTTGKGRS-----KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYNG-IPYKEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 399 DNI-TPIDDVwnTFPGLDQHQIRAMLAKCglKNEHISRplsQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAE 477
Cdd:cd03233 84 EIIyVSEEDV--HFPTLTVRETLDFALRC--KGNEFVR---GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALE 156
|
170 180
....*....|....*....|...
gi 445977555 478 LKKAMK----AYKGTILLVCHEP 496
Cdd:cd03233 157 ILKCIRtmadVLKTTTFVSLYQA 179
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-224 |
1.32e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.18 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTpgthygyldqhtvltpGRT 82
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFE----------------RQS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 IRDVLAdaflplfEKEKALNEVTEKMGTaTPEELEElleqmaeiQDALEAGGFYLLDMKIEEAARGLGIDAIgLDRDVSA 162
Cdd:PRK13540 65 IKKDLC-------TYQKQLCFVGHRSGI-NPYLTLR--------ENCLYDIHFSPGAVGITELCRLFSLEHL-IDYPCGL 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 163 LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPH---AFLLISHDTEFMNK 224
Cdd:PRK13540 128 LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAkggAVLLTSHQDLPLNK 192
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-495 |
1.33e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 23 SMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEW--TPGTHYGYLD----------QHTVLTPGRTIRDvlaDA 90
Cdd:PRK10762 24 ALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgKEVTFNGPKSsqeagigiihQELNLIPQLTIAE---NI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 91 FLPlfekekalNEVTEKMGTatpeeleELLEQMAEIQDALeaggfyLLDMKIEEAARGLgidaigldrdVSALSGGQRTK 170
Cdd:PRK10762 101 FLG--------REFVNRFGR-------IDWKKMYAEADKL------LARLNLRFSSDKL----------VGELSIGEQQM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 171 VLLAKLLLEQPEVLLLDEPTNYL---DVEHIHWLTNYLKEYPHAFLLISHD-TEFMNKCVDVifhlefTKMTRYTATYEK 246
Cdd:PRK10762 150 VEIAKVLSFESKVIIMDEPTDALtdtETESLFRVIRELKSQGRGIVYISHRlKEIFEICDDV------TVFRDGQFIAER 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 247 flELAEINKNQHInayekqrEFI---KKQEDFIAKNKARYSTtgraksrqkqldRMELIDrpetaikpefsfkesrassr 323
Cdd:PRK10762 224 --EVADLTEDSLI-------EMMvgrKLEDQYPRLDKAPGEV------------RLKVDN-------------------- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 324 fvFEGENVEigythpllpKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSL-GDFLEP-----------AY 391
Cdd:PRK10762 263 --LSGPGVN---------DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdGHEVVTrspqdglangiVY 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 392 FEQEVKAD------------NITPIDDVWNTFPGLDQHQ--------IRAMlakcGLKNEHISRPLSQLSGGEQAKVRLC 451
Cdd:PRK10762 332 ISEDRKRDglvlgmsvkenmSLTALRYFSRAGGSLKHADeqqavsdfIRLF----NIKTPSMEQAIGLLSGGNQQKVAIA 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 445977555 452 KLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAYKG---TILLVCHE 495
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeglSIILVSSE 454
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-218 |
1.36e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.35 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 21 DVSMRLLAGEHVGLVGANGVGKSTFMNIITgqLIHdqgrvewTPGTHYGYLDQHTVLTPGRTIRDVLADAFLPLFEKEKA 100
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLT--MIE-------TPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNPYG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 101 -LNEvTEKMGTatpeeleelleQMAE---IQDALEAggfylldmkIEEAARGLGIDA-IGL-----DRDVSALSGGQRTK 170
Cdd:PRK11308 104 sLNP-RKKVGQ-----------ILEEpllINTSLSA---------AERREKALAMMAkVGLrpehyDRYPHMFSGGQRQR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 445977555 171 VLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYL----KEYPHAFLLISHD 218
Cdd:PRK11308 163 IAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMmdlqQELGLSYVFISHD 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
340-507 |
1.41e-06 |
|
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: 50.96 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 340 LPKLSMTIERGEKIAIVGCNGVGKSTLLKTILG--KIKPLSGK-----------------TSLG---------------D 385
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRiiyhvalcekcgyverpSKVGepcpvcggtlepeevD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 386 FLEPA--YFEQEVKADNI------------TPIDDVWNTFPGLDQHQIRAM--------LAKCGLKNEHISRplsQLSGG 443
Cdd:TIGR03269 96 FWNLSdkLRRRIRKRIAImlqrtfalygddTVLDNVLEALEEIGYEGKEAVgravdlieMVQLSHRITHIAR---DLSGG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445977555 444 EQAKVRLCKLMGEESNWLLFDEPTNHLD-VTAK---AELKKAMKAYKGTILLVCHEPDFYEDWITK-VW 507
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDpQTAKlvhNALEEAVKASGISMVLTSHWPEVIEDLSDKaIW 241
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
12-194 |
1.41e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.03 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 12 TFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNII---------TGQLIHDQGRVEWTPGTHYGYLDQHTVLTPGRT 82
Cdd:PLN03211 77 QIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALagriqgnnfTGTILANNRKPTKQILKRTGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 83 IRDVLAdaFLPLFEKEKALNEvTEKMGTAtpeeleelleqmaeiqdaleaggfyllDMKIEEAARGLGIDAIGLDRDVSA 162
Cdd:PLN03211 157 VRETLV--FCSLLRLPKSLTK-QEKILVA---------------------------ESVISELGLTKCENTIIGNSFIRG 206
|
170 180 190
....*....|....*....|....*....|..
gi 445977555 163 LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PLN03211 207 ISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-230 |
1.42e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.85 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRT-LFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygyldqhtvLTPGR 81
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI----------------LFDGK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 82 tirdvladaflPLFEKEKALNEVTEKMGTA--TPEELEELleqmAEIQDALEAGGFYL------LDMKIEEAARGLGIDA 153
Cdd:PRK13636 69 -----------PIDYSRKGLMKLRESVGMVfqDPDNQLFS----ASVYQDVSFGAVNLklpedeVRKRVDNALKRTGIEH 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 154 IGlDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD----VEHIHWLTNYLKEYPHAFLLISHDTEFMNKCVDVI 229
Cdd:PRK13636 134 LK-DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNV 212
|
.
gi 445977555 230 F 230
Cdd:PRK13636 213 F 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-218 |
1.49e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 49.73 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLDQHtVLTPGRT--IRDVLADAFLplfek 97
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI---------IIDGD-LLTEENVwdIRHKIGMVFQ----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 98 ekalNEVTEKMGtatpeeleelleqmAEIQD----ALEAGGFYLLDMK--IEEAARGLGIDAIGlDRDVSALSGGQRTKV 171
Cdd:PRK13650 89 ----NPDNQFVG--------------ATVEDdvafGLENKGIPHEEMKerVNEALELVGMQDFK-EREPARLSGGQKQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 445977555 172 LLAKLLLEQPEVLLLDEPTNYLD----VEHIHWLTNYLKEYPHAFLLISHD 218
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
343-385 |
1.66e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 49.70 E-value: 1.66e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD 385
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG 67
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-218 |
1.69e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 49.60 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITG-------QLIHDQGRVEWTPGthygyldqHT 75
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfykptggTILLRGQHIEGLPG--------HQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 76 VLTPG--RTIRDVladaflPLFeKEKAlneVTEKMGTAtpeeleelleQMAEIQDALEAGGFYLLDMK------IEEAAR 147
Cdd:PRK11300 77 IARMGvvRTFQHV------RLF-REMT---VIENLLVA----------QHQQLKTGLFSGLLKTPAFRraeseaLDRAAT 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445977555 148 GLgiDAIGL----DRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPT---NYLDVEHIHWLTNYLK-EYPHAFLLISHD 218
Cdd:PRK11300 137 WL--ERVGLlehaNRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAaglNPKETKELDELIAELRnEHNVTVLLIEHD 213
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
14-194 |
1.75e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 50.49 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 14 GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLD-------QHTVLTPGRTI--R 84
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI---------RLDgrplsslSHSVLRQGVAMvqQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 85 D--VLADAFLPLFEKEKALNEvtekmgtatpeeleelleqmAEIQDALEAggfylldMKIEEAARGL--GIDAIgLDRDV 160
Cdd:PRK10790 423 DpvVLADTFLANVTLGRDISE--------------------EQVWQALET-------VQLAELARSLpdGLYTP-LGEQG 474
|
170 180 190
....*....|....*....|....*....|....
gi 445977555 161 SALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PRK10790 475 NNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
163-196 |
1.93e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 49.24 E-value: 1.93e-06
10 20 30
....*....|....*....|....*....|....
gi 445977555 163 LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE 196
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
329-380 |
2.05e-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: 48.76 E-value: 2.05e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 445977555 329 ENVEIGY--THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGK 380
Cdd:cd03254 6 ENVNFSYdeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQ 59
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-61 |
2.08e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.51 E-value: 2.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 445977555 6 VEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVE 61
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVE 59
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
336-503 |
2.16e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 48.93 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 336 THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDflepayfeQEVKAdniTPIDDVWNT----- 410
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDG--------LDVAT---TPSRELAKRlailr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 411 -------------------FP-------GLDQHQIRAMLAKCGLKN-EHisRPLSQLSGGEQ-----AKVrLCklmgEES 458
Cdd:COG4604 82 qenhinsrltvrelvafgrFPyskgrltAEDREIIDEAIAYLDLEDlAD--RYLDELSGGQRqrafiAMV-LA----QDT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 445977555 459 NWLLFDEPTNHLDVTAKAE----LKKAMKAYKGTILLVCHEPDF---YEDWI 503
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQmmklLRRLADELGKTVVIVLHDINFascYADHI 206
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
142-247 |
2.25e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 49.28 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 142 IEEAARGLGIDAIGLDR---DVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV---EHIHWLTNYLKEyPHAFLLI 215
Cdd:PRK14246 130 VEECLRKVGLWKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIvnsQAIEKLITELKN-EIAIVIV 208
|
90 100 110
....*....|....*....|....*....|..
gi 445977555 216 SHDTEFMNKCVDVIFHLEFTKMTRYTATYEKF 247
Cdd:PRK14246 209 SHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
344-494 |
2.43e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.03 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 344 SMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGktslgdflEPAYFEQEVK-------------------------- 397
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSG--------EILIDGKPVRirsprdaialgigmvhqhfmlvpnlt 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 398 -ADNIT-PIDDVWNTFPGLDQ--HQIRAMLAKCGLKnehI--SRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD 471
Cdd:COG3845 97 vAENIVlGLEPTKGGRLDRKAarARIRELSERYGLD---VdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLT 173
|
170 180
....*....|....*....|....*.
gi 445977555 472 VTAKAELKKAMKAYKG---TILLVCH 494
Cdd:COG3845 174 PQEADELFEILRRLAAegkSIIFITH 199
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-218 |
2.54e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 49.35 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTFGD-RTLFKDV---SMRLLAGEHVGLVGANGVGKSTFMNIITGqLIHDQGRVEWTPGTHYGyldqhtv 76
Cdd:PRK11022 1 MALLNVDKLSVHFGDeSAPFRAVdriSYSVKQGEVVGIVGESGSGKSVSSLAIMG-LIDYPGRVMAEKLEFNG------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 77 ltpgrtiRDVLAdaflpLFEKEKAL---NEVT----EKMGTATPEELEELleqmaEIQDALEA--GGfylldMKIEEAAR 147
Cdd:PRK11022 73 -------QDLQR-----ISEKERRNlvgAEVAmifqDPMTSLNPCYTVGF-----QIMEAIKVhqGG-----NKKTRRQR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 148 GL------GI--DAIGLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV----EHIHWLTNYLKEYPHAFLLI 215
Cdd:PRK11022 131 AIdllnqvGIpdPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLI 210
|
...
gi 445977555 216 SHD 218
Cdd:PRK11022 211 THD 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-199 |
2.70e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.03 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLgHTFGDR--TLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLDQHTVLtpG 80
Cdd:COG3845 257 VLEVENL-SVRDDRgvPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSI---------RLDGEDIT--G 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 81 RTIRDVLAD--AFLPlfekekalnevtE---KMGTATPEEleelleqMAE-----IQDALEAGGFYLLDMK-IEEAARGL 149
Cdd:COG3845 325 LSPRERRRLgvAYIP------------EdrlGRGLVPDMS-------VAEnlilgRYRRPPFSRGGFLDRKaIRAFAEEL 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 445977555 150 ----GIDAIGLDRDVSALSGG--QrtKVLLAKLLLEQPEVLLLDEPTNYLDV---EHIH 199
Cdd:COG3845 386 ieefDVRTPGPDTPARSLSGGnqQ--KVILARELSRDPKLLIAAQPTRGLDVgaiEFIH 442
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
338-511 |
2.74e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.97 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 338 PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD------------------------FLEPAYFE 393
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknkdikqirkkvglvfqFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 394 QEVkadnitpIDDVW---NTFpGLDQHQI----RAMLAKCGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEP 466
Cdd:PRK13649 101 ETV-------LKDVAfgpQNF-GVSQEEAealaREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 445977555 467 TNHLDVTAKAELkkaMKAYKG------TILLVCHEPDFYEDWITKVWDVEE 511
Cdd:PRK13649 173 TAGLDPKGRKEL---MTLFKKlhqsgmTIVLVTHLMDDVANYADFVYVLEK 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
350-471 |
3.76e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 47.95 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 350 GEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD------------FLEPAY---FEQEVKADNITPIDDVwnTFP-- 412
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrevpFLRRQIgmiFQDHHLLMDRTVYDNV--AIPli 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 413 --GLDQHQIR----AMLAKCGLKNEHISRPLsQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD 471
Cdd:PRK10908 106 iaGASGDDIRrrvsAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
337-497 |
3.84e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 337 HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKI---KPLSGKTSLGDFL---EP-------------AYFEQEVK 397
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtggGAPRGARVTGDVTlngEPlaaidaprlarlrAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 398 ADNITPIDDV--WNTFP-----GLDQHQIR----AMLAKCGlKNEHISRPLSQLSGGEQAKVRLCKLMGE---------E 457
Cdd:PRK13547 94 PAFAFSAREIvlLGRYPharraGALTHRDGeiawQALALAG-ATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 445977555 458 SNWLLFDEPTNHLDVTAKAELKKAMKA----YKGTILLVCHEPD 497
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRlardWNLGVLAIVHDPN 216
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
296-368 |
4.60e-06 |
|
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: 49.43 E-value: 4.60e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 296 LDRM-ELIDR-PETAIKPEF-SFKESRASSRFvfegENVEIGYT--HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLK 368
Cdd:COG5265 329 MERMfDLLDQpPEVADAPDApPLVVGGGEVRF----ENVSFGYDpeRPILKGVSFEVPAGKTVAIVGPSGAGKSTLAR 402
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
157-220 |
5.90e-06 |
|
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: 48.26 E-value: 5.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 157 DRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPH----AFLLISHDTE 220
Cdd:TIGR01187 95 DRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEqlgiTFVFVTHDQE 162
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
162-196 |
6.31e-06 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 47.70 E-value: 6.31e-06
10 20 30
....*....|....*....|....*....|....*
gi 445977555 162 ALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE 196
Cdd:COG4161 141 HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-190 |
7.07e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.57 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPgthygylDQHTVLTPG 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG-------KDITDWQTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 81 RTIRDvlADAFLPlfEKEKALNEVTekmgtatpeeleelleqmaeIQDALEAGGFYLLDMKIEE-AARGLGIDAIGLDRD 159
Cdd:PRK11614 76 KIMRE--AVAIVP--EGRRVFSRMT--------------------VEENLAMGGFFAERDQFQErIKWVYELFPRLHERR 131
|
170 180 190
....*....|....*....|....*....|....
gi 445977555 160 VS---ALSGGQRTKVLLAKLLLEQPEVLLLDEPT 190
Cdd:PRK11614 132 IQragTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
343-465 |
7.18e-06 |
|
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: 48.64 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDflepayfeQEVKADN-------ITPI-------DDVW 408
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG--------QPVTADNreayrqlFSAVfsdfhlfDRLL 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 409 NTFPGLDQHQIRAMLA------KCGLKNEHISRPlsQLSGGeQAKvRLCKLMG--EESNWLLFDE 465
Cdd:COG4615 423 GLDGEADPARARELLErleldhKVSVEDGRFSTT--DLSQG-QRK-RLALLVAllEDRPILVFDE 483
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
354-510 |
7.33e-06 |
|
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: 46.83 E-value: 7.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 354 AIVGCNGVGKSTLLKTILGKIKP-LSGKTSLGDFLEPAYFEQEVKADnitpIDDVWNTFPGLDQHQIR--AMLAKC---- 426
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYALTGeLPPNSKGGAHDPKLIREGEVRAQ----VKLAFENANGKKYTITRslAILENVifch 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 427 -GLKNEHISRPLSQLSGGEQAKV----RLC--KLMGEESNWLLFDEPTNHLDVTAKAE-LKKAMKAYKGT----ILLVCH 494
Cdd:cd03240 102 qGESNWPLLDMRGRCSGGEKVLAsliiRLAlaETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQknfqLIVITH 181
|
170
....*....|....*.
gi 445977555 495 EPDFyEDWITKVWDVE 510
Cdd:cd03240 182 DEEL-VDAADHIYRVE 196
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-196 |
7.64e-06 |
|
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: 47.02 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTpgthygylDQHTVLTPGRTIRDVLAdaFLPlfekek 99
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEID--------GIDISTIPLEDLRSSLT--IIP------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 100 alNEVTEKMGTatpeeleelleqmaeIQDALEAGGFYLlDMKIEEAargLGIDAIGLDrdvsaLSGGQRTKVLLAKLLLE 179
Cdd:cd03369 89 --QDPTLFSGT---------------IRSNLDPFDEYS-DEEIYGA---LRVSEGGLN-----LSQGQRQLLCLARALLK 142
|
170
....*....|....*..
gi 445977555 180 QPEVLLLDEPTNYLDVE 196
Cdd:cd03369 143 RPRVLVLDEATASIDYA 159
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-496 |
7.65e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 47.60 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 339 LLPKLSMTIERGEKIAIVGCNGVGKSTLLKTI--LGKIKP---LSGKTSLG-------DFLEPAYFEQEV-KADNITPID 405
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPearVSGEVYLDgqdifkmDVIELRRRVQMVfQIPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 406 DVW-NTFPGLD-----------QHQIRAMLAKCGLKNEHISR---PLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHL 470
Cdd:PRK14247 98 SIFeNVALGLKlnrlvkskkelQERVRWALEKAQLWDEVKDRldaPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
170 180 190
....*....|....*....|....*....|...
gi 445977555 471 DV--TAKA-----ELKKAMkaykgTILLVCHEP 496
Cdd:PRK14247 178 DPenTAKIeslflELKKDM-----TIVLVTHFP 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
160-195 |
1.03e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 1.03e-05
10 20 30
....*....|....*....|....*....|....*.
gi 445977555 160 VSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV 195
Cdd:PRK10982 389 IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV 424
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
343-494 |
1.03e-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: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDflepayfeQEVKADNItpiddvwNTF---P---GL-- 414
Cdd:COG4152 20 VSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG--------EPLDPEDR-------RRIgylPeerGLyp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 415 -----DQ----------------HQIRAMLAKCGLKnEHISRPLSQLSGGEQAKVRLC-------KLmgeesnwLLFDEP 466
Cdd:COG4152 85 kmkvgEQlvylarlkglskaeakRRADEWLERLGLG-DRANKKVEELSKGNQQKVQLIaallhdpEL-------LILDEP 156
|
170 180 190
....*....|....*....|....*....|.
gi 445977555 467 TNHLDVTAKAELKKAMKAYK--G-TILLVCH 494
Cdd:COG4152 157 FSGLDPVNVELLKDVIRELAakGtTVIFSSH 187
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
151-194 |
1.08e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 47.79 E-value: 1.08e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 445977555 151 IDAIGL-DRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PRK11432 124 VDLAGFeDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-197 |
1.10e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 46.83 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITgQLI--HDQGRVEWTPgthygYLDQHTVL- 77
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFN-RLIelYPEARVSGEV-----YLDGQDIFk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 78 TPGRTIRDVLADAF--------LPLFEkekalnevTEKMGTATPEELEELLEQMAEIQDALEAGGFYlldmkiEEAARGL 149
Cdd:PRK14247 75 MDVIELRRRVQMVFqipnpipnLSIFE--------NVALGLKLNRLVKSKKELQERVRWALEKAQLW------DEVKDRL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 445977555 150 GIDAigldrdvSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEH 197
Cdd:PRK14247 141 DAPA-------GKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPEN 181
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
329-507 |
1.17e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 46.99 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 329 ENVEIGYTHP----LLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD------------------- 385
Cdd:PRK13639 3 ETRDLKYSYPdgteALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkksllevrktvgi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 386 -FLEP--AYFEQEVKAD------NI-TPIDDVwntfpgldQHQIRAMLAKCGLKNeHISRPLSQLSGGEQAKVRLCKLMG 455
Cdd:PRK13639 83 vFQNPddQLFAPTVEEDvafgplNLgLSKEEV--------EKRVKEALKAVGMEG-FENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 456 EESNWLLFDEPTNHLDVTAKAELKKAMKAY--KG-TILLVCHEPDFYEDWITKVW 507
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGiTIIISTHDVDLVPVYADKVY 208
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
123-229 |
1.31e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 123 MAEIQD--ALEAGGFYLLDMKIEE---AARGLGIDAIGLDRDVSALSGGQRTKVLLAKLLL---EQPEVLLLDEPTNYLD 194
Cdd:PRK00635 765 IADILEmtAYEAEKFFLDEPSIHEkihALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLH 844
|
90 100 110
....*....|....*....|....*....|....*...
gi 445977555 195 VEHIHWLTNYLKEYP---HAFLLISHDTEFMNKCVDVI 229
Cdd:PRK00635 845 THDIKALIYVLQSLThqgHTVVIIEHNMHVVKVADYVL 882
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-194 |
1.41e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 46.10 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 8 KLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQlIHDQGRVEWTpgTHYGYLDqhtvltpgrtirdvl 87
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR-TEGNVSVEGD--IHYNGIP--------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 88 ADAFLPLFEKEKALN-EVTEKMGTATpeeleelleqmaeIQDALEAggfylldmkieeAARGLGidaiglDRDVSALSGG 166
Cdd:cd03233 74 YKEFAEKYPGEIIYVsEEDVHFPTLT-------------VRETLDF------------ALRCKG------NEFVRGISGG 122
|
170 180
....*....|....*....|....*...
gi 445977555 167 QRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:cd03233 123 ERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
343-482 |
1.48e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 46.71 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD----FLEPAYFEQEVKA------------DNITPIDD 406
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhFGDYSYRSQRIRMifqdpstslnprQRISQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 407 V---WNT--FPGLDQHQIRAMLAKCGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKA 481
Cdd:PRK15112 112 FplrLNTdlEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINL 191
|
.
gi 445977555 482 M 482
Cdd:PRK15112 192 M 192
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
149-205 |
1.48e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.18 E-value: 1.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 445977555 149 LGIDAIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYL 205
Cdd:PRK11144 116 LGIEPL-LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL 171
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
13-195 |
1.52e-05 |
|
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: 47.81 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 13 FGDRTLfKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGT-----------HYGYLDQHTVLTPGR 81
Cdd:TIGR01193 485 YGSNIL-SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqFINYLPQEPYIFSGS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 82 TIRDVLADAflplfeKEKAlnevtekmgtatpeeleelleqmaEIQDALEAGGFYLLDMKIEEAARGLGIDaigLDRDVS 161
Cdd:TIGR01193 564 ILENLLLGA------KENV------------------------SQDEIWAACEIAEIKDDIENMPLGYQTE---LSEEGS 610
|
170 180 190
....*....|....*....|....*....|....
gi 445977555 162 ALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV 195
Cdd:TIGR01193 611 SISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
338-466 |
1.54e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 46.68 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 338 PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSL-GD--------------------FLEPAYFEQEV 396
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGEnipamsrsrlytvrkrmsmlFQSGALFTDMN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445977555 397 KADNIT-PIDDVWNTFPGLDQHQIRAMLAKCGLKNEHISRPlSQLSGGEQAKVRLCKLMGEESNWLLFDEP 466
Cdd:PRK11831 101 VFDNVAyPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMP-SELSGGMARRAALARAIALEPDLIMFDEP 170
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-268 |
1.55e-05 |
|
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: 47.98 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 11 HTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITgQLIHDQGR-----VEWTPGT------HYGYLDQHTVLTP 79
Cdd:TIGR01271 1227 YTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEiqidgVSWNSVTlqtwrkAFGVIPQKVFIFS 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 80 GrTIRDVLaDAFLPLFEKEkaLNEVTEKMGTATpeeleeLLEQMAEIQD-ALEAGGFylldmkieeaarglgidaigldr 158
Cdd:TIGR01271 1306 G-TFRKNL-DPYEQWSDEE--IWKVAEEVGLKS------VIEQFPDKLDfVLVDGGY----------------------- 1352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 159 dvsALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKeypHAF-----LLISHDTEFMNKCVDVIFhLE 233
Cdd:TIGR01271 1353 ---VLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLK---QSFsnctvILSEHRVEALLECQQFLV-IE 1425
|
250 260 270
....*....|....*....|....*....|....*
gi 445977555 234 FTKMTRYTATyEKFLELAEINKnQHINAYEKQREF 268
Cdd:TIGR01271 1426 GSSVKQYDSI-QKLLNETSLFK-QAMSAADRLKLF 1458
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-194 |
1.97e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.53 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 18 LFKDVSMRLLAGEHVGLVGANGVGKSTFMNII----TGQLIHDQGRVEWTPGTH------YGYLDQHTVLTPGRTIRDVL 87
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagrkTGGYIEGDIRISGFPKKQetfariSGYCEQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 88 A-DAFLPL---FEKEKALNEVTEKMgtatpeeleeLLEQMAEIQDALeaggfylldmkieeaarglgidaIGLDrDVSAL 163
Cdd:PLN03140 975 IySAFLRLpkeVSKEEKMMFVDEVM----------ELVELDNLKDAI-----------------------VGLP-GVTGL 1020
|
170 180 190
....*....|....*....|....*....|.
gi 445977555 164 SGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PLN03140 1021 STEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-194 |
1.98e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 46.86 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 1 MSLLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLD-------- 72
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI---------MLDgqdithvp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 73 ----------QHTVLTPGRTIRDVLADAFlplfekekalnevteKMgTATPEeleelleqmAEIQD-ALEAggfylLDM- 140
Cdd:PRK09452 83 aenrhvntvfQSYALFPHMTVFENVAFGL---------------RM-QKTPA---------AEITPrVMEA-----LRMv 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 445977555 141 KIEEAArglgidaiglDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PRK09452 133 QLEEFA----------QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
303-497 |
2.30e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 46.57 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 303 DRPETAikpeFSFKESRASSRFVFEGENVEIGythplLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTs 382
Cdd:PRK10070 16 EHPQRA----FKYIEQGLSKEQILEKTGLSLG-----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQV- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 383 LGDFLEPAYFE----QEVKADNITPIDDVWNTFPGL-----------------DQHQIRAM--LAKCGLKNEHISRPlSQ 439
Cdd:PRK10070 86 LIDGVDIAKISdaelREVRRKKIAMVFQSFALMPHMtvldntafgmelaginaEERREKALdaLRQVGLENYAHSYP-DE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445977555 440 LSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELK----KAMKAYKGTILLVCHEPD 497
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdelvKLQAKHQRTIVFISHDLD 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
343-480 |
3.11e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 45.65 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGD-----------------FL--EPAYFEQEVKADNITP 403
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplhararrgigYLpqEASIFRRLSVYDNLMA 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 404 IDDVWNTFPGlDQHQIRAMLAKCGLKNEHISRPLSQ-LSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKK 480
Cdd:PRK10895 102 VLQIRDDLSA-EQREDRANELMEEFHIEHLRDSMGQsLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKR 178
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-220 |
3.30e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 45.85 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTF---GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwTPGTHygyLDQHTVLTP 79
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVK-IDGEL---LTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 80 GRTIRDVLADAflplfEKEKALNEVTEKMGTATPEELEELLEQMAEIQDALEAggFYLLDMKIEEAARglgidaigldrd 159
Cdd:PRK13642 80 RRKIGMVFQNP-----DNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLA--VNMLDFKTREPAR------------ 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 160 vsaLSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV---EHIHWLTNYLKEYPHAFLL-ISHDTE 220
Cdd:PRK13642 141 ---LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPtgrQEIMRVIHEIKEKYQLTVLsITHDLD 202
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
343-483 |
3.42e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 45.87 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSG----------KTSLGD------FLEPAYFEQEVKADNI----- 401
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGqifidgedvtHRSIQQrdicmvFQSYALFPHMSLGENVgyglk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 402 ---TPIDDVwntfpgldQHQIRAMLAKCGLKNEHiSRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDvtakAEL 478
Cdd:PRK11432 105 mlgVPKEER--------KQRVKEALELVDLAGFE-DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD----ANL 171
|
....*
gi 445977555 479 KKAMK 483
Cdd:PRK11432 172 RRSMR 176
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
330-494 |
3.46e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 45.47 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 330 NVEIGYT-HPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDFL----------EPAYFEQEV-- 396
Cdd:PRK14271 26 NLTLGFAgKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLlggrsifnyrDVLEFRRRVgm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 397 --KADNITPIDDVWNTFPGLDQHQI----------RAMLAKCGLKN---EHISRPLSQLSGGEQAKVRLCKLMGEESNWL 461
Cdd:PRK14271 106 lfQRPNPFPMSIMDNVLAGVRAHKLvprkefrgvaQARLTEVGLWDavkDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190
....*....|....*....|....*....|....*
gi 445977555 462 LFDEPTNHLDVTAKAELKKAMK--AYKGTILLVCH 494
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRslADRLTVIIVTH 220
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-217 |
3.73e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.40 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 2 SLLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQ----------LIHDQGRVEWTPG--THYG 69
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaykilegdiLFKGESILDLEPEerAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 70 -YLD-QHTVLTPGRTIRDvladaFLPLfekekALNEVTEKMGtatpeeleelleqMAEIqDALEaggFYLLdmkIEEAAR 147
Cdd:CHL00131 86 iFLAfQYPIEIPGVSNAD-----FLRL-----AYNSKRKFQG-------------LPEL-DPLE---FLEI---INEKLK 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445977555 148 GLGIDAIGLDRDVS-ALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLT---NYLKEYPHAFLLISH 217
Cdd:CHL00131 136 LVGMDPSFLSRNVNeGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAegiNKLMTSENSIILITH 209
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-194 |
4.31e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 45.45 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTL-FKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwTPGTHYGYlDQHTVLTPGR 81
Cdd:PRK13639 1 ILETRDLKYSYPDGTEaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL-IKGEPIKY-DKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 82 TIRDVLADA----FLPLFEKEKALNEVTEKMgtatpeeleelleQMAEIQDaleaggfylldmKIEEAARGLGIDaiGLD 157
Cdd:PRK13639 79 TVGIVFQNPddqlFAPTVEEDVAFGPLNLGL-------------SKEEVEK------------RVKEALKAVGME--GFE 131
|
170 180 190
....*....|....*....|....*....|....*...
gi 445977555 158 RDVSA-LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PRK13639 132 NKPPHhLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
343-494 |
5.49e-05 |
|
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: 45.04 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPL---SGK--------TSLGD--------------F------LEPAY 391
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEilfdgedlLKLSEkelrkirgreiqmiFqdpmtsLNPVM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 392 --FEQevkadnitpIDDVWNTFPGLDQHQIRA----MLAKCGLKN--EHISR-PlSQLSGGEQAKV---R--LC--KLmg 455
Cdd:COG0444 104 tvGDQ---------IAEPLRIHGGLSKAEAREraieLLERVGLPDpeRRLDRyP-HELSGGMRQRVmiaRalALepKL-- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 445977555 456 eesnwLLFDEPTNHLDVTAKAE----LKKAMKAYKGTILLVCH 494
Cdd:COG0444 172 -----LIADEPTTALDVTIQAQilnlLKDLQRELGLAILFITH 209
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-229 |
5.57e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 45.18 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 2 SLLTVEKLGHTFGD--RTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQgrvewtpgthygyLDQHTVLTP 79
Cdd:PRK13640 4 NIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD-------------NPNSKITVD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 80 GRTIrdvladaflplfeKEKALNEVTEKMGTA--TPEELEELLEQMAEIQDALEAGGFYLLDMK--IEEAARGLGI-DAI 154
Cdd:PRK13640 71 GITL-------------TAKTVWDIREKVGIVfqNPDNQFVGATVGDDVAFGLENRAVPRPEMIkiVRDVLADVGMlDYI 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445977555 155 glDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV---EHIHWLTNYLKEYPHAFLL-ISHDTEFMNKCVDVI 229
Cdd:PRK13640 138 --DSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPagkEQILKLIRKLKKKNNLTVIsITHDIDEANMADQVL 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-195 |
6.53e-05 |
|
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: 46.06 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 18 LFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwtpgtHYG---YLDQHTVLTPGrTIRDvlaDAFLPL 94
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-----HSGrisFSPQTSWIMPG-TIKD---NIIFGL 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 95 FEKEKALNEVTEKMgtatpeeleelleqmaeiqdALEaggfylldmkiEEAARGLGIDAIGLDRDVSALSGGQRTKVLLA 174
Cdd:TIGR01271 512 SYDEYRYTSVIKAC--------------------QLE-----------EDIALFPEKDKTVLGEGGITLSGGQRARISLA 560
|
170 180
....*....|....*....|.
gi 445977555 175 KLLLEQPEVLLLDEPTNYLDV 195
Cdd:TIGR01271 561 RAVYKDADLYLLDSPFTHLDV 581
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
158-282 |
7.29e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 44.49 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 158 RDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE---HIHWLTNYLKEYPHAFLLISHD----TEFMNKCVDVIF 230
Cdd:PRK15056 138 RQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKteaRIISLLRELRDEGKTMLVSTHNlgsvTEFCDYTVMVKG 217
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 445977555 231 HLEFTKMTRYTATYEKfLELAEINKNQHINAYEKQREFIKKQE-DFIAKNKAR 282
Cdd:PRK15056 218 TVLASGPTETTFTAEN-LELAFSGVLRHVALNGSEESIITDDErPFISHRPAA 269
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-65 |
7.93e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 44.37 E-value: 7.93e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 1 MSLLTVEKLGHTFGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVeWTPG 65
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-LFDG 68
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-217 |
7.95e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 45.51 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 18 LFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGTHYGYLDQHTVLTPGrTIRDVLADAFLPLFEK 97
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLG-TLRDQIIYPDSSEDMK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 98 EKALNE-VTEKMgtatpeeleellEQMAEIQDALEaggfylldmkieeaaRGLGIDAIGLDRDVsaLSGGQRTKVLLAKL 176
Cdd:TIGR00954 546 RRGLSDkDLEQI------------LDNVQLTHILE---------------REGGWSAVQDWMDV--LSGGEKQRIAMARL 596
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 445977555 177 LLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPHAFLLISH 217
Cdd:TIGR00954 597 FYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
149-222 |
8.03e-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: 8.03e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445977555 149 LGIDAIGLDRDVSALSGGQRTKVLLAKLLLEQPE--VLLLDEPTNYLDVEHIHWLTNYLKEY---PHAFLLISHDTEFM 222
Cdd:cd03238 74 VGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVILIEHNLDVL 152
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-223 |
8.45e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 44.39 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 20 KDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwtpgthygyLDQHTVLTPgrtirdvladaflplfEKEK 99
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVT---------VDDITITHK----------------TKDK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 100 ALNEVTEKMGTAtpeeleellEQMAEIQ---DALEAG---GFYLLDMKIEEA---ARGLGIDaIGLDRDVSALS-----G 165
Cdd:PRK13646 79 YIRPVRKRIGMV---------FQFPESQlfeDTVEREiifGPKNFKMNLDEVknyAHRLLMD-LGFSRDVMSQSpfqmsG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445977555 166 GQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLK----EYPHAFLLISHDtefMN 223
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKslqtDENKTIILVSHD---MN 207
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
138-194 |
8.96e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 44.26 E-value: 8.96e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445977555 138 LDMKIEEAARGLGI-----DAigLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:COG1117 127 LDEIVEESLRKAALwdevkDR--LKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
323-496 |
1.01e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 44.06 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 323 RFVFEGENVEIGY-THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTI-----LGKIKPLSGKTSLgdflepayFEQEV 396
Cdd:PRK14267 2 KFAIETVNLRVYYgSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRL--------FGRNI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 397 KADNITPID---------DVWNTFPGLDQHQ---------------------IRAMLAKCGLKNEHISR----PlSQLSG 442
Cdd:PRK14267 74 YSPDVDPIEvrrevgmvfQYPNPFPHLTIYDnvaigvklnglvkskkelderVEWALKKAALWDEVKDRlndyP-SNLSG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 445977555 443 GEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAELKKAMKAYKG--TILLVCHEP 496
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTHSP 208
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
13-224 |
1.03e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 43.71 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 13 FGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVeWTPGTHYGYLDQHTVLTPGRTIRDVLADAFL 92
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKI-WFSGHDITRLKNREVPFLRRQIGMIFQDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 93 plfekekaLNEVTEKMGTATPeeleelleqmaeiqdaLEAGGFYLLDMKIEEAArglGIDAIGL-DRDVS---ALSGGQR 168
Cdd:PRK10908 91 --------LMDRTVYDNVAIP----------------LIIAGASGDDIRRRVSA---ALDKVGLlDKAKNfpiQLSGGEQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 445977555 169 TKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYLKEYPH---AFLLISHDTEFMNK 224
Cdd:PRK10908 144 QRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISR 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
162-218 |
1.17e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.85 E-value: 1.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445977555 162 ALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV----EHIHWLTNYLKEYPHAFLLISHD 218
Cdd:PRK10261 463 EFSGGQRQRICIARALALNPKVIIADEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHD 523
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
336-497 |
1.20e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 43.95 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 336 THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGktslgdflepayfEQEVKADNITPiDDVWN------ 409
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESG-------------QIIIDGDLLTE-ENVWDirhkig 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 410 -TFPGLDQHQIRAML---AKCGLKNEHIS----------------------RPLSQLSGGEQAKVRLCKLMGEESNWLLF 463
Cdd:PRK13650 85 mVFQNPDNQFVGATVeddVAFGLENKGIPheemkervnealelvgmqdfkeREPARLSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 445977555 464 DEPTNHLDVTAKAELKKAMKA----YKGTILLVCHEPD 497
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGirddYQMTVISITHDLD 202
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
163-236 |
1.37e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.35 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 163 LSGGQRTKVLLAKLL---LEQPEVL-LLDEPTNYLDVEHIHWLTNYLKE-YPHA--FLLISHDTEFMNKcVDVIFHLEFT 235
Cdd:cd03227 78 LSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDGQALAEAILEhLVKGaqVIVITHLPELAEL-ADKLIHIKKV 156
|
.
gi 445977555 236 K 236
Cdd:cd03227 157 I 157
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-279 |
1.68e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 43.46 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 4 LTVEKLGHTFGDRTLFK-----DVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygyldqhtvlt 78
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 79 pgrtirdVLADAFLPL-FEKEKALNEVTEKMGTAtpeeleellEQMAE---IQDALE---AGGFYLLDMKIEEAARGLG- 150
Cdd:PRK13645 69 -------IVGDYAIPAnLKKIKEVKRLRKEIGLV---------FQFPEyqlFQETIEkdiAFGPVNLGENKQEAYKKVPe 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 151 -IDAIGLDRDVSA-----LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV----EHIHWLTNYLKEYPHAFLLISHDTE 220
Cdd:PRK13645 133 lLKLVQLPEDYVKrspfeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgeeDFINLFERLNKEYKKRIIMVTHNMD 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445977555 221 FMNKCVDVIFHLEFTKMTRYTATYEKFLELAEINKNQ--HINAYEKQREFIKKQEDFIAKN 279
Cdd:PRK13645 213 QVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIEidPPKLYQLMYKLKNKGIDLLNKN 273
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
162-194 |
1.68e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 1.68e-04
10 20 30
....*....|....*....|....*....|...
gi 445977555 162 ALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
336-471 |
1.73e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.58 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 336 THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLS--------------------GKTSLGDFLEPAYFEQE 395
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtssvvirgsvayvpqvswifNATVRENILFGSDFESE 708
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445977555 396 V--KADNITPIDDVWNTFPGLDQHQIramlakcGLKNEHIsrplsqlSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD 471
Cdd:PLN03232 709 RywRAIDVTALQHDLDLLPGRDLTEI-------GERGVNI-------SGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-194 |
2.19e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 43.19 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 6 VEKLGHTFGDRT-LFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRV-----EWTPGTHYG--------YL 71
Cdd:PRK13647 7 VEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrEVNAENEKWvrskvglvFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 72 DQHTVLTPGRTIRDVladAFLPLfekekalnevteKMGTATpeeleelleqmAEIqdaleaggfyllDMKIEEAARGLGI 151
Cdd:PRK13647 87 DPDDQVFSSTVWDDV---AFGPV------------NMGLDK-----------DEV------------ERRVEEALKAVRM 128
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 445977555 152 DAIGlDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PRK13647 129 WDFR-DKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
163-229 |
2.22e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.25 E-value: 2.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445977555 163 LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD----VEHIHWLTNYLKEYPHAFLLISHDTEFMNKCVDVI 229
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEpttqAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
161-194 |
2.45e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.91 E-value: 2.45e-04
10 20 30
....*....|....*....|....*....|....
gi 445977555 161 SALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANID 181
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
338-498 |
2.51e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 42.71 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 338 PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILG--KIKPLSGK----------------TSLG--------------- 384
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDilfkgesildlepeerAHLGiflafqypieipgvs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 385 --DFLEPAYfEQEVKADNITPIDDVwnTFPGLdqhqIRAMLAKCGLKNEHISRPLSQ-LSGGEQAKVRLCKLMGEESNWL 461
Cdd:CHL00131 101 naDFLRLAY-NSKRKFQGLPELDPL--EFLEI----INEKLKLVGMDPSFLSRNVNEgFSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 445977555 462 LFDEPTNHLDVTAKAELKKAMKAYKGT---ILLVCH--------EPDF 498
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGINKLMTSensIILITHyqrlldyiKPDY 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
157-222 |
2.89e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 42.82 E-value: 2.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445977555 157 DRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE---HIHWLTNYLKEYPHAFLL-ISHD-TEFM 222
Cdd:PRK13648 137 DYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDarqNLLDLVRKVKSEHNITIIsITHDlSEAM 207
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-87 |
3.06e-04 |
|
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: 41.85 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 14 GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNI---------ITGQLIHD--QGRVEWTPGThyGYLDQHTVLTPGRT 82
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVlagrktagvITGEILINgrPLDKNFQRST--GYVEQQDVHSPNLT 95
|
....*
gi 445977555 83 IRDVL 87
Cdd:cd03232 96 VREAL 100
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-478 |
3.39e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.31 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 3 LLTVEKLGHTFGDRTLF----KDVSMRLLAGEHVGLVGANGVGKS----TFMNII--TGQLIHDQGRVEWTPGTHYGYLD 72
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKiaavRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 73 QHTVlTPGRTIRDvlADAFLPLFEKEKALNEVtekMGTATPEELEELLEQMAEIQDALEAGGFYLLDMKIEEAarglgiD 152
Cdd:PRK10261 92 EQSA-AQMRHVRG--ADMAMIFQEPMTSLNPV---FTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEA------Q 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 153 AIgLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDV---EHIHWLTNYL-KEYPHAFLLISHDtefMNKCVDV 228
Cdd:PRK10261 160 TI-LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqAQILQLIKVLqKEMSMGVIFITHD---MGVVAEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 229 ifhleftkMTRYTATYEKflELAEINKNQHInayekqreFIKKQEDFIAKNKARYSTTGrAKSRQKQLDRMELIDRPETA 308
Cdd:PRK10261 236 --------ADRVLVMYQG--EAVETGSVEQI--------FHAPQHPYTRALLAAVPQLG-AMKGLDYPRRFPLISLEHPA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 309 IkpefsfKESRASSRFVFEGENV----EIGYTHPL--------------LPKLSMTIERGEKIAIVGCNGVGKSTLLKTI 370
Cdd:PRK10261 297 K------QEPPIEQDTVVDGEPIlqvrNLVTRFPLrsgllnrvtrevhaVEKVSFDLWPGETLSLVGESGSGKSTTGRAL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 371 LGKIKPLSGKTSLG----DFLePAYFEQEVKAD--------------------NITPIDDVWNTFPG-LDQHQIRAMLAK 425
Cdd:PRK10261 371 LRLVESQGGEIIFNgqriDTL-SPGKLQALRRDiqfifqdpyasldprqtvgdSIMEPLRVHGLLPGkAAAARVAWLLER 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 445977555 426 CGLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAEL 478
Cdd:PRK10261 450 VGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
340-506 |
3.40e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 42.77 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 340 LPKLSMTIERGEKIAIVGCNGVGKSTLL----------------------------------------KTILGKIKPLSG 379
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIehlnalllpdtgtiewifkdeknkkktkekekvleklviqKTRFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 380 -KTSLG---DFLEPAYFEQEVKADNI-TPIDdvWNTFPGLDQHQIRAMLAKCGLKNEHISRPLSQLSGGEQAKVRLCKLM 454
Cdd:PRK13651 103 iRRRVGvvfQFAEYQLFEQTIEKDIIfGPVS--MGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 445977555 455 GEESNWLLFDEPTNHLD-VTAKAELKKAMKAYKG--TILLVCHEPDFYEDWITKV 506
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDpQGVKEILEIFDNLNKQgkTIILVTHDLDNVLEWTKRT 235
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
163-225 |
3.43e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 42.07 E-value: 3.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445977555 163 LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVEHIHWLTNYL----KEYPHAFLLISHDTEFMNKC 225
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDLQLAARC 213
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
133-221 |
3.55e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.20 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 133 GGFYLLDMKIEEAARGLGIDAIGLDRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLDVE---------HIHWLTN 203
Cdd:smart00382 31 GGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqeallllleELRLLLL 110
|
90
....*....|....*...
gi 445977555 204 YLKEYPHAFLLISHDTEF 221
Cdd:smart00382 111 LKSEKNLTVILTTNDEKD 128
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
163-227 |
3.93e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 42.38 E-value: 3.93e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445977555 163 LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD----VEHIHWLTNYLKEYPHAFLLISHdteFMNKCVD 227
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH---YMEEAVE 210
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
162-194 |
3.99e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.46 E-value: 3.99e-04
10 20 30
....*....|....*....|....*....|...
gi 445977555 162 ALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
163-233 |
4.21e-04 |
|
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: 41.82 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 163 LSGGQRTKV------LLAKLLLEQPEVLLLDEPTNYLDVEHI-HWLTNYLKEYPHA--FLLI--SHDTEFMNKcVDVIFH 231
Cdd:cd03240 116 CSGGEKVLAsliirlALAETFGSNCGILALDEPTTNLDEENIeESLAEIIEERKSQknFQLIviTHDEELVDA-ADHIYR 194
|
..
gi 445977555 232 LE 233
Cdd:cd03240 195 VE 196
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-222 |
4.52e-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: 41.93 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 21 DVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEWTPGTHygylDQHTVLTPGRTIRDVLADAFlplfEKEKA 100
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNE----SEPSFEATRSRNRYSVAYAA----QKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 101 LNEVTEK---MGTATPEELEELLEQMAEIQ---DALEAGGfylldmKIEEAARGLGidaigldrdvsaLSGGQRTKVLLA 174
Cdd:cd03290 91 LNATVEEnitFGSPFNKQRYKAVTDACSLQpdiDLLPFGD------QTEIGERGIN------------LSGGQRQRICVA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 445977555 175 KLLLEQPEVLLLDEPTNYLDV---EHI--HWLTNYLKEYPHAFLLISHDTEFM 222
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIhlsDHLmqEGILKFLQDDKRTLVLVTHKLQYL 205
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-194 |
4.56e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 42.01 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 13 FGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNiiTGQLIHDQGRvewtpgthyGYLDQHTVLTPGRTI---RDVLad 89
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLR--TLNRMNDKVS---------GYRYSGDVLLGGRSIfnyRDVL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 90 aflplfekekalnEVTEKMGTATPEELEELLEQMAEIQDALEAggFYLLDMKIEEAARGLGIDAIGL-----DRDVSA-- 162
Cdd:PRK14271 98 -------------EFRRRVGMLFQRPNPFPMSIMDNVLAGVRA--HKLVPRKEFRGVAQARLTEVGLwdavkDRLSDSpf 162
|
170 180 190
....*....|....*....|....*....|...
gi 445977555 163 -LSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PRK14271 163 rLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
343-494 |
5.32e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.14 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSLGDF----LEPA-------------YFEQEVkADNIT--- 402
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvneLEPAdrdiamvfqnyalYPHMSV-RENMAygl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 403 PIDdvwntfpGLDQHQIRAMLAKCG--LKNEHI--SRPlSQLSGGEQAKVRlcklMG----EESNWLLFDEPTNHLD--- 471
Cdd:PRK11650 102 KIR-------GMPKAEIEERVAEAAriLELEPLldRKP-RELSGGQRQRVA----MGraivREPAVFLFDEPLSNLDakl 169
|
170 180
....*....|....*....|....
gi 445977555 472 -VTAKAELKKAMKAYKGTILLVCH 494
Cdd:PRK11650 170 rVQMRLEIQRLHRRLKTTSLYVTH 193
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-61 |
7.05e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.34 E-value: 7.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 445977555 21 DVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVE 61
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
151-194 |
8.58e-04 |
|
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: 41.09 E-value: 8.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 445977555 151 IDAIGL----DRDVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:cd03294 145 LELVGLegweHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-194 |
1.02e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 14 GDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMN---------IITGQLIHDQGR-VEWTPGTHYGYLDQHTVLTPGRTI 83
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNvlaervttgVITGGDRLVNGRpLDSSFQRSIGYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 84 RDVLA-DAFL------PLFEKEKALNEVTEKMGtatpeeleelleqMAEIQDALeaggfylldmkieeaargLGIDAIGL 156
Cdd:TIGR00956 854 RESLRfSAYLrqpksvSKSEKMEYVEEVIKLLE-------------MESYADAV------------------VGVPGEGL 902
|
170 180 190
....*....|....*....|....*....|....*....
gi 445977555 157 DRDvsalsggQRTKVLLAKLLLEQPEVLL-LDEPTNYLD 194
Cdd:TIGR00956 903 NVE-------QRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
343-380 |
1.33e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.50 E-value: 1.33e-03
10 20 30
....*....|....*....|....*....|....*...
gi 445977555 343 LSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGK 380
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGE 379
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
344-379 |
1.55e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 40.29 E-value: 1.55e-03
10 20 30
....*....|....*....|....*....|....*.
gi 445977555 344 SMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSG 379
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAG 61
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-53 |
1.65e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 1.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 445977555 13 FGDRTLFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQL 53
Cdd:NF033858 276 FGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLL 316
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-195 |
1.82e-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: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 18 LFKDVSMRLLAGEHVGLVGANGVGKSTFMNIITGQLIHDQGRVEwtpgtHYG---YLDQHTVLTPGrTIRDVLadaflpL 94
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-----HSGrisFSSQFSWIMPG-TIKENI------I 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 95 FekekalnevtekmGTATPEELEELLEQMAEIQDALeaggfylldMKIEEAarglgiDAIGLDRDVSALSGGQRTKVLLA 174
Cdd:cd03291 120 F-------------GVSYDEYRYKSVVKACQLEEDI---------TKFPEK------DNTVLGEGGITLSGGQRARISLA 171
|
170 180
....*....|....*....|.
gi 445977555 175 KLLLEQPEVLLLDEPTNYLDV 195
Cdd:cd03291 172 RAVYKDADLYLLDSPFGYLDV 192
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
340-510 |
1.92e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.18 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 340 LPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGKTSlgdflepAYFEQEVKADN------ITPIDDVwnTFP- 412
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-------RNGEVSVIAISaglsgqLTGIENI--EFKm 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 413 ---GLDQHQIRAMLAKC---GLKNEHISRPLSQLSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVT-AKAELKK--AMK 483
Cdd:PRK13546 111 lcmGFKRKEIKAMTPKIiefSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTfAQKCLDKiyEFK 190
|
170 180
....*....|....*....|....*..
gi 445977555 484 AYKGTILLVCHEPDFYEDWITKVWDVE 510
Cdd:PRK13546 191 EQNKTIFFVSHNLGQVRQFCTKIAWIE 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
340-467 |
2.02e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 340 LPKLSMTIERGEKIAIVGCNGVGKSTLLKTilgkikpLSG----KTSLGDFL---EPAYFE--------------QEVK- 397
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKV-------LSGvyphGSYEGEILfdgEVCRFKdirdsealgiviihQELAl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 398 ------ADNI---------TPIDdvWN-TFpgldqHQIRAMLAKCGLkNEHISRPLSQLSGGEQAKVRLCKLMGEESNWL 461
Cdd:NF040905 90 ipylsiAENIflgnerakrGVID--WNeTN-----RRARELLAKVGL-DESPDTLVTDIGVGKQQLVEIAKALSKDVKLL 161
|
....*.
gi 445977555 462 LFDEPT 467
Cdd:NF040905 162 ILDEPT 167
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
338-471 |
2.09e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.88 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 338 PLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSG--------------------KTSLGDFLEPAYFEQEV- 396
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDasvvirgtvayvpqvswifnATVRDNILFGSPFDPERy 710
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445977555 397 -KADNITPIDDVWNTFPGLDQHQIramlakcGLKNEHIsrplsqlSGGEQAKVRLCKLMGEESNWLLFDEPTNHLD 471
Cdd:PLN03130 711 eRAIDVTALQHDLDLLPGGDLTEI-------GERGVNI-------SGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
159-194 |
2.40e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.78 E-value: 2.40e-03
10 20 30
....*....|....*....|....*....|....*.
gi 445977555 159 DVSALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:PTZ00265 576 NASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
155-220 |
3.39e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 3.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445977555 155 GLDRDVSALSGGQRTKVLLA-KLLLE-----QPEVLLLDEPTNYLDVEH----IHWLTNYLKEYPHAfLLISHDTE 220
Cdd:PRK03918 781 GKERPLTFLSGGERIALGLAfRLALSlylagNIPLLILDEPTPFLDEERrrklVDIMERYLRKIPQV-IIVSHDEE 855
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-232 |
3.40e-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: 40.38 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 138 LDMKIEEA----------ARGL------GIDAIGLDRDVSALSGGQRTKVLLAKLLLEQ---PEVLLLDEPTNYL---DV 195
Cdd:TIGR00630 789 LDMTVEEAyeffeavpsiSRKLqtlcdvGLGYIRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDI 868
|
90 100 110
....*....|....*....|....*....|....*..
gi 445977555 196 EHIHWLTNYLKEYPHAFLLISHDTEFMnKCVDVIFHL 232
Cdd:TIGR00630 869 KKLLEVLQRLVDKGNTVVVIEHNLDVI-KTADYIIDL 904
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
138-232 |
3.63e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.13 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 138 LDMKIEEA----------ARGL------GIDAIGLDRDVSALSGG--QRTKvlLAKLLLEQ---PEVLLLDEPTNYL--- 193
Cdd:cd03271 129 LDMTVEEAleffenipkiARKLqtlcdvGLGYIKLGQPATTLSGGeaQRIK--LAKELSKRstgKTLYILDEPTTGLhfh 206
|
90 100 110
....*....|....*....|....*....|....*....
gi 445977555 194 DVEHIHWLTNYLKEYPHAFLLISHDTEFMnKCVDVIFHL 232
Cdd:cd03271 207 DVKKLLEVLQRLVDKGNTVVVIEHNLDVI-KCADWIIDL 244
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
340-380 |
3.78e-03 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 39.09 E-value: 3.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 445977555 340 LPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGK 380
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGR 61
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
325-494 |
3.81e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 39.25 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 325 VFEGENVEIGY-THPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTI-----L-------GKIKplsgktslgdflepaY 391
Cdd:COG1117 11 KIEVRNLNVYYgDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLipgarveGEIL---------------L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 392 FEQEVKADNITPID------DVW---NTFP---------GLDQHQIRAM----------LAKCGLKNE---HISRPLSQL 440
Cdd:COG1117 76 DGEDIYDPDVDVVElrrrvgMVFqkpNPFPksiydnvayGLRLHGIKSKseldeiveesLRKAALWDEvkdRLKKSALGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 441 SGGEQAkvRLC---------KLmgeesnwLLFDEPTNHLDV--TAK-----AELKKAMkaykgTILLVCH 494
Cdd:COG1117 156 SGGQQQ--RLCiaralavepEV-------LLMDEPTSALDPisTAKieeliLELKKDY-----TIVIVTH 211
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
34-218 |
4.04e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.84 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 34 LVGANGVGKSTFMNIIT--------------GQLIH---DQGRVE---WTPGTHYgyldqhTVLTP-GRTIRDVLADAFl 92
Cdd:COG0419 28 IVGPNGAGKSTILEAIRyalygkarsrsklrSDLINvgsEEASVElefEHGGKRY------RIERRqGEFAEFLEAKPS- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 93 plfEKEKALNEV--TEKMGTAtpeeleelLEQMAEIQDALEAggfylldmKIEEAARGLGIDAIGLDR-----DVSALSG 165
Cdd:COG0419 101 ---ERKEALKRLlgLEIYEEL--------KERLKELEEALES--------ALEELAELQKLKQEILAQlsgldPIETLSG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 445977555 166 GQRTKVLLAKLLleqpeVLLLDepTNYLDVEHIHWLTNYLKEyphaFLLISHD 218
Cdd:COG0419 162 GERLRLALADLL-----SLILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
155-196 |
7.00e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.11 E-value: 7.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 445977555 155 GLDRDVSALSGGQRT------KVLLAKLLLEQPEVLLLDEPTNYLDVE 196
Cdd:PRK01156 794 GMVEGIDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDED 841
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
440-477 |
7.04e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 7.04e-03
10 20 30
....*....|....*....|....*....|....*...
gi 445977555 440 LSGGEQAKVRLCKLMGEESNWLLFDEPTNHLDVTAKAE 477
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYE 442
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-245 |
7.13e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.19 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 30 EHVGLVGANGVGKSTFMNIITGQLIHDQGRVewtpgthygYLDQHTVLTPGRT-IRDVLadAFLP----LFEkekalnev 104
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRI---------MIDDCDVAKFGLTdLRRVL--SIIPqspvLFS-------- 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445977555 105 tekmGTATPEELEELLEQMAEIQDALEAGgfylldmKIEEAARGlgiDAIGLDRDVS----ALSGGQRTKVLLAKLLLEQ 180
Cdd:PLN03232 1324 ----GTVRFNIDPFSEHNDADLWEALERA-------HIKDVIDR---NPFGLDAEVSeggeNFSVGQRQLLSLARALLRR 1389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445977555 181 PEVLLLDEPTNYLDVEHIHWLTNYLKEYPHA--FLLISHDTEFMNKCvDVIFHLEFTKMTRYTATYE 245
Cdd:PLN03232 1390 SKILVLDEATASVDVRTDSLIQRTIREEFKSctMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQE 1455
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
161-194 |
8.89e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 38.52 E-value: 8.89e-03
10 20 30
....*....|....*....|....*....|....
gi 445977555 161 SALSGGQRTKVLLAKLLLEQPEVLLLDEPTNYLD 194
Cdd:COG1135 139 SQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-51 |
9.45e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.62 E-value: 9.45e-03
10 20 30
....*....|....*....|....*....|.
gi 445977555 21 DVSMRLLAGEHVGLVGANGVGKSTFMNIITG 51
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
330-380 |
9.60e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 38.72 E-value: 9.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 445977555 330 NVEIGYTHPLLPKLSMTIERGEKIAIVGCNGVGKSTLLKTILGKIKPLSGK 380
Cdd:PRK13545 30 RSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT 80
|
|
| |
