|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-506 |
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: 585.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 6 IEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQNPEFYKGDTILT 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 86 SIVRENEGQDHV---------------------------------WDLESQAKTMLTKLGFT--DFDILVETLSGGQRKR 130
Cdd:COG0488 81 TVLDGDAELRALeaeleeleaklaepdedlerlaelqeefealggWEAEARAEEILSGLGFPeeDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 131 VALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKLFSYQTNkvnggga 210
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGN------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 211 drestqgcYEEYLKLKAERLDLLEASERKRQSILRVELQWMQR-GARAR-STKQKAHIERYETLRDQKGLETDQAVELD- 287
Cdd:COG0488 234 --------YSAYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRfRAKARkAKQAQSRIKALEKLEREEPPRRDKTVEIRf 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 288 SIESRLGRTTVELEGISKAYGDKVLMKDFTYILLKNDRigiigpngggKSTLMKIIAGWVEPDEGTITVGQTVKMGYFSQ 367
Cdd:COG0488 306 PPPERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRigligpngagKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 368 ENEELDGRLKVIDYIRGAAEyvktKDGSVSASQMLERFLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTN 447
Cdd:COG0488 386 HQEELDPDKTVLDELRDGAP----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTN 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 448 DLDIQTLTILEDYLESFPGIVITVSHDRYFLDRVVRRIFAFEgNGMVTQYEGGFTDYQA 506
Cdd:COG0488 462 HLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFE-DGGVREYPGGYDDYLE 519
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-506 |
1.22e-139 |
|
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: 417.80 E-value: 1.22e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 5 TIEHMTKSY-TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQNPEFykgDTI 83
Cdd:TIGR03719 6 TMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQL---DPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 84 LTsiVREN--EG-----------------------------------QDHV-----WDLESQAKTMLTKLGFTDFDILVE 121
Cdd:TIGR03719 83 KT--VRENveEGvaeikdaldrfneisakyaepdadfdklaaeqaelQEIIdaadaWDLDSQLEIAMDALRCPPWDADVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 122 TLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKLFSYQ 201
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 202 TNkvngggadrestqgcYEEYLKLKAERLDLLEASERKRQSILRVELQWMQRGARARSTKQKAHIERYETLRDQkglETD 281
Cdd:TIGR03719 241 GN---------------YSSWLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLARYEELLSQ---EFQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 282 QAVELDSIE----SRLGRTTVELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITVG 357
Cdd:TIGR03719 303 KRNETAEIYippgPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 358 QTVKMGYFSQENEELDGRLKVIDYIRGAAEYVKTKDGSVSASQMLERFLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAP 437
Cdd:TIGR03719 383 ETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGG 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 438 NVLLLDEPTNDLDIQTLTILEDYLESFPGIVITVSHDRYFLDRVVRRIFAFEGNGMVTQYEGGFTDYQA 506
Cdd:TIGR03719 463 NVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEWFEGNFSEYEE 531
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-506 |
2.24e-138 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 414.52 E-value: 2.24e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 5 TIEHMTKSY-TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQNPEFykgDTI 83
Cdd:PRK11819 8 TMNRVSKVVpPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQL---DPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 84 LTsiVREN--EG-----------------------------------QDHV-----WDLESQAKTMLTKLGFTDFDILVE 121
Cdd:PRK11819 85 KT--VRENveEGvaevkaaldrfneiyaayaepdadfdalaaeqgelQEIIdaadaWDLDSQLEIAMDALRCPPWDAKVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 122 TLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKLFSYQ 201
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 202 TNkvngggadrestqgcYEEYLKLKAERLDLLEASERKRQSILRVELQWMQRGARARSTKQKAHIERYETLRDQkglETD 281
Cdd:PRK11819 243 GN---------------YSSWLEQKAKRLAQEEKQEAARQKALKRELEWVRQSPKARQAKSKARLARYEELLSE---EYQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 282 QAVELDSIE----SRLGRTTVELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITVG 357
Cdd:PRK11819 305 KRNETNEIFippgPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 358 QTVKMGYFSQENEELDGRLKVIDYIRGAAEYVKTKDGSVSASQMLERFLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAP 437
Cdd:PRK11819 385 ETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKVGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGG 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 438 NVLLLDEPTNDLDIQTLTILEDYLESFPGIVITVSHDRYFLDRVVRRIFAFEGNGMVTQYEGGFTDYQA 506
Cdd:PRK11819 465 NVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDSQVEWFEGNFQEYEE 533
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-618 |
2.46e-108 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 339.62 E-value: 2.46e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQNP----- 75
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPprnve 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 76 ---------------EFYKG-------------DTILTSIVRENEGQDH--VWDLESQAKTMLTKLGFtDFDILVETLSG 125
Cdd:PRK11147 81 gtvydfvaegieeqaEYLKRyhdishlvetdpsEKNLNELAKLQEQLDHhnLWQLENRINEVLAQLGL-DPDAALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 126 GQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKLFSYQTNkv 205
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGN-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 206 ngggadrestqgcYEEYLKLKAE--RLDLLEASERKRQsiLRVELQWMQRGARARSTKQKAHIERYETLRDQKG------ 277
Cdd:PRK11147 238 -------------YDQYLLEKEEalRVEELQNAEFDRK--LAQEEVWIRQGIKARRTRNEGRVRALKALRRERSerrevm 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 278 ----LETDQAveldsieSRLGRTTVELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGT 353
Cdd:PRK11147 303 gtakMQVEEA-------SRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 354 ITVGQTVKMGYFSQENEELDGRLKVIDYIRGAAEYVKTKDGSVSASQMLERFLFPSSVQYTTIEKLSGGEKRRLYLLRIL 433
Cdd:PRK11147 376 IHCGTKLEVAYFDQHRAELDPEKTVMDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLF 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 434 MEAPNVLLLDEPTNDLDIQTLTILEDYLESFPGIVITVSHDRYFLDRVVRRIFAFEGNGMVTQYEGGFTDYQAAYSEKHP 513
Cdd:PRK11147 456 LKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGYHDARQQQAQYLA 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 514 egiLEQSDKKEKKTAAQEKTNPGKKqreRKLKFSFHEQREWDTIEDEITSLEDSIEELENEIlkAASDY---------SK 584
Cdd:PRK11147 536 ---LKQPAVKKKEEAAAPKAETVKR---SSKKLSYKLQRELEQLPQLLEDLEAEIEALQAQV--ADADFfsqpheqtqKV 607
|
650 660 670
....*....|....*....|....*....|....
gi 1524013779 585 LAKLMEEKEEKETCLndkmERWLELnelaEQIKN 618
Cdd:PRK11147 608 LADLADAEQELEVAF----ERWEEL----EALKN 633
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-224 |
6.00e-64 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 219.17 E-value: 6.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQNPEFYKGD- 81
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDk 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 82 TILTSIVRENEGQDhvwdlESQAKTMLTKLGFTDFDIL--VETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAE 159
Cdd:COG0488 395 TVLDELRDGAPGGT-----EQEVRGYLGRFLFSGDDAFkpVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLE 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 160 WLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKLFSYQTNkvngggadrestqgcYEEYLK 224
Cdd:COG0488 470 ALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGG---------------YDDYLE 519
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-616 |
2.68e-62 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 217.73 E-value: 2.68e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 16 RLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQ----------------NPEFYK 79
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQetpalpqpaleyvidgDREYRQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 80 GDTILTSIVRENEGQD-----------HVWDLESQAKTMLTKLGFTDFDIL--VETLSGGQRKRVALVSVLLSTADLLVL 146
Cdd:PRK10636 94 LEAQLHDANERNDGHAiatihgkldaiDAWTIRSRAASLLHGLGFSNEQLErpVSDFSGGWRMRLNLAQALICRSDLLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 147 DEPTNHLDSSMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKLFSYQTNkvngggadrestqgcYEEYLKLK 226
Cdd:PRK10636 174 DEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGN---------------YSSFEVQR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 227 AERLDLLEASERKRQSilRV-ELQWMQRGARARSTKQKAHIERYETLrdqKGLETDQAVELDS--------IESrLGRTT 297
Cdd:PRK10636 239 ATRLAQQQAMYESQQE--RVaHLQSYIDRFRAKATKAKQAQSRIKML---ERMELIAPAHVDNpfhfsfraPES-LPNPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITVGQTVKMGYFSQENEEldgrlk 377
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLE------ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 378 vidYIRgaAEYVKTKDGSVSASQMLER--------FLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDL 449
Cdd:PRK10636 387 ---FLR--ADESPLQHLARLAPQELEQklrdylggFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 450 DIQTLTILEDYLESFPGIVITVSHDRYFLDRVVRRIFAFEgNGMVTQYEGGFTDYQAAYSE-KHPEGILEQSDKKEKKTA 528
Cdd:PRK10636 462 DLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVH-DGKVEPFDGDLEDYQQWLSDvQKQENQTDEAPKENNANS 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 529 AQEKtnpgKKQRERKLKFSFHEQ---REWDTIEDEITSLEDSIEELENEI----LKAASDYSKLAKLMEEKEEKETCLND 601
Cdd:PRK10636 541 AQAR----KDQKRREAELRTQTQplrKEIARLEKEMEKLNAQLAQAEEKLgdseLYDQSRKAELTACLQQQASAKSGLEE 616
|
650
....*....|....*
gi 1524013779 602 KMERWLELNELAEQI 616
Cdd:PRK10636 617 CEMAWLEAQEQLEQM 631
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-504 |
3.02e-62 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 215.14 E-value: 3.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 18 LFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQNPEFYK----------GDTILTSI 87
Cdd:PRK15064 16 LFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEeftvldtvimGHTELWEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 88 VRENEG---------QD--HVWDLESQ------------AKTMLTKLGftdfdILVETLSG-------GQRKRVALVSVL 137
Cdd:PRK15064 96 KQERDRiyalpemseEDgmKVADLEVKfaemdgytaearAGELLLGVG-----IPEEQHYGlmsevapGWKLRVLLAQAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 138 LSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKLFSYQTNkvngggadrestqg 217
Cdd:PRK15064 171 FSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGN-------------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 218 cYEEYLKLKAE-RLDLLEASERKRQSIlrVELQ-WMQR-GARARSTKQKahieryetlrdqkgleTDQAVELDSIE---- 290
Cdd:PRK15064 237 -YDEYMTAATQaRERLLADNAKKKAQI--AELQsFVSRfSANASKAKQA----------------TSRAKQIDKIKleev 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 291 ---SR------------LGRTTVELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTIT 355
Cdd:PRK15064 298 kpsSRqnpfirfeqdkkLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 356 VGQTVKMGYFSQENE-ELDGRLKVIDYIrgaAEYVKTKDGSVSASQMLERFLFPSSVQYTTIEKLSGGEKRRLYLLRILM 434
Cdd:PRK15064 378 WSENANIGYYAQDHAyDFENDLTLFDWM---SQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMM 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 435 EAPNVLLLDEPTNDLDIQTLTILEDYLESFPGIVITVSHDRYFLDRVVRRIFAFEGNGMVtQYEGGFTDY 504
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVV-DFSGTYEEY 523
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-196 |
4.28e-56 |
|
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: 186.12 E-value: 4.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQnpefykgdti 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 84 ltsivrenegqdhvwdlesqaktmltklgftdfdilvetLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEE 163
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|...
gi 1524013779 164 YLRSFNGALLMVTHDRYFLDSVTNRIVELDKGK 196
Cdd:cd03221 112 ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
300-554 |
1.60e-49 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 179.88 E-value: 1.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 300 LEGISKAYGDKVLMKDFTYILLKNDRigiigpngggKSTLMKIIAGWVEPDEGTITVGQTVKMGYFSQENEELDGRlKVI 379
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRiglvgrngagKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDL-TVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 380 DYIRGAAE------------YVKTKDGSVS----------------------ASQMLERFLFPSSVQYTTIEKLSGGEKR 425
Cdd:COG0488 80 DTVLDGDAelraleaeleelEAKLAEPDEDlerlaelqeefealggweaearAEEILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 426 RLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFPGIVITVSHDRYFLDRVVRRIFAFEgNGMVTQYEGGFTDYq 505
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELD-RGKLTLYPGNYSAY- 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1524013779 506 aaysekhpegiLEQSDKKEKKTAAQEKtnpgKKQRERKlkfsfHEQrEW 554
Cdd:COG0488 238 -----------LEQRAERLEQEAAAYA----KQQKKIA-----KEE-EF 265
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
298-492 |
3.23e-47 |
|
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: 162.62 E-value: 3.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITVGQTVKMGYFSQeneeldgrlk 377
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 378 vidyirgaaeyvktkdgsvsasqmlerflfpssvqyttiekLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTIL 457
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*
gi 1524013779 458 EDYLESFPGIVITVSHDRYFLDRVVRRIFAFEGNG 492
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-197 |
3.42e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.82 E-value: 3.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRFLP 72
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyLDGKPLSampppewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 73 QNPEFYkGDTILTSIVRENEGQDHVWDLEsQAKTMLTKLGFTDfDIL---VETLSGGQRKRVALVSVLLSTADLLVLDEP 149
Cdd:COG4619 81 QEPALW-GGTVRDNLPFPFQLRERKFDRE-RALELLERLGLPP-DILdkpVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 150 TNHLDSSMA----EWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:COG4619 158 TSALDPENTrrveELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-196 |
7.51e-42 |
|
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: 150.32 E-value: 7.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTVR---------FLP 72
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVlWNGEPIRDAredyrrrlaYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 73 QNPEFYKGdtiLTsiVREN----EGQDHVWDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLD 147
Cdd:COG4133 82 HADGLKPE---LT--VRENlrfwAALYGLRADREAIDEALEAVGLAGLaDLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 148 EPTNHLDSSMAEWLEEYLRSFN---GALLMVTHDRYFLDSVtnRIVELDKGK 196
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA--RVLDLGDFK 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-196 |
1.13e-40 |
|
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: 147.23 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 6 IEHMTKSY--TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRFLP 72
Cdd:cd03225 2 LKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlVDGKDLTklslkelrrkVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 73 QNPEfykgDTILTSIVRE-------NEGQDHVWDLEsQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLL 144
Cdd:cd03225 82 QNPD----DQFFGPTVEEevafgleNLGLPEEEIEE-RVEEALELVGLEGLrDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 145 VLDEPTNHLDSSMAEWLEEYLRSFNGA---LLMVTHDRYFLDSVTNRIVELDKGK 196
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-505 |
4.67e-40 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 156.17 E-value: 4.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 6 IEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAgLEEPD-----------EGKVVkGRNLTV------ 68
Cdd:PLN03073 180 MENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA-MHAIDgipkncqilhvEQEVV-GDDTTAlqcvln 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 69 -------------------RFLPQNPEFYKG----------DTI---LTSIVRENEGQDhVWDLESQAKTMLTKLGFTDf 116
Cdd:PLN03073 258 tdiertqlleeeaqlvaqqRELEFETETGKGkgankdgvdkDAVsqrLEEIYKRLELID-AYTAEARAASILAGLSFTP- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 117 DILVE---TLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELD 193
Cdd:PLN03073 336 EMQVKatkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLH 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 194 KGKLFSYqtnkvngggadrestQGCYEEYLKLKAERL----DLLEASERKRQSILRVELQWMQRGARAR--STKQKAhIE 267
Cdd:PLN03073 416 GQKLVTY---------------KGDYDTFERTREEQLknqqKAFESNERSRSHMQAFIDKFRYNAKRASlvQSRIKA-LD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 268 RYETLrDQKGLETDQAVELDSIESRLGRTTVELEGISKAY-GDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGW 346
Cdd:PLN03073 480 RLGHV-DAVVNDPDYKFEFPTPDDRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 347 VEPDEGTITVGQTVKMGYFSQEN-EELDGRLKVIDYIR----GAAEY-VKTKDGSVSASQMLErfLFPssvQYTtiekLS 420
Cdd:PLN03073 559 LQPSSGTVFRSAKVRMAVFSQHHvDGLDLSSNPLLYMMrcfpGVPEQkLRAHLGSFGVTGNLA--LQP---MYT----LS 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 421 GGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFPGIVITVSHDRYFLDRVVRRIFAFEgNGMVTQYEGG 500
Cdd:PLN03073 630 GGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVS-EGKVTPFHGT 708
|
....*
gi 1524013779 501 FTDYQ 505
Cdd:PLN03073 709 FHDYK 713
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-197 |
6.15e-39 |
|
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: 142.86 E-value: 6.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYT-ERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTVRFLP--------- 72
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlVDGKDITKKNLRelrrkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 73 -QNPEfykgDTILTSIVRE-------NEGQDHVwDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADL 143
Cdd:COG1122 81 fQNPD----DQLFAPTVEEdvafgpeNLGLPRE-EIRERVEEALELVGLEHLaDRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1524013779 144 LVLDEPTNHLDSSMAEWLEEYLRSFNGA---LLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-197 |
1.28e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 139.43 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT-----VR----FLPQ 73
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrVLGEDVArdpaeVRrrigYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 74 NPEFYKGdtiLTsiVRENE-------GQDHVwDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLV 145
Cdd:COG1131 81 EPALYPD---LT--VRENLrffarlyGLPRK-EARERIDELLELFGLTDAaDRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 146 LDEPTNHLDSSMAEWLEEYLRSFNG---ALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-197 |
1.72e-37 |
|
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: 137.14 E-value: 1.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT---------VRFLPQ 73
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkVLGKDIKkepeevkrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 74 NPEFYKGdtiLTsiVRENegqdhvwdLEsqaktmltklgftdfdilvetLSGGQRKRVALVSVLLSTADLLVLDEPTNHL 153
Cdd:cd03230 81 EPSLYEN---LT--VREN--------LK---------------------LSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1524013779 154 DSSMAEWLEEYLRSFN---GALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03230 127 DPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-197 |
2.46e-37 |
|
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: 138.84 E-value: 2.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV------VKGRNLTVR----FLP 72
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedVRKEPREARrqigVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 73 QNPEFYKGDTiltsiVRENEG----QDHVWDLESQAKT--MLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLV 145
Cdd:COG4555 81 DERGLYDRLT-----VRENIRyfaeLYGLFDEELKKRIeeLIELLGLEEFlDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 146 LDEPTNHLDSSMAEWLEEYLRSF---NGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-199 |
4.98e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.22 E-value: 4.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTVR-----FLPQN 74
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrLFGKPPRRArrrigYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 75 PEFYKG------DTILTSIVREN--------EGQDHVWDLesqaktmLTKLGFTDF-DILVETLSGGQRKRVALVSVLLS 139
Cdd:COG1121 84 AEVDWDfpitvrDVVLMGRYGRRglfrrpsrADREAVDEA-------LERVGLEDLaDRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 140 TADLLVLDEPTNHLDSSMAEWLEEYLRSFNG---ALLMVTHDryfLDSVT---NRIVELDKGKLFS 199
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHD---LGAVReyfDRVLLLNRGLVAH 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-196 |
8.39e-34 |
|
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: 126.21 E-value: 8.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 5 TIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTVRFLPqnpefykgdti 83
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIlIDGKDIAKLPLE----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 84 ltsivrenEGQDHVwdlesqaktmltklgftdfdILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEE 163
Cdd:cd00267 70 --------ELRRRI--------------------GYVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLE 121
|
170 180 190
....*....|....*....|....*....|....*.
gi 1524013779 164 YLRSFNG---ALLMVTHDRYFLDSVTNRIVELDKGK 196
Cdd:cd00267 122 LLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-224 |
1.17e-33 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 135.02 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 2 NLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQNPEF-YKG 80
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYdFEN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 81 DTILTSIVRE--NEGQDhvwdlESQAKTMLTKLGFTDFDIL--VETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSS 156
Cdd:PRK15064 398 DLTLFDWMSQwrQEGDD-----EQAVRGTLGRLLFSQDDIKksVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 157 MAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKLFSYqtnkvngggadrestQGCYEEYLK 224
Cdd:PRK15064 473 SIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDF---------------SGTYEEYLR 525
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-230 |
6.84e-33 |
|
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: 133.14 E-value: 6.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 6 IEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQNPEFYKGD-TIL 84
Cdd:TIGR03719 325 AENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNkTVW 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 85 TSIvreNEGQDH--VWDLESQAKTMLTKLGF--TDFDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEW 160
Cdd:TIGR03719 405 EEI---SGGLDIikLGKREIPSRAYVGRFNFkgSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 161 LEEYLRSFNGALLMVTHDRYFLDSVTNRIVeldkgklfSYQtnkvngGGADRESTQGCYEEYLKLKAERL 230
Cdd:TIGR03719 482 LEEALLNFAGCAVVISHDRWFLDRIATHIL--------AFE------GDSHVEWFEGNFSEYEEDKKRRL 537
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-200 |
3.29e-32 |
|
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: 122.54 E-value: 3.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 5 TIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLtvrflpqnpefykgdti 83
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlLDGKDL----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 84 ltsivrenegqdHVWDLESQAKTM------LTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLD-- 154
Cdd:cd03214 64 ------------ASLSPKELARKIayvpqaLELLGLAHLaDRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDia 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1524013779 155 --SSMAEWLEEYLRSFNGALLMVTHD-----RYFldsvtNRIVELDKGKLFSY 200
Cdd:cd03214 132 hqIELLELLRRLARERGKTVVMVLHDlnlaaRYA-----DRVILLKDGRIVAQ 179
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-482 |
9.30e-32 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 129.25 E-value: 9.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYT--ERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEePDEGKV-----VKGRNLT-------- 67
Cdd:COG1123 4 LLEVRDLSVRYPggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRIsgevlLDGRDLLelsealrg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 --VRFLPQNPE-----FYKGDTILTSIVRENEGQDHVWDlesQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLS 139
Cdd:COG1123 83 rrIGMVFQDPMtqlnpVTVGDQIAEALENLGLSRAEARA---RVLELLEAVGLERRlDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 140 TADLLVLDEPTNHLDSSMA----EWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKLfsyqtnkVNGGGADREST 215
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQaeilDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI-------VEDGPPEEILA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 216 QGCYEEYLKLKAERLDLLEASERKRQSILRVElqwmqrgararstkqkaHIERYETLRDQKGLetdQAVElD-SIESRLG 294
Cdd:COG1123 233 APQALAAVPRLGAARGRAAPAAAAAEPLLEVR-----------------NLSKRYPVRGKGGV---RAVD-DvSLTLRRG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 295 RTTveleGI-----SkayGdkvlmkdftyillkndrigiigpngggKSTLMKIIAGWVEPDEGTITV-GQTV-------- 360
Cdd:COG1123 292 ETL----GLvgesgS---G---------------------------KSTLARLLLGLLRPTSGSILFdGKDLtklsrrsl 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 361 -----KMGY-----FSQeneeLDGRLKVIDYIRGAAEYVKTKDGSVS---ASQMLERFLFPSSVQYTTIEKLSGGEKRRL 427
Cdd:COG1123 338 relrrRVQMvfqdpYSS----LNPRMTVGDIIAEPLRLHGLLSRAERrerVAELLERVGLPPDLADRYPHELSGGQRQRV 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 428 YLLRILMEAPNVLLLDEPTNDLDI----QTLTILEDYLESFpGI-VITVSHD----RYFLDRVV 482
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVsvqaQILNLLRDLQREL-GLtYLFISHDlavvRYIADRVA 476
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-200 |
1.62e-31 |
|
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: 122.84 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRFL 71
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlLDGRDLAslsrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 72 PQNPEFYKG----DTIL------TSIVRENEGQDHvwdleSQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLST 140
Cdd:COG1120 81 PQEPPAPFGltvrELVAlgryphLGLFGRPSAEDR-----EAVEEALERTGLEHLaDRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 141 ADLLVLDEPTNHLDssMA------EWLEEYLRSFNGALLMVTHD-----RYFldsvtNRIVELDKGKLFSY 200
Cdd:COG1120 156 PPLLLLDEPTSHLD--LAhqlevlELLRRLARERGRTVVMVLHDlnlaaRYA-----DRLVLLKDGRIVAQ 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-199 |
1.97e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 121.49 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 6 IEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT-----VRFLPQNPEFYK 79
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrVFGKPLEkerkrIGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 80 G------DTILTSIVRENEGQDHVWDLESQ-AKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEPTN 151
Cdd:cd03235 82 DfpisvrDVVLMGLYGHKGLFRRLSKADKAkVDEALERVGLSELaDRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 152 HLDSSMAEWLEEYLRSFNG---ALLMVTHDryfLDSVT---NRIVELDKGKLFS 199
Cdd:cd03235 162 GVDPKTQEDIYELLRELRRegmTILVVTHD---LGLVLeyfDRVLLLNRTVVAS 212
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-197 |
5.00e-31 |
|
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: 121.45 E-value: 5.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSY----TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT---------- 67
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtFDGRPVTrrrrkafrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 VRFLPQNPE-----FYKGDTILTSIVRENEGQDHvwdlESQAKTMLTKLGFTDfDIL---VETLSGGQRKRVALVSVLLS 139
Cdd:COG1124 81 VQMVFQDPYaslhpRHTVDRILAEPLRIHGLPDR----EERIAELLEQVGLPP-SFLdryPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 140 TADLLVLDEPTNHLDSS----MAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:COG1124 156 EPELLLLDEPTSALDVSvqaeILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-197 |
6.50e-31 |
|
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: 120.29 E-value: 6.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSY----TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTvrflpqnpefY 78
Cdd:cd03255 1 IELKNLSKTYggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrVDGTDIS----------K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 79 KGDTILTSIVRENEG---QDH----------------------VWDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVA 132
Cdd:cd03255 71 LSEKELAAFRRRHIGfvfQSFnllpdltalenvelplllagvpKKERRERAEELLERVGLGDRlNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 133 LVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNG----ALLMVTHDRyFLDSVTNRIVELDKGKL 197
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeagtTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-197 |
1.38e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 125.79 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTER-----LLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT--------- 67
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlFDGKDLTklsrrslre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 ----VRFLPQNPE--FYKGDTILTSIVR--ENEGQDHVWDLESQAKTMLTKLG-FTDF-DILVETLSGGQRKRVALVSVL 137
Cdd:COG1123 340 lrrrVQMVFQDPYssLNPRMTVGDIIAEplRLHGLLSRAERRERVAELLERVGlPPDLaDRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 138 LSTADLLVLDEPTNHLDSS----MAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSvqaqILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-178 |
5.70e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 118.65 E-value: 5.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSYT----ERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV------VKGRNLTVRF 70
Cdd:COG1116 5 APALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVlvdgkpVTGPGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 LPQNPefykgdTIL---TsiVREN-----EGQDHVWD-LESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLST 140
Cdd:COG1116 85 VFQEP------ALLpwlT--VLDNvalglELRGVPKAeRRERARELLELVGLAGFeDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1524013779 141 ADLLVLDEPTNHLDS----SMAEWLEEYLRSFNGALLMVTHD 178
Cdd:COG1116 157 PEVLLMDEPFGALDAltreRLQDELLRLWQETGKTVLFVTHD 198
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-197 |
1.15e-29 |
|
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: 123.72 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTE--RLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNL------TVR----F 70
Cdd:COG4987 334 LELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItLGGVDLrdldedDLRrriaV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 LPQNPEFYKG---DTILtsIVRENEGQDHVWDlesqaktMLTKLGFTDF--------DILV----ETLSGGQRKRVALVS 135
Cdd:COG4987 414 VPQRPHLFDTtlrENLR--LARPDATDEELWA-------ALERVGLGDWlaalpdglDTWLgeggRRLSGGERRRLALAR 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 136 VLLSTADLLVLDEPTNHLDSSMA-EWLEEYLRSFNG-ALLMVTHDRYFLDSVtNRIVELDKGKL 197
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEqALLADLLEALAGrTVLLITHRLAGLERM-DRILVLEDGRI 547
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-151 |
1.36e-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: 114.28 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 19 FDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRFLPQNPEFYKGDTILTSI 87
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlLDGQDLTdderkslrkeIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 88 --VRENEGQDHVWDlESQAKTMLTKLGFTDF-----DILVETLSGGQRKRVALVSVLLSTADLLVLDEPTN 151
Cdd:pfam00005 81 rlGLLLKGLSKREK-DARAEEALEKLGLGDLadrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-196 |
1.60e-29 |
|
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: 114.98 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTvrflpqnpefykgdt 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIlIDGEDLT--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 83 iltsivrenegqdhvwDLESQAKTMLTKLGF-----------TDFDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTN 151
Cdd:cd03229 66 ----------------DLEDELPPLRRRIGMvfqdfalfphlTVLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1524013779 152 HLDSSMAEWLEEYLRS----FNGALLMVTHDRYFLDSVTNRIVELDKGK 196
Cdd:cd03229 130 ALDPITRREVRALLKSlqaqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-197 |
2.07e-29 |
|
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: 115.43 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 5 TIEHMTKSYTE-RLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNL-------TVRFLPQNP 75
Cdd:cd03226 1 RIENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIlLNGKPIkakerrkSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 76 EFYkgdtILTSIVREN--EGQDHVWDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNH 152
Cdd:cd03226 81 DYQ----LFTDSVREEllLGLKELDAGNEQAETVLKDLDLYALkERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1524013779 153 LD----SSMAEWLEEyLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03226 157 LDyknmERVGELIRE-LAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-178 |
2.37e-29 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 115.65 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSY----TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV------VKGRNLTVRFLPQ 73
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 74 NpefykgDTIL---TsiVREN-----EGQDHVW-DLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADL 143
Cdd:cd03293 81 Q------DALLpwlT--VLDNvalglELQGVPKaEARERAEELLELVGLSGFeNAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1524013779 144 LVLDEPTNHLDS----SMAEWLEEYLRSFNGALLMVTHD 178
Cdd:cd03293 153 LLLDEPFSALDAltreQLQEELLDIWRETGKTVLLVTHD 191
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-196 |
2.45e-29 |
|
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: 114.02 E-value: 2.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSY--TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV----VKGRNLTVR-------F 70
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgVDLRDLDLEslrkniaY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 LPQNPEFYKGdTIltsivRENegqdhvwdlesqaktmltklgftdfdILvetlSGGQRKRVALVSVLLSTADLLVLDEPT 150
Cdd:cd03228 81 VPQDPFLFSG-TI-----REN--------------------------IL----SGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1524013779 151 NHLDSSMAEWLEEYLRSFNG--ALLMVTHDryfLDSVTN--RIVELDKGK 196
Cdd:cd03228 125 SALDPETEALILEALRALAKgkTVIVIAHR---LSTIRDadRIIVLDDGR 171
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-230 |
3.81e-29 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 122.15 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 7 EHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQNPEFYKGD-TILT 85
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDPNkTVWE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 86 SIvreNEGQDH--VWDLESQAKTMLTKLGF--TDFDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWL 161
Cdd:PRK11819 408 EI---SGGLDIikVGNREIPSRAYVGRFNFkgGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 162 EEYLRSFNGALLMVTHDRYFLDSVTNRIV--ELDkGKLFSYQTNkvngggadrestqgcYEEYLKLKAERL 230
Cdd:PRK11819 485 EEALLEFPGCAVVISHDRWFLDRIATHILafEGD-SQVEWFEGN---------------FQEYEEDKKRRL 539
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-197 |
3.94e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 118.71 E-value: 3.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGR----NLTVR-----FLPQ 73
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVlNGRdlftNLPPRerrvgFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 74 NPEFYKGdtiLTsiVREN-----------EGQdhvwdLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTA 141
Cdd:COG1118 83 HYALFPH---MT--VAENiafglrvrppsKAE-----IRARVEELLELVQLEGLaDRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 142 DLLVLDEPTNHLDSS----MAEWLEEYLRSFNGALLMVTHDRyfLDS--VTNRIVELDKGKL 197
Cdd:COG1118 153 EVLLLDEPFGALDAKvrkeLRRWLRRLHDELGGTTVFVTHDQ--EEAleLADRVVVMNQGRI 212
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-199 |
7.62e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 114.76 E-value: 7.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MN-LLTIEHMTKSY----TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT------- 67
Cdd:COG1136 1 MSpLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlIDGQDISslserel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 --VR-----FLPQN----PEfykgdtiLTsiVREN-------EGQDHvWDLESQAKTMLTKLGFTDF-DILVETLSGGQR 128
Cdd:COG1136 81 arLRrrhigFVFQFfnllPE-------LT--ALENvalplllAGVSR-KERRERARELLERVGLGDRlDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 129 KRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNG----ALLMVTHDRyFLDSVTNRIVELDKGKLFS 199
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelgtTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
299-493 |
1.76e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 112.99 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 299 ELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITV-GQTV----------KMGYFSQ 367
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdGKPLsampppewrrQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 368 ENEELDGRlkVIDYIRGAAEYVKTKDGSVSASQMLERFLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTN 447
Cdd:COG4619 82 EPALWGGT--VRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1524013779 448 DLDIQTLTILEDYLESF---PGI-VITVSHDRYFLDRVVRRIFAFEGNGM 493
Cdd:COG4619 160 ALDPENTRRVEELLREYlaeEGRaVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-197 |
2.70e-28 |
|
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: 120.32 E-value: 2.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSY--TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRF 70
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlIDGIDLRqidpaslrrqIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 LPQNPEFYKGdTIltsivREN--EGQDHVwDLEsQAKTMLTKLGFTDF--------DILV----ETLSGGQRKRVALVSV 136
Cdd:COG2274 554 VLQDVFLFSG-TI-----RENitLGDPDA-TDE-EIIEAARLAGLHDFiealpmgyDTVVgeggSNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1524013779 137 LLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNG--ALLMVTHDRYFLDSVtNRIVELDKGKL 197
Cdd:COG2274 626 LLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRLA-DRIIVLDKGRI 687
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-197 |
3.88e-28 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 112.60 E-value: 3.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLF----DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT---------- 67
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIiFDGKDLLklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 ---VRFLPQ------NPEFykgdTILTSIVRENEGQDHVWDLESQAKTMLTKL-GFTD----FDILVETLSGGQRKRVAL 133
Cdd:cd03257 81 rkeIQMVFQdpmsslNPRM----TIGEQIAEPLRIHGKLSKKEARKEAVLLLLvGVGLpeevLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 134 VSVLLSTADLLVLDEPTNHLD-SSMAEWLEEYLR---SFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDvSVQAQILDLLKKlqeELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
336-554 |
9.68e-28 |
|
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: 117.73 E-value: 9.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVGQTVKMGYFSQE---NEELDGRLKVIDyirGAAEYVKTKD--GSVSA------SQM--- 401
Cdd:TIGR03719 44 KSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEpqlDPTKTVRENVEE---GVAEIKDALDrfNEISAkyaepdADFdkl 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 402 ------------------LERFL--------FPSSVQytTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLT 455
Cdd:TIGR03719 121 aaeqaelqeiidaadawdLDSQLeiamdalrCPPWDA--DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 456 ILEDYLESFPGIVITVSHDRYFLDRVVRRIFAFEgNGMVTQYEGGFTDYqaaysekhpegiLEQsdkKEKKTAAQEKTnp 535
Cdd:TIGR03719 199 WLERHLQEYPGTVVAVTHDRYFLDNVAGWILELD-RGRGIPWEGNYSSW------------LEQ---KQKRLEQEEKE-- 260
|
250
....*....|....*....
gi 1524013779 536 gKKQRERKLKfsfhEQREW 554
Cdd:TIGR03719 261 -ESARQKTLK----RELEW 274
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-197 |
9.73e-28 |
|
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: 111.07 E-value: 9.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT--------VRFLPQN 74
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlIDGRDVTgvpperrnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 75 PEFYkgdTILTsiVREN---------EGQDHVwdlESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLL 144
Cdd:cd03259 81 YALF---PHLT--VAENiafglklrgVPKAEI---RARVRELLELVGLEGLlNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1524013779 145 VLDEPTNHLDSSMAEWLEEYLRSFNGAL----LMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELgittIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-197 |
1.04e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 111.30 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSY-TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT------VRFLpqnp 75
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlVNGQDLSrlkrreIPYL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 76 efykgdtiltsivRENEG---QDH-------VWD---------------LESQAKTMLTKLGFTDF-DILVETLSGGQRK 129
Cdd:COG2884 78 -------------RRRIGvvfQDFrllpdrtVYEnvalplrvtgksrkeIRRRVREVLDLVGLSDKaKALPHELSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 130 RVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFN--G-ALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINrrGtTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-197 |
1.81e-27 |
|
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: 110.37 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 14 TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRFLPQNPEFYKGDt 82
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlLDGTDIRqldpadlrrnIGYVPQDVTLFYGT- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 83 iltsiVREN--EGQDHVWDLESQAKTMLTklGFTDF--------DILV----ETLSGGQRKRVALVSVLLSTADLLVLDE 148
Cdd:cd03245 94 -----LRDNitLGAPLADDERILRAAELA--GVTDFvnkhpnglDLQIgergRGLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 149 PTNHLDSSMAEWLEEYLRSFNG--ALLMVTHdRYFLDSVTNRIVELDKGKL 197
Cdd:cd03245 167 PTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
20-197 |
6.57e-27 |
|
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: 116.12 E-value: 6.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 20 DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRFLPQNPEFYKGDtiltsiV 88
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVlLDGVDIRqidpadlrrnIGYVPQDPRLFYGT------L 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 89 REN--EGQDHVWDLESQAKTMLTklGFTDF--------DILV----ETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLD 154
Cdd:TIGR03375 556 RDNiaLGAPYADDEEILRAAELA--GVTEFvrrhpdglDMQIgergRSLSGGQRQAVALARALLRDPPILLLDEPTSAMD 633
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1524013779 155 SSMAEWLEEYLRSFNG--ALLMVTHDRYFLDSVTnRIVELDKGKL 197
Cdd:TIGR03375 634 NRSEERFKDRLKRWLAgkTLVLVTHRTSLLDLVD-RIIVMDNGRI 677
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-197 |
1.52e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 111.34 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT--------VRFL 71
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIlLDGRDVTglppekrnVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 72 PQN----PEfykgdtiLTsiVREN-------EGQDHVwDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLS 139
Cdd:COG3842 83 FQDyalfPH-------LT--VAENvafglrmRGVPKA-EIRARVAELLELVGLEGLaDRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 140 TADLLVLDEPTNHLD----SSMAEWLEEYLRSFNGALLMVTHDRY--FldSVTNRIVELDKGKL 197
Cdd:COG3842 153 EPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHDQEeaL--ALADRIAVMNDGRI 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-197 |
3.37e-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: 112.93 E-value: 3.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTE-RLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRFL 71
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlINGVDLSdldpaswrrqIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 72 PQNPEFYKG---DTILtsIVRENEGQDHVWdlesQAktmLTKLGFTDFdilVET---------------LSGGQRKRVAL 133
Cdd:COG4988 417 PQNPYLFAGtirENLR--LGRPDASDEELE----AA---LEAAGLDEF---VAAlpdgldtplgeggrgLSGGQAQRLAL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 134 VSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSF--NGALLMVTHDryfLDSVTN--RIVELDKGKL 197
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHR---LALLAQadRILVLDDGRI 549
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-197 |
5.15e-26 |
|
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: 106.75 E-value: 5.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRNLT------------VR- 69
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfDGEDITglppheiarlgiGRt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 70 FlpQNPEFYKGdtiLTsiVREN----------------EGQDHVWDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVA 132
Cdd:cd03219 81 F--QIPRLFPE---LT--VLENvmvaaqartgsglllaRARREEREARERAEELLERVGLADLaDRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 133 LVSVLLSTADLLVLDEPT---NHLDS-SMAEWLEEyLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03219 154 IARALATDPKLLLLDEPAaglNPEETeELAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
336-554 |
5.27e-26 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 112.52 E-value: 5.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVGQTVKMGYFSQE---NEELDGRLKVIDyirGAAEyvkTKDgsvsasqMLERF-----LF 407
Cdd:PRK11819 46 KSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEpqlDPEKTVRENVEE---GVAE---VKA-------ALDRFneiyaAY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 408 PSSVQY----------------------------------------TTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTN 447
Cdd:PRK11819 113 AEPDADfdalaaeqgelqeiidaadawdldsqleiamdalrcppwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTN 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 448 DLDIQTLTILEDYLESFPGIVITVSHDRYFLDRVVRRIFAFE-GNGMvtQYEGGFTDYqaaysekhpegiLEQsdkKEKK 526
Cdd:PRK11819 193 HLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDrGRGI--PWEGNYSSW------------LEQ---KAKR 255
|
250 260
....*....|....*....|....*...
gi 1524013779 527 TAAQEKTNpgkKQRERKLKfsfhEQREW 554
Cdd:PRK11819 256 LAQEEKQE---AARQKALK----RELEW 276
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-298 |
1.02e-25 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 112.19 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQNP-EFYKGD 81
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQlEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 82 -TILTSIVRENEGQdhvwdLESQAKTMLTKLGFTDFDILVET--LSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMA 158
Cdd:PRK10636 392 eSPLQHLARLAPQE-----LEQKLRDYLGGFGFQGDKVTEETrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 159 EWLEEYLRSFNGALLMVTHDRYFLDSVTNRI-------VELDKGKLFSYQTNKVNgggADRESTQGCYEEylklkaERLD 231
Cdd:PRK10636 467 QALTEALIDFEGALVVVSHDRHLLRSTTDDLylvhdgkVEPFDGDLEDYQQWLSD---VQKQENQTDEAP------KENN 537
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 232 LLEASERKRQSilrvelqwmQRGARARSTKQ--KAHIERYEtlrdqKGLETDQAvELDSIESRLGRTTV 298
Cdd:PRK10636 538 ANSAQARKDQK---------RREAELRTQTQplRKEIARLE-----KEMEKLNA-QLAQAEEKLGDSEL 591
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-197 |
1.98e-24 |
|
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: 101.50 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGeKIGLIGINGTGKSTLLKIVAGLEEPDEGKV------VKGRNLTVR----FLPQ 73
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIridgqdVLKQPQKLRrrigYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 74 NPEFYKGDTILtsivrenEGQDHV-W-------DLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLL 144
Cdd:cd03264 80 EFGVYPNFTVR-------EFLDYIaWlkgipskEVKARVDEVLELVNLGDRaKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 145 VLDEPTNHLDSsmaewlEEYLR--------SFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03264 153 IVDEPTAGLDP------EERIRfrnllselGEDRIVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-177 |
3.64e-24 |
|
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: 100.51 E-value: 3.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNL-TVRFLPQNPEFYKG- 80
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrWNGTPLaEQRDEPHENILYLGh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 81 ----DTILTsiVREN---------EGQDHVWDLesqaktmLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVL 146
Cdd:TIGR01189 81 lpglKPELS--ALENlhfwaaihgGAQRTIEDA-------LAAVGLTGFeDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 1524013779 147 DEPTNHLDSSMAEWLEEYLRSF---NGALLMVTH 177
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-177 |
4.68e-24 |
|
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: 100.26 E-value: 4.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVkgrnltvrfLPQNPEFYKGDTI 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVL---------LNGGPLDFQRDSI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 84 LTSI--------------VRENEGQDHVWDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDE 148
Cdd:cd03231 72 ARGLlylghapgikttlsVLENLRFWHADHSDEQVEEALARVGLNGFeDRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|..
gi 1524013779 149 PTNHLDSSMAEWLEEYLRSF---NGALLMVTH 177
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHcarGGMVVLTTH 183
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-193 |
5.36e-24 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 99.88 E-value: 5.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRNLTvrflPQNPEF---- 77
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwQGEPIR----RQRDEYhqdl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 78 -YKG-----DTILTSIvrEN----------EGQDHVWDLesqaktmLTKLGFTDF-DILVETLSGGQRKRVALVSVLLST 140
Cdd:PRK13538 77 lYLGhqpgiKTELTAL--ENlrfyqrlhgpGDDEALWEA-------LAQVGLAGFeDVPVRQLSAGQQRRVALARLWLTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 141 ADLLVLDEPTNHLDSSMAEWLEEYLRSF---NGALLMVTHDRYFLDSVTNRIVELD 193
Cdd:PRK13538 148 APLWILDEPFTAIDKQGVARLEALLAQHaeqGGMVILTTHQDLPVASDKVRKLRLG 203
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
23-179 |
5.78e-24 |
|
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: 105.83 E-value: 5.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 23 SFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRFLPQNPEFYKGdTILTSI-VRE 90
Cdd:TIGR02857 342 SFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIaVNGVPLAdadadswrdqIAWVPQHPFLFAG-TIAENIrLAR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 91 NEGQDH----------VWDLESQAKTML-TKLGftdfdilvET---LSGGQRKRVALVSVLLSTADLLVLDEPTNHLDS- 155
Cdd:TIGR02857 421 PDASDAeirealeragLDEFVAALPQGLdTPIG--------EGgagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAe 492
|
170 180
....*....|....*....|....*
gi 1524013779 156 SMAEWLEEYLRSFNGA-LLMVTHDR 179
Cdd:TIGR02857 493 TEAEVLEALRALAQGRtVLLVTHRL 517
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-197 |
6.38e-24 |
|
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: 99.91 E-value: 6.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT------------VRF 70
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiIDGLKLTddkkninelrqkVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 LPQNPEFYKGDTILTSIVrenEGQDHVWDL---ESQAKTM--LTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLL 144
Cdd:cd03262 81 VFQQFNLFPHLTVLENIT---LAPIKVKGMskaEAEERALelLEKVGLADKaDAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 145 VLDEPTNHLDSSMAEWLEEYLRSF---NGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-197 |
9.33e-24 |
|
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: 99.60 E-value: 9.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTVRFLPQN-------- 74
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItFDGKSYQKNIEALRrigaliea 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 75 PEFYKGDTiltsiVREN-EGQDHVWDLESQA-KTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEPTN 151
Cdd:cd03268 81 PGFYPNLT-----ARENlRLLARLLGIRKKRiDEVLDVVGLKDSaKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1524013779 152 HLDSSMAEWLEEYLRS---FNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03268 156 GLDPDGIKELRELILSlrdQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-178 |
1.17e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.09 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPD---EGKV-VKGRNLT--------VRFL 71
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVlLNGRRLTalpaeqrrIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 72 PQ----NPEFYKGDTIL----TSIVRENEGQdhvwdlesQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTAD 142
Cdd:COG4136 82 FQddllFPHLSVGENLAfalpPTIGRAQRRA--------RVEQALEEAGLAGFaDRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1524013779 143 LLVLDEPTNHLDSSMA----EWLEEYLRSFNGALLMVTHD 178
Cdd:COG4136 154 ALLLDEPFSKLDAALRaqfrEFVFEQIRQRGIPALLVTHD 193
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-178 |
1.25e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.46 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 12 SYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQNPEfykGDTILTSIVRE- 90
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSE---VPDSLPLTVRDl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 91 ---------NEGQDHVWDLESQAKTMLTKLGFTDFDIL-VETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSS---- 156
Cdd:NF040873 78 vamgrwarrGLWRRLTRDDRAAVDDALERVGLADLAGRqLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAEsrer 157
|
170 180
....*....|....*....|....*.
gi 1524013779 157 ----MAEWLEEylrsfNGALLMVTHD 178
Cdd:NF040873 158 iialLAEEHAR-----GATVVVVTHD 178
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-193 |
1.52e-23 |
|
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: 99.79 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 25 SINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNlTVRFLPQNPEF-YKG--DTILTSIVReNEGQDHVWDLE 101
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQYIKAdYEGtvRDLLSSITK-DFYTHPYFKTE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 102 SQAKTMLTKLgftdFDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSF----NGALLMVTH 177
Cdd:cd03237 99 IAKPLQIEQI----LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEH 174
|
170
....*....|....*.
gi 1524013779 178 DRYFLDSVTNRIVELD 193
Cdd:cd03237 175 DIIMIDYLADRLIVFE 190
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-197 |
2.90e-23 |
|
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: 99.34 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSyterllF------DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRNLT------ 67
Cdd:COG0411 2 DPLLEVRGLTKR------FgglvavDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfDGRDITglpphr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 ------VR-FlpQNPEFYKGDTiltsiVREN--------------EGQDHVW-------DLESQAKTMLTKLGFTDF-DI 118
Cdd:COG0411 76 iarlgiARtF--QNPRLFPELT-----VLENvlvaaharlgrgllAALLRLPrarreerEARERAEELLERVGLADRaDE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 119 LVETLSGGQRKRVALVSVLLSTADLLVLDEPT---NHLDS-SMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDK 194
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETeELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF 228
|
...
gi 1524013779 195 GKL 197
Cdd:COG0411 229 GRV 231
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-198 |
3.67e-23 |
|
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: 99.45 E-value: 3.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 20 DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT-------------VRFLPQNPE---FykGDT 82
Cdd:TIGR04521 22 DDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVtIDGRDITakkkkklkdlrkkVGLVFQFPEhqlF--EET 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 83 ILTSI--------VRENEgqdhvwdLESQAKTMLTKLGFTD-------FDilvetLSGGQRKRVALVSVLLSTADLLVLD 147
Cdd:TIGR04521 100 VYKDIafgpknlgLSEEE-------AEERVKEALELVGLDEeylerspFE-----LSGGQMRRVAIAGVLAMEPEVLILD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 148 EPTNHLD----SSMAEWLEEYLRSFNGALLMVTHDryfLDSV---TNRIVELDKGKLF 198
Cdd:TIGR04521 168 EPTAGLDpkgrKEILDLFKRLHKEKGLTVILVTHS---MEDVaeyADRVIVMHKGKIV 222
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-190 |
3.94e-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: 103.71 E-value: 3.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTErllfddtsFS-------INEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKgrNLTVRFLPQnp 75
Cdd:COG1245 341 LVEYPDLTKSYGG--------FSleveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE--DLKISYKPQ-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 76 eFYKGDTILTsiVRENEGQDHVWDLE-SQAKTMLTK-LGFTD-FDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNH 152
Cdd:COG1245 409 -YISPDYDGT--VEEFLRSANTDDFGsSYYKTEIIKpLGLEKlLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1524013779 153 LDS----SMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIV 190
Cdd:COG1245 486 LDVeqrlAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-190 |
4.90e-23 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 103.35 E-value: 4.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFsINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKgrNLTVRFLPQnpeFYKGDT 82
Cdd:PRK13409 340 LVEYPDLTKKLGDFSLEVEGGE-IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--ELKISYKPQ---YIKPDY 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 83 ILTsivrenegqdhVWDLESQAKTMLT----------KLGFTD-FDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTN 151
Cdd:PRK13409 414 DGT-----------VEDLLRSITDDLGssyykseiikPLQLERlLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1524013779 152 HLDSS----MAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIV 190
Cdd:PRK13409 483 HLDVEqrlaVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-196 |
5.30e-23 |
|
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: 97.35 E-value: 5.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTVR------FLPQNPE 76
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlFDGKPLDIAarnrigYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 77 FYKGDTILTSIV--RENEGQDHVwDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHL 153
Cdd:cd03269 81 LYPKMKVIDQLVylAQLKGLKKE-EARRRIDEWLERLELSEYaNKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1524013779 154 DSSMAEWLEEYLRSFNGA---LLMVTHDRYFLDSVTNRIVELDKGK 196
Cdd:cd03269 160 DPVNVELLKDVIRELARAgktVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-196 |
5.58e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 97.90 E-value: 5.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLL-FDdtsFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTvrflPQNPE----- 76
Cdd:COG3840 2 LRLDDLTYRYGDFPLrFD---LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlWNGQDLT----ALPPAerpvs 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 77 --------FykgdTILTsiVRENEG-----------QDHvwdleSQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSV 136
Cdd:COG3840 75 mlfqennlF----PHLT--VAQNIGlglrpglkltaEQR-----AQVEQALERVGLAGLlDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1524013779 137 LLSTADLLVLDEPTNHLD----SSMAEWLEEYLRSFNGALLMVTHDryfLD---SVTNRIVELDKGK 196
Cdd:COG3840 144 LVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD---PEdaaRIADRVLLVADGR 207
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-197 |
6.45e-23 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 97.80 E-value: 6.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRNLT--------VRFLPQN 74
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILfGGEDATdvpvqernVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 75 PEFYKGDTILTSI---VRENEGQDHVWDLESQAKTM-------LTKLGftdfDILVETLSGGQRKRVALVSVLLSTADLL 144
Cdd:cd03296 83 YALFRHMTVFDNVafgLRVKPRSERPPEAEIRAKVHellklvqLDWLA----DRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1524013779 145 VLDEPTNHLDSSMAEWLEEYLRSFNGAL----LMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELhvttVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-197 |
6.98e-23 |
|
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: 95.57 E-value: 6.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRnlTVRFLpqNPefykgdt 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIlVDGK--EVSFA--SP------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 83 iltsivrenegqdhvwdleSQAKtmltKLGFTdfdiLVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLE 162
Cdd:cd03216 70 -------------------RDAR----RAGIA----MVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1524013779 163 EYLRSF--NG-ALLMVTHdryFLD---SVTNRIVELDKGKL 197
Cdd:cd03216 123 KVIRRLraQGvAVIFISH---RLDevfEIADRVTVLRDGRV 160
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-196 |
1.22e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 98.64 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTVR------FLPQNPE 76
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVlWDGEPLDPEdrrrigYLPEERG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 77 FYKGDTILTSIVR--ENEGQDHVwDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHL 153
Cdd:COG4152 82 LYPKMKVGEQLVYlaRLKGLSKA-EAKRRADEWLERLGLGDRaNKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1524013779 154 DSSMAEWLEEYLRSF--NGA-LLMVTHDryfLDSVT---NRIVELDKGK 196
Cdd:COG4152 161 DPVNVELLKDVIRELaaKGTtVIFSSHQ---MELVEelcDRIVIINKGR 206
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-198 |
1.30e-22 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 97.43 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSY-TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT------------- 67
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEIlVDGQDVTalrgralrrlrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 VRFLPQNPE--------------------FYKGdtiLTSIVRENEGQdhvwdlesQAKTMLTKLGFTDF-DILVETLSGG 126
Cdd:COG3638 82 IGMIFQQFNlvprlsvltnvlagrlgrtsTWRS---LLGLFPPEDRE--------RALEALERVGLADKaYQRADQLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 127 QRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNG----ALLMVTHD-----RYFldsvtNRIVELDKGKL 197
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedgiTVVVNLHQvdlarRYA-----DRIIGLRDGRV 225
|
.
gi 1524013779 198 F 198
Cdd:COG3638 226 V 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-197 |
2.10e-22 |
|
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: 96.59 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 2 NLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRN--------------- 65
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIlVDGQDitglsekelyelrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 66 -------------LTVRflpQNPEFYkgdtiltsiVRENEGQDHvWDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRV 131
Cdd:COG1127 84 igmlfqggalfdsLTVF---ENVAFP---------LREHTDLSE-AEIRELVLEKLELVGLPGAaDKMPSELSGGMRKRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 132 ALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNGAL----LMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELgltsVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
4-197 |
2.54e-22 |
|
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: 96.81 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-----------KGRNLTVRFLP 72
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhglsrRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 73 QNpefykGDTILTSIVRENEGQDHV-----WDLESQ-----AKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTA 141
Cdd:TIGR03873 82 QD-----SDTAVPLTVRDVVALGRIphrslWAGDSPhdaavVDRALARTELSHLaDRDMSTLSGGERQRVHVARALAQEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 142 DLLVLDEPTNHLDSSMAEWLEEYLRSFNG---ALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:TIGR03873 157 KLLLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHDLNLAASYCDHVVVLDGGRV 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-197 |
3.10e-22 |
|
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: 95.65 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 6 IEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT---------VR----FL 71
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlIDGEDISglseaelyrLRrrmgML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 72 PQNPEFYkgdTILTsiVREN-------EGQDHVWDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADL 143
Cdd:cd03261 83 FQSGALF---DSLT--VFENvafplreHTRLSEEEIREIVLEKLEAVGLRGAeDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 144 LVLDEPTNHLDSSMAEWLEEYLRSFNGAL----LMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELgltsIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-197 |
3.30e-22 |
|
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: 95.77 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT--------VRFLPQN 74
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlLDGKDITnlpphkrpVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 75 ----PEFYKGDTILTSIVRENEGQDhvwDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEP 149
Cdd:cd03300 81 yalfPHLTVFENIAFGLRLKKLPKA---EIKERVAEALDLVQLEGYaNRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 150 TNHLDSSMAEWLEEYLRSFNGAL----LMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKELgitfVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-193 |
4.18e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 95.95 E-value: 4.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQNPEFykg 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 81 DTILTSIVRenegqdhvwdlesqaKTMLTKLGFTDFDIL---------------VETLSGGQRKRVALVSVLLSTADLLV 145
Cdd:PRK09544 79 DTTLPLTVN---------------RFLRLRPGTKKEDILpalkrvqaghlidapMQKLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 146 LDEPTNHLDS----SMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELD 193
Cdd:PRK09544 144 LDEPTQGVDVngqvALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN 195
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-200 |
8.27e-22 |
|
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: 94.14 E-value: 8.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 11 KSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGR-----NLTVRFLPQnpefykgdtiL 84
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVtVRGRvssllGLGGGFNPE----------L 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 85 TsiVREN-------------EGQDHVWDLEsqaktMLTKLGfTDFDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTN 151
Cdd:cd03220 100 T--GRENiylngrllglsrkEIDEKIDEII-----EFSELG-DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 152 HLDSSMAEWLEEYLRSF---NGALLMVTHDRYFLDSVTNRIVELDKGKLFSY 200
Cdd:cd03220 172 VGDAAFQEKCQRRLRELlkqGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-197 |
1.04e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.10 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 2 NLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTVRFLPQN------ 74
Cdd:PRK11432 5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfIDGEDVTHRSIQQRdicmvf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 75 ------PEFYKGDTILTSIVRENEGQDHVWDLESQAKTMLTKLGFTDFdiLVETLSGGQRKRVALVSVLLSTADLLVLDE 148
Cdd:PRK11432 85 qsyalfPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDR--YVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1524013779 149 PTNHLDS----SMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:PRK11432 163 PLSNLDAnlrrSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-197 |
1.07e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.38 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 11 KSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGR-----NLTVRFlpqNPEfykgdtiL 84
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVeVNGRvsallELGAGF---HPE-------L 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 85 TsiVREN----------------EGQDHVWD-------LESQAKT----MLTKLGF-----TDFDILV--ETLSGG---- 126
Cdd:COG1134 104 T--GRENiylngrllglsrkeidEKFDEIVEfaelgdfIDQPVKTyssgMRARLAFavataVDPDILLvdEVLAVGdaaf 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 127 QRKrvalvsvllstadllvldeptnhldsSMAEwLEEYLRSfNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:COG1134 182 QKK--------------------------CLAR-IRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-197 |
1.11e-21 |
|
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: 93.47 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-----------KGRNLTVRFlp 72
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdlppKDRDIAMVF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 73 QNPEFYKGDTILTSI--------VRENEGQDHVwdlESQAKTM-LTKLgftdFDILVETLSGGQRKRVALVSVLLSTADL 143
Cdd:cd03301 79 QNYALYPHMTVYDNIafglklrkVPKDEIDERV---REVAELLqIEHL----LDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 144 LVLDEPTNHLDS----SMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03301 152 FLMDEPLSNLDAklrvQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-197 |
1.35e-21 |
|
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: 92.28 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 14 TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRFLPQNPEFYKGdT 82
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrLDGADISqwdpnelgdhVGYLPQDDELFSG-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 83 ILTSIvrenegqdhvwdlesqaktmltklgftdfdilvetLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLE 162
Cdd:cd03246 92 IAENI-----------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 1524013779 163 EYLRSFNGA---LLMVTHDRYFLDSVtNRIVELDKGKL 197
Cdd:cd03246 137 QAIAALKAAgatRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
299-485 |
1.45e-21 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 94.15 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 299 ELEGISKAYGDKVLMKDFTY---------ILLKNdrigiigpnGGGKSTLMKIIAGWVEPDEGTITV-GQTV-------- 360
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFtakdgeitgLLGPN---------GAGKTTLLRMLAGLLKPDSGSILIdGEDVrkeprear 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 361 -KMGYFSQENeELDGRLKVIDYIR--GAAEYVKTKDGSVSASQMLERFLFpSSVQYTTIEKLSGGEKRRLYLLRILMEAP 437
Cdd:COG4555 74 rQIGVLPDER-GLYDRLTVRENIRyfAELYGLFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 438 NVLLLDEPTNDLDIQTLTILEDYLESF---PGIVITVSHDRYFLDRVVRRI 485
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRV 202
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-198 |
2.70e-21 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 93.40 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSY---TERLlfDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV---------VKGRNL-TVR- 69
Cdd:cd03256 1 IEVENLSKTYpngKKAL--KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinkLKGKALrQLRr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 70 ---FLPQN----PEFYKGDTILT------SIVRENEGQDHVWDLEsQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVS 135
Cdd:cd03256 79 qigMIFQQfnliERLSVLENVLSgrlgrrSTWRSLFGLFPKEEKQ-RALAALERVGLLDKaYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1524013779 136 VLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNG----ALLMVTHDRYFLDSVTNRIVELDKGKLF 198
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINReegiTVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-196 |
3.05e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.06 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRNLT-----VRflPQNPE 76
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMlDGVDLShvppyQR--PINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 77 FYKGDTILTSIVRENEG----QDHV--WDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEP 149
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAfglkQDKLpkAEIASRVNEMLGLVHMQEFaKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 150 TNHLDSSMAEWLE----EYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGK 196
Cdd:PRK11607 177 MGALDKKLRDRMQlevvDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-178 |
3.13e-21 |
|
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: 97.43 E-value: 3.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSY-TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNL----------TVRFL 71
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtLDGVPVssldqdevrrRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 72 PQNPEfykgdtILTSIVREN------EGQD--------------HVWDLESQAKTMLTKLGftdfdilvETLSGGQRKRV 131
Cdd:TIGR02868 415 AQDAH------LFDTTVRENlrlarpDATDeelwaalervgladWLRALPDGLDTVLGEGG--------ARLSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 132 ALVSVLLSTADLLVLDEPTNHLDssmAEWLEEYLRSFNGAL-----LMVTHD 178
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLD---AETADELLEDLLAALsgrtvVLITHH 529
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-200 |
5.84e-21 |
|
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: 91.59 E-value: 5.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 21 DTSFSINEgEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV----------KGRNLTVR-----FLPQN----PEFYKGD 81
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrKKINLPPQqrkigLVFQQyalfPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 82 TILTSIVRENEGQDHVWDLESQAKTMLTKLGFTDfdilVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWL 161
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDELLDLLGLDHLLNRY----PAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1524013779 162 EEYLRS----FNGALLMVTHDRYFLDSVTNRIVELDKGKLFSY 200
Cdd:cd03297 171 LPELKQikknLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-197 |
7.53e-21 |
|
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: 91.28 E-value: 7.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 6 IEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGK-VVKGRNLT-----VR----FLPQNP 75
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHDVVrepreVRrrigIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 76 EFykgDTILTSivREN-EGQDHVWDLESQ-----AKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDE 148
Cdd:cd03265 83 SV---DDELTG--WENlYIHARLYGVPGAerrerIDELLDFVGLLEAaDRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1524013779 149 PTNHLD----SSMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03265 158 PTIGLDpqtrAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-202 |
9.77e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.77 E-value: 9.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 2 NLLTIEHMTKSY--TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------V 68
Cdd:PRK13635 4 EIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItVGGMVLSeetvwdvrrqV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 69 RFLPQNPEF-YKGDTILTSIV--RENEGQDHVwDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLL 144
Cdd:PRK13635 84 GMVFQNPDNqFVGATVQDDVAfgLENIGVPRE-EMVERVDQALRQVGMEDFlNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 145 VLDEPTNHLDSSMAEWLEEYLRSFNG----ALLMVTHDryfLDSV--TNRIVELDKGKLFSYQT 202
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEqkgiTVLSITHD---LDEAaqADRVIVMNKGEILEEGT 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-197 |
1.00e-20 |
|
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: 91.34 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 2 NLLTIEHMTKSYT---ERL-LFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT--------- 67
Cdd:COG4181 7 PIIELRGLTKTVGtgaGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVrLAGQDLFaldedarar 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 VR-----FLPQN----PEfykgdtiLTSIvrEN-------EGQDhvwDLESQAKTMLTKLGFTD-FDILVETLSGGQRKR 130
Cdd:COG4181 87 LRarhvgFVFQSfqllPT-------LTAL--ENvmlplelAGRR---DARARARALLERVGLGHrLDHYPAQLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 131 VALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFN---GA-LLMVTHDRYfLDSVTNRIVELDKGKL 197
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNrerGTtLVLVTHDPA-LAARCDRVLRLRAGRL 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-197 |
1.15e-20 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 92.11 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 6 IEHMTKSY--TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNL-------TVR------ 69
Cdd:TIGR04520 3 VENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVtVDGLDTldeenlwEIRkkvgmv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 70 FlpQNPEfykgDTILTSIVR-------ENEG--QDHVWDLESQAktmLTKLGFTDFdILVET--LSGGQRKRVALVSVLL 138
Cdd:TIGR04520 83 F--QNPD----NQFVGATVEddvafglENLGvpREEMRKRVDEA---LKLVGMEDF-RDREPhlLSGGQKQRVAIAGVLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 139 STADLLVLDEPTNHLD-SSMAEWLE--EYLRSFNG-ALLMVTHDryfLDSVTN--RIVELDKGKL 197
Cdd:TIGR04520 153 MRPDIIILDEATSMLDpKGRKEVLEtiRKLNKEEGiTVISITHD---MEEAVLadRVIVMNKGKI 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-197 |
1.72e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 91.23 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRFLP 72
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVfLGDKPISmlssrqlarrLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 73 QNPEFYKGDTiltsiVRE---------------NEGQDHVWDLESQAKTMLTKLGftdfDILVETLSGGQRKRVALVSVL 137
Cdd:PRK11231 83 QHHLTPEGIT-----VRElvaygrspwlslwgrLSAEDNARVNQAMEQTRINHLA----DRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 138 LSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNGA---LLMVTHD-----RYfldsvTNRIVELDKGKL 197
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgktVVTVLHDlnqasRY-----CDHLVVLANGHV 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-490 |
1.89e-20 |
|
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: 95.24 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 28 EGEKIGLIGINGTGKSTLLKIVAGLEEPDEG-------------------------KVVKGrNLTVRFLPQN----PEFY 78
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGdydeepswdevlkrfrgtelqdyfkKLANG-EIKVAHKPQYvdliPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 79 KGDT--ILTSI--------VRENEGQDHVWDLEsqaktmltklgftdfdilVETLSGGQRKRVALVSVLLSTADLLVLDE 148
Cdd:COG1245 177 KGTVreLLEKVdergkldeLAEKLGLENILDRD------------------ISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 149 PTNHLDSS----MAEWLEEYLRSfNGALLMVTHDRYFLDSVTNRIVELdkgklfsYQTNKVNGGGADRESTQGCYEEYLK 224
Cdd:COG1245 239 PSSYLDIYqrlnVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHIL-------YGEPGVYGVVSKPKSVRVGINQYLD 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 225 --LKAERLdlleaserkrqsilrvelqwmqrgaRARSTKqkahIErYETLRDQKGLETDQAVELDSIESRLGRTTVELEG 302
Cdd:COG1245 311 gyLPEENV-------------------------RIRDEP----IE-FEVHAPRREKEEETLVEYPDLTKSYGGFSLEVEG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 303 iSKAYGDKVLMkdftyILLKNdrigiigpnGGGKSTLMKIIAGWVEPDEGTITVgqTVKMGYFSQE-NEELDGRlkVIDY 381
Cdd:COG1245 361 -GEIREGEVLG-----IVGPN---------GIGKTTFAKILAGVLKPDEGEVDE--DLKISYKPQYiSPDYDGT--VEEF 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 382 IRGAAEyvKTKDGSVSASQMLERF----LFPSSVqyttiEKLSGGEKRRLY----LLRilmEApNVLLLDEPTNDLD--- 450
Cdd:COG1245 422 LRSANT--DDFGSSYYKTEIIKPLglekLLDKNV-----KDLSGGELQRVAiaacLSR---DA-DLYLLDEPSAHLDveq 490
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1524013779 451 -IQTLTILEDYLESFPGIVITVSHDRYFLDRVVRRIFAFEG 490
Cdd:COG1245 491 rLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-197 |
2.17e-20 |
|
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: 90.33 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTER----LLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTVRFLPQNPEF 77
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 78 -------YKGDTILTS-IVREN-------EGQDHVwDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTA 141
Cdd:cd03258 81 rrrigmiFQHFNLLSSrTVFENvalpleiAGVPKA-EIEERVLELLELVGLEDKaDAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 142 DLLVLDEPTNHLD----SSMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03258 160 KVLLCDEATSALDpettQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-202 |
2.81e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 90.90 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSYTERLLF---------DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRNL---- 66
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLSgkhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwRGEPLakln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 67 ---------TVRFLPQ------NPEFYKGDTI------LTSIVREnegqdhvwDLESQAKTMLTKLGFTD--FDILVETL 123
Cdd:PRK10419 81 raqrkafrrDIQMVFQdsisavNPRKTVREIIreplrhLLSLDKA--------ERLARASEMLRAVDLDDsvLDKRPPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 124 SGGQRKRVALVSVLLSTADLLVLDEPTNHLD----SSMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKLFS 199
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
...
gi 1524013779 200 YQT 202
Cdd:PRK10419 233 TQP 235
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-197 |
3.05e-20 |
|
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: 89.49 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSY--TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT---------VRFL 71
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyINGYSIRtdrkaarqsLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 72 PQNpefykgDTI---LTsivreneGQDHV-----------WDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSV 136
Cdd:cd03263 81 PQF------DALfdeLT-------VREHLrfyarlkglpkSEIKEEVELLLRVLGLTDKaNKRARTLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 137 LLSTADLLVLDEPTNHLDSSM--AEW--LEEYLRsfNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASrrAIWdlILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-197 |
6.27e-20 |
|
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: 88.58 E-value: 6.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSY----TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKG-----------RNL 66
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAtVDGfdvvkepaearRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 67 TvrFLPQNPEFYKGDTiltsiVREN----------EGQdhvwDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVS 135
Cdd:cd03266 81 G--FVSDSTGLYDRLT-----ARENleyfaglyglKGD----ELTARLEELADRLGMEELlDRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 136 VLLSTADLLVLDEPTNHLDSSMAEWLEEY---LRSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFirqLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-177 |
7.82e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.01 E-value: 7.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 15 ERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGkvvkgrnlTVRFLPQNPEFYKGDTILTSI------- 87
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAG--------TIKLDGGDIDDPDVAEACHYLghrnamk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 88 ----VREN-------EGQDhvwdlESQAKTMLTKLGFTD-FDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDS 155
Cdd:PRK13539 86 paltVAENlefwaafLGGE-----ELDIAAALEAVGLAPlAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180
....*....|....*....|....*.
gi 1524013779 156 S----MAEWLEEYLRSfNGALLMVTH 177
Cdd:PRK13539 161 AavalFAELIRAHLAQ-GGIVIAATH 185
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-197 |
7.93e-20 |
|
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: 87.37 E-value: 7.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTE--RLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNL----------TVRFL 71
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPvsdlekalssLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 72 PQNPEFYkgDTILtsivRENEGqdhvwdlesqaktmltklgftdfdilvETLSGGQRKRVALVSVLLSTADLLVLDEPTN 151
Cdd:cd03247 81 NQRPYLF--DTTL----RNNLG---------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1524013779 152 HLD----SSMAEWLEEYLRsfNGALLMVTHDRYFLDSVtNRIVELDKGKL 197
Cdd:cd03247 128 GLDpiteRQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-149 |
8.96e-20 |
|
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: 88.75 E-value: 8.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT-----------VRFL 71
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlLDGQDITklpmhkrarlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 72 PQNPEFYKGdtiLTsiVREN-----EGQ-DHVWDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLL 144
Cdd:cd03218 81 PQEASIFRK---LT--VEENilavlEIRgLSKKEREEKLEELLEEFHITHLrKSKASSLSGGERRRVEIARALATNPKFL 155
|
....*
gi 1524013779 145 VLDEP 149
Cdd:cd03218 156 LLDEP 160
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-198 |
1.39e-19 |
|
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: 88.60 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVK--GR-------------- 64
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfGErrggedvwelrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 65 -------------NLTVRflpqnpefykgDTILT----SIVRENEGQDhvwDLESQAKTMLTKLGFTDF-DILVETLSGG 126
Cdd:COG1119 81 glvspalqlrfprDETVL-----------DVVLSgffdSIGLYREPTD---EQRERARELLELLGLAHLaDRPFGTLSQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 127 QRKRV----ALVsvllstAD--LLVLDEPTNHLDSSMAEWLEEYLRSFNG----ALLMVTHDRYFLDSVTNRIVELDKGK 196
Cdd:COG1119 147 EQRRVliarALV------KDpeLLILDEPTAGLDLGARELLLALLDKLAAegapTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
..
gi 1524013779 197 LF 198
Cdd:COG1119 221 VV 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-178 |
1.40e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 90.52 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT--------VRFL 71
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIlIGGRDVTdlppkdrnIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 72 PQNPEFYKGdtiLTsiVREN---------EGQDhvwDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTA 141
Cdd:COG3839 81 FQSYALYPH---MT--VYENiafplklrkVPKA---EIDRRVREAAELLGLEDLlDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1524013779 142 DLLVLDEPTNHLD----SSMAEWLEEYLRSFNGALLMVTHD 178
Cdd:COG3839 153 KVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-197 |
3.00e-19 |
|
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: 87.94 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLF---------DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTvRFLP 72
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFgakqrapvlTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVsFRGQDLY-QLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 73 QNPEFYKGDTILT-----------SIVRE--NEGQDHVWDL---ESQAKT--MLTKLGF--TDFDILVETLSGGQRKRVA 132
Cdd:TIGR02769 81 KQRRAFRRDVQLVfqdspsavnprMTVRQiiGEPLRHLTSLdesEQKARIaeLLDMVGLrsEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 133 LVSVLLSTADLLVLDEPTNHLD----SSMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDmvlqAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-197 |
4.15e-19 |
|
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: 86.62 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 20 DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGrnltvrFLP--QNPEFYKGDTILTsivreneGQDH 96
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrVAG------LVPwkRRKKFLRRIGVVF-------GQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 97 --VWDL----------------ESQAKTMLTK----LGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHL 153
Cdd:cd03267 105 qlWWDLpvidsfyllaaiydlpPARFKKRLDElselLDLEELlDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1524013779 154 DSSMAEWLEEYLRSFN----GALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03267 185 DVVAQENIRNFLKEYNrergTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
336-481 |
4.30e-19 |
|
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: 85.99 E-value: 4.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTVK---------MGYFSQENeELDGRLKVIDYIRGAAEYVKTKDGSVSASQMLERF 405
Cdd:COG4133 41 KTTLLRILAGLLPPSAGEVLWnGEPIRdaredyrrrLAYLGHAD-GLKPELTVRENLRFWAALYGLRADREAIDEALEAV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 406 -LfpSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFP---GIVITVSHDRYFLDRV 481
Cdd:COG4133 120 gL--AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA 197
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-196 |
4.82e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 87.06 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSY-----TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTvrFLP----- 72
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlIDGKDVT--KLPeykra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 73 -------QNPefYKGD----TILtsivrEN------EGQ----------DHVWDLESQAKTMltKLGFTD-FDILVETLS 124
Cdd:COG1101 80 kyigrvfQDP--MMGTapsmTIE-----ENlalayrRGKrrglrrgltkKRRELFRELLATL--GLGLENrLDTKVGLLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1524013779 125 GGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWL----EEYLRSFNGALLMVTHD-RYFLDsVTNRIVELDKGK 196
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVleltEKIVEENNLTTLMVTHNmEQALD-YGNRLIMMHEGR 226
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-490 |
4.91e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 91.02 E-value: 4.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 28 EGEKIGLIGINGTGKSTLLKIVAGL---------EEPDEGKVVK---------------GRNLTVRFLPQN----PEFYK 79
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGElipnlgdyeEEPSWDEVLKrfrgtelqnyfkklyNGEIKVVHKPQYvdliPKVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 80 GDT--ILTSI--------VRENEGQDHVWDLEsqaktmltklgftdfdilVETLSGGQRKRVALVSVLLSTADLLVLDEP 149
Cdd:PRK13409 178 GKVreLLKKVdergkldeVVERLGLENILDRD------------------ISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 150 TNHLD----SSMAEWLEEYLRsfNGALLMVTHDRYFLDSVTNRIVELdkgklfsYQTNKVNGGGADRESTQGCYEEYLK- 224
Cdd:PRK13409 240 TSYLDirqrLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIA-------YGEPGAYGVVSKPKGVRVGINEYLKg 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 225 -LKAERLdlleaseRKRQSILRVELqwmqrgaraRSTKQKAHIERYetlrdqkgletdqaVELDSIESRLGRTTVELEGi 303
Cdd:PRK13409 311 yLPEENM-------RIRPEPIEFEE---------RPPRDESERETL--------------VEYPDLTKKLGDFSLEVEG- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 304 SKAYGDKVLMkdftyILLKNdrigiigpnGGGKSTLMKIIAGWVEPDEGTITvgQTVKMGYFSQENE-ELDGRlkVIDYI 382
Cdd:PRK13409 360 GEIYEGEVIG-----IVGPN---------GIGKTTFAKLLAGVLKPDEGEVD--PELKISYKPQYIKpDYDGT--VEDLL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 383 RGAAEYVktkDGSVSASQMLERF----LFPSSVqyttiEKLSGGEKRRLY----LLRilmEApNVLLLDEPTNDLD---- 450
Cdd:PRK13409 422 RSITDDL---GSSYYKSEIIKPLqlerLLDKNV-----KDLSGGELQRVAiaacLSR---DA-DLYLLDEPSAHLDveqr 489
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1524013779 451 IQTLTILEDYLESFPGIVITVSHDRYFLDRVVRRIFAFEG 490
Cdd:PRK13409 490 LAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-197 |
5.50e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 90.61 E-value: 5.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSY-TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRFL 71
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlIDGVDIRdltleslrrqIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 72 PQNPEFYKGdTILTSIV--RENEGQDHVWD-LE-SQAKTMLTKL--GFtdfDILVE----TLSGGQRKRVALVSVLLSTA 141
Cdd:COG1132 420 PQDTFLFSG-TIRENIRygRPDATDEEVEEaAKaAQAHEFIEALpdGY---DTVVGergvNLSGGQRQRIAIARALLKDP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 142 DLLVLDEPTNHLDSSMAEWLEEYLRSF--NGALLMVTHdRyfLDSVTN--RIVELDKGKL 197
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERLmkGRTTIVIAH-R--LSTIRNadRILVLDDGRI 552
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-197 |
5.75e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.60 E-value: 5.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV---------VKGRNLTVRFLPQN 74
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrfhgtdvsrLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 75 PEFYKGDTILTSIV--------RENEGQDHVwdleSQAKTMLtkLGFTDFDILVE----TLSGGQRKRVALVSVLLSTAD 142
Cdd:PRK10851 83 YALFRHMTVFDNIAfgltvlprRERPNAAAI----KAKVTQL--LEMVQLAHLADrypaQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 143 LLVLDEPTNHLDSSMAEWLEEYLRSFNGAL----LMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELkftsVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-197 |
1.01e-18 |
|
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: 84.52 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLfDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGL--EEPDEGKV-VKGRNLT-------VRFLPQ 73
Cdd:cd03213 11 VTVKSSPSKSGKQLL-KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVlINGRPLDkrsfrkiIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 74 NPEFYKGDTiltsiVRENegqdhvwdLESQAKtmltklgftdfdilVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHL 153
Cdd:cd03213 90 DDILHPTLT-----VRET--------LMFAAK--------------LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1524013779 154 DSSMAEWLEEYLRSF---NGALLMVTHD-RYFLDSVTNRIVELDKGKL 197
Cdd:cd03213 143 DSSSALQVMSLLRRLadtGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-197 |
3.65e-18 |
|
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: 83.92 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLfDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT--------VRFLPQN 74
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIlLNGKDITnlppekrdISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 75 PEFYKGDTILTSI------VRENEGQDhvwdlESQAKTMLTKLGFTD-FDILVETLSGGQRKRVALVSVLLSTADLLVLD 147
Cdd:cd03299 80 YALFPHMTVYKNIayglkkRKVDKKEI-----ERKVLEIAEMLGIDHlLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 148 EPTNHLD----SSMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03299 155 EPFSALDvrtkEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
298-453 |
4.61e-18 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 83.57 E-value: 4.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDFT--------YILLkndrigiigpngggKSTLMKIIAGWVEPDEGTITV-GQTV-------- 360
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSltvepgeiFGLLgpn--------gagKTTTIRMLLGLLRPTSGEVRVlGEDVardpaevr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 361 -KMGYFSQENeELDGRLKVIDYIRGAAEY--VKTKDGSVSASQMLERF-LfpSSVQYTTIEKLSGGEKRRLYLLRILMEA 436
Cdd:COG1131 73 rRIGYVPQEP-ALYPDLTVRENLRFFARLygLPRKEARERIDELLELFgL--TDAADRKVGTLSGGMKQRLGLALALLHD 149
|
170
....*....|....*..
gi 1524013779 437 PNVLLLDEPTNDLDIQT 453
Cdd:COG1131 150 PELLILDEPTSGLDPEA 166
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-196 |
4.76e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 85.24 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV------VKGR----NLTVRFLPQ 73
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIslcgepVPSRarhaRQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 74 ----NPEFykgdtiltsIVRENE---GQdhVWDLESQA--KTMLTKLGFTDF----DILVETLSGGQRKRVALVSVLLST 140
Cdd:PRK13537 88 fdnlDPDF---------TVRENLlvfGR--YFGLSAAAarALVPPLLEFAKLenkaDAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 141 ADLLVLDEPTNHLDSSMAEWLEEYLRSFNGA---LLMVTHDRYFLDSVTNRIVELDKGK 196
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARgktILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-196 |
5.73e-18 |
|
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: 83.25 E-value: 5.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRNLT-------VR----FL 71
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfDGRDITglppherARagigYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 72 PQNPEFYKGdtiLTsiVREN--------EGQDHVWDLESQaktmltklgFTDFDILVE-------TLSGGQRKRVALVSV 136
Cdd:cd03224 81 PEGRRIFPE---LT--VEENlllgayarRRAKRKARLERV---------YELFPRLKErrkqlagTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1524013779 137 LLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNG---ALLMVTHDRYFLDSVTNRIVELDKGK 196
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDegvTILLVEQNARFALEIADRAYVLERGR 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-196 |
7.43e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 85.27 E-value: 7.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 9 MTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV------VKGRNLTVR----FLPQ----N 74
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvlgvpVPARARLARarigVVPQfdnlD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 75 PEFykgdtiltsIVREN------EGQDHVWDLESQAKTMLtklgftDF-------DILVETLSGGQRKRVALVSVLLSTA 141
Cdd:PRK13536 127 LEF---------TVRENllvfgrYFGMSTREIEAVIPSLL------EFarleskaDARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 142 DLLVLDEPTNHLDSSMAEWLEEYLRSF---NGALLMVTHDRYFLDSVTNRIVELDKGK 196
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLlarGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-199 |
1.26e-17 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 84.33 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSY-TERLLF---DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEP---DEGKVV-KGRNLT------- 67
Cdd:COG0444 1 LLEVRNLKVYFpTRRGVVkavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILfDGEDLLklsekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 --VR-----FLPQNPE-----FYKGDTILTSIVRENEGQDHVwDLESQAKTMLTKLGFTDFDILVE----TLSGGQRKRV 131
Cdd:COG0444 81 rkIRgreiqMIFQDPMtslnpVMTVGDQIAEPLRIHGGLSKA-EARERAIELLERVGLPDPERRLDryphELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 132 ALVSVLLSTADLLVLDEPTNHLDSSM-AEWLE---EYLRSFNGALLMVTHD----RYFLDSVT----NRIVEL-DKGKLF 198
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIqAQILNllkDLQRELGLAILFITHDlgvvAEIADRVAvmyaGRIVEEgPVEELF 239
|
.
gi 1524013779 199 S 199
Cdd:COG0444 240 E 240
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-194 |
1.31e-17 |
|
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: 80.66 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMT-KSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQNPEFYKGdT 82
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLG-T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 83 ILTSIVrenegqdHVWDlesqaktmltklgftdfdilvETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLE 162
Cdd:cd03223 80 LREQLI-------YPWD---------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170 180 190
....*....|....*....|....*....|..
gi 1524013779 163 EYLRSFNGALLMVTHdRYFLDSVTNRIVELDK 194
Cdd:cd03223 132 QLLKELGITVISVGH-RPSLWKFHDRVLDLDG 162
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
298-485 |
1.35e-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: 80.52 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDFTYILLKNDRigiigpngggKSTLMKIIAGWVEPDEGTITV-GQTV---------KMGYFSQ 367
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIygllgpngagKTTLIKIILGLLKPDSGEIKVlGKDIkkepeevkrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 368 ENEeLDGRLKVIDYIrgaaeyvktkdgsvsasqmlerflfpssvqyttieKLSGGEKRRLYLLRILMEAPNVLLLDEPTN 447
Cdd:cd03230 81 EPS-LYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1524013779 448 DLDIQTLTILEDYLESF---PGIVITVSHDRYFLDRVVRRI 485
Cdd:cd03230 125 GLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRV 165
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-197 |
2.30e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.13 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT------------Vr 69
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrLNGRPLAdwspaelarrraV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 70 fLPQNpefykgdtilTSI-----VRE---------NEGQDHVWDLESQAktmLTKLGFTDF-DILVETLSGGQRKRVALV 134
Cdd:PRK13548 81 -LPQH----------SSLsfpftVEEvvamgraphGLSRAEDDALVAAA---LAQVDLAHLaGRDYPQLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 135 SVL--LSTAD----LLVLDEPTNHLDSSMAEWLEEYLRSF----NGALLMVTHD-----RYfldsvTNRIVELDKGKL 197
Cdd:PRK13548 147 RVLaqLWEPDgpprWLLLDEPTSALDLAHQHHVLRLARQLaherGLAVIVVLHDlnlaaRY-----ADRIVLLHQGRL 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-197 |
2.31e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.11 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKG----------------- 63
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtarslsqqkgli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 64 RNLT--VRFLPQNPEFYKGDTILTSIVrenEGQDHV-----WDLESQAKTMLTKLGFT-DFDILVETLSGGQRKRVALVS 135
Cdd:PRK11264 81 RQLRqhVGFVFQNFNLFPHRTVLENII---EGPVIVkgepkEEATARARELLAKVGLAgKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 136 VLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSF---NGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-197 |
2.33e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.79 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTE-RLLFD---DTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KG-------------- 63
Cdd:PRK11629 5 LLQCDNLCKRYQEgSVQTDvlhNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIfNGqpmsklssaakael 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 64 RNLTVRFLPQN----PEFYKGDTI----LTSIVRENEGQDhvwdlesQAKTMLTKLGFTD-FDILVETLSGGQRKRVALV 134
Cdd:PRK11629 85 RNQKLGFIYQFhhllPDFTALENVamplLIGKKKPAEINS-------RALEMLAAVGLEHrANHRPSELSGGERQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1524013779 135 SVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFN----GALLMVTHDRYfLDSVTNRIVELDKGKL 197
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGELNrlqgTAFLVVTHDLQ-LAKRMSRQLEMRDGRL 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-197 |
2.76e-17 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 80.91 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 7 EHMTKSYTERLL-FDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------------- 67
Cdd:cd03292 4 INVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrVNGQDVSdlrgraipylrrkigvv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 ---VRFLPQNPEFykgDTILTSIVRENEGQDhvwDLESQAKTMLTKLGFTD-FDILVETLSGGQRKRVALVSVLLSTADL 143
Cdd:cd03292 84 fqdFRLLPDRNVY---ENVAFALEVTGVPPR---EIRKRVPAALELVGLSHkHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1524013779 144 LVLDEPTNHLDSSMAEWLEEYLRSFNGA---LLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAgttVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-154 |
2.98e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 81.67 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 5 TIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRFLPQ 73
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVlVDGLDVAttpsrelakrLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 74 NPEFykgDTILTsiVRE---------------NEGQDHVwdleSQAktmLTKLGFTDF-DILVETLSGGQRKRVALVSVL 137
Cdd:COG4604 83 ENHI---NSRLT--VRElvafgrfpyskgrltAEDREII----DEA---IAYLDLEDLaDRYLDELSGGQRQRAFIAMVL 150
|
170
....*....|....*..
gi 1524013779 138 LSTADLLVLDEPTNHLD 154
Cdd:COG4604 151 AQDTDYVLLDEPLNNLD 167
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-190 |
3.39e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.68 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT-----------VRF 70
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIlLDGEPVRfrsprdaqaagIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 LPQN----PEfykgdtiLTsiVREN-----EGQDHVW----DLESQAKTMLTKLGFT-DFDILVETLSGGQRKRVALVSV 136
Cdd:COG1129 84 IHQElnlvPN-------LS--VAENiflgrEPRRGGLidwrAMRRRARELLARLGLDiDPDTPVGDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 137 LLSTADLLVLDEPTNHLDSSMAEWL----EEyLRSFNGALLMVTHdryFLD---SVTNRIV 190
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLfriiRR-LKAQGVAIIYISH---RLDevfEIADRVT 211
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-197 |
3.72e-17 |
|
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: 85.18 E-value: 3.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYT-ERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRFL 71
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIlLNGFSLKdidrhtlrqfINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 72 PQNPEFYKGdTILTSIV---RENEGQDHVWDLESQA--KTMLTK--LGF-TDFDILVETLSGGQRKRVALVSVLLSTADL 143
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLlgaKENVSQDEIWAACEIAeiKDDIENmpLGYqTELSEEGSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 144 LVLDEPTNHLDSSMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-197 |
4.61e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 80.91 E-value: 4.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 10 TKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV------VKGRNLTVRFLPQNP-----EFY 78
Cdd:PRK09493 8 SKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLivdglkVNDPKVDERLIRQEAgmvfqQFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 79 KGDTiLTSIvrENE--GQDHV-----WDLESQAKTMLTKLGFTD-FDILVETLSGGQRKRVALVSVLLSTADLLVLDEPT 150
Cdd:PRK09493 88 LFPH-LTAL--ENVmfGPLRVrgaskEEAEKQARELLAKVGLAErAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1524013779 151 NHLDssmAEWLEEYLRSFNG------ALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:PRK09493 165 SALD---PELRHEVLKVMQDlaeegmTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-197 |
4.77e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.31 E-value: 4.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTVRflpqNPefykGD 81
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEIlIDGKPVRIR----SP----RD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 82 TI----------------LTsiVREN------EGQDHVWDLeSQAKTMLTKL----GFT-DFDILVETLSGGQRKRVALV 134
Cdd:COG3845 77 AIalgigmvhqhfmlvpnLT--VAENivlglePTKGGRLDR-KAARARIRELseryGLDvDPDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 135 SVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSF--NG-ALLMVTHDryfLD---SVTNRIVELDKGKL 197
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITHK---LRevmAIADRVTVLRRGKV 219
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-179 |
4.85e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.53 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 2 NLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRNLT----------VRF 70
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLfEGEDIStlkpeiyrqqVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 LPQNPEFYkGDTILTSIVrenegqdHVWDLESQAKTM------LTKLGFTDfDIL---VETLSGGQRKRVALVSVLLSTA 141
Cdd:PRK10247 86 CAQTPTLF-GDTVYDNLI-------FPWQIRNQQPDPaiflddLERFALPD-TILtknIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1524013779 142 DLLVLDEPTNHLDSS----MAEWLEEYLRSFNGALLMVTHDR 179
Cdd:PRK10247 157 KVLLLDEITSALDESnkhnVNEIIHRYVREQNIAVLWVTHDK 198
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-178 |
5.41e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.06 E-value: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSY----TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT-------V 68
Cdd:COG4525 1 MSMLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEItLDGVPVTgpgadrgV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 69 RFlpQNpefykgDTILTSI-VREN-------EGQDHVwDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLS 139
Cdd:COG4525 81 VF--QK------DALLPWLnVLDNvafglrlRGVPKA-ERRARAEELLALVGLADFaRRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1524013779 140 TADLLVLDEPTNHLDS----SMAEWLEEYLRSFNGALLMVTHD 178
Cdd:COG4525 152 DPRFLLMDEPFGALDAltreQMQELLLDVWQRTGKGVFLITHS 194
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
335-447 |
6.27e-17 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 78.07 E-value: 6.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 335 GKSTLMKIIAGWVEPDEGTITV-GQTV----------KMGYFSQENeELDGRLKVIDYIRGAA--EYVKTKDGSVSASQM 401
Cdd:pfam00005 23 GKSTLLKLIAGLLSPTEGTILLdGQDLtdderkslrkEIGYVFQDP-QLFPRLTVRENLRLGLllKGLSKREKDARAEEA 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1524013779 402 LERF---LFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTN 447
Cdd:pfam00005 102 LEKLglgDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-198 |
6.31e-17 |
|
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: 80.42 E-value: 6.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSY-TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT---------VR-- 69
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSIlLEGTDITklrgkklrkLRrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 70 --FLPQNPEFYKGDTILTSIVRENEGQDHVWDLESQ---------AKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVL 137
Cdd:TIGR02315 81 igMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLGrfseedkerALSALERVGLADKaYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 138 LSTADLLVLDEPTNHLDSSMAEWLEEYLRSFN---GALLMVT-HDRYFLDSVTNRIVELDKGKLF 198
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINkedGITVIINlHQVDLAKKYADRIVGLKAGEIV 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-178 |
6.67e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.88 E-value: 6.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKG-------RNLT------VRF 70
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGtaplaeaREDTrlmfqdARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 LPqnpefYKGdtiltsiVRENEGQDHVWDLESQAKTMLTKLGFTD-FDILVETLSGGQRKRVALVSVLLSTADLLVLDEP 149
Cdd:PRK11247 93 LP-----WKK-------VIDNVGLGLKGQWRDAALQALAAVGLADrANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190
....*....|....*....|....*....|...
gi 1524013779 150 TNHLDS----SMAEWLEEYLRSFNGALLMVTHD 178
Cdd:PRK11247 161 LGALDAltriEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-197 |
7.75e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.00 E-value: 7.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 2 NLLTIEHMTKSY--TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGK----VVKGRNLT-------- 67
Cdd:PRK13640 4 NIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskiTVDGITLTaktvwdir 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 --VRFLPQNPEF-YKGDTIltsivreneGQDHVWDLESQA----------KTMLTKLGFTDF-DILVETLSGGQRKRVAL 133
Cdd:PRK13640 84 ekVGIVFQNPDNqFVGATV---------GDDVAFGLENRAvprpemikivRDVLADVGMLDYiDSEPANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 134 VSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSF----NGALLMVTHDryfLD--SVTNRIVELDKGKL 197
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITHD---IDeaNMADQVLVLDDGKL 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
299-488 |
7.85e-17 |
|
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: 78.63 E-value: 7.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 299 ELEGISKAYGDKVLMKD---------FTYILLKNdrigiigpnGGGKSTLMKIIAGWVEPDEGTITV-GQTVKmGYFSQE 368
Cdd:cd03214 1 EVENLSVGYGGRTVLDDlslsieageIVGILGPN---------GAGKSTLLKTLAGLLKPSSGEILLdGKDLA-SLSPKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 369 neeldgRLKVIDYIRGAAEYVKTKDgsvsasqMLERFlfpssvqyttIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTND 448
Cdd:cd03214 71 ------LARKIAYVPQALELLGLAH-------LADRP----------FNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1524013779 449 LDI----QTLTILEDYLESFPGIVITVSHD-----RYFlDRVV----RRIFAF 488
Cdd:cd03214 128 LDIahqiELLELLRRLARERGKTVVMVLHDlnlaaRYA-DRVIllkdGRIVAQ 179
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
23-204 |
8.70e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.89 E-value: 8.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 23 SFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNL------------TVRFLPQNPEfykgDTILTSIVR 89
Cdd:PRK13639 22 NFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlIKGEPIkydkksllevrkTVGIVFQNPD----DQLFAPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 90 E-------NEGQDHVwDLESQAKTMLTKLGFTDFDILV-ETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWL 161
Cdd:PRK13639 98 EdvafgplNLGLSKE-EVEKRVKEALKAVGMEGFENKPpHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1524013779 162 EEYLRSFNG---ALLMVTHDRYFLDSVTNRIVELDKGKLFSYQTNK 204
Cdd:PRK13639 177 MKLLYDLNKegiTIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-197 |
9.46e-17 |
|
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: 79.46 E-value: 9.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 21 DTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRNLT--------VRFLPQNPEFYKGDTILTSIVREN 91
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLiNGVDVTaappadrpVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 92 EGQDHVWDLESQA-KTMLTKLGFTDFDI-LVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLD----SSMAEWLEEYL 165
Cdd:cd03298 96 SPGLKLTAEDRQAiEVALARVGLAGLEKrLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|..
gi 1524013779 166 RSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
336-488 |
9.84e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 80.13 E-value: 9.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV-----KMGYFSQeNEELDGR--LKVIDYI-------RGAAEYVKTKDGSVsASQ 400
Cdd:COG1121 45 KSTLLKAILGLLPPTSGTVRLfGKPPrrarrRIGYVPQ-RAEVDWDfpITVRDVVlmgrygrRGLFRRPSRADREA-VDE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 401 MLERF-LfpSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFP--GI-VITVSHD-- 474
Cdd:COG1121 123 ALERVgL--EDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRreGKtILVVTHDlg 200
|
170 180
....*....|....*....|
gi 1524013779 475 ---RYFlDRVV---RRIFAF 488
Cdd:COG1121 201 avrEYF-DRVLllnRGLVAH 219
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-178 |
1.02e-16 |
|
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: 79.51 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 24 FSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRN-----LTVRFLPQNPEF------------YKGDTILT 85
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVkVAGASpgkgwRHIGYVPQRHEFawdfpisvahtvMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 86 SIVRENEGQDHVWDLESQAKTMLTKLGftdfDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYL 165
Cdd:TIGR03771 81 GWLRRPCVADFAAVRDALRRVGLTELA----DRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELF 156
|
170
....*....|....*.
gi 1524013779 166 RSFNG---ALLMVTHD 178
Cdd:TIGR03771 157 IELAGagtAILMTTHD 172
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
21-200 |
1.33e-16 |
|
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: 83.17 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 21 DTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNL----------TVRFLPQNPEFYKGdTILTSIVR 89
Cdd:TIGR01842 336 GISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVrLDGADLkqwdretfgkHIGYLPQDVELFPG-TVAENIAR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 90 ENEGQDHVWDLE----SQAKTMLTKL--GFtDFDILV--ETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSS----M 157
Cdd:TIGR01842 415 FGENADPEKIIEaaklAGVHELILRLpdGY-DTVIGPggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEgeqaL 493
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1524013779 158 AEWLEEyLRSFNGALLMVTHdRYFLDSVTNRIVELDKGKLFSY 200
Cdd:TIGR01842 494 ANAIKA-LKARGITVVVITH-RPSLLGCVDKILVLQDGRIARF 534
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
336-488 |
1.45e-16 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 79.70 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV----------KMGYFSQENEeLDGRLKVIDYI-RGAAEYVK-----TKDGSVSA 398
Cdd:COG1120 40 KSTLLRALAGLLKPSSGEVLLdGRDLaslsrrelarRIAYVPQEPP-APFGLTVRELVaLGRYPHLGlfgrpSAEDREAV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 399 SQMLERF----LfpssvQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI----QTLTILEDYLESFPGIVIT 470
Cdd:COG1120 119 EEALERTglehL-----ADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVM 193
|
170 180
....*....|....*....|....*..
gi 1524013779 471 VSHD-----RYFlDRVV----RRIFAF 488
Cdd:COG1120 194 VLHDlnlaaRYA-DRLVllkdGRIVAQ 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-197 |
1.52e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 79.05 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 2 NLLTIEHMTKSYTErllfDDTSFSINEG--------EKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----- 67
Cdd:PRK10584 5 NIVEVHHLKKSVGQ----GEHELSILTGvelvvkrgETIALIGESGSGKSTLLAILAGLDDGSSGEVsLVGQPLHqmdee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 ---------VRFLPQN----PEFYKGDTI-LTSIVR-ENEGQDHvwdleSQAKTMLTKLGFTD-FDILVETLSGGQRKRV 131
Cdd:PRK10584 81 araklrakhVGFVFQSfmliPTLNALENVeLPALLRgESSRQSR-----NGAKALLEQLGLGKrLDHLPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 132 ALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFN----GALLMVTHDRYfLDSVTNRIVELDKGKL 197
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNrehgTTLILVTHDLQ-LAARCDRRLRLVNGQL 224
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-194 |
1.54e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 78.74 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT-------VRFLPQN 74
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqIDGKTATrgdrsrfMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 75 PEFyKGDtiLTSIvrenEGQDHVWDLES-QAKTM----LTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDE 148
Cdd:PRK13543 91 PGL-KAD--LSTL----ENLHFLCGLHGrRAKQMpgsaLAIVGLAGYeDTLVRQLSAGQKKRLALARLWLSPAPLWLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1524013779 149 PTNHLD----SSMAEWLEEYLRSfNGALLMVTHDRYFLDSVTNRIVELDK 194
Cdd:PRK13543 164 PYANLDlegiTLVNRMISAHLRG-GGAALVTTHGAYAAPPVRTRMLTLEA 212
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-200 |
2.16e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.78 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 2 NLLTIEHMTKSY---TERLlfDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT---------- 67
Cdd:PRK13647 3 NIIEVEDLHFRYkdgTKAL--KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGREVNaenekwvrsk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 VRFLPQNPEfykgDTILTSIVRE-------NEGQDHVwDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLS 139
Cdd:PRK13647 81 VGLVFQDPD----DQVFSSTVWDdvafgpvNMGLDKD-EVERRVEEALKAVRMWDFrDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 140 TADLLVLDEPTNHLDSSMAEWLEEYLRSFNGA---LLMVTHDRYFLDSVTNRIVELDKGKLFSY 200
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgktVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-197 |
2.22e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 78.38 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTE-RLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKG-------RNLTVRFLPQN 74
Cdd:PRK10908 1 MIRFEHVSKAYLGgRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghditrlKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 75 PE--FYKGDTILTSIVRENEGQDHVW------DLESQAKTMLTKLGFTD----FDIlveTLSGGQRKRVALVSVLLSTAD 142
Cdd:PRK10908 81 IGmiFQDHHLLMDRTVYDNVAIPLIIagasgdDIRRRVSAALDKVGLLDkaknFPI---QLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 143 LLVLDEPTNHLDSSMAEWLEEYLRSFNG---ALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
336-489 |
2.60e-16 |
|
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: 76.51 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVgqtvkmgyfsqeneeldgrlkvidyirgaaeyvktkDGSVSASQMLERFLFPSSVqytt 415
Cdd:cd00267 38 KSTLLRAIAGLLKPTSGEILI------------------------------------DGKDIAKLPLEELRRRIGY---- 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1524013779 416 IEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFPG---IVITVSHDRYFLDRVVRRIFAFE 489
Cdd:cd00267 78 VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLK 154
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-197 |
4.06e-16 |
|
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: 77.18 E-value: 4.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLE--EPDEGKV-VKGRNLT-------VR---F 70
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEIlFKGEDITdlppeerARlgiF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 L-PQNPEFYKGDTILTSIVRENEGqdhvwdlesqaktmltklgftdfdilvetLSGGQRKRVALVSVLLSTADLLVLDEP 149
Cdd:cd03217 81 LaFQYPPEIPGVKNADFLRYVNEG-----------------------------FSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 150 TNHLDSSMAEWLEE---YLRSFNGALLMVTHDRYFLDSV-TNRIVELDKGKL 197
Cdd:cd03217 132 DSGLDIDALRLVAEvinKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRI 183
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-198 |
4.15e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 78.64 E-value: 4.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 2 NLLTIEHMTKSYT--ERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV------VKGRNLT-----V 68
Cdd:PRK13648 6 SIIVFKNVSFQYQsdASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaITDDNFEklrkhI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 69 RFLPQNPEfykgDTILTSIVR-------ENEGQDHVwDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLST 140
Cdd:PRK13648 86 GIVFQNPD----NQFVGSIVKydvafglENHAVPYD-EMHRRVSEALKQVDMLERaDYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 141 ADLLVLDEPTNHLD----SSMAEWLEEYLRSFNGALLMVTHDryfLDSV--TNRIVELDKGKLF 198
Cdd:PRK13648 161 PSVIILDEATSMLDpdarQNLLDLVRKVKSEHNITIISITHD---LSEAmeADHVIVMNKGTVY 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-202 |
6.08e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 78.62 E-value: 6.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSY---TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT--------- 67
Cdd:PRK13650 2 SNIIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiIDGDLLTeenvwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 -VRFLPQNPEF-YKGDTILTSIV--RENEGQDHVwDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTAD 142
Cdd:PRK13650 82 kIGMVFQNPDNqFVGATVEDDVAfgLENKGIPHE-EMKERVNEALELVGMQDFkEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 143 LLVLDEPTNHLDSSMAEWLEEYLRS----FNGALLMVTHDryfLDSVT--NRIVELDKGKLFSYQT 202
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGirddYQMTVISITHD---LDEVAlsDRVLVMKNGQVESTST 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-197 |
6.89e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.11 E-value: 6.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 6 IEHMTKSYT--ERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV------VKGRNLT-----VRFLP 72
Cdd:PRK13632 10 VENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkidgitISKENLKeirkkIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 73 QNPEF-YKGDTILTSI--------VRENEGQDHVWDLEsqaktmlTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTAD 142
Cdd:PRK13632 90 QNPDNqFIGATVEDDIafglenkkVPPKKMKDIIDDLA-------KKVGMEDYlDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 143 LLVLDEPTNHLD----SSMAEWLEEYLRSFNGALLMVTHDryfLDSVTN--RIVELDKGKL 197
Cdd:PRK13632 163 IIIFDESTSMLDpkgkREIKKIMVDLRKTRKKTLISITHD---MDEAILadKVIVFSEGKL 220
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-197 |
7.98e-16 |
|
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: 76.82 E-value: 7.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 23 SFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTVRFLPQNPE---FYKGDTILTSIVRENEG----- 93
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIkVNDQSHTGLAPYQRPVsmlFQENNLFAHLTVRQNIGlglhp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 94 --------QDHVWDLESQaktmltkLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEY 164
Cdd:TIGR01277 98 glklnaeqQEKVVDAAQQ-------VGIADYlDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 1524013779 165 LRSF----NGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:TIGR01277 171 VKQLcserQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
366-511 |
9.05e-16 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 81.06 E-value: 9.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 366 SQENEELDGRLKVIDYIRGAAEyvktkdgsvsASQMLERFLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEP 445
Cdd:PLN03073 302 SQRLEEIYKRLELIDAYTAEAR----------AASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEP 371
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 446 TNDLDIQTLTILEDYLESFPGIVITVSHDRYFLDRVVRRIFAFEGNGMVTqYEGGFTDYQAAYSEK 511
Cdd:PLN03073 372 TNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVT-YKGDYDTFERTREEQ 436
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-178 |
9.53e-16 |
|
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: 76.84 E-value: 9.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEE-----PDEGKV-VKGRN--------LTVR 69
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVlLDGKDiydldvdvLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 70 ------FLPQNPeF----------------YKGDTILTSIVRENEGQDHVWDlesQAKTMLTKLGftdfdilvetLSGGQ 127
Cdd:cd03260 81 rrvgmvFQKPNP-FpgsiydnvayglrlhgIKLKEELDERVEEALRKAALWD---EVKDRLHALG----------LSGGQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1524013779 128 RKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNG--ALLMVTHD 178
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
298-482 |
1.03e-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: 75.30 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTItvgqtvkmgyfsqeneELDGRLk 377
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI----------------LIDGED- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 378 vidyIRGAAEYVKTKDGSVSAsqMLERF-LFPS-SVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLT 455
Cdd:cd03229 64 ----LTDLEDELPPLRRRIGM--VFQDFaLFPHlTVLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190
....*....|....*....|....*....|....*
gi 1524013779 456 ILEDYLESF---PGI-VITVSHD----RYFLDRVV 482
Cdd:cd03229 138 EVRALLKSLqaqLGItVVLVTHDldeaARLADRVV 172
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-202 |
1.26e-15 |
|
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: 76.57 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTE-RLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTvrflPQNPEFYK-- 79
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfIDGEDIR----EQDPVELRrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 80 -GDTIlTSI-------VRENEG---QDHVWDLESQAKTMLTKLGFTDFDILV------ETLSGGQRKRVALVSVLLSTAD 142
Cdd:cd03295 77 iGYVI-QQIglfphmtVEENIAlvpKLLKWPKEKIRERADELLALVGLDPAEfadrypHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 143 LLVLDEPTNHLDSSMAEWLEEYLRSFNGAL----LMVTHDRYFLDSVTNRIVELDKGKLFSYQT 202
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELgktiVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-197 |
1.46e-15 |
|
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: 79.85 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 20 DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV---------------VKGRNLTVR---FLPQNPEFYKGD 81
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpgPDGRGRAKRyigILHQEYDLYPHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 82 TILTSIVrENEGQDHVWDL-ESQAKTMLTKLGFTD------FDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLD 154
Cdd:TIGR03269 381 TVLDNLT-EAIGLELPDELaRMKAVITLKMVGFDEekaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1524013779 155 S----SMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:TIGR03269 460 PitkvDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3-177 |
1.53e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 76.16 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTE-RLLFDdtsFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT--------VRFLP 72
Cdd:PRK10771 1 MLKLTDITWLYHHlPMRFD---LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtLNGQDHTttppsrrpVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 73 QNPEFYKGDTILTSI-------VRENEGQDHvwdlesQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLL 144
Cdd:PRK10771 78 QENNLFSHLTVAQNIglglnpgLKLNAAQRE------KLHAIARQMGIEDLlARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 1524013779 145 VLDEPTNHLDSS----MAEWLEEYLRSFNGALLMVTH 177
Cdd:PRK10771 152 LLDEPFSALDPAlrqeMLTLVSQVCQERQLTLLMVSH 188
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-199 |
1.54e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.15 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 15 ERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEE--PDEGKVVkgrnltvrfLPQNPeFYKGDTILtsivrene 92
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVD---------VPDNQ-FGREASLI-------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 93 gqDHVWDLES--QAKTMLTKLGFTD---FDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEW----LEE 163
Cdd:COG2401 104 --DAIGRKGDfkDAVELLNAVGLSDavlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRvarnLQK 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 1524013779 164 YLRSFNGALLMVTHDRYFLDSVT-NRIVELDKGKLFS 199
Cdd:COG2401 182 LARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
336-489 |
1.81e-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: 75.79 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVGQTV---------------KMGYFSQENEeLDGRLKVIDYIRGAAEYVKTKDGSVSASQ 400
Cdd:cd03297 36 KSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLVFQQYA-LFPHLNVRENLAFGLKRKRNREDRISVDE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 401 MLERFLFpSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLES----FPGIVITVSHDRY 476
Cdd:cd03297 115 LLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQikknLNIPVIFVTHDLS 193
|
170
....*....|...
gi 1524013779 477 FLDRVVRRIFAFE 489
Cdd:cd03297 194 EAEYLADRIVVME 206
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-203 |
2.02e-15 |
|
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: 79.46 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 23 SFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTvrflPQNPEFYKGdtiLTSIV-------RENEGQ 94
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEIlLDGQPVT----ADNREAYRQ---LFSAVfsdfhlfDRLLGL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 95 DHVwDLESQAKTMLTKLG-----------FTDFDilvetLSGGQRKRVALVSVLLSTADLLVLDE------PTN-----H 152
Cdd:COG4615 425 DGE-ADPARARELLERLEldhkvsvedgrFSTTD-----LSQGQRKRLALLVALLEDRPILVFDEwaadqdPEFrrvfyT 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 153 ldssmaEWLEEyLRSFNGALLMVTHD-RYFldSVTNRIVELDKGKLFSYQTN 203
Cdd:COG4615 499 ------ELLPE-LKARGKTVIAISHDdRYF--DLADRVLKMDYGKLVELTGP 541
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-197 |
2.31e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.48 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTER--LLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VR 69
Cdd:PRK11160 338 SLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIlLNGQPIAdyseaalrqaIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 70 FLPQNPEfykgdtILTSIVREN------EGQDHvwdlesQAKTMLTKLGFTDfdiLVET--------------LSGGQRK 129
Cdd:PRK11160 418 VVSQRVH------LFSATLRDNlllaapNASDE------ALIEVLQQVGLEK---LLEDdkglnawlgeggrqLSGGEQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 130 RVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSF--NGALLMVTHDRYFLDSVtNRIVELDKGKL 197
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTVLMITHRLTGLEQF-DRICVMDNGQI 551
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-197 |
2.52e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.43 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 20 DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNltvrflP--QNPEFYKgdTIltSIVRENEGQDH 96
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVrVLGYV------PfkRRKEFAR--RI--GVVFGQRSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 97 vWDL----------------ESQAKT---MLTK-LGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLD- 154
Cdd:COG4586 109 -WDLpaidsfrllkaiyripDAEYKKrldELVElLDLGELlDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDv 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1524013779 155 ---SSMAEWLEEYLRSFNGALLMVTHDryfLDSVT---NRIVELDKGKL 197
Cdd:COG4586 188 vskEAIREFLKEYNRERGTTILLTSHD---MDDIEalcDRVIVIDHGRI 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1-196 |
2.79e-15 |
|
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: 74.81 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVkgRNLTVRFLPQNPefykg 80
Cdd:cd03250 3 VEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS--VPGSIAYVSQEP----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 81 dTILTSIVRENEGQDHVWDLESQAKTM----LTKlgftDFDILVE-----------TLSGGQRKRVALVSVLLSTADLLV 145
Cdd:cd03250 76 -WIQNGTIRENILFGKPFDEERYEKVIkacaLEP----DLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1524013779 146 LDEPTNHLDSSMAEWLEEYLrsFNGALL------MVTHDRYFLDSVtNRIVELDKGK 196
Cdd:cd03250 151 LDDPLSAVDAHVGRHIFENC--ILGLLLnnktriLVTHQLQLLPHA-DQIVVLDNGR 204
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
10-197 |
2.80e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 76.66 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 10 TKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKG------RNL-TVR----FLPQNPEf 77
Cdd:PRK13633 17 NEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyVDGldtsdeENLwDIRnkagMVFQNPD- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 78 ykgDTILTSIVR-------ENEGQDHVwDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEP 149
Cdd:PRK13633 96 ---NQIVATIVEedvafgpENLGIPPE-EIRERVDESLKKVGMYEYrRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 150 TNHLDSS----MAEWLEEYLRSFNGALLMVTHdryFLDSV--TNRIVELDKGKL 197
Cdd:PRK13633 172 TAMLDPSgrreVVNTIKELNKKYGITIILITH---YMEEAveADRIIVMDSGKV 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
336-488 |
3.65e-15 |
|
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: 74.88 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTVKM-----GYFSQeNEELD-------------GRLKVIDYIRGAAEYVKTKdgsv 396
Cdd:cd03235 38 KSTLLKAILGLLKPTSGSIRVfGKPLEKerkriGYVPQ-RRSIDrdfpisvrdvvlmGLYGHKGLFRRLSKADKAK---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 397 sASQMLERflfpssVQYT-----TIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT----LTILEDYLESfpGI 467
Cdd:cd03235 113 -VDEALER------VGLSeladrQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTqediYELLRELRRE--GM 183
|
170 180
....*....|....*....|....*....
gi 1524013779 468 -VITVSHD----RYFLDRVV---RRIFAF 488
Cdd:cd03235 184 tILVVTHDlglvLEYFDRVLllnRTVVAS 212
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-200 |
3.95e-15 |
|
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: 74.37 E-value: 3.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERL--LFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNL------TVR----F 70
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIeIDGIDIstipleDLRssltI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 LPQNPEFYKGdTILTSIVRENEgqdhvwdlesqaktmltklgFTDFDILV--------ETLSGGQRKRVALVSVLLSTAD 142
Cdd:cd03369 87 IPQDPTLFSG-TIRSNLDPFDE--------------------YSDEEIYGalrvseggLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 143 LLVLDEPTNHLDSSMAEWLEEYLR-SFNGALLMVTHDRyfLDSVT--NRIVELDKGKLFSY 200
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIReEFTNSTILTIAHR--LRTIIdyDKILVMDAGEVKEY 204
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-196 |
4.28e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 76.24 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT------------VRF 70
Cdd:PRK13637 8 LTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiIDGVDITdkkvklsdirkkVGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 LPQNPEFYK-GDTILTSI----VRENEGQDHVWDLESQAKTM--LTKLGFTD---FDilvetLSGGQRKRVALVSVLLST 140
Cdd:PRK13637 88 VFQYPEYQLfEETIEKDIafgpINLGLSEEEIENRVKRAMNIvgLDYEDYKDkspFE-----LSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 141 ADLLVLDEPTNHLD----SSMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGK 196
Cdd:PRK13637 163 PKILILDEPTAGLDpkgrDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
16-178 |
4.74e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.35 E-value: 4.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 16 RLLfdDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEePDEGKV-VKGRNLT---------VR-FLPQN-------PEF 77
Cdd:PRK03695 11 RLG--PLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIqFAGQPLEawsaaelarHRaYLSQQqtppfamPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 78 YKGDTILTSIVRENEGQDHVWDLESQaktmltkLGFTDFdiL---VETLSGGQRKRVALVSVLL-------STADLLVLD 147
Cdd:PRK03695 88 QYLTLHQPDKTRTEAVASALNEVAEA-------LGLDDK--LgrsVNQLSGGEWQRVRLAAVVLqvwpdinPAGQLLLLD 158
|
170 180 190
....*....|....*....|....*....|....
gi 1524013779 148 EPTNHLDSSMAEWLEEYLRSF---NGALLMVTHD 178
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELcqqGIAVVMSSHD 192
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-200 |
5.64e-15 |
|
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: 74.45 E-value: 5.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 20 DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT------VR----FLPQNPefykgdTILTSIV 88
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIlIDGVDISkiglhdLRsrisIIPQDP------VLFSGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 89 REN-----EGQDH-VWD-LE-SQAKTMLTKL-GFTDFDILV--ETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSM 157
Cdd:cd03244 95 RSNldpfgEYSDEeLWQaLErVGLKEFVESLpGGLDTVVEEggENLSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1524013779 158 AEWLEEYLRS-FNGA-LLMVTHdRyfLDSVT--NRIVELDKGKLFSY 200
Cdd:cd03244 175 DALIQKTIREaFKDCtVLTIAH-R--LDTIIdsDRILVLDKGRVVEF 218
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-199 |
6.09e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 76.31 E-value: 6.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYT-ERLLF----------DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRNLT--- 67
Cdd:COG4608 7 LLEVRDLKKHFPvRGGLFgrtvgvvkavDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfDGQDITgls 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 ------VR------FlpQNPefYK--------GDTILTSIvrENEGQDHVWDLESQAKTMLTKLG------------Ftd 115
Cdd:COG4608 87 grelrpLRrrmqmvF--QDP--YAslnprmtvGDIIAEPL--RIHGLASKAERRERVAELLELVGlrpehadrypheF-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 116 fdilvetlSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSM-AE---WLEEYLRSFNGALLMVTHD----RYFLDSVT- 186
Cdd:COG4608 159 --------SGGQRQRIGIARALALNPKLIVCDEPVSALDVSIqAQvlnLLEDLQDELGLTYLFISHDlsvvRHISDRVAv 230
|
250
....*....|....*..
gi 1524013779 187 ---NRIVEL-DKGKLFS 199
Cdd:COG4608 231 mylGKIVEIaPRDELYA 247
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-202 |
7.32e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.54 E-value: 7.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-------------KGRNlT 67
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllplhaRARR-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 VRFLPQNPEFYKGDTILTSI-----VRENEGQDHvwdLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTA 141
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLmavlqIRDDLSAEQ---REDRANELMEEFHIEHLrDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 142 DLLVLDEPTNHLDSSMA---EWLEEYLRSFNGALLMVTHD-RYFLDsVTNRIVELDKGKLFSYQT 202
Cdd:PRK10895 157 KFILLDEPFAGVDPISVidiKRIIEHLRDSGLGVLITDHNvRETLA-VCERAYIVSQGHLIAHGT 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-197 |
7.40e-15 |
|
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: 74.19 E-value: 7.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 7 EHMTKSY-TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKG---RNLTVRFL-------PQN 74
Cdd:cd03253 4 ENVTFAYdPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIlIDGqdiREVTLDSLrraigvvPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 75 -PEFykGDTILTSIV--RENEGQDHVWDLESQAKTMLTKLGFTD-FDILV-E---TLSGGQRKRVALVSVLLSTADLLVL 146
Cdd:cd03253 84 tVLF--NDTIGYNIRygRPDATDEEVIEAAKAAQIHDKIMRFPDgYDTIVgErglKLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 147 DEPTNHLDSSMAEWLEEYLRSF--NGALLMVTHDryfLDSVTN--RIVELDKGKL 197
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVskGRTTIVIAHR---LSTIVNadKIIVLKDGRI 213
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-197 |
1.06e-14 |
|
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: 75.92 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 21 DTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGK-VVKGRNL----TVRFLPqnPE------FYKGDTILTSI-V 88
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEiVLNGRTLfdsrKGIFLP--PEkrrigyVFQEARLFPHLsV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 89 RENegqdhvwdLESQAKTMLTKLGFTDFDILVE-------------TLSGGQRKRVALVSVLLSTADLLVLDEPTNHLD- 154
Cdd:TIGR02142 93 RGN--------LRYGMKRARPSERRISFERVIEllgighllgrlpgRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDd 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1524013779 155 SSMAE---WLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:TIGR02142 165 PRKYEilpYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-196 |
1.11e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 73.86 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRNLT-------VR--- 69
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfDGEDITglpphriARlgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 70 -FLPQnpefykGDTI---LTsiVREN---------EGQDHVWDLESQaktmltklgFTDFDILVE-------TLSGGQRK 129
Cdd:COG0410 81 gYVPE------GRRIfpsLT--VEENlllgayarrDRAEVRADLERV---------YELFPRLKErrrqragTLSGGEQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 130 RVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNG---ALLMVTHDRYFLDSVTNRIVELDKGK 196
Cdd:COG0410 144 MLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRegvTILLVEQNARFALEIADRAYVLERGR 213
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-178 |
1.65e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.81 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRNLTVR------------ 69
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyRMRDGQLRdlyalseaerrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 70 -------FLPQNP------EFYKGDTI---LTSIvreneGQDHVWDLESQAKTMLTK--LGFTDFDILVETLSGGQRKRV 131
Cdd:PRK11701 86 llrtewgFVHQHPrdglrmQVSAGGNIgerLMAV-----GARHYGDIRATAGDWLERveIDAARIDDLPTTFSGGMQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 132 ALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRS----FNGALLMVTHD 178
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlvreLGLAVVIVTHD 211
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
545-611 |
1.71e-14 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 68.26 E-value: 1.71e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 545 KFSFHEQREWDTIEDEITSLEDSIEELENEILKAA--SDYSKLAKLMEEKEEKETCLNDKMERWLELNE 611
Cdd:pfam16326 1 KLSYKEQRELEELEAEIEKLEEEIAELEAQLADPElySDYEKLQELSAELEELEAELEELYERWEELEE 69
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
336-489 |
2.28e-14 |
|
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: 72.50 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV----------KMGY-------------------FSQENEELDgRLKVIDYIRGA 385
Cdd:cd03225 40 KSTLLRLLNGLLGPTSGEVLVdGKDLtklslkelrrKVGLvfqnpddqffgptveeevaFGLENLGLP-EEEIEERVEEA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 386 AEYVKTKDgsvsasqMLERFLFpssvqyttieKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFP 465
Cdd:cd03225 119 LELVGLEG-------LRDRSPF----------TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLK 181
|
170 180
....*....|....*....|....*..
gi 1524013779 466 --GI-VITVSHDRYFLDRVVRRIFAFE 489
Cdd:cd03225 182 aeGKtIIIVTHDLDLLLELADRVIVLE 208
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
336-490 |
2.69e-14 |
|
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: 71.26 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVGqtvkmgyfSQENEELDgrlkvIDYIRGAAEYVktkdgsvsaSQmlERFLFPssvqyTT 415
Cdd:cd03228 41 KSTLLKLLLRLYDPTSGEILID--------GVDLRDLD-----LESLRKNIAYV---------PQ--DPFLFS-----GT 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 416 IEK--LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFPG--IVITVSHdRYFLDRVVRRIFAFEG 490
Cdd:cd03228 92 IREniLSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAH-RLSTIRDADRIIVLDD 169
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-197 |
2.88e-14 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 75.94 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 14 TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRFLPQNPEFYKGdT 82
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrLDGADLSqwdreelgrhIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 83 ILTSIVRENEGQDHvwDLESQAKT-----MLTKL--GFtDFDILVE--TLSGGQRKRVALvsvllstA-----D--LLVL 146
Cdd:COG4618 422 IAENIARFGDADPE--KVVAAAKLagvheMILRLpdGY-DTRIGEGgaRLSGGQRQRIGL-------AralygDprLVVL 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 147 DEPTNHLDS----SMAEWLEEyLRSFNGALLMVTHDRYFLdSVTNRIVELDKGKL 197
Cdd:COG4618 492 DEPNSNLDDegeaALAAAIRA-LKARGATVVVITHRPSLL-AAVDKLLVLRDGRV 544
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-178 |
3.18e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.81 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTvrflpqNPEFYKGd 81
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSItLDGKPVE------GPGAERG- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 82 tiltsIVRENEG-------QDHVW-----------DLESQAKTMLTKLGFTDFDI-LVETLSGGQRKRVALVSVLLSTAD 142
Cdd:PRK11248 74 -----VVFQNEGllpwrnvQDNVAfglqlagvekmQRLEIAHQMLKKVGLEGAEKrYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1524013779 143 LLVLDEPTNHLDSSMAEWLEEYL----RSFNGALLMVTHD 178
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLlklwQETGKQVLLITHD 188
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-178 |
3.61e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.57 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 23 SFSINEGEKIGLIGINGTGKSTLLKIVAGLeEPDEGKV-VKGRNLT---------VR-FLPQN--PEF------Ykgdti 83
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEIlLNGRPLSdwsaaelarHRaYLSQQqsPPFampvfqY----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 84 LTSIVRENEGQDHVWDLESQaktmLT-KLGFTDF-DILVETLSGGQRKRVALVSVLL-------STADLLVLDEPTNHLD 154
Cdd:COG4138 90 LALHQPAGASSEAVEQLLAQ----LAeALGLEDKlSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSLD 165
|
170 180
....*....|....*....|....*...
gi 1524013779 155 ----SSMAEWLEEYLRSfNGALLMVTHD 178
Cdd:COG4138 166 vaqqAALDRLLRELCQQ-GITVVMSSHD 192
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-195 |
3.91e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 75.23 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMT-KSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQNPEFYKGdT 82
Cdd:COG4178 363 LALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLG-T 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 83 ILTSIVRENEGQDHVwdlESQAKTMLTKLGFTDfdiLVE----------TLSGGQRKRVALVSVLLSTADLLVLDEPTNH 152
Cdd:COG4178 442 LREALLYPATAEAFS---DAELREALEAVGLGH---LAErldeeadwdqVLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1524013779 153 LDSSMAEWLEEYLRS--FNGALLMVTHdRYFLDSVTNRIVELDKG 195
Cdd:COG4178 516 LDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-197 |
5.71e-14 |
|
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: 73.30 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 34 LIGINGTGKSTLLKIVAGLEEPDEGKVVKG-----------RNLTVRFlpQNPEFYKGDTILTSIV----RENEGQDhvw 98
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDgedvtnvpphlRHINMVF--QSYALFPHMTVEENVAfglkMRKVPRA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 99 DLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNGAL----L 173
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFaDRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLgitfV 155
|
170 180
....*....|....*....|....
gi 1524013779 174 MVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKI 179
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
336-490 |
6.36e-14 |
|
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: 71.59 E-value: 6.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV----------KMGY-------------------FSQEN-----EELDGRlkvid 380
Cdd:COG1122 40 KSTLLRLLNGLLKPTSGEVLVdGKDItkknlrelrrKVGLvfqnpddqlfaptveedvaFGPENlglprEEIRER----- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 381 yIRGAAEYVKTKDgsvsasqMLERFLFpssvqyttieKLSGGEKRRLYLLRIL-MEaPNVLLLDEPTNDLDIQTLTILED 459
Cdd:COG1122 115 -VEEALELVGLEH-------LADRPPH----------ELSGGQKQRVAIAGVLaME-PEVLVLDEPTAGLDPRGRRELLE 175
|
170 180 190
....*....|....*....|....*....|....
gi 1524013779 460 YLESFP--GI-VITVSHDRYFLDRVVRRIFAFEG 490
Cdd:COG1122 176 LLKRLNkeGKtVIIVTHDLDLVAELADRVIVLDD 209
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-226 |
8.11e-14 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 71.10 E-value: 8.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 12 SYTE-RLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNL------TVR----FLPQNPEFYK 79
Cdd:cd03254 11 SYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlIDGIDIrdisrkSLRsmigVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 80 GdTILTSI-VRENEGQDHVWDLESQAktmltkLGFTDF---------DILVE---TLSGGQRKRVALVSVLLSTADLLVL 146
Cdd:cd03254 91 G-TIMENIrLGRPNATDEEVIEAAKE------AGAHDFimklpngydTVLGEnggNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 147 DEPTNHLDSSMAEWLEEYLRSF--NGALLMVTHDryfLDSVTN--RIVELDKGKLFSyqtnkvngggadrestQGCYEEY 222
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKLmkGRTSIIIAHR---LSTIKNadKILVLDDGKIIE----------------EGTHDEL 224
|
....
gi 1524013779 223 LKLK 226
Cdd:cd03254 225 LAKK 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-196 |
9.05e-14 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 71.11 E-value: 9.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSY--TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRF 70
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIlIDGHDVRdytlaslrrqIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 LPQNPeFYKGDTILTSIV--RENEGQDHVWDLESQAKTMLTKLGFTD-FDILVE----TLSGGQRKRVALVSVLLSTADL 143
Cdd:cd03251 81 VSQDV-FLFNDTVAENIAygRPGATREEVEEAARAANAHEFIMELPEgYDTVIGergvKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1524013779 144 LVLDEPTNHLDSSMAEWLEEYLRSF--NGALLMVTHDryfLDSVTN--RIVELDKGK 196
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLmkNRTTFVIAHR---LSTIENadRIVVLEDGK 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-196 |
1.04e-13 |
|
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: 72.83 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 21 DTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV----------KGRN--------------------LTVRf 70
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdsaRGIFlpphrrrigyvfqearlfphLSVR- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 lpQNPEF-YKGdtilTSIVRENEGQDHVWDLesqaktmltkLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDE 148
Cdd:COG4148 96 --GNLLYgRKR----APRAERRISFDEVVEL----------LGIGHLlDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 149 PTNHLD-SSMAE---WLEEYLRSFNGALLMVTHDryfLDSV---TNRIVELDKGK 196
Cdd:COG4148 160 PLAALDlARKAEilpYLERLRDELDIPILYVSHS---LDEVarlADHVVLLEQGR 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-198 |
1.07e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.58 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPD----------------EGKVV----K 62
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksagshiellgrtvqrEGRLArdirK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 63 GRNLTvRFLPQNPEFYKGDTILTSIVRENEGQDHVWDL---------ESQAKTMLTKLGFTDF-DILVETLSGGQRKRVA 132
Cdd:PRK09984 84 SRANT-GYIFQQFNLVNRLSVLENVLIGALGSTPFWRTcfswftreqKQRALQALTRVGMVHFaHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 133 LVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFN---GALLMVT-HDRYFLDSVTNRIVELDKGKLF 198
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINqndGITVVVTlHQVDYALRYCERIVALRQGHVF 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-202 |
1.11e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 71.76 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSYT-ERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------V 68
Cdd:PRK13652 1 MHLIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlIRGEPITkenirevrkfV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 69 RFLPQNPEfykgDTILTSIVRE-------NEGQDHVwDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLST 140
Cdd:PRK13652 81 GLVFQNPD----DQIFSPTVEQdiafgpiNLGLDEE-TVAHRVSSALHMLGLEELrDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 141 ADLLVLDEPTNHLDSSMAEWLEEYLRSFNGALLMV----THDRYFLDSVTNRIVELDKGKLFSYQT 202
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTvifsTHQLDLVPEMADYIYVMDKGRIVAYGT 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-195 |
1.24e-13 |
|
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: 70.57 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 20 DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRNLT-------VRFlpQNPEFYKGDTILTSI-VRE 90
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIlEGKQITepgpdrmVVF--QNYSLLPWLTVRENIaLAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 91 NEGQDHVWDLESQA--KTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWL-EEYLR 166
Cdd:TIGR01184 80 DRVLPDLSKSERRAivEEHIALVGLTEAaDKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLqEELMQ 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1524013779 167 SFNGA---LLMVTHDryfLDS---VTNRIVELDKG 195
Cdd:TIGR01184 160 IWEEHrvtVLMVTHD---VDEallLSDRVVMLTNG 191
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
15-198 |
1.26e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.59 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 15 ERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV----------VKGRNLT-----VRFLPQNPE--- 76
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervitagKKNKKLKplrkkVGIVFQFPEhql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 77 FYkgDTILTSI--------VRENEGqdhvwdlESQAKTMLTKLGFTDfDILVET---LSGGQRKRVALVSVLLSTADLLV 145
Cdd:PRK13634 99 FE--ETVEKDIcfgpmnfgVSEEDA-------KQKAREMIELVGLPE-ELLARSpfeLSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 146 LDEPTNHLDSS----MAEWLEEYLRSFNGALLMVTHDryfLDSVTN---RIVELDKGKLF 198
Cdd:PRK13634 169 LDEPTAGLDPKgrkeMMEMFYKLHKEKGLTTVLVTHS---MEDAARyadQIVVMHKGTVF 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
273-450 |
1.50e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.17 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 273 RDQKGLETDqavelDSIESRLGRTTVELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEG 352
Cdd:PRK13536 22 KHQGISEAK-----ASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 353 TITV-GQTV---------KMGYFSQeNEELDGRLKVIDYIRGAAEY--VKTKDGSVSASQMLErFLFPSSVQYTTIEKLS 420
Cdd:PRK13536 97 KITVlGVPVpararlaraRIGVVPQ-FDNLDLEFTVRENLLVFGRYfgMSTREIEAVIPSLLE-FARLESKADARVSDLS 174
|
170 180 190
....*....|....*....|....*....|
gi 1524013779 421 GGEKRRLYLLRILMEAPNVLLLDEPTNDLD 450
Cdd:PRK13536 175 GGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
336-482 |
2.81e-13 |
|
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: 69.83 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV----------KMGYFSQENEE-LDGRLKVIDYIRGAAEYVKTKDGSVSASQMLE 403
Cdd:COG1124 44 KSTLLRALAGLERPWSGEVTFdGRPVtrrrrkafrrRVQMVFQDPYAsLHPRHTVDRILAEPLRIHGLPDREERIAELLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 404 RFLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI----QTLTILEDYLESFPGIVITVSHD----R 475
Cdd:COG1124 124 QVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDlavvA 203
|
....*..
gi 1524013779 476 YFLDRVV 482
Cdd:COG1124 204 HLCDRVA 210
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-200 |
3.11e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 69.66 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 6 IEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNltvRF-LPQNPefykgDTIL 84
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGH---QFdFSQKP-----SEKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 85 TSIVRENEG----QDHVW----------------------DLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVL 137
Cdd:COG4161 77 IRLLRQKVGmvfqQYNLWphltvmenlieapckvlglskeQAREKAMKLLARLRLTDKaDRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 138 LSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNG---ALLMVTHDRYFLDSVTNRIVELDKGKLFSY 200
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
336-486 |
3.47e-13 |
|
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: 69.06 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV--------------KMGY-FSQENeeLDGRLKVIDYIRGAAEYVKTKDGSVS-- 397
Cdd:cd03255 43 KSTLLNILGGLDRPTSGEVRVdGTDIsklsekelaafrrrHIGFvFQSFN--LLPDLTALENVELPLLLAGVPKKERRer 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 398 ASQMLERF-------LFPSsvqyttieKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT----LTILEDYLESFPG 466
Cdd:cd03255 121 AEELLERVglgdrlnHYPS--------ELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGT 192
|
170 180
....*....|....*....|
gi 1524013779 467 IVITVSHDRYFLDRVVRRIF 486
Cdd:cd03255 193 TIVVVTHDPELAEYADRIIE 212
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
336-486 |
3.94e-13 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 72.11 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVG---------QTV--KMGYFSQENEELDGRLKviDYIRGAAEyvktkdgsvSAS----- 399
Cdd:COG4987 374 KSTLLALLLRFLDPQSGSITLGgvdlrdldeDDLrrRIAVVPQRPHLFDTTLR--ENLRLARP---------DATdeelw 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 400 QMLERflfpssVQ-----------YTTI-----EKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT-LTILEDYLE 462
Cdd:COG4987 443 AALER------VGlgdwlaalpdgLDTWlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATeQALLADLLE 516
|
170 180
....*....|....*....|....*
gi 1524013779 463 SFPG-IVITVSHDRYFLDRVVRRIF 486
Cdd:COG4987 517 ALAGrTVLLITHRLAGLERMDRILV 541
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-197 |
3.98e-13 |
|
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: 69.44 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYT--ERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTVrflpQNPEFYK- 79
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlVDGHDLAL----ADPAWLRr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 80 -------GDTILTSIVREN-EGQDHVWDLE--------SQAKTMLTKLGFTDFDILVET---LSGGQRKRVALVSVLLST 140
Cdd:cd03252 77 qvgvvlqENVLFNRSIRDNiALADPGMSMErvieaaklAGAHDFISELPEGYDTIVGEQgagLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 141 ADLLVLDEPTNHLDSSMAEWLEEYLRSF--NGALLMVTHDryfLDSVTN--RIVELDKGKL 197
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAHR---LSTVKNadRIIVMEKGRI 214
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-178 |
4.24e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.63 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 7 EHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRFLPQNP 75
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwLDGEHIQhyaskevarrIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 76 EfYKGDTILTSIVRENEGQDHV----W---DLESQAKTMLTKlGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLD 147
Cdd:PRK10253 91 T-TPGDITVQELVARGRYPHQPlftrWrkeDEEAVTKAMQAT-GITHLaDQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190
....*....|....*....|....*....|....*
gi 1524013779 148 EPTNHLDSS----MAEWLEEYLRSFNGALLMVTHD 178
Cdd:PRK10253 169 EPTTWLDIShqidLLELLSELNREKGYTLAAVLHD 203
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-197 |
4.38e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 69.61 E-value: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 2 NLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTvrflpqnpefykg 80
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvVNGQTIN------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 81 dtiltsIVRENEGQDHVWDlESQAKTMLTKLG--FTDFDI-----LVET------------------------------- 122
Cdd:PRK10619 71 ------LVRDKDGQLKVAD-KNQLRLLRTRLTmvFQHFNLwshmtVLENvmeapiqvlglskqeareravkylakvgide 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 123 ---------LSGGQRKRVALVSVLLSTADLLVLDEPTNHLDssmAEWLEEYLRSFN------GALLMVTHDRYFLDSVTN 187
Cdd:PRK10619 144 raqgkypvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALD---PELVGEVLRIMQqlaeegKTMVVVTHEMGFARHVSS 220
|
250
....*....|
gi 1524013779 188 RIVELDKGKL 197
Cdd:PRK10619 221 HVIFLHQGKI 230
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-197 |
4.44e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.18 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 23 SFSINEGEKIGLIGINGTGKSTLLKIVAGLeEPDEGKV-VKG---RNL-------TVRFLPQNPEFYKGdTILTSIV--R 89
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLkINGielRELdpeswrkHLSWVGQNPQLPHG-TLRDNVLlgN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 90 ENEGQDHVWDL--ESQAKTMLTKL--GFtDFDILVET--LSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEE 163
Cdd:PRK11174 448 PDASDEQLQQAleNAWVSEFLPLLpqGL-DTPIGDQAagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQ 526
|
170 180 190
....*....|....*....|....*....|....*.
gi 1524013779 164 YLR--SFNGALLMVTHDRYFLDSVtNRIVELDKGKL 197
Cdd:PRK11174 527 ALNaaSRRQTTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
296-474 |
4.44e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.37 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 296 TTVELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITVGQTVKMGYFSQEnEELDGR 375
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK-LYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 376 --LKVIDYIRgAAEYVKTKD-----GSVSASQMLErflFPssvqyttIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTND 448
Cdd:PRK09544 82 lpLTVNRFLR-LRPGTKKEDilpalKRVQAGHLID---AP-------MQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190
....*....|....*....|....*....|
gi 1524013779 449 LDIQTLTILEDYLE----SFPGIVITVSHD 474
Cdd:PRK09544 151 VDVNGQVALYDLIDqlrrELDCAVLMVSHD 180
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-154 |
5.57e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.03 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGR---NLTVRFLPQNPE 76
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVlVAGDdveALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 77 FYKGDTILT------SIVR----ENEGQDHVWDLESQA--KTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADL 143
Cdd:PRK09536 81 SVPQDTSLSfefdvrQVVEmgrtPHRSRFDTWTETDRAavERAMERTGVAQFaDRPVTSLSGGERQRVLLARALAQATPV 160
|
170
....*....|.
gi 1524013779 144 LVLDEPTNHLD 154
Cdd:PRK09536 161 LLLDEPTASLD 171
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-154 |
8.17e-13 |
|
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: 71.87 E-value: 8.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 21 DTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRnltVRFLPQNPEFYKG---DTIL----------TS 86
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKhSGR---ISFSPQTSWIMPGtikDNIIfglsydeyryTS 520
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 87 IVRENEGQDHVWDLESQAKTMLTKLGFTdfdilvetLSGGQRKRVALVSVLLSTADLLVLDEPTNHLD 154
Cdd:TIGR01271 521 VIKACQLEEDIALFPEKDKTVLGEGGIT--------LSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-189 |
8.89e-13 |
|
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: 68.55 E-value: 8.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 28 EGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV------------------------VKGRNLTVRFLPQN----PEFYK 79
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildefrgselqnyftkLLEGDVKVIVKPQYvdliPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 80 GDTI-LTSIVRENEGQDHVWDlesqaKTMLTKLgftdFDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDS--- 155
Cdd:cd03236 105 GKVGeLLKKKDERGKLDELVD-----QLELRHV----LDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqr 175
|
170 180 190
....*....|....*....|....*....|....*
gi 1524013779 156 -SMAEWLEEYLRSFNgALLMVTHDRYFLDSVTNRI 189
Cdd:cd03236 176 lNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYI 209
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-183 |
1.03e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.28 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTV-RFLPQNPEFYKG 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlFERQSIKKdLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 81 -----DTILTsiVRENegqdHVWDLESQAKTM-------LTKLGFTdFDILVETLSGGQRKRVALVSVLLSTADLLVLDE 148
Cdd:PRK13540 81 hrsgiNPYLT--LREN----CLYDIHFSPGAVgitelcrLFSLEHL-IDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1524013779 149 PTNHLDSSMAEW----LEEYlRSFNGALLMVTHDRYFLD 183
Cdd:PRK13540 154 PLVALDELSLLTiitkIQEH-RAKGGAVLLTSHQDLPLN 191
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-197 |
1.13e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.12 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 6 IEHMTKSY-TERLLFDdTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNltvRF-LPQNPEFYKGDTI 83
Cdd:PRK11124 5 LNGINCFYgAHQALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN---HFdFSKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 84 ltsivRENEG----QDHVW----------------------DLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSV 136
Cdd:PRK11124 81 -----RRNVGmvfqQYNLWphltvqqnlieapcrvlglskdQALARAEKLLERLRLKPYaDRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 137 LLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNG---ALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtgiTQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
11-197 |
1.20e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.96 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 11 KSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGkvvkgrnlTVRFLPQNPEFYKGDTILTSIVRE 90
Cdd:PRK13651 15 KLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTG--------TIEWIFKDEKNKKKTKEKEKVLEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 91 NEGQDHVWDLESQAKTMLTKLG----FTDFDILVET-------------------------------------------L 123
Cdd:PRK13651 87 LVIQKTRFKKIKKIKEIRRRVGvvfqFAEYQLFEQTiekdiifgpvsmgvskeeakkraakyielvgldesylqrspfeL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 124 SGGQRKRVALVSVLLSTADLLVLDEPTNHLD----SSMAEWLEEyLRSFNGALLMVTHDryfLDSV---TNRIVELDKGK 196
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDN-LNKQGKTIILVTHD---LDNVlewTKRTIFFKDGK 242
|
.
gi 1524013779 197 L 197
Cdd:PRK13651 243 I 243
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-484 |
1.45e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.22 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLE--EPDEGKVV-----------------KGR 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIyhvalcekcgyverpskVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 65 NLTV---RFLPQNPEFYK-GDTILTSIVRENE----------GQDHVWD--LESqaktmLTKLGFTD-------FDILVE 121
Cdd:TIGR03269 81 PCPVcggTLEPEEVDFWNlSDKLRRRIRKRIAimlqrtfalyGDDTVLDnvLEA-----LEEIGYEGkeavgraVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 122 T------------LSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEW----LEEYLRSFNGALLMVTHDRYFLDSV 185
Cdd:TIGR03269 156 VqlshrithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 186 TNRIVELDKGKLfsyqtnkvngggadrestqgcyeeylklkAERLDLLEASERKRQSILRVElqwmqrgaRARSTKQKAH 265
Cdd:TIGR03269 236 SDKAIWLENGEI-----------------------------KEEGTPDEVVAVFMEGVSEVE--------KECEVEVGEP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 266 IERYETLRD-----QKGLEtdQAVELDSIESRLGrttvELEGISKAYGdkvlmkdftyillkndrigiigpngGGKSTLM 340
Cdd:TIGR03269 279 IIKVRNVSKryisvDRGVV--KAVDNVSLEVKEG----EIFGIVGTSG-------------------------AGKTTLS 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 341 KIIAGWVEPDEGTITV-----------------GQTVK-MGYFSQE------NEELDGRLKVI------DYIRGAAEYVK 390
Cdd:TIGR03269 328 KIIAGVLEPTSGEVNVrvgdewvdmtkpgpdgrGRAKRyIGILHQEydlyphRTVLDNLTEAIglelpdELARMKAVITL 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 391 TKDG--SVSASQMLERflFPSsvqyttieKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD-IQTLTILEDYL---ESF 464
Cdd:TIGR03269 408 KMVGfdEEKAEEILDK--YPD--------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpITKVDVTHSILkarEEM 477
|
570 580
....*....|....*....|
gi 1524013779 465 PGIVITVSHDRYFLDRVVRR 484
Cdd:TIGR03269 478 EQTFIIVSHDMDFVLDVCDR 497
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-196 |
1.58e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 69.59 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTvrFLPqnPEFYK 79
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImLDGQDIT--HVP--AENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 80 GDTILTS-------IVREN-------------EGQDHVWDlesqAKTMLTKLGFTDFDILveTLSGGQRKRVALVSVLLS 139
Cdd:PRK09452 88 VNTVFQSyalfphmTVFENvafglrmqktpaaEITPRVME----ALRMVQLEEFAQRKPH--QLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 140 TADLLVLDEPTNHLD----SSMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGK 196
Cdd:PRK09452 162 KPKVLLLDESLSALDyklrKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-197 |
2.01e-12 |
|
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: 66.91 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 15 ERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDE---GKV-VKGRNLT-------VRFLPQNPEFYKGDTI 83
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQIlFNGQPRKpdqfqkcVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 84 -----LTSIVRENEGQDHVWDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSM 157
Cdd:cd03234 99 retltYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIgGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1524013779 158 A----EWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:cd03234 179 AlnlvSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
298-450 |
2.17e-12 |
|
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: 66.45 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDFTYILLK--------NDrigiigpngGGKSTLMKIIAGWVEPDEGTITV-GQTVK------- 361
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPgmygllgpNG---------AGKTTLMRILATLTPPSSGTIRIdGQDVLkqpqklr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 362 --MGYFSQENeELDGRLKVIDYIR--GAAEYVKTKDGSVSASQMLERF-LFPSSVQYttIEKLSGGEKRRLYLLRILMEA 436
Cdd:cd03264 72 rrIGYLPQEF-GVYPNFTVREFLDyiAWLKGIPSKEVKARVDEVLELVnLGDRAKKK--IGSLSGGMRRRVGIAQALVGD 148
|
170
....*....|....
gi 1524013779 437 PNVLLLDEPTNDLD 450
Cdd:cd03264 149 PSILIVDEPTAGLD 162
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-197 |
2.51e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.90 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKG-----------RNLTVR 69
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGekrmndvppaeRGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 70 FlpQNPEFYKGDTILTSI--------VRENEGQDHVwdleSQAKTMLtKLGFTdFDILVETLSGGQRKRVALVSVLLSTA 141
Cdd:PRK11000 81 F--QSYALYPHLSVAENMsfglklagAKKEEINQRV----NQVAEVL-QLAHL-LDRKPKALSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 142 DLLVLDEPTNHLDSS----MAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:PRK11000 153 SVFLLDEPLSNLDAAlrvqMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-177 |
2.60e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.55 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 20 DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRnlTVRFLPQNPEFYKGDTI----------LTsiV 88
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIlIDGQ--EMRFASTTAALAAGVAIiyqelhlvpeMT--V 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 89 REN---------EGQDHVWDLESQAKTMLTKLGF-TDFDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMA 158
Cdd:PRK11288 97 AENlylgqlphkGGIVNRRLLNYEAREQLEHLGVdIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREI 176
|
170 180
....*....|....*....|..
gi 1524013779 159 EWLE---EYLRSFNGALLMVTH 177
Cdd:PRK11288 177 EQLFrviRELRAEGRVILYVSH 198
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-176 |
3.28e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 65.75 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 11 KSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGkvVKGrnlTVRF----LPQNPEFYKGDTILTS 86
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS--VEG---DIHYngipYKEFAEKYPGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 87 ivrenEGQDHVWDLESQaKTMltklgftDF------DILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMA-E 159
Cdd:cd03233 90 -----EEDVHFPTLTVR-ETL-------DFalrckgNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAlE 156
|
170
....*....|....*..
gi 1524013779 160 WLeEYLRSFNGALLMVT 176
Cdd:cd03233 157 IL-KCIRTMADVLKTTT 172
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-190 |
3.86e-12 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 64.90 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 26 INEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRnLTVRFLPQNPEfykgdtiltsivrenegqdhvwdlesqak 105
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-ITPVYKPQYID----------------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 106 tmltklgftdfdilvetLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDS----SMAEWLEEYLRSFNGALLMVTHDRYF 181
Cdd:cd03222 72 -----------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAIRRLSEEGKKTALVVEHDLAV 134
|
....*....
gi 1524013779 182 LDSVTNRIV 190
Cdd:cd03222 135 LDYLSDRIH 143
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-197 |
3.99e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 67.80 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTER------LlfDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT--------- 67
Cdd:COG1135 2 IELENLSKTFPTKggpvtaL--DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVlVDGVDLTalserelra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 VR------FlpQNpeFYkgdtILTSI-VREN-------EGQDHVwDLESQAKTMLTKLGFTDF-DILVETLSGGQRKRV- 131
Cdd:COG1135 80 ARrkigmiF--QH--FN----LLSSRtVAENvalpleiAGVPKA-EIRKRVAELLELVGLSDKaDAYPSQLSGGQKQRVg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 132 ---ALV---SVLLStadllvlDEPTNHLDSSMAEWLEEYLRSFNGAL----LMVTHD----RyfldSVTNRIVELDKGKL 197
Cdd:COG1135 151 iarALAnnpKVLLC-------DEATSALDPETTRSILDLLKDINRELgltiVLITHEmdvvR----RICDRVAVLENGRI 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
336-474 |
4.22e-12 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 65.99 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVGQT----------VKMGYFSQENeELDGRLKVIDY------IRGaaeyVKTKDGSVSAS 399
Cdd:cd03263 41 KTTTLKMLTGELRPTSGTAYINGYsirtdrkaarQSLGYCPQFD-ALFDELTVREHlrfyarLKG----LPKSEIKEEVE 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 400 QMLERFLFpSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESF---PGIVITvSHD 474
Cdd:cd03263 116 LLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVrkgRSIILT-THS 191
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-197 |
4.69e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.85 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 23 SFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTvrflPQNPEFYKG-------DTILTSIVRENEGQ 94
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIlLDGKPVT----AEQPEDYRKlfsavftDFHLFDQLLGPEGK 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 95 D-HVWDLESQAKT--MLTKLGFTDFDILVETLSGGQRKRVALVSVLLSTADLLVLDE------PtnHLDSSMAEWLEEYL 165
Cdd:PRK10522 419 PaNPALVEKWLERlkMAHKLELEDGRISNLKLSKGQKKRLALLLALAEERDILLLDEwaadqdP--HFRREFYQVLLPLL 496
|
170 180 190
....*....|....*....|....*....|..
gi 1524013779 166 RSFNGALLMVTHDRYFLDSvTNRIVELDKGKL 197
Cdd:PRK10522 497 QEMGKTIFAISHDDHYFIH-ADRLLEMRNGQL 527
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-197 |
5.13e-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: 5.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSY--TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV---------KGRNL--TVR 69
Cdd:TIGR02203 330 DVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILldghdladyTLASLrrQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 70 FLPQNPEFYKgDTILTSIVRENEGQDHVWDLES-----QAKTMLTKL--GFtDFDILVE--TLSGGQRKRVALVSVLLST 140
Cdd:TIGR02203 410 LVSQDVVLFN-DTIANNIAYGRTEQADRAEIERalaaaYAQDFVDKLplGL-DTPIGENgvLLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1524013779 141 ADLLVLDEPTNHLDSS----MAEWLEEYLRsfNGALLMVTHDryfLDSVTN--RIVELDKGKL 197
Cdd:TIGR02203 488 APILILDEATSALDNEserlVQAALERLMQ--GRTTLVIAHR---LSTIEKadRIVVMDDGRI 545
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-204 |
5.26e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.78 E-value: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 20 DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT--------------VRFLPQNPE---FYkgD 81
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItIAGYHITpetgnknlkklrkkVSLVFQFPEaqlFE--N 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 82 TILTSI--------VRENEGqdhvwdlESQAKTMLTKLGFTDfDILVET---LSGGQRKRVALVSVLLSTADLLVLDEPT 150
Cdd:PRK13641 102 TVLKDVefgpknfgFSEDEA-------KEKALKWLKKVGLSE-DLISKSpfeLSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 151 NHLD----SSMAEWLEEYLRSFNGALLmVTHDRYFLDSVTNRIVELDKGKLFSYQTNK 204
Cdd:PRK13641 174 AGLDpegrKEMMQLFKDYQKAGHTVIL-VTHNMDDVAEYADDVLVLEHGKLIKHASPK 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
336-482 |
7.54e-12 |
|
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: 65.19 E-value: 7.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV------GQTVKMGYFSQeneelDGRL----KVIDYIRGAAEYVKTKDGSVS--ASQMLE 403
Cdd:cd03293 43 KSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ-----QDALlpwlTVLDNVALGLELQGVPKAEARerAEELLE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 404 RF-------LFPSSvqyttiekLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYL----ESFPGIVITVS 472
Cdd:cd03293 118 LVglsgfenAYPHQ--------LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELldiwRETGKTVLLVT 189
|
170
....*....|....
gi 1524013779 473 HD---RYFL-DRVV 482
Cdd:cd03293 190 HDideAVFLaDRVV 203
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-197 |
9.08e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.78 E-value: 9.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERL-LFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKG------------RNLtV 68
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlVSGidtgdfsklqgiRKL-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 69 RFLPQNPEF-YKGDTILTSIV--RENEGQDHVwDLESQAKTMLTKLGFTDFDILV-ETLSGGQRKRVALVSVLLSTADLL 144
Cdd:PRK13644 80 GIVFQNPETqFVGRTVEEDLAfgPENLCLPPI-EIRKRVDRALAEIGLEKYRHRSpKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 145 VLDEPTNHLDSSMAEWLEEYLRSFN---GALLMVTHDRYFLdSVTNRIVELDKGKL 197
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHekgKTIVYITHNLEEL-HDADRIIVMDRGKI 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-216 |
1.15e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.83 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYT----ERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTV--------- 68
Cdd:PRK10535 4 LLELKDIRRSYPsgeeQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYrVAGQDVATldadalaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 69 ------------RFLP-----QN---PEFYKGdtiltsiVRENEGQdhvwdleSQAKTMLTKLGFTD-FDILVETLSGGQ 127
Cdd:PRK10535 84 rrehfgfifqryHLLShltaaQNvevPAVYAG-------LERKQRL-------LRAQELLQRLGLEDrVEYQPSQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 128 RKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNG---ALLMVTHDRYfLDSVTNRIVELDKGKLFSYQTNK 204
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrghTVIIVTHDPQ-VAAQAERVIEIRDGEIVRNPPAQ 228
|
250
....*....|....
gi 1524013779 205 V--NGGGADRESTQ 216
Cdd:PRK10535 229 EkvNVAGGTEPVVN 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-195 |
1.16e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRN-----------LTVRF 70
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItINNINynkldhklaaqLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 LPQNPEFYKGDTILTSI------VRENEGQDHV-W-DLESQAKTMLTKLGF-TDFDILVETLSGGQRKRVALVSVLLSTA 141
Cdd:PRK09700 85 IYQELSVIDELTVLENLyigrhlTKKVCGVNIIdWrEMRVRAAMMLLRVGLkVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1524013779 142 DLLVLDEPTNHLDSSMAEWL---EEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKG 195
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
336-486 |
1.18e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.79 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVGQTVKMGYFSQENeELDGRL--KVIDYI-------RGAAEYVkTKDGSVSASQMLERfl 406
Cdd:NF040873 31 KSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRS-EVPDSLplTVRDLVamgrwarRGLWRRL-TRDDRAAVDDALER-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 407 fpssVQYTTIEK-----LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYL--ESFPGI-VITVSHDryfL 478
Cdd:NF040873 107 ----VGLADLAGrqlgeLSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLaeEHARGAtVVVVTHD---L 179
|
....*...
gi 1524013779 479 DrVVRRIF 486
Cdd:NF040873 180 E-LVRRAD 186
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
336-494 |
1.31e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 64.35 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV-------------KMGYFSQENEELDGRlKVIDYIRGAAE--YVKTKDGSVSAS 399
Cdd:cd03292 40 KSTLLKLIYKEELPTSGTIRVnGQDVsdlrgraipylrrKIGVVFQDFRLLPDR-NVYENVAFALEvtGVPPREIRKRVP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 400 QMLERfLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESF--PGIVITVS-HDRY 476
Cdd:cd03292 119 AALEL-VGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInkAGTTVVVAtHAKE 197
|
170
....*....|....*...
gi 1524013779 477 FLDRVVRRIFAFEgNGMV 494
Cdd:cd03292 198 LVDTTRHRVIALE-RGKL 214
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-150 |
1.40e-11 |
|
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: 64.47 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTVR-----------FL 71
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIrLDGEDITKLppheraragiaYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 72 PQNPEFYkgdTILTsiVREN-----EGQ--------DHVWDLESQAKTMLTKLGftdfdilvETLSGGQRKRVALVSVLL 138
Cdd:TIGR03410 81 PQGREIF---PRLT--VEENlltglAALprrsrkipDEIYELFPVLKEMLGRRG--------GDLSGGQQQQLAIARALV 147
|
170
....*....|..
gi 1524013779 139 STADLLVLDEPT 150
Cdd:TIGR03410 148 TRPKLLLLDEPT 159
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-153 |
1.47e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT-----------VRF 70
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeIGGNPCArltpakahqlgIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 LPQNPEFYKGDTILTSI-VRENEGQdhvwDLESQAKTMLTKLGFT-DFDILVETLSGGQRKRVALVSVLLSTADLLVLDE 148
Cdd:PRK15439 91 VPQEPLLFPNLSVKENIlFGLPKRQ----ASMQKMKQLLAALGCQlDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
....*
gi 1524013779 149 PTNHL 153
Cdd:PRK15439 167 PTASL 171
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-154 |
1.76e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.81 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 5 TIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-----------KGRNLTVRFLPQ 73
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILldaqpleswssKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 74 NPEFYKGDTI--LTSIVRE----NEGQDHVWDLEsQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVL 146
Cdd:PRK10575 93 QLPAAEGMTVreLVAIGRYpwhgALGRFGAADRE-KVEEAISLVGLKPLaHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
....*...
gi 1524013779 147 DEPTNHLD 154
Cdd:PRK10575 172 DEPTSALD 179
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
336-483 |
1.79e-11 |
|
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: 66.93 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV----------KMGYFSQ----------ENEELDGRLKVIDYIRGAAEYVKTKDG 394
Cdd:TIGR02857 361 KSTLLNLLLGFVDPTEGSIAVnGVPLadadadswrdQIAWVPQhpflfagtiaENIRLARPDASDAEIREALERAGLDEF 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 395 SVSASQMLERFLFPSSvqyttiEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFPG--IVITVS 472
Cdd:TIGR02857 441 VAALPQGLDTPIGEGG------AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVT 514
|
170
....*....|....
gi 1524013779 473 HDR---YFLDRVVR 483
Cdd:TIGR02857 515 HRLalaALADRIVV 528
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-196 |
2.21e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 64.32 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLE--EPDEGKV-VKGRNLT-------VR---F 70
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSIlLDGEDILelspderARagiF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 LP-QNPEFYKG---DTILTSIVRENEGQD-HVWDLESQAKTMLTKLGFtDFDIL---V-ETLSGGQRKRVALVSVLLSTA 141
Cdd:COG0396 81 LAfQYPVEIPGvsvSNFLRTALNARRGEElSAREFLKLLKEKMKELGL-DEDFLdryVnEGFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 142 DLLVLDEPTNHLD----SSMAEWLEEyLRSFNGALLMVTHDRYFLDSVT-NRIVELDKGK 196
Cdd:COG0396 160 KLAILDETDSGLDidalRIVAEGVNK-LRSPDRGILIITHYQRILDYIKpDFVHVLVDGR 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
299-482 |
2.39e-11 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 64.13 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 299 ELEGISKAYGD-KVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITVGQTV--------------KMG 363
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrqlrrQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 364 YFSQEN---EELD-------GRLKVIDYIRGAAEYVKTKDgSVSASQMLERF-LfpSSVQYTTIEKLSGGEKRRLYLLRI 432
Cdd:cd03256 82 MIFQQFnliERLSvlenvlsGRLGRRSTWRSLFGLFPKEE-KQRALAALERVgL--LDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 433 LMEAPNVLLLDEPTNDLDIQTLTILEDYLESFP---GIVITVS-HD----RYFLDRVV 482
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINreeGITVIVSlHQvdlaREYADRIV 216
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
7-197 |
2.40e-11 |
|
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: 64.03 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 7 EHMTKSYTER---LLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRFLP 72
Cdd:cd03248 15 QNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlLDGKPISqyehkylhskVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 73 QNPEFYKGDtiltsiVREN-------EGQDHVWDLESQAKT----MLTKLGF-TDFDILVETLSGGQRKRVALVSVLLST 140
Cdd:cd03248 95 QEPVLFARS------LQDNiayglqsCSFECVKEAAQKAHAhsfiSELASGYdTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 141 ADLLVLDEPTNHLDSSMAEWLEEYLRSF--NGALLMVTHdRYFLDSVTNRIVELDKGKL 197
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
298-492 |
2.60e-11 |
|
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: 64.06 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITV-GQTV-------------KMG 363
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdGEDIsglseaelyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 364 YFSQENEELDGrLKVID----YIRgaaEYVKTKDGSVS--ASQMLERFLFPSSVQYTTIEkLSGGEKRRLYLLRILMEAP 437
Cdd:cd03261 81 MLFQSGALFDS-LTVFEnvafPLR---EHTRLSEEEIReiVLEKLEAVGLRGAEDLYPAE-LSGGMKKRVALARALALDP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 438 NVLLLDEPTNDLDIQTLTILEDYL----ESFPGIVITVSHDRYFLDRVVRRIfAFEGNG 492
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIrslkKELGLTSIMVTHDLDTAFAIADRI-AVLYDG 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-197 |
4.42e-11 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 63.82 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 21 DTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT---------VR------------FLPQNpefy 78
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVlIDGQDIAamsrkelreLRrkkismvfqsfaLLPHR---- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 79 kgdTILTSIVRENEGQdHVWDLESQAKTM--LTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLD- 154
Cdd:cd03294 118 ---TVLENVAFGLEVQ-GVPRAEREERAAeaLELVGLEGWeHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDp 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1524013779 155 ---SSMAEWLEEYLRSFNGALLMVTHDryfLDS---VTNRIVELDKGKL 197
Cdd:cd03294 194 lirREMQDELLRLQAELQKTIVFITHD---LDEalrLGDRIAIMKDGRL 239
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
336-482 |
4.72e-11 |
|
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: 65.63 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTVK----------MGYFSQENEELDGRLKviDYIRGAAEYVkTKDGSVSASQM--L 402
Cdd:COG2274 514 KSTLLKLLLGLYEPTSGRILIdGIDLRqidpaslrrqIGVVLQDVFLFSGTIR--ENITLGDPDA-TDEEIIEAARLagL 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 403 ERFL--FPSsvQYTTI-----EKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFPG--IVITVSH 473
Cdd:COG2274 591 HDFIeaLPM--GYDTVvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAH 668
|
170
....*....|..
gi 1524013779 474 DRYFL---DRVV 482
Cdd:COG2274 669 RLSTIrlaDRII 680
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-483 |
5.14e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.50 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSY----TERLLFDDTSFSINEGEKIGLIGINGTGKS-TLLKIVAGLEEP-------------------D 56
Cdd:PRK15134 3 QPLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvypsgdirfhgesllhaS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 57 EGKV--VKGRNLTVRF----LPQNP------EFYKGDTILTSIVRENEGQDHVWDLES----QAKTMLTklgftDFDilv 120
Cdd:PRK15134 83 EQTLrgVRGNKIAMIFqepmVSLNPlhtlekQLYEVLSLHRGMRREAARGEILNCLDRvgirQAAKRLT-----DYP--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 121 ETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMA----EWLEEYLRSFNGALLMVTHD----RYFLDSVT----NR 188
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQaqilQLLRELQQELNMGLLFITHNlsivRKLADRVAvmqnGR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 189 IVELDKGK-LFSyqtnkvngggadreSTQGCYEEYLkLKAERLDLLEASERKRQSILRVE-LQW---MQRGARARSTKQK 263
Cdd:PRK15134 235 CVEQNRAAtLFS--------------APTHPYTQKL-LNSEPSGDPVPLPEPASPLLDVEqLQVafpIRKGILKRTVDHN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 264 ahieryetlrdqkgletdQAVELDSIESRLGRtTVELEGISKAygdkvlmkdftyillkndrigiigpnggGKST----L 339
Cdd:PRK15134 300 ------------------VVVKNISFTLRPGE-TLGLVGESGS----------------------------GKSTtglaL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 340 MKIIAGwvepdEGTITVG-------------------QTVkmgyFSQENEELDGRLKVIDYIrgaAEYVKTKDGSVSASQ 400
Cdd:PRK15134 333 LRLINS-----QGEIWFDgqplhnlnrrqllpvrhriQVV----FQDPNSSLNPRLNVLQII---EEGLRVHQPTLSAAQ 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 401 --------MLERFLFPSSVQYTTIEkLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD----IQTLTILEDYLESFPGIV 468
Cdd:PRK15134 401 reqqviavMEEVGLDPETRHRYPAE-FSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAY 479
|
570
....*....|....*
gi 1524013779 469 ITVSHDRyfldRVVR 483
Cdd:PRK15134 480 LFISHDL----HVVR 490
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
254-474 |
5.28e-11 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 65.46 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 254 GARARSTKQKAHIERYETLRDQKGLETDQAVELDSIESrLGRTTVELEGISKAY-GDKVLMKDFTYILLKNDRIGIIGPN 332
Cdd:TIGR02868 292 AAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVG-LGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPS 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 333 GGGKSTLMKIIAGWVEPDEGTITVG----QTVK-------MGYFSQ----------EN----------EELDG---RLKV 378
Cdd:TIGR02868 371 GSGKSTLLATLAGLLDPLQGEVTLDgvpvSSLDqdevrrrVSVCAQdahlfdttvrENlrlarpdatdEELWAaleRVGL 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 379 IDYIRGAAEYVKTKDGSVSASqmlerflfpssvqyttiekLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT-LTIL 457
Cdd:TIGR02868 451 ADWLRALPDGLDTVLGEGGAR-------------------LSGGERQRLALARALLADAPILLLDEPTEHLDAETaDELL 511
|
250
....*....|....*...
gi 1524013779 458 EDYLESFPG-IVITVSHD 474
Cdd:TIGR02868 512 EDLLAALSGrTVVLITHH 529
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
298-450 |
5.98e-11 |
|
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: 62.30 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITV-GQTV------KMGYFSQEnE 370
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdGKPLdiaarnRIGYLPEE-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 371 ELDGRLKVIDYIRGAAEY--VKTKDGSVSASQMLERFLFpSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTND 448
Cdd:cd03269 80 GLYPKMKVIDQLVYLAQLkgLKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
..
gi 1524013779 449 LD 450
Cdd:cd03269 159 LD 160
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-190 |
9.04e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.61 E-value: 9.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSY-TERLLF---DDTSFSINEGEKIGLIGINGTGKS-TLLKIVAGLEEPdeGKVV------KGRNLT-- 67
Cdd:PRK11022 1 MALLNVDKLSVHFgDESAPFravDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMaeklefNGQDLQri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 ------------VRFLPQ------NPEFYKGDTILTSIvRENEGQDHVWdLESQAKTMLTKLGFTD----FDILVETLSG 125
Cdd:PRK11022 79 sekerrnlvgaeVAMIFQdpmtslNPCYTVGFQIMEAI-KVHQGGNKKT-RRQRAIDLLNQVGIPDpasrLDVYPHQLSG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 126 GQRKRVALVSVLLSTADLLVLDEPTNHLD----SSMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIV 190
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDvtiqAQIIELLLELQQKENMALVLITHDLALVAEAAHKII 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-197 |
1.02e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.84 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 16 RLLFDdTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-------------------KGRNLTVRFlPQNPE 76
Cdd:PRK13649 21 RALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlitstsknkdikqirKKVGLVFQF-PESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 77 FykGDTILTSIV--RENEGQDHVwDLESQAKTMLTKLGFTD--FDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNH 152
Cdd:PRK13649 99 F--EETVLKDVAfgPQNFGVSQE-EAEALAREKLALVGISEslFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 153 LDSSMAEWLEEYLRSFNGA---LLMVTHdryFLDSVTN---RIVELDKGKL 197
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQSgmtIVLVTH---LMDDVANyadFVYVLEKGKL 223
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
298-463 |
1.15e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.90 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITV-GQTV---------KMGYFSQ 367
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVpsrarharqRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 368 eNEELDGRLKVIDYIRGAAEYVktkdgSVSASQMleRFLFPSSVQYTTIE--------KLSGGEKRRLYLLRILMEAPNV 439
Cdd:PRK13537 88 -FDNLDPDFTVRENLLVFGRYF-----GLSAAAA--RALVPPLLEFAKLEnkadakvgELSGGMKRRLTLARALVNDPDV 159
|
170 180
....*....|....*....|....
gi 1524013779 440 LLLDEPTNDLDIQTLTILEDYLES 463
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRS 183
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-197 |
1.20e-10 |
|
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: 64.97 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 2 NLLTIEHMTKSYTERL--LFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGrnlTVRFLPQNPeFY 78
Cdd:TIGR00957 635 NSITVHNATFTWARDLppTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVhMKG---SVAYVPQQA-WI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 79 KGDTILTSIVRENEGQDHVWDLESQAKTMLTklgftDFDILVE-----------TLSGGQRKRVALVSVLLSTADLLVLD 147
Cdd:TIGR00957 711 QNDSLRENILFGKALNEKYYQQVLEACALLP-----DLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 148 EPTNHLDSSMAEWLEEYLRSFNGAL-----LMVTHDRYFLDSVtNRIVELDKGKL 197
Cdd:TIGR00957 786 DPLSAVDAHVGKHIFEHVIGPEGVLknktrILVTHGISYLPQV-DVIIVMSGGKI 839
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
298-475 |
1.29e-10 |
|
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: 61.38 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITV-GQTV--------KMGYFSQe 368
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDVtgvpperrNIGMVFQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 369 neelDGRL----KVIDYIRGAAEYVKTKDGSV--SASQMLERFLFpSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLL 442
Cdd:cd03259 80 ----DYALfphlTVAENIAFGLKLRGVPKAEIraRVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1524013779 443 DEPTNDLDIQT----LTILEDYLESFPGIVITVSHDR 475
Cdd:cd03259 155 DEPLSALDAKLreelREELKELQRELGITTIYVTHDQ 191
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-155 |
1.71e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.88 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYT--ERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNL----------TVRF 70
Cdd:PRK11176 342 IEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIlLDGHDLrdytlaslrnQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 LPQNPEFYKgDTILTSIVRENEGQDHVWDLESQAKtMLTKLGFTD-----FDILV----ETLSGGQRKRVALVSVLLSTA 141
Cdd:PRK11176 422 VSQNVHLFN-DTIANNIAYARTEQYSREQIEEAAR-MAYAMDFINkmdngLDTVIgengVLLSGGQRQRIAIARALLRDS 499
|
170
....*....|....
gi 1524013779 142 DLLVLDEPTNHLDS 155
Cdd:PRK11176 500 PILILDEATSALDT 513
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
336-494 |
1.81e-10 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 61.07 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVGQT-----------VKMGYFSQENEELDGRLKviDYIRGAAEYVKTKDgSVSASQM--L 402
Cdd:cd03245 43 KSTLLKLLAGLYKPTSGSVLLDGTdirqldpadlrRNIGYVPQDVTLFYGTLR--DNITLGAPLADDER-ILRAAELagV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 403 ERFL--FPSSVQYTTIEK---LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFPG--IVITVSHdR 475
Cdd:cd03245 120 TDFVnkHPNGLDLQIGERgrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-R 198
|
170
....*....|....*....
gi 1524013779 476 YFLDRVVRRIFAFEGNGMV 494
Cdd:cd03245 199 PSLLDLVDRIIVMDSGRIV 217
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
336-483 |
1.96e-10 |
|
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: 63.62 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVGQTV-----------KMGYFSQENEELDGRLKviDYIRGAAEyvktkdgSVSASQM--- 401
Cdd:COG4988 376 KSTLLNLLLGFLPPYSGSILINGVDlsdldpaswrrQIAWVPQNPYLFAGTIR--ENLRLGRP-------DASDEELeaa 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 402 -----LERFLFPSSVQYTTI-----EKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFPG--IVI 469
Cdd:COG4988 447 leaagLDEFVAALPDGLDTPlgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVI 526
|
170
....*....|....*..
gi 1524013779 470 TVSHDRYFL---DRVVR 483
Cdd:COG4988 527 LITHRLALLaqaDRILV 543
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-196 |
2.06e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.17 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 2 NLLTIEHMTKSY---TERLlfDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGrnltvrflpQNPEFY 78
Cdd:PRK13636 4 YILKVEELNYNYsdgTHAL--KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFD---------GKPIDY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 79 KGDTILTsiVRENEG----------------QDHVW----------DLESQAKTMLTKLGFTDF-DILVETLSGGQRKRV 131
Cdd:PRK13636 73 SRKGLMK--LRESVGmvfqdpdnqlfsasvyQDVSFgavnlklpedEVRKRVDNALKRTGIEHLkDKPTHCLSFGQKKRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 132 ALVSVLLSTADLLVLDEPTNHLD----SSMAEWLEEYLRSFNGALLMVTHDryfLDSVT---NRIVELDKGK 196
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD---IDIVPlycDNVFVMKEGR 219
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-197 |
2.06e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 63.59 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTER---LLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------V 68
Cdd:TIGR00958 478 LIEFQDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlLDGVPLVqydhhylhrqV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 69 RFLPQNPEFYKGDtiltsiVREN--EGQDHVWDLESQAKTM----------LTKLGFTDFDILVETLSGGQRKRVALVSV 136
Cdd:TIGR00958 558 ALVGQEPVLFSGS------VRENiaYGLTDTPDEEIMAAAKaanahdfimeFPNGYDTEVGEKGSQLSGGQKQRIAIARA 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 137 LLSTADLLVLDEPTNHLDSSMAEWLEEyLRSFNG-ALLMVTHdRYFLDSVTNRIVELDKGKL 197
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAECEQLLQE-SRSRASrTVLLIAH-RLSTVERADQILVLKKGSV 691
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
336-482 |
2.09e-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: 61.64 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTVK-----MGYFSQENeeldgRL----KVIDYIRGAAEYVKTKDGSVS--ASQMLE 403
Cdd:COG1116 50 KSTLLRLIAGLEKPTSGEVLVdGKPVTgpgpdRGVVFQEP-----ALlpwlTVLDNVALGLELRGVPKAERRerARELLE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 404 RF-------LFPSSvqyttiekLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYL----ESFPGIVITVS 472
Cdd:COG1116 125 LVglagfedAYPHQ--------LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELlrlwQETGKTVLFVT 196
|
170
....*....|....
gi 1524013779 473 HDRY---FL-DRVV 482
Cdd:COG1116 197 HDVDeavFLaDRVV 210
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
336-475 |
2.46e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.88 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV----------KMGYFSQE----NEELDGRLKVIDYIRG-AAEYVKTKDGsvsas 399
Cdd:PRK10247 46 KSTLLKIVASLISPTSGTLLFeGEDIstlkpeiyrqQVSYCAQTptlfGDTVYDNLIFPWQIRNqQPDPAIFLDD----- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 400 qmLERFLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILED----YLESFPGIVITVSHDR 475
Cdd:PRK10247 121 --LERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEiihrYVREQNIAVLWVTHDK 198
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-197 |
2.97e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 61.65 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 19 FDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRFLPQNPEF-YKGDTILTS 86
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVkIDGELLTaenvwnlrrkIGMVFQNPDNqFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 87 IV--RENEGQDHVwDLESQAKTMLTKLGFTDFDILVET-LSGGQRKRVALVSVLLSTADLLVLDEPTNHLD----SSMAE 159
Cdd:PRK13642 103 VAfgMENQGIPRE-EMIKRVDEALLAVNMLDFKTREPArLSGGQKQRVAVAGIIALRPEIIILDESTSMLDptgrQEIMR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1524013779 160 WLEEYLRSFNGALLMVTHDryfLDSV--TNRIVELDKGKL 197
Cdd:PRK13642 182 VIHEIKEKYQLTVLSITHD---LDEAasSDRILVMKAGEI 218
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-154 |
3.12e-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: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 21 DTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRnltVRFLPQNPEFYKGdTILTSI---VRENEGQDH 96
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKhSGR---ISFSSQFSWIMPG-TIKENIifgVSYDEYRYK 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 97 VWDLESQAKTMLTKLGFTDFDILVE---TLSGGQRKRVALVSVLLSTADLLVLDEPTNHLD 154
Cdd:cd03291 131 SVVKACQLEEDITKFPEKDNTVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
33-200 |
4.36e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.79 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 33 GLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRNL------------TVRFLPQNPE---FYKG--DTILTSIVRENEGQ 94
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSGLLRPQKGAVLwQGKPLdyskrgllalrqQVATVFQDPEqqiFYTDidSDIAFSLRNLGVPE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 95 DHVWDLESQAKTMLTKLGFTDFDIlvETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNGA--- 171
Cdd:PRK13638 111 AEITRRVDEALTLVDAQHFRHQPI--QCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnh 188
|
170 180
....*....|....*....|....*....
gi 1524013779 172 LLMVTHDRYFLDSVTNRIVELDKGKLFSY 200
Cdd:PRK13638 189 VIISSHDIDLIYEISDAVYVLRQGQILTH 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-204 |
6.54e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.56 E-value: 6.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 20 DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV--------KGRNLTVRFLPQNP----EFYKGDTILTSI 87
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTvdditithKTKDKYIRPVRKRIgmvfQFPESQLFEDTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 88 VRE------NEGQDhVWDLESQAKTMLTKLGFTDfDILVET---LSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMA 158
Cdd:PRK13646 104 EREiifgpkNFKMN-LDEVKNYAHRLLMDLGFSR-DVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1524013779 159 EWLEEYLRSF----NGALLMVTHDRYFLDSVTNRIVELDKGKLFSYQTNK 204
Cdd:PRK13646 182 RQVMRLLKSLqtdeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPK 231
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-197 |
7.14e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.23 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAG-LEEP--DEGKVVKGRnLTVR---------- 69
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGgaPRGARVTGD-VTLNgeplaaidap 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 70 -------FLPQ--NPEF-YKGDTILT-----SIVRENEGQDHVWDLESQAktmltkLGFTDFDIL----VETLSGGQRKR 130
Cdd:PRK13547 80 rlarlraVLPQaaQPAFaFSAREIVLlgrypHARRAGALTHRDGEIAWQA------LALAGATALvgrdVTTLSGGELAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 131 VALVSVL---------LSTADLLVLDEPTNHLDSSMAEWLEEYLRS----FNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:PRK13547 154 VQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRlardWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
5-158 |
7.30e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.82 E-value: 7.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 5 TIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPD--EGKV-VKGRNLT------VRFLPQNP 75
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTIlANNRKPTkqilkrTGFVTQDD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 76 EFYKGDTILTSIV--------RENEGQDHVwdleSQAKTMLTKLGFTDF------DILVETLSGGQRKRVALVSVLLSTA 141
Cdd:PLN03211 150 ILYPHLTVRETLVfcsllrlpKSLTKQEKI----LVAESVISELGLTKCentiigNSFIRGISGGERKRVSIAHEMLINP 225
|
170
....*....|....*..
gi 1524013779 142 DLLVLDEPTNHLDSSMA 158
Cdd:PLN03211 226 SLLILDEPTSGLDATAA 242
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
12-155 |
7.41e-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: 59.48 E-value: 7.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 12 SYTER---LLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV----VKGRNLTVRFL-------PQNPEF 77
Cdd:cd03249 9 RYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgVDIRDLNLRWLrsqiglvSQEPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 78 YKGdTILTSIV--RENEGQDHVWDLESQAKTMLTKLGFTD-FDILV----ETLSGGQRKRVALVSVLLSTADLLVLDEPT 150
Cdd:cd03249 89 FDG-TIAENIRygKPDATDEEVEEAAKKANIHDFIMSLPDgYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
....*
gi 1524013779 151 NHLDS 155
Cdd:cd03249 168 SALDA 172
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-195 |
7.55e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.34 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 2 NLLTIEHMTKSY--TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGK-VVKGRNL--TVRFLPQN-- 74
Cdd:TIGR01257 1936 DILRLNELTKVYsgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDaTVAGKSIltNISDVHQNmg 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 75 --PEFYKGDTILTsivreneGQDHVW-----------DLESQAKTMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLST 140
Cdd:TIGR01257 2016 ycPQFDAIDDLLT-------GREHLYlyarlrgvpaeEIEKVANWSIQSLGLSLYaDRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 141 ADLLVLDEPTNHLDSSMAEWLEEYLRSF---NGALLMVTHDRYFLDSVTNRIVELDKG 195
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIireGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-200 |
7.90e-10 |
|
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: 62.27 E-value: 7.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 17 LLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT------VRF----LPQNPEFYKGDTILT 85
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIiIDGLNIAkiglhdLRFkitiIPQDPVLFSGSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 86 SIVRENEGQDHVW-DLE-SQAKTMLTKL-GFTDFDILV--ETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEW 160
Cdd:TIGR00957 1380 LDPFSQYSDEEVWwALElAHLKTFVSALpDKLDHECAEggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNL 1459
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1524013779 161 LEEYLRS-FNGALLMVTHDRyfLDSVTN--RIVELDKGKLFSY 200
Cdd:TIGR00957 1460 IQSTIRTqFEDCTVLTIAHR--LNTIMDytRVIVLDKGEVAEF 1500
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-197 |
8.93e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 60.58 E-value: 8.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 5 TIEHMTKSYT----ERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTVrfLPQNP---- 75
Cdd:PRK11153 3 ELKNISKVFPqggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlVDGQDLTA--LSEKElrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 76 ---------EFYkgdtILTS-IVREN-------EGQDhvwDLESQAKT--MLTKLGFTDF-DILVETLSGGQRKRVALVS 135
Cdd:PRK11153 81 rrqigmifqHFN----LLSSrTVFDNvalplelAGTP---KAEIKARVteLLELVGLSDKaDRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 136 VLLSTADLLVLDEPTNHLDS----SMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPattrSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-158 |
9.28e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.60 E-value: 9.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 18 LFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPD----EGKVVKGRNLTVRFLPQNPEFYKGDTIL--TSIVREN 91
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgsGSVLLNGMPIDAKEMRAISAYVQQDDLFipTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 92 -------EGQDHVWDLESQA--KTMLTKLGFTD-------FDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDS 155
Cdd:TIGR00955 120 lmfqahlRMPRRVTKKEKRErvDEVLQALGLRKcantrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
...
gi 1524013779 156 SMA 158
Cdd:TIGR00955 200 FMA 202
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
336-482 |
9.58e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.79 E-value: 9.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVGQTVKMGYFSQEneeLDGRL-------------KVIDYIR-GAAEY--VKTKDGSVSAS 399
Cdd:PRK13548 41 KSTLLRALSGELSPDSGEVRLNGRPLADWSPAE---LARRRavlpqhsslsfpfTVEEVVAmGRAPHglSRAEDDALVAA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 400 QM----LERFlfpSSVQYTTiekLSGGEKRRLYLLRILM------EAPNVLLLDEPTNDLDIQ----TLTILEDYLESFP 465
Cdd:PRK13548 118 ALaqvdLAHL---AGRDYPQ---LSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAhqhhVLRLARQLAHERG 191
|
170 180
....*....|....*....|..
gi 1524013779 466 GIVITVSHD-----RYfLDRVV 482
Cdd:PRK13548 192 LAVIVVLHDlnlaaRY-ADRIV 212
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
336-483 |
9.83e-10 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 60.51 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVGQTV---------------KMGYFSQEnEELDGRLKVidyiRGAAEY-VKTKDGSvsas 399
Cdd:TIGR02142 36 KTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrRIGYVFQE-ARLFPHLSV----RGNLRYgMKRARPS---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 400 qmLERFLFPSSVQYTTIE--------KLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFP---GI- 467
Cdd:TIGR02142 107 --ERRISFERVIELLGIGhllgrlpgRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHaefGIp 184
|
170
....*....|....*.
gi 1524013779 468 VITVSHDryfLDRVVR 483
Cdd:TIGR02142 185 ILYVSHS---LQEVLR 197
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-154 |
1.04e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.85 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTE--RLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEpDEGKV----VKGRNLTVR-------F 70
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIqidgVSWNSVTLQtwrkafgV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 LPQNPEFYKGDTILTSIVRENEGQDHVWDL--ESQAKTMLTKL-GFTDFdILVE---TLSGGQRKRVALVSVLLSTADLL 144
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNLDPYEQWSDEEIWKVaeEVGLKSVIEQFpDKLDF-VLVDggyVLSNGHKQLMCLARSILSKAKIL 1375
|
170
....*....|
gi 1524013779 145 VLDEPTNHLD 154
Cdd:TIGR01271 1376 LLDEPSAHLD 1385
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-197 |
1.32e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.86 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 20 DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEG---------------------------KVVKGRNLTVRFLP 72
Cdd:PRK13631 43 NNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdkknnhelitnpyskkiKNFKELRRRVSMVF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 73 QNPEF--YKgDTILTSIV--RENEGQdHVWDLESQAKTMLTKLGFtDFDILVET---LSGGQRKRVALVSVLLSTADLLV 145
Cdd:PRK13631 123 QFPEYqlFK-DTIEKDIMfgPVALGV-KKSEAKKLAKFYLNKMGL-DDSYLERSpfgLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 146 LDEPTNHLD----SSMAEWLEEYLRSfNGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:PRK13631 200 FDEPTAGLDpkgeHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
336-482 |
1.40e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 60.16 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV---------KMGYFSQE-----NeeldgrLKVIDYI--------RGAAEyVKTK 392
Cdd:COG1118 41 KTTLLRIIAGLETPDSGRIVLnGRDLftnlpprerRVGFVFQHyalfpH------MTVAENIafglrvrpPSKAE-IRAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 393 dgsvsASQMLERflfpssVQYTTIEK-----LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILE----DYLES 463
Cdd:COG1118 114 -----VEELLEL------VQLEGLADrypsqLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRrwlrRLHDE 182
|
170 180
....*....|....*....|...
gi 1524013779 464 FPGIVITVSHDR---YFL-DRVV 482
Cdd:COG1118 183 LGGTTVFVTHDQeeaLELaDRVV 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-485 |
2.10e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.25 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 21 DTSFSINEGEKIGLIGINGTGKS----TLLKIV--AGLEEPDEGKVVKGRNLTVRFLPQ--------------------- 73
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLRRRSRQVIELSEqsaaqmrhvrgadmamifqep 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 74 ----NPEFYKGDTILTSIvRENEGQDHVWDLeSQAKTMLTKLGFTDFDILV----ETLSGGQRKRVALVSVLLSTADLLV 145
Cdd:PRK10261 114 mtslNPVFTVGEQIAESI-RLHQGASREEAM-VEAKRMLDQVRIPEAQTILsrypHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 146 LDEPTNHLDSSMAEWLEEYLRSFNGALLM----VTHDRYFLDSVTNRIveldkgkLFSYQTNKVNGGGADR--ESTQGCY 219
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMgvifITHDMGVVAEIADRV-------LVMYQGEAVETGSVEQifHAPQHPY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 220 EEYLKLKAERLDLLEASERKRqsilRVELQWMQRGARARSTKQKAHIERYETLRDQKGLETDQAVElDSIESRLGRTTVE 299
Cdd:PRK10261 265 TRALLAAVPQLGAMKGLDYPR----RFPLISLEHPAKQEPPIEQDTVVDGEPILQVRNLVTRFPLR-SGLLNRVTREVHA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 300 LEGISkaygdkvlmkdftYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITVG------------QTVKMGY--- 364
Cdd:PRK10261 340 VEKVS-------------FDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgqridtlspgklQALRRDIqfi 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 365 FSQENEELDGRLKVIDYIRGAAEYVKTKDGSVSASQ---MLERFLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLL 441
Cdd:PRK10261 407 FQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARvawLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVII 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1524013779 442 LDEPTNDLDI----QTLTILEDYLESFPGIVITVSHDRYFLDRVVRRI 485
Cdd:PRK10261 487 ADEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHDMAVVERISHRV 534
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
336-473 |
2.57e-09 |
|
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: 56.84 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTVK----------MGYFSQENEELDGrlKVIDYIrgaaeyvktkdgsvsasqmler 404
Cdd:cd03246 41 KSTLARLILGLLRPTSGRVRLdGADISqwdpnelgdhVGYLPQDDELFSG--SIAENI---------------------- 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 405 flfpssvqyttiekLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFP---GIVITVSH 473
Cdd:cd03246 97 --------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaagATRIVIAH 154
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
298-482 |
2.62e-09 |
|
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: 58.07 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDF---------TYILlkndrigiigpngggKSTLMKIIAGWVEPDEGTITV-GQTV------- 360
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVsldvprgeiLAIIggs---------gsgKSVLLKLIIGLLRPDSGEILVdGQDItglseke 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 361 ------KMGY-------FS------------QENEELDGRLkvidyIRgaaEYVKTKDGSVSASQMLErfLFPSSvqytt 415
Cdd:COG1127 77 lyelrrRIGMlfqggalFDsltvfenvafplREHTDLSEAE-----IR---ELVLEKLELVGLPGAAD--KMPSE----- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 416 iekLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYL----ESFPGIVITVSHD----RYFLDRVV 482
Cdd:COG1127 142 ---LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIrelrDELGLTSVVVTHDldsaFAIADRVA 213
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
336-489 |
2.81e-09 |
|
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: 57.83 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV---GQTVKM----------------GYFSQeneeldgRLKVIDYI------------RG 384
Cdd:COG4778 50 KSTLLKCIYGNYLPDSGSILVrhdGGWVDLaqaspreilalrrrtiGYVSQ-------FLRVIPRVsaldvvaeplleRG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 385 AAEyvktKDGSVSASQMLERFLFPssvqyttiEKL--------SGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT--- 453
Cdd:COG4778 123 VDR----EEARARARELLARLNLP--------ERLwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANrav 190
|
170 180 190
....*....|....*....|....*....|....*...
gi 1524013779 454 -LTILEDYLESfpGI-VITVSHDRYFLDRVVRRIFAFE 489
Cdd:COG4778 191 vVELIEEAKAR--GTaIIGIFHDEEVREAVADRVVDVT 226
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
336-473 |
2.87e-09 |
|
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: 56.28 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTVKmgyFSQENEELdgRLKVidyirgaaeyvktkdgsvsasqmlerflfpssvqyT 414
Cdd:cd03216 39 KSTLMKILSGLYKPDSGEILVdGKEVS---FASPRDAR--RAGI-----------------------------------A 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 415 TIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESF--PGI-VITVSH 473
Cdd:cd03216 79 MVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraQGVaVIFISH 140
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
298-490 |
3.36e-09 |
|
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: 57.15 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITV-GQTV------------KMGY 364
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdGLKLtddkkninelrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 365 -FSQENeeLDGRLKVIDYIRGAAEYVKTKDGS---VSASQMLERF-LFPSSVQYttIEKLSGGEKRRLYLLRILMEAPNV 439
Cdd:cd03262 81 vFQQFN--LFPHLTVLENITLAPIKVKGMSKAeaeERALELLEKVgLADKADAY--PAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 440 LLLDEPTNDLDIQT----LTILEDYLESfpGI-VITVSHDRYFLDRVVRRIFAFEG 490
Cdd:cd03262 157 MLFDEPTSALDPELvgevLDVMKDLAEE--GMtMVVVTHEMGFAREVADRVIFMDD 210
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-166 |
3.62e-09 |
|
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: 59.45 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGL--------EEPDEGKVVKGRNLT------V 68
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwdgEIYWSGSPLKASNIRdteragI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 69 RFLPQNPEFYKGDTILTSIVRENE-----GQDHVWDLESQAKTMLTKLGFTDFDI--LVETLSGGQRKRVALVSVLLSTA 141
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEitlpgGRMAYNAMYLRAKNLLRELQLDADNVtrPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180
....*....|....*....|....*
gi 1524013779 142 DLLVLDEPTNHLDSSMAEWLEEYLR 166
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIR 185
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-195 |
4.36e-09 |
|
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: 55.46 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 29 GEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVkgrnltvrflpqnpefykgdtiltsivrenegqdhVWDLESQAKTML 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI-----------------------------------YIDGEDILEEVL 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 109 TKLGFTDFDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNGALLMVTHDRYFLDsVTNR 188
Cdd:smart00382 47 DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVIL-TTND 125
|
....*..
gi 1524013779 189 IVELDKG 195
Cdd:smart00382 126 EKDLGPA 132
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
336-486 |
4.76e-09 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 56.98 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV--------------KMGY-FSQENeeLDGRLKVIDYIRGAAEY--VKTKDGSVS 397
Cdd:COG1136 47 KSTLLNILGGLDRPTSGEVLIdGQDIsslserelarlrrrHIGFvFQFFN--LLPELTALENVALPLLLagVSRKERRER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 398 ASQMLERF-------LFPSsvqyttieKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT----LTILEDYLESFPG 466
Cdd:COG1136 125 ARELLERVglgdrldHRPS--------QLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGT 196
|
170 180
....*....|....*....|
gi 1524013779 467 IVITVSHDRYFLDRVVRRIF 486
Cdd:COG1136 197 TIVMVTHDPELAARADRVIR 216
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-166 |
5.81e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.79 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGL--------EEPDEGKVVKGRNLT------V 68
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyegEIIFEGEELQASNIRdteragI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 69 RFLPQNPEFYKGDTILTSIVRENE-GQDHVWD---LESQAKTMLTKLGFT-DFDILVETLSGGQRKRVALVSVLLSTADL 143
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGNEiTPGGIMDydaMYLRAQKLLAQLKLDiNPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180
....*....|....*....|...
gi 1524013779 144 LVLDEPTNHLDSSMAEWLEEYLR 166
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIR 187
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-166 |
5.83e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.96 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSY-TERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT----------VRFL 71
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIrLDGRPLSslshsvlrqgVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 72 PQNPEFYkGDTILTSI-VRENEGQDHVWD------LESQAKTM----LTKLGFTDfdilvETLSGGQRKRVALVSVLLST 140
Cdd:PRK10790 421 QQDPVVL-ADTFLANVtLGRDISEEQVWQaletvqLAELARSLpdglYTPLGEQG-----NNLSVGQKQLLALARVLVQT 494
|
170 180
....*....|....*....|....*.
gi 1524013779 141 ADLLVLDEPTNHLDSSMAEWLEEYLR 166
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALA 520
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
298-474 |
6.11e-09 |
|
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: 56.86 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITV-GQTV--------KMGYFSQe 368
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLdGKDItnlpphkrPVNTVFQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 369 NEELDGRLKVIDYIRGAAEYVKTKDGSVSA--SQMLeRFLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPT 446
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKErvAEAL-DLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190
....*....|....*....|....*....|..
gi 1524013779 447 NDLDI---QTLTILEDYLESFPGI-VITVSHD 474
Cdd:cd03300 159 GALDLklrKDMQLELKRLQKELGItFVFVTHD 190
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
335-482 |
6.71e-09 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 57.05 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 335 GKSTLMKIIAGWVEPDEGTI--------------------------------TVGQTVKMG-----YFSQENEELdgrlk 377
Cdd:COG4559 39 GKSTLLKLLTGELTPSSGEVrlngrplaawspwelarrravlpqhsslafpfTVEEVVALGraphgSSAAQDRQI----- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 378 vidyirgAAEYVKTkdgsVSASQMLERFlfpssvqYTTiekLSGGEKRRLYLLRIL-------MEAPNVLLLDEPTNDLD 450
Cdd:COG4559 114 -------VREALAL----VGLAHLAGRS-------YQT---LSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1524013779 451 I----QTLTILEDYLESfPGIVITVSHD-----RYfLDRVV 482
Cdd:COG4559 173 LahqhAVLRLARQLARR-GGGVVAVLHDlnlaaQY-ADRIL 211
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-199 |
7.40e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 57.67 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYT-ERLLF---------DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGK-VVKGRNLT---- 67
Cdd:PRK11308 5 LLQAIDLKKHYPvKRGLFkperlvkalDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGElYYQGQDLLkadp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 ---------VRFLPQNPefY-------KGDTIL-------TSIVREnegqdhvwDLESQAKTMLTKLGF--TDFDILVET 122
Cdd:PRK11308 85 eaqkllrqkIQIVFQNP--YgslnprkKVGQILeepllinTSLSAA--------ERREKALAMMAKVGLrpEHYDRYPHM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 123 LSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSS--------MAEWLEEylrsFNGALLMVTHD----RYFLDSVT---- 186
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSvqaqvlnlMMDLQQE----LGLSYVFISHDlsvvEHIADEVMvmyl 230
|
250
....*....|....
gi 1524013779 187 NRIVEL-DKGKLFS 199
Cdd:PRK11308 231 GRCVEKgTKEQIFN 244
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-196 |
7.71e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 56.92 E-value: 7.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRNLT------------VR 69
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILlRGQHIEglpghqiarmgvVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 70 FLpQNPEFYKGDTIL---------------------TSIVRENEGQDhvwdLEsQAKTMLTKLGFTDF-DILVETLSGGQ 127
Cdd:PRK11300 85 TF-QHVRLFREMTVIenllvaqhqqlktglfsgllkTPAFRRAESEA----LD-RAATWLERVGLLEHaNRQAGNLAYGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1524013779 128 RKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYL----RSFNGALLMVTHDRYFLDSVTNRIVELDKGK 196
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIaelrNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-189 |
8.38e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.41 E-value: 8.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 20 DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRNLT---------VRFLPQ----------NPEFYK 79
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLgmkddewraVRSDIQmifqdplaslNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 80 GDtILTSIVRENEGQDHVWDLESQAKTMLTKLGftdfdiLVETL--------SGGQRKRVALVSVLLSTADLLVLDEPTN 151
Cdd:PRK15079 118 GE-IIAEPLRTYHPKLSRQEVKDRVKAMMLKVG------LLPNLinryphefSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1524013779 152 HLDSSM----AEWLEEYLRSFNGALLMVTHDRYFLDSVTNRI 189
Cdd:PRK15079 191 ALDVSIqaqvVNLLQQLQREMGLSLIFIAHDLAVVKHISDRV 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-150 |
8.41e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.60 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 20 DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEG------KVVKGRNLTVR----FLPQNPEFYkgdTILTsiVR 89
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeawlfgQPVDAGDIATRrrvgYMSQAFSLY---GELT--VR 357
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 90 ENegqdhvwdLESQAK--------------TMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEPT 150
Cdd:NF033858 358 QN--------LELHARlfhlpaaeiaarvaEMLERFDLADVaDALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-150 |
8.59e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.11 E-value: 8.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKsyteRLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTVR-----------F 70
Cdd:COG1129 256 VLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIrLDGKPVRIRsprdairagiaY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 LPQNpefYKGDTI-LTSIVREN---EGQDHVWDL--------ESQAKTMLTKLG--FTDFDILVETLSGG-QRKrVALVS 135
Cdd:COG1129 332 VPED---RKGEGLvLDLSIRENitlASLDRLSRGglldrrreRALAEEYIKRLRikTPSPEQPVGNLSGGnQQK-VVLAK 407
|
170
....*....|....*
gi 1524013779 136 VLLSTADLLVLDEPT 150
Cdd:COG1129 408 WLATDPKVLILDEPT 422
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
336-473 |
9.13e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 55.83 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVGQTvkmgyfsQENEELDGRLKVIDYIrGAAEYVKtkdGSVSASQMLeRFL--FPSSVQY 413
Cdd:TIGR01189 39 KTTLLRILAGLLRPDSGEVRWNGT-------PLAEQRDEPHENILYL-GHLPGLK---PELSALENL-HFWaaIHGGAQR 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 414 TTIE----------------KLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESF---PGIVITVSH 473
Cdd:TIGR01189 107 TIEDalaavgltgfedlpaaQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
335-485 |
1.13e-08 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 56.19 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 335 GKSTLMKIIAGWVEPDEGTITVGQTV----------KMGYFSQENEELDGRLKVID--------YIRGAAEYVKTKDGSV 396
Cdd:cd03267 59 GKTTTLKILSGLLQPTSGEVRVAGLVpwkrrkkflrRIGVVFGQKTQLWWDLPVIDsfyllaaiYDLPPARFKKRLDELS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 397 SASQmLERFLfpssvqYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT-LTI---LEDYLESFPGIVITVS 472
Cdd:cd03267 139 ELLD-LEELL------DTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAqENIrnfLKEYNRERGTTVLLTS 211
|
170
....*....|...
gi 1524013779 473 HDRYFLDRVVRRI 485
Cdd:cd03267 212 HYMKDIEALARRV 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-199 |
1.30e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.55 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTERLLF-----DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEG----------------KVVK 62
Cdd:PRK13645 7 IILDNVSYTYAKKTPFefkalNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyaipanlkkiKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 63 GRNLTVRFLPQNPEFYK-GDTILTSI----VRENEGQDHVW-------DLESQAKTMLTKLGFTdfdilvetLSGGQRKR 130
Cdd:PRK13645 87 RLRKEIGLVFQFPEYQLfQETIEKDIafgpVNLGENKQEAYkkvpellKLVQLPEDYVKRSPFE--------LSGGQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1524013779 131 VALVSVLLSTADLLVLDEPTNHLDSSMAE-WLEEYLR---SFNGALLMVTHDRYFLDSVTNRIVELDKGKLFS 199
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEdFINLFERlnkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
336-482 |
1.49e-08 |
|
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: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGW--VEPDEGTITV-GQTV---------KMGYF--SQENEELDGrLKVIDYIRgaaeYVKtkdgsvsasqm 401
Cdd:cd03217 39 KSTLAKTIMGHpkYEVTEGEILFkGEDItdlppeeraRLGIFlaFQYPPEIPG-VKNADFLR----YVN----------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 402 lerflfpssvqyttiEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESF-----PGIVITvsHDRY 476
Cdd:cd03217 103 ---------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreegkSVLIIT--HYQR 165
|
....*.
gi 1524013779 477 FLDRVV 482
Cdd:cd03217 166 LLDYIK 171
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
298-474 |
1.56e-08 |
|
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: 55.34 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITVG-----------QTVKMGYfs 366
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvtdlppkdRDIAMVF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 367 qENEELDGRLKVIDYIRGAAEYVKTKDGSVSA-----------SQMLERflFPSsvqyttieKLSGGEKRRLYLLRILME 435
Cdd:cd03301 79 -QNYALYPHMTVYDNIAFGLKLRKVPKDEIDErvrevaellqiEHLLDR--KPK--------QLSGGQRQRVALGRAIVR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1524013779 436 APNVLLLDEPTNDLD----IQTLTILEDYLESFPGIVITVSHD 474
Cdd:cd03301 148 EPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-166 |
1.71e-08 |
|
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: 54.94 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 16 RLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEpdeGKVVKGrNLTVRFLPQNPEFykgdTILTSIVRENegqd 95
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKT---AGVITG-EILINGRPLDKNF----QRSTGYVEQQ---- 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 96 hvwDLESQAKTMLTKLgftDFDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLR 166
Cdd:cd03232 88 ---DVHSPNLTVREAL---RFSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
336-495 |
1.78e-08 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 55.06 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV-------------KMGYFSQENEELDGR---------LKVIDYIRGAAEYvktk 392
Cdd:COG2884 41 KSTLLKLLYGEERPTSGQVLVnGQDLsrlkrreipylrrRIGVVFQDFRLLPDRtvyenvalpLRVTGKSRKEIRR---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 393 dgsvSASQMLERF-------LFPssvqyttiEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESF- 464
Cdd:COG2884 117 ----RVREVLDLVglsdkakALP--------HELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEIn 184
|
170 180 190
....*....|....*....|....*....|...
gi 1524013779 465 -PGI-VITVSHDRYFLDRVVRRIFAFEgNGMVT 495
Cdd:COG2884 185 rRGTtVLIATHDLELVDRMPKRVLELE-DGRLV 216
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-184 |
1.81e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 54.92 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 34 LIGINGTGKSTLLkivagleepdEGkvvkgrnLTVRFLPQNPEFYKGDTILTSIVRENEGQDHVwdlesqaktmltKLGF 113
Cdd:cd03240 27 IVGQNGAGKTTII----------EA-------LKYALTGELPPNSKGGAHDPKLIREGEVRAQV------------KLAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 114 TD-----------FDIL------------------VETLSGGQRK------RVALVSVLLSTADLLVLDEPTNHLDS--- 155
Cdd:cd03240 78 ENangkkytitrsLAILenvifchqgesnwplldmRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeni 157
|
170 180 190
....*....|....*....|....*....|.
gi 1524013779 156 --SMAEWLEEYLRSFNGALLMVTHDRYFLDS 184
Cdd:cd03240 158 eeSLAEIIEERKSQKNFQLIVITHDEELVDA 188
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
336-473 |
1.83e-08 |
|
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: 54.24 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITvgqtvkmgyfsqeneeLDGRLkVIDYIRGAAEYVKTKDGSVsasqmlerFLFPSSVQYTT 415
Cdd:cd03247 41 KSTLLQLLTGDLKPQQGEIT----------------LDGVP-VSDLEKALSSLISVLNQRP--------YLFDTTLRNNL 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 416 IEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT-LTILEDYLESFPG-IVITVSH 473
Cdd:cd03247 96 GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITeRQLLSLIFEVLKDkTLIWITH 155
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
336-483 |
2.50e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.04 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVGQTV---------------KMGYFSQeneelDGRL----KVidyiRGAAEY-VKTKDGS 395
Cdd:PRK11144 37 KTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrRIGYVFQ-----DARLfphyKV----RGNLRYgMAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 396 --------VSASQMLERflFPSSvqyttiekLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFPGI 467
Cdd:PRK11144 108 qfdkivalLGIEPLLDR--YPGS--------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLARE 177
|
170 180
....*....|....*....|
gi 1524013779 468 V----ITVSHDryfLDRVVR 483
Cdd:PRK11144 178 InipiLYVSHS---LDEILR 194
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-202 |
3.65e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.12 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 13 YTERLLFDdTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKG-----------------RNLTVRF-LPQN 74
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvsstskqkeikpvrKKVGVVFqFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 75 PEFYkgDTILTSIV--RENEGQDHVwDLESQAKTMLTKLGFTD--FDILVETLSGGQRKRVALVSVLLSTADLLVLDEPT 150
Cdd:PRK13643 96 QLFE--ETVLKDVAfgPQNFGIPKE-KAEKIAAEKLEMVGLADefWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 151 NHLD-SSMAEWLE--EYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKLFSYQT 202
Cdd:PRK13643 173 AGLDpKARIEMMQlfESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
336-446 |
3.66e-08 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 54.36 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVG----------QTVKMGY-FSQENEELDGRLKVIDYIRgAAEYVKTKDGsvsASQMLER 404
Cdd:cd03224 39 KTTLLKTIMGLLPPRSGSIRFDgrditglpphERARAGIgYVPEGRRIFPELTVEENLL-LGAYARRRAK---RKARLER 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1524013779 405 F--LFP------SSVQYTtiekLSGGEKRRLYLLRILMEAPNVLLLDEPT 446
Cdd:cd03224 115 VyeLFPrlkerrKQLAGT----LSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-202 |
3.76e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.91 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 23 SFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV------VKGRNLT-----VRFLPQNPEFYKGdTILTSIVREN 91
Cdd:PLN03232 1256 SFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRImiddcdVAKFGLTdlrrvLSIIPQSPVLFSG-TVRFNIDPFS 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 92 EGQD-HVWDLESQA--KTMLTKLGFtDFDILV----ETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEY 164
Cdd:PLN03232 1335 EHNDaDLWEALERAhiKDVIDRNPF-GLDAEVseggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRT 1413
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1524013779 165 LR-SFNGALLMVTHDRyfLDSVT--NRIVELDKGKLFSYQT 202
Cdd:PLN03232 1414 IReEFKSCTMLVIAHR--LNTIIdcDKILVLSSGQVLEYDS 1452
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
298-474 |
4.27e-08 |
|
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: 54.26 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLmKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITV-GQTV--------KMGYFSQ- 367
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDItnlppekrDISYVPQn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 368 ----------ENEELDGRLKVIDYIRGAAEyVKTKDGSVSASQMLERflfpssvqytTIEKLSGGEKRRLYLLRILMEAP 437
Cdd:cd03299 80 yalfphmtvyKNIAYGLKKRKVDKKEIERK-VLEIAEMLGIDHLLNR----------KPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1524013779 438 NVLLLDEPTNDLDIQT----LTILEDYLESFPGIVITVSHD 474
Cdd:cd03299 149 KILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHD 189
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
335-445 |
4.50e-08 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 54.09 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 335 GKSTLMKIIAGWVEPDEGTITVGQT------------VKMGYFSQEnEELDGRLKVIDYIRGAAE--YVKTKDGSVSASQ 400
Cdd:cd03218 38 GKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarLGIGYLPQE-ASIFRKLTVEENILAVLEirGLSKKEREEKLEE 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1524013779 401 MLERFlfpssvQYTTIEK-----LSGGEKRRLYLLRILMEAPNVLLLDEP 445
Cdd:cd03218 117 LLEEF------HITHLRKskassLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-202 |
5.01e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.56 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 16 RLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNL---------TVRFLPQNPEFYKGDTILT 85
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlVGGKDIetnldavrqSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 86 SIVRENEGQDHVWD---LESQAktMLTKLGF-TDFDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLD----SSM 157
Cdd:TIGR01257 1023 HILFYAQLKGRSWEeaqLEMEA--MLEDTGLhHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDpysrRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1524013779 158 AEWLEEYlRSfNGALLMVTHDRYFLDSVTNRIVELDKGKLFSYQT 202
Cdd:TIGR01257 1101 WDLLLKY-RS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-177 |
5.11e-08 |
|
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: 55.91 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 18 LFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQNPEFYKG---------DTILTSIV 88
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGtlrdqiiypDSSEDMKR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 89 RENEGQDHVWDLES-QAKTMLTKLGftDFDIL---VETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEY 164
Cdd:TIGR00954 547 RGLSDKDLEQILDNvQLTHILEREG--GWSAVqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRL 624
|
170
....*....|...
gi 1524013779 165 LRSFNGALLMVTH 177
Cdd:TIGR00954 625 CREFGITLFSVSH 637
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-196 |
5.42e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 55.27 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 36 GINGTGKSTLLKIVAGLEEPDEGKVV----------KGRNLTV------------RFLPQnpefYKgdtiltsiVRENeg 93
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVlngrvlfdaeKGICLPPekrrigyvfqdaRLFPH----YK--------VRGN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 94 qdhvwdLE-SQAKTMLTKlgftdFDILVE-------------TLSGGQRKRVALVSVLLSTADLLVLDEPTNHLD----S 155
Cdd:PRK11144 97 ------LRyGMAKSMVAQ-----FDKIVAllgieplldrypgSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlprkR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1524013779 156 SMAEWLEEYLRSFNGALLMVTHDryfLDSV---TNRIVELDKGK 196
Cdd:PRK11144 166 ELLPYLERLAREINIPILYVSHS---LDEIlrlADRVVVLEQGK 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
418-474 |
6.05e-08 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 53.72 E-value: 6.05e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 418 KLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD-IQTLTIlEDYLESF---PGIVItVSHD 474
Cdd:cd03260 141 GLSGGQQQRLCLARALANEPEVLLLDEPTSALDpISTAKI-EELIAELkkeYTIVI-VTHN 199
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
336-483 |
6.09e-08 |
|
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: 55.11 E-value: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVGQTV---------------KMGYFSQeneelDGRL----KVIDYIRGAAEYVKTKDGSV 396
Cdd:COG4148 38 KTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrRIGYVFQ-----EARLfphlSVRGNLLYGRKRAPRAERRI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 397 SASQ---------MLERFlfpssvqyttIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT-LTILeDYLESFP- 465
Cdd:COG4148 113 SFDEvvellgighLLDRR----------PATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARkAEIL-PYLERLRd 181
|
170 180
....*....|....*....|.
gi 1524013779 466 --GI-VITVSHDryfLDRVVR 483
Cdd:COG4148 182 elDIpILYVSHS---LDEVAR 199
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
124-178 |
6.55e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 54.73 E-value: 6.55e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 124 SGGQRKRVALVSVLLSTADLLVLDEPTNHLD----SSMAEWLEEYLRSFNGALLMVTHD 178
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
336-482 |
6.87e-08 |
|
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: 53.66 E-value: 6.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV-------------KMGYFSQE-NEELDGRLKVIDYIRGAAEYVKTKDGS----V 396
Cdd:cd03257 44 KSTLARAILGLLKPTSGSIIFdGKDLlklsrrlrkirrkEIQMVFQDpMSSLNPRMTIGEQIAEPLRIHGKLSKKearkE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 397 SASQMLERFLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD----IQTLTILEDYLESFPGIVITVS 472
Cdd:cd03257 124 AVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDvsvqAQILDLLKKLQEELGLTLLFIT 203
|
170
....*....|....
gi 1524013779 473 HD----RYFLDRVV 482
Cdd:cd03257 204 HDlgvvAKIADRVA 217
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-197 |
7.60e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 55.35 E-value: 7.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 20 DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKG------------RNLTVRFlpQNPEFYK---GDTI 83
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIlIDGtdirtvtraslrRNIAVVF--QDAGLFNrsiEDNI 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 84 ltSIVRENEGQDHVWDLESQAKT---MLTKLGftDFDILV----ETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSs 156
Cdd:PRK13657 430 --RVGRPDATDEEMRAAAERAQAhdfIERKPD--GYDTVVgergRQLSGGERQRLAIARALLKDPPILILDEATSALDV- 504
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1524013779 157 maewleEYLRSFNGALLMVTHDR------YFLDSVTN--RIVELDKGKL 197
Cdd:PRK13657 505 ------ETEAKVKAALDELMKGRttfiiaHRLSTVRNadRILVFDNGRV 547
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
336-471 |
8.21e-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: 53.43 E-value: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDE---GTITV-GQTVK-------MGYFSQENEELDGrLKVIDYIRGAAEY---VKTKDG--SVSAS 399
Cdd:cd03234 46 KTTLLDAISGRVEGGGttsGQILFnGQPRKpdqfqkcVAYVRQDDILLPG-LTVRETLTYTAILrlpRKSSDAirKKRVE 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 400 QMLERFLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD----IQTLTILEDYLESFPGIVITV 471
Cdd:cd03234 125 DVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDsftaLNLVSTLSQLARRNRIVILTI 200
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-204 |
9.30e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.63 E-value: 9.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEE--PD---EGKVV-KGRNL------TVR- 69
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVyNGHNIysprtdTVDl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 70 -------FLPQNP---EFY------------KGDTILTSIVRENEGQDHVWDlESQAKTMLTKLGftdfdilvetLSGGQ 127
Cdd:PRK14239 85 rkeigmvFQQPNPfpmSIYenvvyglrlkgiKDKQVLDEAVEKSLKGASIWD-EVKDRLHDSALG----------LSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 128 RKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNG--ALLMVTHDRYFLDSVTNRIVELDKGKLFSYQTNK 204
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTK 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
291-474 |
9.79e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.53 E-value: 9.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 291 SRLGR-TTVELEGISKAYGDKVLMKD---------FTYILLKNDrigiigpngGGKSTLMKIIAGWVEPDEGTITVGQTV 360
Cdd:PRK11247 5 ARLNQgTPLLLNAVSKRYGERTVLNQldlhipagqFVAVVGRSG---------CGKSTLLRLLAGLETPSAGELLAGTAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 361 kmgyFSQENEEL-----DGRL----KVIDYI----RGaaeyvktkDGSVSASQMLERF-LFPSSVQYTTieKLSGGEKRR 426
Cdd:PRK11247 76 ----LAEAREDTrlmfqDARLlpwkKVIDNVglglKG--------QWRDAALQALAAVgLADRANEWPA--ALSGGQKQR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 427 LYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLES------FpgIVITVSHD 474
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESlwqqhgF--TVLLVTHD 193
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
336-473 |
1.26e-07 |
|
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: 53.16 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEG-TITV-GQTV----------KMGYFSQE-NEELDGRLKVIDYIRGAAE-----YVKTKDGSVS 397
Cdd:COG1119 42 KSTLLSLITGDLPPTYGnDVRLfGERRggedvwelrkRIGLVSPAlQLRFPRDETVLDVVLSGFFdsiglYREPTDEQRE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 398 -ASQMLERF-LfpSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI----QTLTILEDYLESFPGIVITV 471
Cdd:COG1119 122 rARELLELLgL--AHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLgareLLLALLDKLAAEGAPTLVLV 199
|
..
gi 1524013779 472 SH 473
Cdd:COG1119 200 TH 201
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-150 |
1.30e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.96 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRNLT-----------V 68
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVfDGKDITdwqtakimreaV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 69 RFLPQNPEFYKGDTiltsiVRENEGQDHVWDLESQAKTMLTKLgFTDFDILVE-------TLSGGQRKRVALVSVLLSTA 141
Cdd:PRK11614 83 AIVPEGRRVFSRMT-----VEENLAMGGFFAERDQFQERIKWV-YELFPRLHErriqragTMSGGEQQMLAIGRALMSQP 156
|
....*....
gi 1524013779 142 DLLVLDEPT 150
Cdd:PRK11614 157 RLLLLDEPS 165
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
336-495 |
1.70e-07 |
|
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: 51.87 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVG-------QTVKMGYFSQEN-----------EELDGRLKVI-DYIRGAAEYVKTkdgsV 396
Cdd:cd03226 39 KTTLAKILAGLIKESSGSILLNgkpikakERRKSIGYVMQDvdyqlftdsvrEELLLGLKELdAGNEQAETVLKD----L 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 397 SASQMLERFlfPSSvqyttiekLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFPG---IVITVSH 473
Cdd:cd03226 115 DLYALKERH--PLS--------LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAqgkAVIVITH 184
|
170 180
....*....|....*....|..
gi 1524013779 474 DRYFLDRVVRRIFaFEGNGMVT 495
Cdd:cd03226 185 DYEFLAKVCDRVL-LLANGAIV 205
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-197 |
1.93e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.79 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 8 HMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGK------VVKGRNL-----------TVRF 70
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdvLLGGRSIfnyrdvlefrrRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 71 LPQNPEFYKGdTILTSIVRENEGQDHV--WDLESQAKTMLTKLGFTDF--DILVET---LSGGQRKRVALVSVLLSTADL 143
Cdd:PRK14271 106 LFQRPNPFPM-SIMDNVLAGVRAHKLVprKEFRGVAQARLTEVGLWDAvkDRLSDSpfrLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 144 LVLDEPTNHLDSSMAEWLEEYLRSFNGAL--LMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLtvIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-191 |
1.97e-07 |
|
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: 53.92 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSY----TERLLFDDTSFSINEGEKIGLIGINGTGKS-TLLKIVAGLEEPD---EGKVV-KGRNL----- 66
Cdd:COG4172 4 MPLLSVEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILfDGQDLlglse 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 67 ----TVR-------FlpQ------NPEFykgdTI---LTSIVRENEGQDHVwDLESQAKTMLTKLGFTDfdilVET---- 122
Cdd:COG4172 84 relrRIRgnriamiF--QepmtslNPLH----TIgkqIAEVLRLHRGLSGA-AARARALELLERVGIPD----PERrlda 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 123 ----LSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSM-AEWLE---EYLRSFNGALLMVTHD----RYFLDSVT---- 186
Cdd:COG4172 153 yphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVqAQILDllkDLQRELGMALLLITHDlgvvRRFADRVAvmrq 232
|
....*
gi 1524013779 187 NRIVE 191
Cdd:COG4172 233 GEIVE 237
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
336-462 |
2.19e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 53.31 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVG--------------------------------QTVKMGYFSQEneeldGRLKVIDYIR 383
Cdd:PRK09536 42 KTTLLRAINGTLTPTAGTVLVAgddvealsaraasrrvasvpqdtslsfefdvrQVVEMGRTPHR-----SRFDTWTETD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 384 GAAeyVKTKDGSVSASQMLERflfpssvqytTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI----QTLTILED 459
Cdd:PRK09536 117 RAA--VERAMERTGVAQFADR----------PVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDInhqvRTLELVRR 184
|
...
gi 1524013779 460 YLE 462
Cdd:PRK09536 185 LVD 187
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
21-186 |
2.19e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.58 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 21 DTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQNpefykgdtiLTSIVRENEGQDHVWDL 100
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKN---------LVAYVPQSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 101 ESQAKTMLTKLGFTDF-------------------DIL------VETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLD- 154
Cdd:PRK15056 96 LVEDVVMMGRYGHMGWlrrakkrdrqivtaalarvDMVefrhrqIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDv 175
|
170 180 190
....*....|....*....|....*....|....*
gi 1524013779 155 ---SSMAEWLEEyLRSFNGALLMVTHDryfLDSVT 186
Cdd:PRK15056 176 kteARIISLLRE-LRDEGKTMLVSTHN---LGSVT 206
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
336-446 |
2.60e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.49 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTVKMG---------------YFSQ-------ENEEL---DGRLKVIDyIRGAAEYV 389
Cdd:COG3845 44 KSTLMKILYGLYQPDSGEILIdGKPVRIRsprdaialgigmvhqHFMLvpnltvaENIVLglePTKGGRLD-RKAARARI 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 390 KtkdgsvsasQMLERFLFPssVQ-YTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPT 446
Cdd:COG3845 123 R---------ELSERYGLD--VDpDAKVEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-150 |
2.62e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.98 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 6 IEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTVR-----------FLPQ 73
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGDMADArhrravcpriaYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 74 ----N--PEfykgdtiLTsiVRENE-------GQDHvwdLESQAK--TMLTKLGFTDF-DILVETLSGGQRKRVALVSVL 137
Cdd:NF033858 84 glgkNlyPT-------LS--VFENLdffgrlfGQDA---AERRRRidELLRATGLAPFaDRPAGKLSGGMKQKLGLCCAL 151
|
170
....*....|...
gi 1524013779 138 LSTADLLVLDEPT 150
Cdd:NF033858 152 IHDPDLLILDEPT 164
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-195 |
2.68e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.92 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSY---TERLlfDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEG------KVV-----KGRNL 66
Cdd:PRK11650 1 MAGLKLQAVRKSYdgkTQVI--KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGeiwiggRVVnelepADRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 67 TVRFlpQNPEFYKGDTiltsiVRENEGqdhvWDLE-------------SQAKTMLtKLGftdfdILVE----TLSGGQRK 129
Cdd:PRK11650 79 AMVF--QNYALYPHMS-----VRENMA----YGLKirgmpkaeieervAEAARIL-ELE-----PLLDrkprELSGGQRQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 130 RVALVSVLLSTADLLVLDEPTNHLDS----SMAEWLEEYLRSFNGALLMVTHDRyfLDSVT--NRIVELDKG 195
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDAklrvQMRLEIQRLHRRLKTTSLYVTHDQ--VEAMTlaDRVVVMNGG 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
297-482 |
2.92e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 52.78 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 297 TVELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITV-GQTV--------KMGYFSQ 367
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhGTDVsrlhardrKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 368 eNEELDGRLKVIDYI-----------RGAAEYVKTKDGS----VSASQMLERFlfPSsvqyttieKLSGGEKRRLYLLRI 432
Cdd:PRK10851 82 -HYALFRHMTVFDNIafgltvlprreRPNAAAIKAKVTQllemVQLAHLADRY--PA--------QLSGGQKQRVALARA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 433 LMEAPNVLLLDEPTNDLDIQTLTILEDYL----ESFPGIVITVSHDRY----FLDRVV 482
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEeameVADRVV 208
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
23-195 |
3.15e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.78 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 23 SFSINEGEKIGLIGINGTGKSTLLKivAGLEEPDEGKVVKGRnltvrflpqnPEFYKGDTILTsivrenegqdhvwdleS 102
Cdd:cd03238 15 DVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARLISFL----------PKFSRNKLIFI----------------D 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 103 QAKTML-TKLGFTDFDILVETLSGGQRKRVALVSVLLSTAD--LLVLDEPTNHLDSSMAEWLEEYLRSF---NGALLMVT 176
Cdd:cd03238 67 QLQFLIdVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVILIE 146
|
170
....*....|....*....
gi 1524013779 177 HDRYFLDSvTNRIVELDKG 195
Cdd:cd03238 147 HNLDVLSS-ADWIIDFGPG 164
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
336-473 |
3.58e-07 |
|
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: 51.06 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTVkmgyfsQENEELDGRLKV-IDY-----IRGAAEYVKTKD-----GSVSASQMLE 403
Cdd:cd03268 39 KTTTMKIILGLIKPDSGEITFdGKSY------QKNIEALRRIGAlIEApgfypNLTARENLRLLArllgiRKKRIDEVLD 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1524013779 404 RFLFpSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFPGIVITV---SH 473
Cdd:cd03268 113 VVGL-KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVlisSH 184
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-196 |
3.61e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.17 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 21 DTSFSINEGEKIGLIGINGTGKST----LLKIVAGLEEPD-EGKVVKGRN----LTVRFLPQ----------NPEFykgd 81
Cdd:PRK15134 304 NISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGEIWfDGQPLHNLNrrqlLPVRHRIQvvfqdpnsslNPRL---- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 82 TILTSIVrenEG-QDHVWDL-----ESQAKTMLTKLGF---------TDFdilvetlSGGQRKRVALVSVLLSTADLLVL 146
Cdd:PRK15134 380 NVLQIIE---EGlRVHQPTLsaaqrEQQVIAVMEEVGLdpetrhrypAEF-------SGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 147 DEPTNHLDSSMAEWLEEYLRSFNG----ALLMVTHDRYFLDSVTNRIVELDKGK 196
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQkhqlAYLFISHDLHVVRALCHQVIVLRQGE 503
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
298-462 |
3.63e-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: 51.22 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITV-GQTV---------KMGYFSQ 367
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaGHDVvreprevrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 368 E---NEELDGRLKVidYIRGAAEYVKTKDGSVSASQMLErFLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDE 444
Cdd:cd03265 81 DlsvDDELTGWENL--YIHARLYGVPGAERRERIDELLD-FVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170
....*....|....*...
gi 1524013779 445 PTNDLDIQTLTILEDYLE 462
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIE 175
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-178 |
3.67e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 51.62 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 13 YTERLLFDDTSFSINEGEKIGLIGINGTGKS----TLLKIV-AGLE----------EPDEGKVVKGRnlTVRFLPQNPE- 76
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRqtagrvlldgKPVAPCALRGR--KIATIMQNPRs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 77 -FYKGDTIlTSIVRENEGQDHVWDLESQAKTMLTKLGFTDFDILVET----LSGG--QRKRVALVsvLLSTADLLVLDEP 149
Cdd:PRK10418 91 aFNPLHTM-HTHARETCLALGKPADDATLTAALEAVGLENAARVLKLypfeMSGGmlQRMMIALA--LLCEAPFIIADEP 167
|
170 180 190
....*....|....*....|....*....|...
gi 1524013779 150 TNHLD----SSMAEWLEEYLRSFNGALLMVTHD 178
Cdd:PRK10418 168 TTDLDvvaqARILDLLESIVQKRALGMLLVTHD 200
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-199 |
3.83e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 16 RLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRnlTVRFLPQNPefykgdTILTSIVREN---- 91
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER--SIAYVPQQA------WIMNATVRGNilff 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 92 ------EGQDHV------WDLESQAKTMLTKLGFTDFDilvetLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAE 159
Cdd:PTZ00243 745 deedaaRLADAVrvsqleADLAQLGGGLETEIGEKGVN-----LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1524013779 160 WLEEYLrsFNGAL-----LMVTHDRYFLdSVTNRIVELDKGKL-FS 199
Cdd:PTZ00243 820 RVVEEC--FLGALagktrVLATHQVHVV-PRADYVVALGDGRVeFS 862
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
12-195 |
3.97e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 12 SYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNlTVRFLPQNPefykgdTILTSIVREN 91
Cdd:PLN03232 626 SKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRG-SVAYVPQVS------WIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 92 E--GQDH----VW----------DLESQAKTMLTKLGFTDFDIlvetlSGGQRKRVALVSVLLSTADLLVLDEPTNHLDS 155
Cdd:PLN03232 699 IlfGSDFeserYWraidvtalqhDLDLLPGRDLTEIGERGVNI-----SGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1524013779 156 SMAEW-----LEEYLRSfnGALLMVTHDRYFLDSVtNRIVELDKG 195
Cdd:PLN03232 774 HVAHQvfdscMKDELKG--KTRVLVTNQLHFLPLM-DRIILVSEG 815
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
190-284 |
4.04e-07 |
|
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: 47.95 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 190 VELDKGKLFSYQTNkvngggadrestqgcYEEYLKLKAERLDLLEASERKRQSILRVELQWMQR-GARARSTKQ-KAHIE 267
Cdd:pfam12848 1 VELERGKLTTYKGN---------------YSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRfRAKASKAKQaQSRIK 65
|
90
....*....|....*..
gi 1524013779 268 RYETLRDQKGLETDQAV 284
Cdd:pfam12848 66 ALEKMERIEKPERDKPK 82
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
297-452 |
4.51e-07 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 51.19 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 297 TVELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITVG---------QTVKMGYFSQ 367
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedatdvpvQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 368 eNEELDGRLKVIDYIRGAAEyVKTKDGSVSASQMLERFL-FPSSVQYTTIEK-----LSGGEKRRLYLLRILMEAPNVLL 441
Cdd:cd03296 82 -HYALFRHMTVFDNVAFGLR-VKPRSERPPEAEIRAKVHeLLKLVQLDWLADrypaqLSGGQRQRVALARALAVEPKVLL 159
|
170
....*....|.
gi 1524013779 442 LDEPTNDLDIQ 452
Cdd:cd03296 160 LDEPFGALDAK 170
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-157 |
4.69e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 51.71 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERL-LF--------DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGK-VVKGRNLT----- 67
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgWFrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGElLIDDHPLHfgdys 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 -----VRFLPQNPEF-----YKGDTILTSIVRENEgqdhvwDLESQAKTMLTKLGFTDFDILVE-------TLSGGQRKR 130
Cdd:PRK15112 84 yrsqrIRMIFQDPSTslnprQRISQILDFPLRLNT------DLEPEQREKQIIETLRQVGLLPDhasyyphMLAPGQKQR 157
|
170 180
....*....|....*....|....*..
gi 1524013779 131 VALVSVLLSTADLLVLDEPTNHLDSSM 157
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSM 184
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-197 |
4.70e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.75 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 19 FDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-KGRNLTVR-----------FLPQNPEFYkgDTILTS 86
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMlNGKEINALstaqrlarglvYLPEDRQSS--GLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 87 IVREN-----EGQDHVWDLESQAKTMLTK----LG--FTDFDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDS 155
Cdd:PRK15439 357 PLAWNvcaltHNRRGFWIKPARENAVLERyrraLNikFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1524013779 156 SMAEWLEEYLRSF---NGALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:PRK15439 437 SARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-252 |
4.90e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 51.78 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 4 LTIEHMTKSYTE--RLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRFLPQNPEFY--- 78
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFgvi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 79 -KGDTILTSIVREN---EGQ---DHVWDL--ESQAKTMLTKL-GFTDFdILVE---TLSGGQRKRVALVSVLLSTADLLV 145
Cdd:cd03289 83 pQKVFIFSGTFRKNldpYGKwsdEEIWKVaeEVGLKSVIEQFpGQLDF-VLVDggcVLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 146 LDEPTNHLDSSMAEWLEEYLR-SFNGALLMVTHDRYFLDSVTNRIVELDKGKLFSYqtnkvngggadrESTQGCYEEYLK 224
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTLKqAFADCTVILSEHRIEAMLECQRFLVIEENKVRQY------------DSIQKLLNEKSH 229
|
250 260 270
....*....|....*....|....*....|....
gi 1524013779 225 LK-----AERLDLLEASER-KRQSILRVELQWMQ 252
Cdd:cd03289 230 FKqaispSDRLKLFPRRNSsKSKRKPRPQIQALQ 263
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
336-462 |
5.34e-07 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 50.83 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV---------KMGYFSqENEELDGRLKVIDYIR--GAAEYVKTKDGSVSASQMLE 403
Cdd:cd03266 44 KTTTLRMLAGLLEPDAGFATVdGFDVvkepaearrRLGFVS-DSTGLYDRLTARENLEyfAGLYGLKGDELTARLEELAD 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 404 RFLFPSSVQYTTiEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLE 462
Cdd:cd03266 123 RLGMEELLDRRV-GGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIR 180
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
419-483 |
6.39e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.50 E-value: 6.39e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYL-ESFPGI-VITVSH----DRYFlDRVVR 483
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLrEELPGTtVISVGHrstlAAFH-DRVLE 555
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
297-491 |
6.80e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 50.66 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 297 TVELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITVGQT------------VKMGY 364
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 365 FSQEnEELDGRLKVIDYIRGAAEYVK---TKDGSVSASQMLERFLFpSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLL 441
Cdd:PRK10895 83 LPQE-ASIFRRLSVYDNLMAVLQIRDdlsAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 442 LDEPTNDLD----IQTLTILEDYLESFPGIVITVSHDRYFLDRVVRRIFAFEGN 491
Cdd:PRK10895 161 LDEPFAGVDpisvIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGH 214
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
417-473 |
7.32e-07 |
|
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: 49.46 E-value: 7.32e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1524013779 417 EKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFPGIVITVSH 473
Cdd:cd03223 90 DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH 146
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
298-497 |
7.77e-07 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 50.76 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGD-KVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITV-GQTV----------KMGYF 365
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdGEDIreqdpvelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 366 SQ-----------ENEELDGRLKVID---YIRGAAEYVKTKDgsVSASQMLERflFPSsvqyttieKLSGGEKRRLYLLR 431
Cdd:cd03295 81 IQqiglfphmtveENIALVPKLLKWPkekIRERADELLALVG--LDPAEFADR--YPH--------ELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1524013779 432 ILMEAPNVLLLDEPTNDLDIQTLTILEDYL----ESFPGIVITVSHDryfLDRVVR---RIfAFEGNGMVTQY 497
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFkrlqQELGKTIVFVTHD---IDEAFRladRI-AIMKNGEIVQV 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-178 |
8.22e-07 |
|
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: 51.99 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 20 DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEePDEGKVV-KGRNLTVR----FLP---------Q------NPEFYK 79
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRfDGQDLDGLsrraLRPlrrrmqvvfQdpfgslSPRMTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 80 GDtiltsIVRE-----NEGQDHVwDLESQAKTMLTKLGFTDfdilvETL-------SGGQRKRVALVSVLLSTADLLVLD 147
Cdd:COG4172 382 GQ-----IIAEglrvhGPGLSAA-ERRARVAEALEEVGLDP-----AARhryphefSGGQRQRIAIARALILEPKLLVLD 450
|
170 180 190
....*....|....*....|....*....|....*
gi 1524013779 148 EPTNHLDSS----MAEWLEEYLRSFNGALLMVTHD 178
Cdd:COG4172 451 EPTSALDVSvqaqILDLLRDLQREHGLAYLFISHD 485
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
336-485 |
8.31e-07 |
|
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: 50.51 E-value: 8.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVG----------QTVKMGY---FsQeNEELDGRLKVIDYIRGAAEYVKTKDGSVS----- 397
Cdd:cd03219 39 KTTLFNLISGFLRPTSGSVLFDgeditglpphEIARLGIgrtF-Q-IPRLFPELTVLENVMVAAQARTGSGLLLArarre 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 398 -------ASQMLERF-LfpSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFP--GI 467
Cdd:cd03219 117 erearerAEELLERVgL--ADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRerGI 194
|
170
....*....|....*....
gi 1524013779 468 -VITVSHDRYFLDRVVRRI 485
Cdd:cd03219 195 tVLLVEHDMDVVMSLADRV 213
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-178 |
1.00e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.53 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNL---------TVR- 69
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlFDGENIpamsrsrlyTVRk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 70 ---FLPQNPEFYkgdTILTsiVRENEGqdhvWDLESQAK--------TMLTKLGFTDF----DILVETLSGGQRKRVALV 134
Cdd:PRK11831 85 rmsMLFQSGALF---TDMN--VFDNVA----YPLREHTQlpapllhsTVMMKLEAVGLrgaaKLMPSELSGGMARRAALA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1524013779 135 SVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNGAL----LMVTHD 178
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvtcVVVSHD 203
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
298-474 |
1.12e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 50.08 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDFTYILLK---------NdrigiigpnGGGKSTLMKIIAGWVEPDEGTITV-GQTV------- 360
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKggitaligpN---------GAGKSTLLSMISRLLPPDSGEVLVdGLDVattpsre 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 361 ---KMGYFSQEN--------EEL---------DGRLKVID--YIRGAAEYVKTKDgsvsasqMLERFLfpssvqyttiEK 418
Cdd:COG4604 73 lakRLAILRQENhinsrltvRELvafgrfpysKGRLTAEDreIIDEAIAYLDLED-------LADRYL----------DE 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI----QTLTILEDYLESFPGIVITVSHD 474
Cdd:COG4604 136 LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
336-453 |
1.13e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 50.65 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTVK-------MGYFSQeNEELD-------------GRLKVIDYIRGAAEYVKTK-D 393
Cdd:PRK15056 46 KSTLFKALMGFVRLASGKISIlGQPTRqalqknlVAYVPQ-SEEVDwsfpvlvedvvmmGRYGHMGWLRRAKKRDRQIvT 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 394 GSVSASQMLErflfpssVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT 453
Cdd:PRK15056 125 AALARVDMVE-------FRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
336-474 |
1.17e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 50.22 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGwVEPDEGTITVGQT-----------VKMGYFSQENEELDGrLKVIDYIR------GAAEYVKTKDGSVSA 398
Cdd:COG4138 35 KSTLLARMAG-LLPGQGEILLNGRplsdwsaaelaRHRAYLSQQQSPPFA-MPVFQYLAlhqpagASSEAVEQLLAQLAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 399 SQMLERFLfPSSVQyttieKLSGGEKRRLYLLRILME-------APNVLLLDEPTNDLDIQTLTILEDYLESF--PGI-V 468
Cdd:COG4138 113 ALGLEDKL-SRPLT-----QLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLRELcqQGItV 186
|
....*.
gi 1524013779 469 ITVSHD 474
Cdd:COG4138 187 VMSSHD 192
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
297-470 |
1.68e-06 |
|
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: 49.58 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 297 TVELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITV-GQTVK-----------MGY 364
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIdGQDIThlpmherarlgIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 365 FSQEnEELDGRLKVIDYIRGAAEYVKTKDGSVSASQ---MLERFlfpssvQYTTIEK-----LSGGEKRRLYLLRILMEA 436
Cdd:TIGR04406 81 LPQE-ASIFRKLTVEENIMAVLEIRKDLDRAEREERleaLLEEF------QISHLRDnkamsLSGGERRRVEIARALATN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1524013779 437 PNVLLLDE------PTNDLDIQTLTileDYLESFP-GIVIT 470
Cdd:TIGR04406 154 PKFILLDEpfagvdPIAVGDIKKII---KHLKERGiGVLIT 191
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
334-490 |
1.74e-06 |
|
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: 49.71 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 334 GGKSTLMKIIAGWVEPDEGTITVgQTVKMGYFSQENE-ELDGR----LKVIDYIRGAAEYVKTKdgsVSASQMLERFLfp 408
Cdd:cd03237 36 IGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIKaDYEGTvrdlLSSITKDFYTHPYFKTE---IAKPLQIEQIL-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 409 sSVQYTTiekLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI-QTL---TILEDYLESFPGIVITVSHDRYFLDRVVRR 484
Cdd:cd03237 110 -DREVPE---LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeQRLmasKVIRRFAENNEKTAFVVEHDIIMIDYLADR 185
|
....*.
gi 1524013779 485 IFAFEG 490
Cdd:cd03237 186 LIVFEG 191
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
336-450 |
2.01e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 49.72 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV------KMGYFSqenEE--LDGRLKVIDYI------RGaaeyVKTKDGSVSASQ 400
Cdd:COG4152 40 KTTTIRIILGILAPDSGEVLWdGEPLdpedrrRIGYLP---EErgLYPKMKVGEQLvylarlKG----LSKAEAKRRADE 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 401 MLERF-LfpSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD 450
Cdd:COG4152 113 WLERLgL--GDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
336-453 |
2.25e-06 |
|
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: 48.97 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTvkmgyFSQENEelDGRLKVidyiRG-----------------AAEYVKT------ 391
Cdd:COG4181 51 KSTLLGLLAGLDRPTSGTVRLaGQD-----LFALDE--DARARL----RArhvgfvfqsfqllptltALENVMLplelag 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 392 -KDGSVSASQMLERF-L------FPSsvqyttieKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT 453
Cdd:COG4181 120 rRDARARARALLERVgLghrldhYPA--------QLSGGEQQRVALARAFATEPAILFADEPTGNLDAAT 181
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
307-480 |
2.30e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 307 YGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITV-GQTVK--MGYFSQENEELDGRLKVIDY-- 381
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKkdLCTYQKQLCFVGHRSGINPYlt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 382 IRGAAEY-VKTKDGSVSASQMLERFLFPSSVQYTTiEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDY 460
Cdd:PRK13540 91 LRENCLYdIHFSPGAVGITELCRLFSLEHLIDYPC-GLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITK 169
|
170 180
....*....|....*....|...
gi 1524013779 461 LESF---PGIVITVSHDRYFLDR 480
Cdd:PRK13540 170 IQEHrakGGAVLLTSHQDLPLNK 192
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
419-483 |
2.43e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 50.59 E-value: 2.43e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 419 LSGGEKRRLYLLRILM-EAPnVLLLDEPTNDLDIQT-LTILEDYLESFPG-IVITVSHDRYFL---DRVVR 483
Cdd:PRK11160 476 LSGGEQRRLGIARALLhDAP-LLLLDEPTEGLDAETeRQILELLAEHAQNkTVLMITHRLTGLeqfDRICV 545
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
336-453 |
2.47e-06 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTVK----------MGYFSQE----NEELD-----GRLKVIDY-IRGAAEyvktkdg 394
Cdd:cd03253 40 KSTILRLLFRFYDVSSGSILIdGQDIRevtldslrraIGVVPQDtvlfNDTIGyniryGRPDATDEeVIEAAK------- 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 395 svsASQMLERFL-FPSsvQYTTI--E---KLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT 453
Cdd:cd03253 113 ---AAQIHDKIMrFPD--GYDTIvgErglKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHT 172
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-68 |
2.58e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.43 E-value: 2.58e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1524013779 20 DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTV 68
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSV 89
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
387-538 |
2.86e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 387 EYVKTKDG---SVSASQMLERFLFPSSVQYTTI-----EKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILE 458
Cdd:PTZ00265 540 NYQTIKDSevvDVSKKVLIHDFVSALPDKYETLvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 459 DYLESFPG----IVITVSHdRYFLDRVVRRIFafegngMVTQYEGGFTDYQAAYSEKHPEGILEQSDKKEKKTAAQEKTN 534
Cdd:PTZ00265 620 KTINNLKGnenrITIIIAH-RLSTIRYANTIF------VLSNRERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNN 692
|
....
gi 1524013779 535 PGKK 538
Cdd:PTZ00265 693 NNNK 696
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
418-514 |
2.86e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 49.32 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 418 KLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFPG--IVITVSHDRYFLDRVVRRIFAFEGNGMVt 495
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRAALFFDGRLV- 241
|
90
....*....|....*....
gi 1524013779 496 qyEGGFTDyQAAYSEKHPE 514
Cdd:PRK14271 242 --EEGPTE-QLFSSPKHAE 257
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-63 |
2.92e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.27 E-value: 2.92e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1524013779 20 DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKG 63
Cdd:PRK13545 41 NNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVdIKG 85
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
419-484 |
3.04e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 49.31 E-value: 3.04e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQ-TLTILE--DYLESFPGIVITVSHDryfLDRVVRR 484
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEifDNLNKQGKTIILVTHD---LDNVLEW 231
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
336-479 |
3.04e-06 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 48.80 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGW--VEPDEGTITV-GQTV---------KMGYF--SQENEELDGrLKVIDYIRGAAEYVKTKDGS--VSAS 399
Cdd:TIGR01978 39 KSTLSKTIAGHpsYEVTSGTILFkGQDLlelepderaRAGLFlaFQYPEEIPG-VSNLEFLRSALNARRSARGEepLDLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 400 Q-----------------MLERFLFpssvqyttiEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTI----LE 458
Cdd:TIGR01978 118 DfekllkeklalldmdeeFLNRSVN---------EGFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIvaegIN 188
|
170 180
....*....|....*....|.
gi 1524013779 459 DYLESFPGIVItVSHDRYFLD 479
Cdd:TIGR01978 189 RLREPDRSFLI-ITHYQRLLN 208
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
336-473 |
3.18e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 48.33 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV---GQTV-----KMGYFSQENEeLDGRLKVIDYIRGAAEYVKTKDGSVSASqmLERF-- 405
Cdd:PRK13539 41 KTTLLRLIAGLLPPAAGTIKLdggDIDDpdvaeACHYLGHRNA-MKPALTVAENLEFWAAFLGGEELDIAAA--LEAVgl 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 406 --LFPSSVQYttiekLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT----LTILEDYLESfPGIVITVSH 473
Cdd:PRK13539 118 apLAHLPFGY-----LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAvalfAELIRAHLAQ-GGIVIAATH 185
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
336-482 |
3.37e-06 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 48.60 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQT----------VKMgyFSQEN--------EE-----LDGRLKV----IDYIRGAAE 387
Cdd:COG3840 38 KSTLLNLIAGFLPPDSGRILWnGQDltalppaerpVSM--LFQENnlfphltvAQniglgLRPGLKLtaeqRAQVEQALE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 388 yvktkdgSVSASQMLERFlfPSSvqyttiekLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI----QTLTILEDYLES 463
Cdd:COG3840 116 -------RVGLAGLLDRL--PGQ--------LSGGQRQRVALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDELCRE 178
|
170 180
....*....|....*....|...
gi 1524013779 464 FPGIVITVSHD----RYFLDRVV 482
Cdd:COG3840 179 RGLTVLMVTHDpedaARIADRVL 201
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
7-155 |
3.82e-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: 49.82 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 7 EHMTKSYT-ERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNL------------------ 66
Cdd:COG5265 361 ENVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlIDGQDIrdvtqaslraaigivpqd 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 67 TVRFlpqNpefykgDTILTSIV--RENEGQDHVWD----------LESQAKTMLTKLGftdfdilvE---TLSGGQRKRV 131
Cdd:COG5265 441 TVLF---N------DTIAYNIAygRPDASEEEVEAaaraaqihdfIESLPDGYDTRVG--------ErglKLSGGEKQRV 503
|
170 180
....*....|....*....|....
gi 1524013779 132 ALVSVLLSTADLLVLDEPTNHLDS 155
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSALDS 527
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
298-475 |
4.68e-06 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 48.94 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDFT-------YI-LL------KndrigiigpngggkSTLMKIIAGWVEPDEGTITV-GQTV-- 360
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSlsiepgeFVaLLgpsgcgK--------------TTLLRMIAGFETPDSGRILLdGRDVtg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 361 ------KMGYFSQ-----------ENeeldgrlkvIDY---IRG-AAEYVKTKdgsvsASQMLERflfpssVQYTTIEK- 418
Cdd:COG3842 72 lppekrNVGMVFQdyalfphltvaEN---------VAFglrMRGvPKAEIRAR-----VAELLEL------VGLEGLADr 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 419 ----LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD----IQTLTILEDYLESFpGI-VITVSHDR 475
Cdd:COG3842 132 yphqLSGGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQREL-GItFIYVTHDQ 196
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
336-453 |
5.02e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 48.16 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTVK-----MGYFSQeNEELDGRLKVIDYIRGAAEY--VKTKDGSVSASQMLERFLF 407
Cdd:PRK11248 40 KTTLLNLIAGFVPYQHGSITLdGKPVEgpgaeRGVVFQ-NEGLLPWRNVQDNVAFGLQLagVEKMQRLEIAHQMLKKVGL 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1524013779 408 pSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT 453
Cdd:PRK11248 119 -EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-197 |
5.74e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.25 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMT-KSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLT-----------VR 69
Cdd:COG3845 257 VLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIrLDGEDITglsprerrrlgVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 70 FLPQNPefyKGD-TILTSIVRENEGqdhvwdLESQAKTMLTKLGF--------------TDFDI-------LVETLSGGQ 127
Cdd:COG3845 337 YIPEDR---LGRgLVPDMSVAENLI------LGRYRRPPFSRGGFldrkairafaeeliEEFDVrtpgpdtPARSLSGGN 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 128 RKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYL---RSFNGALLMVTHDryfLD---SVTNRIVELDKGKL 197
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLlelRDAGAAVLLISED---LDeilALSDRIAVMYEGRI 480
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
336-473 |
6.64e-06 |
|
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: 47.49 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVGQTvkmgyfsQENEELDGRLKVIDYIrGAAEYVKtkdGSVSASQMLeRFLFP------- 408
Cdd:cd03231 39 KTTLLRILAGLSPPLAGRVLLNGG-------PLDFQRDSIARGLLYL-GHAPGIK---TTLSVLENL-RFWHAdhsdeqv 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1524013779 409 ---------SSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFP---GIVITVSH 473
Cdd:cd03231 107 eealarvglNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCargGMVVLTTH 183
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
336-459 |
6.70e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 47.65 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQT----------VKMGYfsQENE-------------ELDGRLKVIDYIRgaaEYVKT 391
Cdd:PRK10771 38 KSTLLNLIAGFLTPASGSLTLnGQDhtttppsrrpVSMLF--QENNlfshltvaqniglGLNPGLKLNAAQR---EKLHA 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 392 KDGSVSASQMLERFlfPSsvqyttieKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD----IQTLTILED 459
Cdd:PRK10771 113 IARQMGIEDLLARL--PG--------QLSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQ 174
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
336-485 |
6.71e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.85 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTIT-VGQTVkmgyfSQENEELDGRLKVID------------------------YIRGAAEyvk 390
Cdd:PRK10584 49 KSTLLAILAGLDDGSSGEVSlVGQPL-----HQMDEEARAKLRAKHvgfvfqsfmliptlnalenvelpaLLRGESS--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 391 tKDGSVSASQMLERFLFPSSVQYTTIEkLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLES----FPG 466
Cdd:PRK10584 121 -RQSRNGAKALLEQLGLGKRLDHLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSlnreHGT 198
|
170
....*....|....*....
gi 1524013779 467 IVITVSHDRYFLDRVVRRI 485
Cdd:PRK10584 199 TLILVTHDLQLAARCDRRL 217
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
336-473 |
7.98e-06 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 47.53 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTVK----------MGYFSQENEELDGRLKviDYIRGAAEYVKTKDgSVSASQMLER 404
Cdd:cd03249 42 KSTVVSLLERFYDPTSGEILLdGVDIRdlnlrwlrsqIGLVSQEPVLFDGTIA--ENIRYGKPDATDEE-VEEAAKKANI 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 405 FLFPSSV--QYTTI-----EKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFPG--IVITVSH 473
Cdd:cd03249 119 HDFIMSLpdGYDTLvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKgrTTIVIAH 196
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
419-474 |
8.00e-06 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 47.09 E-value: 8.00e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD----IQTLTILEDYLESFPGIVITVSHD 474
Cdd:COG4136 134 LSGGQRARVALLRALLAEPRALLLDEPFSKLDaalrAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
336-450 |
9.82e-06 |
|
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: 46.78 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEP--DEGTITV-GQTVK-------MGYFSQENeELDGRLKVIDYIRGAAEyvktkdgsvsasqmlerf 405
Cdd:cd03213 48 KSTLLNALAGRRTGlgVSGEVLInGRPLDkrsfrkiIGYVPQDD-ILHPTLTVRETLMFAAK------------------ 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1524013779 406 lfpssvqyttIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD 450
Cdd:cd03213 109 ----------LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
336-482 |
9.84e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 47.37 E-value: 9.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAG--WVEPDEGTITV-GQTV---------KMGYF--SQENEELDGrLKVIDYIRGAAEYVKTKDGSVSASQ- 400
Cdd:COG0396 39 KSTLAKVLMGhpKYEVTSGSILLdGEDIlelspderaRAGIFlaFQYPVEIPG-VSVSNFLRTALNARRGEELSAREFLk 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 401 --------------MLERFLFpssvqyttiEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESF-- 464
Cdd:COG0396 118 llkekmkelgldedFLDRYVN---------EGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLrs 188
|
170 180
....*....|....*....|.
gi 1524013779 465 PG---IVITvsHDRYFLDRVV 482
Cdd:COG0396 189 PDrgiLIIT--HYQRILDYIK 207
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-202 |
1.16e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 48.11 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 21 DTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV---------------KGRNLTVRFLPQNPEFYKGDTILT 85
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLidgvdiakisdaelrEVRRKKIAMVFQSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 86 SI--------VRENEGQDHVWDLESQAKTMLTKLGFTDfdilveTLSGGQRKRVALVSVLLSTADLLVLDEPTNHLD--- 154
Cdd:PRK10070 126 NTafgmelagINAEERREKALDALRQVGLENYAHSYPD------ELSGGMRQRVGLARALAINPDILLMDEAFSALDpli 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1524013779 155 -SSMAEWLEEYLRSFNGALLMVTHDRYFLDSVTNRIVELDKGKLFSYQT 202
Cdd:PRK10070 200 rTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
416-496 |
1.20e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.47 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 416 IEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI----QTLTILEDYLESFPGIVITVSHDRYFLDRVVRRIFAFEGN 491
Cdd:PRK10575 145 VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGG 224
|
....*
gi 1524013779 492 GMVTQ 496
Cdd:PRK10575 225 EMIAQ 229
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-187 |
1.27e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 47.59 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 1 MNLL-----TIEHMTKSYTERLLfDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEE--------------------- 54
Cdd:COG4170 1 MPLLdirnlTIEIDTPQGRVKAV-DRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhvtadrfrwngidllkls 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 55 PDEGKVVKGRNLTVRFlpQNPEFYK------GDTILTSI-VRENEG---QDHVWDLEsQAKTMLTKLGFTDFDILVET-- 122
Cdd:COG4170 80 PRERRKIIGREIAMIF--QEPSSCLdpsakiGDQLIEAIpSWTFKGkwwQRFKWRKK-RAIELLHRVGIKDHKDIMNSyp 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 123 --LSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNG----ALLMVTHDryfLDSVTN 187
Cdd:COG4170 157 heLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlqgtSILLISHD---LESISQ 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
336-453 |
1.30e-05 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 48.24 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTVK----------MGYFSQENEELDG------RLKVIDY----IRGAAEyvktkdg 394
Cdd:COG1132 379 KSTLVNLLLRFYDPTSGRILIdGVDIRdltleslrrqIGVVPQDTFLFSGtireniRYGRPDAtdeeVEEAAK------- 451
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 395 SVSASQMLERFlfPSsvQYTTI-----EKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT 453
Cdd:COG1132 452 AAQAHEFIEAL--PD--GYDTVvgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTET 511
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
15-178 |
1.55e-05 |
|
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: 45.43 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 15 ERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVagleepdegkvvkGRNLTVRFLPQNPEFYKGdtiltsiVRENEGQ 94
Cdd:cd03227 7 FPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAI-------------GLALGGAQSATRRRSGVK-------AGCIVAA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 95 DHVwdlesqaktmltklgftDFDILVETLSGGQRKRVALVSVL----LSTADLLVLDEPTNHLDSSMAEWLEEYLRSF-- 168
Cdd:cd03227 67 VSA-----------------ELIFTRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHlv 129
|
170
....*....|.
gi 1524013779 169 NGALLMV-THD 178
Cdd:cd03227 130 KGAQVIViTHL 140
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
304-496 |
1.69e-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: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 304 SKAYGDKVLmKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITVGQTV-----------KMGYFSQE---- 368
Cdd:TIGR01193 482 SYGYGSNIL-SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqFINYLPQEpyif 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 369 ------NEELDGRLKV-IDYIRGAAEYVKTKDGSVSASQMLERFLfpsSVQYTTIeklSGGEKRRLYLLRILMEAPNVLL 441
Cdd:TIGR01193 561 sgsileNLLLGAKENVsQDEIWAACEIAEIKDDIENMPLGYQTEL---SEEGSSI---SGGQKQRIALARALLTDSKVLI 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 442 LDEPTNDLDIQT-LTILEDYLESFPGIVITVSHdRYFLDRVVRRIFAFEGNGMVTQ 496
Cdd:TIGR01193 635 LDESTSNLDTITeKKIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIEQ 689
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
336-482 |
1.88e-05 |
|
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: 46.30 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV------KMGYFsqENEELDGRLKVIDYIRGAAEYVKTKDGSVSASQMLERFLFP 408
Cdd:TIGR01184 24 KSTLLNLISGLAQPTSGGVILeGKQItepgpdRMVVF--QNYSLLPWLTVRENIALAVDRVLPDLSKSERRAIVEEHIAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 409 SSVQYTT---IEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYL----ESFPGIVITVSHD---RYFL 478
Cdd:TIGR01184 102 VGLTEAAdkrPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHDvdeALLL 181
|
....*
gi 1524013779 479 -DRVV 482
Cdd:TIGR01184 182 sDRVV 186
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
353-463 |
2.03e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.04 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 353 TITVGQTVKMGyfsqENEELDGRLKVidYIRGAAEYVKTKDGSVSASQMLERFLFPSSVQYTTiEKLSGGEKRRLYLLRI 432
Cdd:NF000106 86 TIG*HRPVR*G----RRESFSGRENL--YMIGR*LDLSRKDARARADELLERFSLTEAAGRAA-AKYSGGMRRRLDLAAS 158
|
90 100 110
....*....|....*....|....*....|.
gi 1524013779 433 LMEAPNVLLLDEPTNDLDIQTLTILEDYLES 463
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWDEVRS 189
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-197 |
2.11e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.81 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 12 SYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGlEEP---DEGKVVKGR-----------NLTVR----F-LP 72
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPprsDASVVIRGTvayvpqvswifNATVRdnilFgSP 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 73 QNPEFYKGDTILTSIVRenegqdhvwDLESQAKTMLTKLGFTDFDIlvetlSGGQRKRVALVSVLLSTADLLVLDEPTNH 152
Cdd:PLN03130 705 FDPERYERAIDVTALQH---------DLDLLPGGDLTEIGERGVNI-----SGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1524013779 153 LDSSMAEW-----LEEYLRsfNGALLMVTHDRYFLDSVtNRIVELDKGKL 197
Cdd:PLN03130 771 LDAHVGRQvfdkcIKDELR--GKTRVLVTNQLHFLSQV-DRIILVHEGMI 817
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
336-445 |
2.27e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 46.18 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTVK-----------MGYFSQENEeLDGRLKVIDYIRGAAEYVKtkdgsVSASQ--- 400
Cdd:COG1137 42 KTTTFYMIVGLVKPDSGRIFLdGEDIThlpmhkrarlgIGYLPQEAS-IFRKLTVEDNILAVLELRK-----LSKKEree 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 401 ----MLERFlfpssvQYTTIEK-----LSGGEKRRLYLLRILMEAPNVLLLDEP 445
Cdd:COG1137 116 rleeLLEEF------GITHLRKskaysLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-185 |
2.97e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.79 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 2 NLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGleEPD----EGKV-VKGRNLTVR------- 69
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDIlFKGESILDLepeerah 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 70 ---FLP-QNPEFYKGDT------ILTSIVRENEGQDHVWDLESqAKTMLTKLGFTDFDI------LVETLSGGQRKRVAL 133
Cdd:CHL00131 84 lgiFLAfQYPIEIPGVSnadflrLAYNSKRKFQGLPELDPLEF-LEIINEKLKLVGMDPsflsrnVNEGFSGGEKKRNEI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 134 VSVLLSTADLLVLDEPTNHLD----SSMAEWLEEYLRSFNGALLmVTHDRYFLDSV 185
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDidalKIIAEGINKLMTSENSIIL-ITHYQRLLDYI 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
336-446 |
2.98e-05 |
|
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: 45.80 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTI---------------------------------TVGQTVKMGYFSQENEELDGRLkvIDYI 382
Cdd:COG0411 43 KTTLFNLITGFYRPTSGRIlfdgrditglpphriarlgiartfqnprlfpelTVLENVLVAAHARLGRGLLAAL--LRLP 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 383 RGAAEYVKTKDgsvSASQMLERF-LfpSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPT 446
Cdd:COG0411 121 RARREEREARE---RAEELLERVgL--ADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPA 180
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
336-450 |
2.99e-05 |
|
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: 45.56 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVG-----------QTVKMGYfsQENE-------------ELDGRLKVIDYIRGAaeyVKT 391
Cdd:cd03298 37 KSTLLNLIAGFETPQSGRVLINgvdvtaappadRPVSMLF--QENNlfahltveqnvglGLSPGLKLTAEDRQA---IEV 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 392 KDGSVSASQMLERFlfPssvqyttiEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD 450
Cdd:cd03298 112 ALARVGLAGLEKRL--P--------GELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-185 |
3.10e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.94 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 3 LLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLE--EPDEGKVV-KGRNLtvrfLPQNPEFYK 79
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEfKGKDL----LELSPEDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 80 GDTIL-------------------TSI--VRENEGQDHvwdlesqaktmLTKLGFTDF------------DILVETL--- 123
Cdd:PRK09580 77 GEGIFmafqypveipgvsnqfflqTALnaVRSYRGQEP-----------LDRFDFQDLmeekiallkmpeDLLTRSVnvg 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 124 -SGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEE---YLRSFNGALLMVTHDRYFLDSV 185
Cdd:PRK09580 146 fSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADgvnSLRDGKRSFIIVTHYQRILDYI 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
336-446 |
3.15e-05 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 45.74 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVG----------QTVKMGY-FSQENEELDGRLKVIDYIRgAAEYVKTKDGSVSASqmLER 404
Cdd:COG0410 42 KTTLLKAISGLLPPRSGSIRFDgeditglpphRIARLGIgYVPEGRRIFPSLTVEENLL-LGAYARRDRAEVRAD--LER 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1524013779 405 F--LFP-----SSVQYTTiekLSGGEKRRLYLLRILMEAPNVLLLDEPT 446
Cdd:COG0410 119 VyeLFPrlkerRRQRAGT---LSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
336-462 |
3.49e-05 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 45.68 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV----------KMGYFSQENEELDGrlKVIDYIRGAAEYVkTKDGSVSASQM--L 402
Cdd:cd03251 41 KSTLVNLIPRFYDVDSGRILIdGHDVrdytlaslrrQIGLVSQDVFLFND--TVAENIAYGRPGA-TREEVEEAARAanA 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 403 ERFLFPSSVQYTTI-----EKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLE 462
Cdd:cd03251 118 HEFIMELPEGYDTVigergVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALE 182
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
419-474 |
3.50e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 45.78 E-value: 3.50e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD----IQTLTILEDYLESfpGI--VItVSHD 474
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitAQIVSIIRELAET--GItqVI-VTHE 200
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
298-499 |
3.66e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 45.25 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAY-GDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITVGQ--------------TVKM 362
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrevpflRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 363 GYFSQENEELDGRlKVID------YIRGAAeyvkTKDGSVSASQMLERFLFPSSVQYTTIEkLSGGEKRRLYLLRILMEA 436
Cdd:PRK10908 82 GMIFQDHHLLMDR-TVYDnvaiplIIAGAS----GDDIRRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 437 PNVLLLDEPTNDLDIQTLTILEDYLESFPGIVITV---SHDRYFLDRVVRRIFAFEGNGMVTQYEG 499
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVlmaTHDIGLISRRSYRMLTLSDGHLHGGVGG 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
336-473 |
4.20e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 45.88 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVGQTV---------------KMGYFSQENE-ELDGRLKVIDYIRGAAEY-VKTKDGSVSA 398
Cdd:PRK13643 45 KSTLLQHLNGLLQPTEGKVTVGDIVvsstskqkeikpvrkKVGVVFQFPEsQLFEETVLKDVAFGPQNFgIPKEKAEKIA 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 399 SQMLERFLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD----IQTLTILEDYLESFPGIVItVSH 473
Cdd:PRK13643 125 AEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQSGQTVVL-VTH 202
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
298-476 |
4.72e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITVGQT------------VKMGYF 365
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 366 SQENEELD----------GRL--------KVIDYirgaaeyvktKDGSVSASQMLERFLFPSSVQyTTIEKLSGGEKRRL 427
Cdd:PRK09700 86 YQELSVIDeltvlenlyiGRHltkkvcgvNIIDW----------REMRVRAAMMLLRVGLKVDLD-EKVANLSISHKQML 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 428 YLLRILMEAPNVLLLDEPTNDL---DIQTLTILEDYLESFPGIVITVSH---------DRY 476
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHklaeirricDRY 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
336-450 |
5.78e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 45.40 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVGQTVKMGyfSQENEEL-DGRLKV-----------------IDYIRGAAEY-VKTKDGSV 396
Cdd:PRK13634 46 KSTLLQHLNGLLQPTSGTVTIGERVITA--GKKNKKLkPLRKKVgivfqfpehqlfeetveKDICFGPMNFgVSEEDAKQ 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1524013779 397 SASQMLERFLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD 450
Cdd:PRK13634 124 KAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
298-485 |
5.81e-05 |
|
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: 44.88 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDK----VLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITV-GQTV------------ 360
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdGTDLtllsgkelrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 361 -KMGYFSQENEELDGRlKVIDYIRGAAEYVKTKDGSVS--ASQMLE-------RFLFPSSvqyttiekLSGGEKRRLYLL 430
Cdd:cd03258 82 rRIGMIFQHFNLLSSR-TVFENVALPLEIAGVPKAEIEerVLELLElvgledkADAYPAQ--------LSGGQKQRVGIA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 431 RILMEAPNVLLLDEPTNDLDIQT----LTILEDYLESFPGIVITVSHDryfLDrVVRRI 485
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETtqsiLALLRDINRELGLTIVLITHE---ME-VVKRI 207
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
68-183 |
5.85e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 45.46 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 68 VRFLPQNPEFYKGDTILTSIVRENEGQDHVWDLESQAKTMLTKLGFTDFDILVETLSGGQRKRVALVSVLLSTAD---LL 144
Cdd:pfam13304 182 KELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLSALPkggLL 261
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1524013779 145 VLDEPTNHLD----SSMAEWLEEyLRSFNGALLMVTHDRYFLD 183
Cdd:pfam13304 262 LIDEPESGLHpkllRRLLELLKE-LSRNGAQLILTTHSPLLLD 303
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
336-446 |
6.24e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.78 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTVKmgyFS--------------QE---------------NEELdGRLKVIDYIRGA 385
Cdd:COG1129 43 KSTLMKILSGVYQPDSGEILLdGEPVR---FRsprdaqaagiaiihQElnlvpnlsvaeniflGREP-RRGGLIDWRAMR 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 386 AEyvktkdgsvsASQMLERFLFPSSVQyTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPT 446
Cdd:COG1129 119 RR----------ARELLARLGLDIDPD-TPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-158 |
6.31e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 26 INEGEKIGLIGINGTGKSTLLKIVAGleEPDEGKVVKGRNLTVRFLPQNP--EFYKGDTILTS----------------- 86
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIAS--NTDGFHIGVEGVITYDGITPEEikKHYRGDVVYNAetdvhfphltvgetldf 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 87 ------------IVRENEGQDHVWDLESQA----KTMLTKLGfTDFdilVETLSGGQRKRVALVSVLLSTADLLVLDEPT 150
Cdd:TIGR00956 162 aarcktpqnrpdGVSREEYAKHIADVYMATyglsHTRNTKVG-NDF---VRGVSGGERKRVSIAEASLGGAKIQCWDNAT 237
|
....*...
gi 1524013779 151 NHLDSSMA 158
Cdd:TIGR00956 238 RGLDSATA 245
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
398-474 |
7.26e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 45.16 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 398 ASQMLERFLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD----IQTLTILEDYLESFPGIVITVSH 473
Cdd:PRK13646 125 AHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDpqskRQVMRLLKSLQTDENKTIILVSH 204
|
.
gi 1524013779 474 D 474
Cdd:PRK13646 205 D 205
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
419-491 |
7.28e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 45.03 E-value: 7.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD------IQTLtILEDYLESFPGIVItVSHDRYFLDRVVRRIFAFEGN 491
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasmkVESL-IQSLRLRSELTMVI-VSHNLHQVSRLSDFTAFFKGN 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
336-484 |
7.50e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 44.54 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGwVEPDEGTITVGQT-----------VKMGYFSQENEELdGRLKVIDYIR-----GAAEYVKTKD-GSVSA 398
Cdd:PRK03695 35 KSTLLARMAG-LLPGSGSIQFAGQpleawsaaelaRHRAYLSQQQTPP-FAMPVFQYLTlhqpdKTRTEAVASAlNEVAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 399 SQMLERFLfPSSVQyttieKLSGGEKRRLYL----LRILMEA-PN--VLLLDEPTNDLDIQTLTILEDYLESFP--GIVI 469
Cdd:PRK03695 113 ALGLDDKL-GRSVN-----QLSGGEWQRVRLaavvLQVWPDInPAgqLLLLDEPMNSLDVAQQAALDRLLSELCqqGIAV 186
|
170
....*....|....*.
gi 1524013779 470 TVS-HDryfLDRVVRR 484
Cdd:PRK03695 187 VMSsHD---LNHTLRH 199
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-165 |
7.87e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 18 LFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVV-------KGRNL-----TVRFLPQNP---------- 75
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIindshnlKDINLkwwrsKIGVVSQDPllfsnsiknn 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 76 ---------------EFYKGDTILT---SIVRENEGQDHVWDLESQAKTMLT-----------------------KLGFT 114
Cdd:PTZ00265 480 ikyslyslkdlealsNYYNEDGNDSqenKNKRNSCRAKCAGDLNDMSNTTDSneliemrknyqtikdsevvdvskKVLIH 559
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1524013779 115 DF--------DILVET----LSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSmaewlEEYL 165
Cdd:PTZ00265 560 DFvsalpdkyETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-----SEYL 617
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
336-450 |
7.89e-05 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 44.60 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVgqtvkmgyfsqENEELDGRLKVIDYIRG-----------------------AAEYVK-- 390
Cdd:COG1126 40 KSTLLRCINLLEEPDSGTITV-----------DGEDLTDSKKDINKLRRkvgmvfqqfnlfphltvlenvtlAPIKVKkm 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 391 -TKDGSVSASQMLERF-------LFPSSvqyttiekLSGGEKRRLYLLRIL-MEaPNVLLLDEPTNDLD 450
Cdd:COG1126 109 sKAEAEERAMELLERVgladkadAYPAQ--------LSGGQQQRVAIARALaME-PKVMLFDEPTSALD 168
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
416-476 |
8.51e-05 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 44.62 E-value: 8.51e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 416 IEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQ---TLTILEDYLESFPGIVITVSHD-----RY 476
Cdd:PRK11231 136 LTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHDlnqasRY 204
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
19-197 |
8.56e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 44.60 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 19 FDDTSFSINEGEKIG-LIGINGTGKSTLLKIVAGLEEPDEGKV--VKGRNLTVRflpqNPEFYKGDTILTSIvrenEGQD 95
Cdd:COG3950 14 FEDLEIDFDNPPRLTvLVGENGSGKTTLLEAIALALSGLLSRLddVKFRKLLIR----NGEFGDSAKLILYY----GTSR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 96 HVWDLESQAKTMLTKLGFTDFDILVETLSGGQRKRvALVSVLLSTADLLvldepTNHLDSSMAEWLEEYLRSFNGALLMV 175
Cdd:COG3950 86 LLLDGPLKKLERLKEEYFSRLDGYDSLLDEDSNLR-EFLEWLREYLEDL-----ENKLSDELDEKLEAVREALNKLLPDF 159
|
170 180
....*....|....*....|..
gi 1524013779 176 THDRYFLDSVTNRIVELDKGKL 197
Cdd:COG3950 160 KDIRIDRDPGRLVILDKNGEEL 181
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
336-520 |
9.75e-05 |
|
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: 44.41 E-value: 9.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTIT----------------VGQTVKMgYFSQENEELDGRLKVIDYIRGAAEYVKTKDGS---V 396
Cdd:TIGR02769 50 KSTLARLLLGLEKPAQGTVSfrgqdlyqldrkqrraFRRDVQL-VFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESeqkA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 397 SASQMLERFLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI----QTLTILEDYLESFPGIVITVS 472
Cdd:TIGR02769 129 RIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFIT 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1524013779 473 HDRYFLDRVVRRIFAFEGNGMVTQYEGGFTDyqaaySEKHPEGILEQS 520
Cdd:TIGR02769 209 HDLRLVQSFCQRVAVMDKGQIVEECDVAQLL-----SFKHPAGRNLQS 251
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
417-473 |
1.11e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 1.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 417 EKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILE----DYLESFPGIVITVSH 473
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEktivDIKDKADKTIITIAH 1417
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
419-480 |
1.12e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.08 E-value: 1.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 419 LSGGEKRRLYLLRILMEAP--NVLLLDEPTNDLDIQTLTILedyLESFPGI------VITVSHDRYFLDR 480
Cdd:cd03238 88 LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQL---LEVIKGLidlgntVILIEHNLDVLSS 154
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
419-450 |
1.20e-04 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 43.85 E-value: 1.20e-04
10 20 30
....*....|....*....|....*....|..
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD 450
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
336-454 |
1.26e-04 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 44.08 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVGQTVKMG-------YFsqENEELDGRLKVID------YIRGaaeyVKTKDGSVSASQML 402
Cdd:COG4525 46 KTTLLNLIAGFLAPSSGEITLDGVPVTGpgadrgvVF--QKDALLPWLNVLDnvafglRLRG----VPKAERRARAEELL 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1524013779 403 ---------ERFlfpssvqyttIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD------IQTL 454
Cdd:COG4525 120 alvgladfaRRR----------IWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDaltreqMQEL 176
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
413-488 |
1.37e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 43.85 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 413 YTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESF---PGIVITVS-HDRYFLDRVVRRIFAF 488
Cdd:PRK09984 147 HQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqnDGITVVVTlHQVDYALRYCERIVAL 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
419-465 |
1.48e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 44.02 E-value: 1.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFP 465
Cdd:PRK13652 138 LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLP 184
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
418-453 |
1.62e-04 |
|
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: 44.81 E-value: 1.62e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1524013779 418 KLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT 453
Cdd:COG5265 494 KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-154 |
1.74e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 36 GINGTGKSTLLKIVAGLEEPDEGKVVKgRNLTVRFLPQNPEFYKGDTI---LTSIVREN-EGQDHVWDLESQAKTMLTKL 111
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYY-KNCNINNIAKPYCTYIGHNLglkLEMTVFENlKFWSEIYNSAETLYAAIHYF 111
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1524013779 112 GFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLD 154
Cdd:PRK13541 112 KLHDLlDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
419-486 |
1.78e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 43.88 E-value: 1.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT----LTILEDYLESFPGIVITVSHDRYFLDRVVRRIF 486
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGrdeiLNKIKELHKEYNMTIILVSHSMEDVAKLADRII 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
336-474 |
1.90e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 43.85 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITVG------QTV-----KMGY-FSQENEELDGRlKVIDYIRGAAEyvktkDGSVSASQMLE 403
Cdd:PRK13635 46 KSTLAKLLNGLLLPEAGTITVGgmvlseETVwdvrrQVGMvFQNPDNQFVGA-TVQDDVAFGLE-----NIGVPREEMVE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 404 RFlfPSSVQYTTIE--------KLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD----IQTLTILEDYLESFPGIVITV 471
Cdd:PRK13635 120 RV--DQALRQVGMEdflnrephRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSI 197
|
...
gi 1524013779 472 SHD 474
Cdd:PRK13635 198 THD 200
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
294-512 |
2.06e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 43.50 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 294 GRTTVELEGISKAY---GDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITVGQtvKMGYFSQENE 370
Cdd:PRK14246 4 GKSAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYFGKDIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 371 ELDG------------------RLKVIDY---------IRGAAEYVKTKDGSVSA----SQMLERFLFPSSvqyttieKL 419
Cdd:PRK14246 82 QIDAiklrkevgmvfqqpnpfpHLSIYDNiayplkshgIKEKREIKKIVEECLRKvglwKEVYDRLNSPAS-------QL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 420 SGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFPG--IVITVSHDRYFLDRVVRRIfAFEGNGMVTQY 497
Cdd:PRK14246 155 SGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYV-AFLYNGELVEW 233
|
250
....*....|....*...
gi 1524013779 498 EGG---FTDYQAAYSEKH 512
Cdd:PRK14246 234 GSSneiFTSPKNELTEKY 251
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
298-450 |
2.21e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 43.69 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDK-----VLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITVGQTV---KMGYFSQEN 369
Cdd:PRK13631 22 LRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYigdKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 370 EELDGRLK-------VIDYIRGAAEYVKTKD--------GSVS-------ASQMLERFLFPSSVQYTTIEK----LSGGE 423
Cdd:PRK13631 102 NPYSKKIKnfkelrrRVSMVFQFPEYQLFKDtiekdimfGPVAlgvkkseAKKLAKFYLNKMGLDDSYLERspfgLSGGQ 181
|
170 180
....*....|....*....|....*..
gi 1524013779 424 KRRLYLLRILMEAPNVLLLDEPTNDLD 450
Cdd:PRK13631 182 KRRVAIAGILAIQPEILIFDEPTAGLD 208
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-450 |
2.28e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.24 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 23 SFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGRNLTVRF----LPQ--NPEFYKGDTILTSIVRENEG--- 93
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLsfeqLQKlvSDEWQRNNTDMLSPGEDDTGrtt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 94 ----QDHVWDLESQAKtMLTKLGFTDF-DILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSF 168
Cdd:PRK10938 103 aeiiQDEVKDPARCEQ-LAQQFGITALlDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 169 NGAllmvthdRYFLDSVTNRiveldkgklFSYQTNKVNGGG--ADREST-QGcyeeylklkaerldlleaserKRQSILR 245
Cdd:PRK10938 182 HQS-------GITLVLVLNR---------FDEIPDFVQFAGvlADCTLAeTG---------------------EREEILQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 246 VELqwmqrgararsTKQKAHIERYETLRDQKGLETDQAVELDSIESRlgrttVELEGISKAYGDKVLMKDFTYILLKNDR 325
Cdd:PRK10938 225 QAL-----------VAQLAHSEQLEGVQLPEPDEPSARHALPANEPR-----IVLNNGVVSYNDRPILHNLSWQVNPGEH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 326 IGIIGPNGGGKSTLMKIIAGwvEPDEG---TITV-------GQTV-----KMGYFSQEnEELDGR-----LKVI-----D 380
Cdd:PRK10938 289 WQIVGPNGAGKSTLLSLITG--DHPQGysnDLTLfgrrrgsGETIwdikkHIGYVSSS-LHLDYRvstsvRNVIlsgffD 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 381 YIrGAAEYVKTKDgSVSASQMLERFLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD 450
Cdd:PRK10938 366 SI-GIYQAVSDRQ-QKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
419-486 |
2.32e-04 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 43.16 E-value: 2.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQ----TLTILEDYLESFPGIVItVSHDRYFLDRVVRR-IF 486
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPElrheVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRlIF 208
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
121-225 |
2.42e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.25 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 121 ETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEYLRSFNGALlmvthDRYFLdSVTNRIVELDKG-KLFS 199
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA-----DKTII-TIAHRIASIKRSdKIVV 1430
|
90 100 110
....*....|....*....|....*....|....
gi 1524013779 200 YQTNKVNGGGADRESTQ--------GCYEEYLKL 225
Cdd:PTZ00265 1431 FNNPDRTGSFVQAHGTHeellsvqdGVYKKYVKL 1464
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-197 |
2.52e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 43.29 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 34 LIGINGTGKSTLLKIVAGLEEPD-----EGKV-VKGRNL------------TVRFLPQNPEFYKGDTI---------LTS 86
Cdd:PRK14267 35 LMGPSGCGKSTLLRTFNRLLELNeearvEGEVrLFGRNIyspdvdpievrrEVGMVFQYPNPFPHLTIydnvaigvkLNG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 87 IVRENEGQDHV--WDLESQAKTMLTKLGFTDFDilvETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSSMAEWLEEY 164
Cdd:PRK14267 115 LVKSKKELDERveWALKKAALWDEVKDRLNDYP---SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEEL 191
|
170 180 190
....*....|....*....|....*....|....*
gi 1524013779 165 LRSFNG--ALLMVTHDRYFLDSVTNRIVELDKGKL 197
Cdd:PRK14267 192 LFELKKeyTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
418-462 |
2.69e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 42.98 E-value: 2.69e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1524013779 418 KLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD-IQTLTILEDYLE 462
Cdd:PRK14247 146 KLSGGQQQRLCIARALAFQPEVLLADEPTANLDpENTAKIESLFLE 191
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-182 |
2.75e-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: 42.70 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 21 DTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV--------------VKGRN-LTVRFLPQNPEFYKGdTILT 85
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeaTRSRNrYSVAYAAQKPWLLNA-TVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 86 SIVRENEGQDHVWDLESQAKTMLTKLGFTDFDILVE------TLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSS--- 156
Cdd:cd03290 98 NITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsd 177
|
170 180
....*....|....*....|....*...
gi 1524013779 157 --MAEWLEEYLRSFNGALLMVTHDRYFL 182
Cdd:cd03290 178 hlMQEGILKFLQDDKRTLVLVTHKLQYL 205
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
336-490 |
2.98e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 43.03 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTVKMgyfsqeNEELDGRLKVIDyiRGAAEYVKTKDGSV-------SASQMLERFLf 407
Cdd:PRK10619 44 KSTFLRCINFLEKPSEGSIVVnGQTINL------VRDKDGQLKVAD--KNQLRLLRTRLTMVfqhfnlwSHMTVLENVM- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 408 PSSVQYTTIEK---------------------------LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI----QTLTI 456
Cdd:PRK10619 115 EAPIQVLGLSKqeareravkylakvgideraqgkypvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPelvgEVLRI 194
|
170 180 190
....*....|....*....|....*....|....*
gi 1524013779 457 LEDYLESFPGIVItVSHDRYFLDRVVRR-IFAFEG 490
Cdd:PRK10619 195 MQQLAEEGKTMVV-VTHEMGFARHVSSHvIFLHQG 228
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
419-471 |
3.00e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 3.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFPGIVITV 471
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITL 188
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
336-479 |
3.43e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 42.74 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTItvgqtvkmgyfsQENEELDGrlkVIDYIRGAA--EYV-KTKDGSVSASQMLERF-LFPSSV 411
Cdd:cd03236 39 KSTALKILAGKLKPNLGKF------------DDPPDWDE---ILDEFRGSElqNYFtKLLEGDVKVIVKPQYVdLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 412 QYTT-----------------------------IEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI-QTLT--ILED 459
Cdd:cd03236 104 KGKVgellkkkdergkldelvdqlelrhvldrnIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkQRLNaaRLIR 183
|
170 180
....*....|....*....|
gi 1524013779 460 YLESFPGIVITVSHDRYFLD 479
Cdd:cd03236 184 ELAEDDNYVLVVEHDLAVLD 203
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
418-521 |
3.98e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 42.90 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 418 KLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD--IQTLTILE--DYLESFPGIVITVSHDRYFLDRVVRRIfAFEGNGM 493
Cdd:PRK11607 149 QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQEEAMTMAGRI-AIMNRGK 227
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1524013779 494 VTQ-------YEGGFTDYQAAY-----------SEKHPEGILEQSD 521
Cdd:PRK11607 228 FVQigepeeiYEHPTTRYSAEFigsvnvfegvlKERQEDGLVIDSP 273
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
288-450 |
4.06e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 43.01 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 288 SIESRLGRTTVELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTI------------- 354
Cdd:PRK09452 5 NKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgqdithvpae 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 355 -----------------TVGQTVKMGYFSQE--NEELDGRlkVIDYIRgaaeyvktkdgSVSASQMLERflfpssvqytT 415
Cdd:PRK09452 85 nrhvntvfqsyalfphmTVFENVAFGLRMQKtpAAEITPR--VMEALR-----------MVQLEEFAQR----------K 141
|
170 180 190
....*....|....*....|....*....|....*
gi 1524013779 416 IEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD 450
Cdd:PRK09452 142 PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
336-496 |
4.08e-04 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 42.47 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV----------KMGYFSQENEELDGrlKVIDYIRGAAEYVKTKDgSVSASQMLER 404
Cdd:cd03252 41 KSTLTKLIQRFYVPENGRVLVdGHDLaladpawlrrQVGVVLQENVLFNR--SIRDNIALADPGMSMER-VIEAAKLAGA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 405 FLFPSSVQ--YTTI--EK---LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFPG--IVITVSHdR 475
Cdd:cd03252 118 HDFISELPegYDTIvgEQgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAgrTVIIIAH-R 196
|
170 180
....*....|....*....|.
gi 1524013779 476 YFLDRVVRRIFAFEGNGMVTQ 496
Cdd:cd03252 197 LSTVKNADRIIVMEKGRIVEQ 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
362-451 |
4.21e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.07 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 362 MGYFSQENEELDG---RLKVIDYIRgaAEYVKTkdgsvsasqmlerflfPSSVQytTIEKLSGGEKRRLYLLRILMEAPN 438
Cdd:PRK10762 356 LRYFSRAGGSLKHadeQQAVSDFIR--LFNIKT----------------PSMEQ--AIGLLSGGNQQKVAIARGLMTRPK 415
|
90
....*....|...
gi 1524013779 439 VLLLDEPTNDLDI 451
Cdd:PRK10762 416 VLILDEPTRGVDV 428
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-153 |
4.28e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 20 DDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVkgrnltvrFLPQNPEFYKGDTILTS----------IVR 89
Cdd:PRK10982 15 DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIL--------FQGKEIDFKSSKEALENgismvhqelnLVL 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 90 ENEGQDHVWDLESQAKTML---------TKLGFTDFDI------LVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHL 153
Cdd:PRK10982 87 QRSVMDNMWLGRYPTKGMFvdqdkmyrdTKAIFDELDIdidpraKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
336-454 |
4.56e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 43.11 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPD---EGTITV-GQTV------KMGYFSQENEELDGRLKVIDYIRGAAEyVKTKDgSVSASQMLERF 405
Cdd:TIGR00955 64 KTTLMNALAFRSPKGvkgSGSVLLnGMPIdakemrAISAYVQQDDLFIPTLTVREHLMFQAH-LRMPR-RVTKKEKRERV 141
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 406 ------LFPSSVQYTTI------EKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD-------IQTL 454
Cdd:TIGR00955 142 devlqaLGLRKCANTRIgvpgrvKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDsfmaysvVQVL 209
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
418-473 |
5.01e-04 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 42.33 E-value: 5.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 418 KLSGGEKRRLYLLRIL-MEaPNVLLLDEPTNDLD-IQTLTIlEDYLESFPG---IVItVSH 473
Cdd:COG1117 154 GLSGGQQQRLCIARALaVE-PEVLLMDEPTSALDpISTAKI-EELILELKKdytIVI-VTH 211
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
17-64 |
5.21e-04 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 41.97 E-value: 5.21e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1524013779 17 LLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKVVKGR 64
Cdd:PRK15177 1 VVLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFIGLR 48
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
418-475 |
5.23e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 43.03 E-value: 5.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 418 KLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLEsfpgiviTVSHDR 475
Cdd:PRK13657 471 QLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALD-------ELMKGR 521
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-206 |
5.36e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 2 NLLTIEHMTKSYTERLLFDDTSFSINEGEKIGLIGINGTGKSTLLKIVAGleepdegkvvkgrnltvrflpQNPEFYKGD 81
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG---------------------DHPQGYSND 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 82 tiLTSIVRENEGQDHVWDLES-----------------------------------------QAKTM--LTKLGFTDF-- 116
Cdd:PRK10938 318 --LTLFGRRRGSGETIWDIKKhigyvssslhldyrvstsvrnvilsgffdsigiyqavsdrqQKLAQqwLDILGIDKRta 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 117 DILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLDSS----MAEWLEEYLRSFNGALLMVTH-DRYFLDSVTNRIVE 191
Cdd:PRK10938 396 DAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLnrqlVRRFVDVLISEGETQLLFVSHhAEDAPACITHRLEF 475
|
250
....*....|....*
gi 1524013779 192 LDKGKLFSYQTNKVN 206
Cdd:PRK10938 476 VPDGDIYRYVQTKLN 490
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
419-453 |
5.43e-04 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 41.69 E-value: 5.43e-04
10 20 30
....*....|....*....|....*....|....*
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT 453
Cdd:cd03248 151 LSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-154 |
5.81e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.59 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 23 SFSINEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGKV-VKGRNLTVRfLPQN---------PEFYKGDTIL-TSIVREN 91
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVyLDGKPIDIR-SPRDairagimlcPEDRKAEGIIpVHSVADN 351
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1524013779 92 EG-------------QDHVWDlESQAKTMLTKLGFT--DFDILVETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLD 154
Cdd:PRK11288 352 INisarrhhlragclINNRWE-AENADRFIRSLNIKtpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
336-457 |
6.48e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 41.37 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTI--------TVGQTVKMGYFSQE---NEELDGrLKVIDYIRGAAEYvktkdgsvSASQMler 404
Cdd:PRK13543 50 KTTLLRVLAGLLHVESGQIqidgktatRGDRSRFMAYLGHLpglKADLST-LENLHFLCGLHGR--------RAKQM--- 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 405 flfPSSV---------QYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTIL 457
Cdd:PRK13543 118 ---PGSAlaivglagyEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLV 176
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
420-485 |
6.98e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 42.26 E-value: 6.98e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 420 SGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI----QTLTILEDYLESFPGIVITVSHDRyfldRVVRRI 485
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVsvqaQVLNLMMDLQQELGLSYVFISHDL----SVVEHI 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
419-473 |
7.86e-04 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 42.40 E-value: 7.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLESFPGIVITVSH 473
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
336-482 |
7.86e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 41.60 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTIT-----VGQ-----------TVKMgYFSQENEELDGRLKVIDYIRGAAEYVKTKDGS---V 396
Cdd:PRK10419 51 KSTLARLLVGLESPSQGNVSwrgepLAKlnraqrkafrrDIQM-VFQDSISAVNPRKTVREIIREPLRHLLSLDKAerlA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 397 SASQMLERFLFPSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI----QTLTILEDYLESFPGIVITVS 472
Cdd:PRK10419 130 RASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFIT 209
|
170
....*....|....
gi 1524013779 473 HD----RYFLDRVV 482
Cdd:PRK10419 210 HDlrlvERFCQRVM 223
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
307-453 |
7.98e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 42.59 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 307 YGDKVLmKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITvgQTVKMGYFSQENEELDGRLKviDYIRGAA 386
Cdd:TIGR01271 437 YVTPVL-KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK--HSGRISFSPQTSWIMPGTIK--DNIIFGL 511
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524013779 387 EYVKTKDGSV-SASQMLERF-LFPSSVQYTTIE---KLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT 453
Cdd:TIGR01271 512 SYDEYRYTSViKACQLEEDIaLFPEKDKTVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
419-450 |
8.04e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 41.75 E-value: 8.04e-04
10 20 30
....*....|....*....|....*....|..
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD 450
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANID 181
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
398-474 |
8.76e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 42.40 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 398 ASQMLERFLFPSSVQYTTiEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT----LTILEDyLESFPGIVITVSH 473
Cdd:PRK10535 125 AQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSgeevMAILHQ-LRDRGHTVIIVTH 202
|
.
gi 1524013779 474 D 474
Cdd:PRK10535 203 D 203
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
298-357 |
8.78e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 42.35 E-value: 8.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYGDKVLMKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITVG 357
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG 71
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
120-194 |
8.93e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 120 VETLSGGQRK------RVALVSVLLSTADLLVLDEPTNHLD----SSMAEWLEEYLRSFNG--ALLMVTHDRYFLdSVTN 187
Cdd:PRK01156 799 IDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDedrrTNLKDIIEYSLKDSSDipQVIMISHHRELL-SVAD 877
|
....*..
gi 1524013779 188 RIVELDK 194
Cdd:PRK01156 878 VAYEVKK 884
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
418-496 |
8.97e-04 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 41.27 E-value: 8.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 418 KLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI----QTLTILEDYLESFPGIVItVSHDRYFLDRVVRRIFAFEGNGM 493
Cdd:PRK11264 144 RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPelvgEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRI 222
|
...
gi 1524013779 494 VTQ 496
Cdd:PRK11264 223 VEQ 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
419-450 |
1.04e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 41.30 E-value: 1.04e-03
10 20 30
....*....|....*....|....*....|..
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD 450
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
336-463 |
1.23e-03 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 40.67 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTVK----------MGYFSQENEELDGrlKVIDYIRGAAEYVKTKDGSVSASQM-LE 403
Cdd:cd03254 42 KTTLINLLMRFYDPQKGQILIdGIDIRdisrkslrsmIGVVLQDTFLFSG--TIMENIRLGRPNATDEEVIEAAKEAgAH 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 404 RFLFPSSVQYTTI-----EKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLES 463
Cdd:cd03254 120 DFIMKLPNGYDTVlgengGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEK 184
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
419-458 |
1.48e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.92 E-value: 1.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD-IQTLTILE 458
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDpISTLRIEE 192
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
298-473 |
1.60e-03 |
|
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: 40.09 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 298 VELEGISKAYG---DKVLmKDFTYILLKNDRIGIIGPNGGGKSTLMKIIAGWVEPDEGTITV-GQTVKmgyfSQENEELD 373
Cdd:cd03369 7 IEVENLSVRYApdlPPVL-KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdGIDIS----TIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 374 GRLKVIdyirgaAEYVKTKDGSVSASqmLERFLFPSSVQ-YTTI------EKLSGGEKRRLYLLRILMEAPNVLLLDEPT 446
Cdd:cd03369 82 SSLTII------PQDPTLFSGTIRSN--LDPFDEYSDEEiYGALrvseggLNLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180
....*....|....*....|....*....
gi 1524013779 447 NDLDIQT-LTILEDYLESFPGI-VITVSH 473
Cdd:cd03369 154 ASIDYATdALIQKTIREEFTNStILTIAH 182
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
389-453 |
1.62e-03 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 40.57 E-value: 1.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524013779 389 VKTKDGSVSASQMLERFLFPSSVQYTTIEkLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT 453
Cdd:PRK11629 117 KKPAEINSRALEMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
336-453 |
1.70e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 40.33 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVE--PDEGTITVGQtvkmGYFSQENEELDGRLKVIDYirGAAEYVKTKDGSVSASQMLERFlfpssvqy 413
Cdd:COG2401 69 KSTLLRLLAGALKgtPVAGCVDVPD----NQFGREASLIDAIGRKGDF--KDAVELLNAVGLSDAVLWLRRF-------- 134
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1524013779 414 ttiEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQT 453
Cdd:COG2401 135 ---KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
419-474 |
1.77e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 40.83 E-value: 1.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD----IQTLTILEDYLESfpGIVITVS-HD 474
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmgaSQIMKLLYDLNKE--GITIIIStHD 196
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
419-450 |
1.97e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 40.78 E-value: 1.97e-03
10 20 30
....*....|....*....|....*....|..
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD 450
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
416-450 |
2.23e-03 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 40.47 E-value: 2.23e-03
10 20 30
....*....|....*....|....*....|....*
gi 1524013779 416 IEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD 450
Cdd:PRK11432 134 VDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
418-490 |
2.29e-03 |
|
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: 39.48 E-value: 2.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1524013779 418 KLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI-QTLT---ILEDYLESFPGIVITVSHDRYFLDRVVRRIFAFEG 490
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeQRLNaarAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
336-356 |
2.41e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 40.06 E-value: 2.41e-03
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
415-451 |
2.45e-03 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 40.35 E-value: 2.45e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1524013779 415 TIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI 451
Cdd:PRK10253 140 SVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
296-450 |
2.66e-03 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 40.44 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 296 TTVELEGISKAYGDKVLMKDFT--------YILL------KndrigiigpngggkSTLMKIIAGWVEPDEGTITVGQTV- 360
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDldiedgefLVLLgpsgcgK--------------STLLRMIAGLEDPTSGEILIGGRDv 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 361 --------KMGYFSQ-----------EN------------EELDGRlkvidyIRGAAEyvktkdgSVSASQMLERflFPS 409
Cdd:COG3839 68 tdlppkdrNIAMVFQsyalyphmtvyENiafplklrkvpkAEIDRR------VREAAE-------LLGLEDLLDR--KPK 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1524013779 410 svqyttieKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD 450
Cdd:COG3839 133 --------QLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
420-474 |
3.34e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 40.09 E-value: 3.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1524013779 420 SGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI----QTLTILEDYLESFPGIVITVSHD 474
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvqaQIMTLLNELKREFNTAIIMITHD 221
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
419-473 |
3.47e-03 |
|
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: 39.40 E-value: 3.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTLTILEDYLES-FPG-IVITVSH 473
Cdd:cd03244 140 LSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREaFKDcTVLTIAH 196
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
416-451 |
3.60e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.30 E-value: 3.60e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1524013779 416 IEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI 451
Cdd:PRK13549 403 IARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
336-446 |
3.84e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.49 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 336 KSTLMKIIAGWVEPDEGTITV-GQTV---------KMGYFSQ-----------ENEELDGRLKVIDYIRgAAEYVKtkdg 394
Cdd:NF033858 305 KSTTMKMLTGLLPASEGEAWLfGQPVdagdiatrrRVGYMSQafslygeltvrQNLELHARLFHLPAAE-IAARVA---- 379
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1524013779 395 svsasQMLERF-LfpSSVQYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPT 446
Cdd:NF033858 380 -----EMLERFdL--ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
419-474 |
4.14e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 39.40 E-value: 4.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD----IQTLTILEDYLESFPGIVITVSHD 474
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDpagkEQILKLIRKLKKKNNLTVISITHD 203
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
418-483 |
4.92e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 39.22 E-value: 4.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1524013779 418 KLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQTltiLEDYLESFPGI-------VITVSHDryfLDRVVR 483
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG---EEDFINLFERLnkeykkrIIMVTHN---MDQVLR 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
412-451 |
5.71e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 5.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1524013779 412 QYTTIEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDI 451
Cdd:PRK10982 385 HRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV 424
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
26-154 |
6.09e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 38.74 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524013779 26 INEGEKIGLIGINGTGKSTLLKIVAGLEEPDEGK-VVKGRNL------TVR----FLPQNPEFYKGDTILTSIVRENEGQ 94
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKiVIDGIDIsklplhTLRsrlsIILQDPILFSGSIRFNLDPECKCTD 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524013779 95 DHVWD-LE-SQAKTMLTKLGfTDFDILV----ETLSGGQRKRVALVSVLLSTADLLVLDEPTNHLD 154
Cdd:cd03288 124 DRLWEaLEiAQLKNMVKSLP-GGLDAVVteggENFSVGQRQLFCLARAFVRKSSILIMDEATASID 188
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
419-452 |
6.14e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 39.44 E-value: 6.14e-03
10 20 30
....*....|....*....|....*....|....
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLDIQ 452
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
419-450 |
6.89e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 38.96 E-value: 6.89e-03
10 20 30
....*....|....*....|....*....|..
gi 1524013779 419 LSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD 450
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
416-450 |
7.10e-03 |
|
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: 38.40 E-value: 7.10e-03
10 20 30
....*....|....*....|....*....|....*
gi 1524013779 416 IEKLSGGEKRRLYLLRILMEAPNVLLLDEPTNDLD 450
Cdd:cd03233 116 VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| |
