|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
190-742 |
0e+00 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 562.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 190 GSSAGKSKDIHIDTFDLYVGdGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELN-VPKHVSILHVEQELRGD 268
Cdd:PLN03073 169 NGGGPAIKDIHMENFSISVG-GRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIDgIPKNCQILHVEQEVVGD 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 269 DTKALQSVLDADVWRKQLLSEEAKINERLKEMDVlRQEFEEDSLEVKKLDNErEDLDNHLIQISDKLVDMESDKAEARAA 348
Cdd:PLN03073 248 DTTALQCVLNTDIERTQLLEEEAQLVAQQRELEF-ETETGKGKGANKDGVDK-DAVSQRLEEIYKRLELIDAYTAEARAA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 349 SILYGLGFSTEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVSHDRAFLN 428
Cdd:PLN03073 326 SILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLN 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 429 EVATDIIYQHNERLDYYRGqDFDTFYTTKEERRKNAQREYDNQMVYRKHLQEFIDKYRYNAAKSQEAQSRIKKLEKLPVL 508
Cdd:PLN03073 406 TVVTDILHLHGQKLVTYKG-DYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLGHV 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 509 EPPEQDKTIDFKFPEC-DKLSPPIIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKG 587
Cdd:PLN03073 485 DAVVNDPDYKFEFPTPdDRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 588 FVSRNPRLRIGYFTQHHVDSMDLTTSAVDWMSKSFPGKTDEEYRRHLGSFGITGTLGLQKMQLLSGGQKSRVAFAALCLN 667
Cdd:PLN03073 565 TVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFK 644
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 668 NPHILVLDEPSNHLDTTGLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVKRFEGTIYDYRDyILQS 742
Cdd:PLN03073 645 KPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKK-TLQS 718
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
211-738 |
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: 529.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 211 GQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRR------ELNVPKHVSILHVEQELRGDDTK-ALQSVLDADVWR 283
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGElepdsgEVSIPKGLRIGYLPQEPPLDDDLtVLDTVLDGDAEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 284 KQLLSEEAKINERLKEMDvlrqefeedslevkkldnerEDLDnHLIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQ 363
Cdd:COG0488 90 RALEAELEELEAKLAEPD--------------------EDLE-RLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 364 PTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVSHDRAFLNEVATDIIYQHNERLD 443
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 444 YYRGqDFDTFYTTKEERRKNAQREYDNQMVYRKHLQEFIDKYRYNAAKSQEAQSRIKKLEKLPVLEPPEQDKTIDFKFPE 523
Cdd:COG0488 229 LYPG-NYSAYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDKTVEIRFPP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 524 CDKLSPPIIQLQDVSFGYDEnNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRLRIGYFTQH 603
Cdd:COG0488 308 PERLGKKVLELEGLSKSYGD-KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQH 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 604 HvDSMDLTTSAVDWMSKSFPGKTDEEYRRHLGSFGITGTLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDT 683
Cdd:COG0488 387 Q-EELDPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 684 TGLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVKRFEGTIYDYRDY 738
Cdd:COG0488 466 ETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
214-740 |
2.23e-109 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 346.39 E-value: 2.23e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 214 ILSNAQLTLSFGHRYGLVGQNGIGKSTLLrALSRREL-------NVPKHVSILHVEQELRGDDTKALQSVLDADVWRKQL 286
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLL-ALLKNEIsadggsyTFPGNWQLAWVNQETPALPQPALEYVIDGDREYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 287 LSEEAKINERlkemdvlrqefeedslevkkldNeredlDNHLI-QISDKLVDMESDKAEARAASILYGLGFSTEAQQQPT 365
Cdd:PRK10636 95 EAQLHDANER----------------------N-----DGHAIaTIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 366 NSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVSHDRAFLNEVATDIIYQHNERLDYY 445
Cdd:PRK10636 148 SDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 446 RGqDFDTFYTTKEERRKNAQREYDNQMVYRKHLQEFIDKYRYNAAKSQEAQSRIKKLEKLPVLEPPEQDKTIDFKFPECD 525
Cdd:PRK10636 228 TG-NYSSFEVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFHFSFRAPE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 526 KLSPPIIQLQDVSFGYDENnLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRLRIGYFTQHHV 605
Cdd:PRK10636 307 SLPNPLLKMEKVSAGYGDR-IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 606 DSMDLTTSAVDWMSKSFPGKTDEEYRRHLGSFGITGTLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTG 685
Cdd:PRK10636 386 EFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 686 LDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVKRFEGTIYDYRDYIL 740
Cdd:PRK10636 466 RQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLS 520
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
214-735 |
1.13e-78 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 262.14 E-value: 1.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 214 ILSNAQLTLSFG---------------HRYGLVGQNGIGKSTLLRALSRrELnVPK--HVSILHVEQ--ELRGD-----D 269
Cdd:PRK15064 1 MLSTANITMQFGakplfenisvkfgggNRYGLIGANGCGKSTFMKILGG-DL-EPSagNVSLDPNERlgKLRQDqfafeE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 270 TKALQSVL--DADVWrkqllseEAKiNER-----LKEMDvlrqefEEDSLEVKKLDNEREDLDNHliqisdklvdmesdK 342
Cdd:PRK15064 79 FTVLDTVImgHTELW-------EVK-QERdriyaLPEMS------EEDGMKVADLEVKFAEMDGY--------------T 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 343 AEARAASILYGLGFSTEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVSH 422
Cdd:PRK15064 131 AEARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISH 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 423 DRAFLNEVATdiiyqHNERLDY-----YRGqDFDTFYTTKEERRK-----NAQREydNQMvyrKHLQEFIDKYRYNAAKS 492
Cdd:PRK15064 211 DRHFLNSVCT-----HMADLDYgelrvYPG-NYDEYMTAATQARErlladNAKKK--AQI---AELQSFVSRFSANASKA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 493 QEAQSRIKKLEKLPVLE---PPEQDKTIDFKFPEcdKLSPPIIQLQDVSFGYDeNNLLLKDVNLDVQMDSRIALVGANGC 569
Cdd:PRK15064 280 KQATSRAKQIDKIKLEEvkpSSRQNPFIRFEQDK--KLHRNALEVENLTKGFD-NGPLFKNLNLLLEAGERLAIIGENGV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 570 GKTTLLKIMMEQLRPLKGFVSRNPRLRIGYFTQHHVDSMDLTTSAVDWMSKSFPGKTDEEYRRhlgsfgitGTLG----- 644
Cdd:PRK15064 357 GKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDLTLFDWMSQWRQEGDDEQAVR--------GTLGrllfs 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 645 ----LQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGGVLMVSHDISVIDSVCKEIW-V 719
Cdd:PRK15064 429 qddiKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIeI 508
|
570
....*....|....*.
gi 14318531 720 SEQGTVKrFEGTIYDY 735
Cdd:PRK15064 509 TPDGVVD-FSGTYEEY 523
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
214-734 |
4.75e-67 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 233.69 E-value: 4.75e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 214 ILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRR------ELNVPKHVSILHVEQelrgDDTKALQ-SVLDadvwrkqL 286
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEvllddgRIIYEQDLIVARLQQ----DPPRNVEgTVYD-------F 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 287 LSEE-AKINERLKEMDVLRQEFEEDSLE--VKKLDNEREDLDNH-LIQIsdklvdmesdkaEARAASILYGLGFSTEAqq 362
Cdd:PRK11147 87 VAEGiEEQAEYLKRYHDISHLVETDPSEknLNELAKLQEQLDHHnLWQL------------ENRINEVLAQLGLDPDA-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 363 qPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVSHDRAFLNEVATDIIyqhnerl 442
Cdd:PRK11147 153 -ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIV------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 443 DYYRGQ------DFDTFYTTKE-----ERRKNAqrEYDnqmvyRKHLQEFIDKYRYNAAKSQEAQSRIKKLEKLPV--LE 509
Cdd:PRK11147 225 DLDRGKlvsypgNYDQYLLEKEealrvEELQNA--EFD-----RKLAQEEVWIRQGIKARRTRNEGRVRALKALRRerSE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 510 PPEQDKTIDFKFPECDKLSPPIIQLQDVSFGYDENNlLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV 589
Cdd:PRK11147 298 RREVMGTAKMQVEEASRSGKIVFEMENVNYQIDGKQ-LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 590 SRNPRLRIGYFTQHHVDsMDLTTSAVDWMSKsfpGKTDEEY---RRH----LGSFGITGTLGLQKMQLLSGGQKSRVAFA 662
Cdd:PRK11147 377 HCGTKLEVAYFDQHRAE-LDPEKTVMDNLAE---GKQEVMVngrPRHvlgyLQDFLFHPKRAMTPVKALSGGERNRLLLA 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 663 ALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSE-QGTVKRFEGTIYD 734
Cdd:PRK11147 453 RLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEgNGKIGRYVGGYHD 525
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
208-738 |
3.00e-63 |
|
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: 220.96 E-value: 3.00e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 208 VGDGQRILSNaqLTLSF--GHRYGLVGQNGIGKSTLLRAL------SRRELNVPKHVSILHVEQELRGDDTKALQSVLDA 279
Cdd:TIGR03719 14 VPPKKEILKD--ISLSFfpGAKIGVLGLNGAGKSTLLRIMagvdkdFNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 280 DVwrkqllseeAKINERLKEMDVLRQEFEEDSLEVKKLDNEREDLDNhLIQISDkLVDMESdKAEaRAASILyglgfSTE 359
Cdd:TIGR03719 92 GV---------AEIKDALDRFNEISAKYAEPDADFDKLAAEQAELQE-IIDAAD-AWDLDS-QLE-IAMDAL-----RCP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 360 AQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVSHDRAFLNEVATDIIyqhn 439
Cdd:TIGR03719 154 PWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWIL---- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 440 eRLDYYRGQDFDTFYTT----KEERRKNAQREYDNQmvyRKHLQEFIDKYRYNaAKSQEAQS--RIKKLEKLPVLEPPEQ 513
Cdd:TIGR03719 230 -ELDRGRGIPWEGNYSSwleqKQKRLEQEEKEESAR---QKTLKRELEWVRQS-PKGRQAKSkaRLARYEELLSQEFQKR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 514 DKTIDFKFPECDKLSPPIIQLQDVSFGYDEnNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNP 593
Cdd:TIGR03719 305 NETAEIYIPPGPRLGDKVIEAENLTKAFGD-KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 594 RLRIGYFTQHHvDSMDLTTSAVDWMSKSFP----GKTDEEYRRHLGSFGITGTLGLQKMQLLSGGQKSRVAFAALCLNNP 669
Cdd:TIGR03719 384 TVKLAYVDQSR-DALDPNKTVWEEISGGLDiiklGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGG 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 670 HILVLDEPSNHLDTTGLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSE-QGTVKRFEGTIYDYRDY 738
Cdd:TIGR03719 463 NVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEYEED 532
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
532-724 |
1.64e-54 |
|
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: 184.19 E-value: 1.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYdENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRLRIGYFTQhhvdsmdlt 611
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 612 tsavdwmsksfpgktdeeyrrhlgsfgitgtlglqkmqlLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVE 691
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|...
gi 14318531 692 ALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGT 724
Cdd:cd03221 112 ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
208-738 |
2.53e-49 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 182.24 E-value: 2.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 208 VGDGQRILSNaqLTLSF--GHRYGLVGQNGIGKSTLLRAL------SRRELNVPKHVSILHVEQELRGDDTK-ALQSVLD 278
Cdd:PRK11819 16 VPPKKQILKD--ISLSFfpGAKIGVLGLNGAGKSTLLRIMagvdkeFEGEARPAPGIKVGYLPQEPQLDPEKtVRENVEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 279 ADVWRKQLLSEEAKINERLKEMDVlrqEFEEDSLEVKKLDNERE-----DLDNHLIQISDKLVDMESDkaearaasilyg 353
Cdd:PRK11819 94 GVAEVKAALDRFNEIYAAYAEPDA---DFDALAAEQGELQEIIDaadawDLDSQLEIAMDALRCPPWD------------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 354 lgfsteaqqQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVSHDRAFLNEVATD 433
Cdd:PRK11819 159 ---------AKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGW 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 434 IIyqhneRLDYYRGQDFDTFYTT----KEERRKNAQREYDNQmvyRKHLQEFIDKYRYNA----AKSqeaQSRIKKLEKL 505
Cdd:PRK11819 230 IL-----ELDRGRGIPWEGNYSSwleqKAKRLAQEEKQEAAR---QKALKRELEWVRQSPkarqAKS---KARLARYEEL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 506 PVLEPPEQDKTIDFKFPECDKLSPPIIQLQDVSFGYDEnNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPL 585
Cdd:PRK11819 299 LSEEYQKRNETNEIFIPPGPRLGDKVIEAENLSKSFGD-RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 586 KGFVSRNPRLRIGYFTQHHvDSMDLTTSAVDWMSKSFP----GKTDEEYRRHLGSFGITGTLGLQKMQLLSGGQKSRVAF 661
Cdd:PRK11819 378 SGTIKIGETVKLAYVDQSR-DALDPNKTVWEEISGGLDiikvGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHL 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 662 AALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSE-QGTVKRFEGtiyDYRDY 738
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEgDSQVEWFEG---NFQEY 531
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
207-725 |
1.07e-40 |
|
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: 156.60 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 207 YVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRelnVPKHVSIlHVEQELRGDDTKALqsvldadvwrkql 286
Cdd:COG1123 14 YPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL---LPHGGRI-SGEVLLDGRDLLEL------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 287 lseeaKINERLKEMDVLRQEFEEDSLEVKKLDNEREDLDNHliqisdklvDMESDKAEARAASILYGLGFSTEAQQQPtN 366
Cdd:COG1123 77 -----SEALRGRRIGMVFQDPMTQLNPVTVGDQIAEALENL---------GLSRAEARARVLELLEAVGLERRLDRYP-H 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 367 SFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLK----TYPNTVLTVSHDRAFLNEVATDIIYQHNERL 442
Cdd:COG1123 142 QLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRelqrERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 443 dyyrgqdfdtfyttkeerrknaqreydnqmvyrkhlQEfidkyrynAAKSQEAQSRIKKLEKLPVLEPPEQDKtidfkfP 522
Cdd:COG1123 222 ------------------------------------VE--------DGPPEEILAAPQALAAVPRLGAARGRA------A 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 523 ECDKLSPPIIQLQDVSFGYDENN----LLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMM--------------EQLRP 584
Cdd:COG1123 252 PAAAAAEPLLEVRNLSKRYPVRGkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLgllrptsgsilfdgKDLTK 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 585 LKGFVSRNPRLRIGYFTQHHVDSMDLTTSAVDWMS---KSFPGKTDEEYRRH----LGSFGitgtLGLQKMQL----LSG 653
Cdd:COG1123 332 LSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAeplRLHGLLSRAERRERvaelLERVG----LPPDLADRypheLSG 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 654 GQKSRVAFA-ALCLNnPHILVLDEPsnhldTTGLDALVEA-----LKN----FNGGVLMVSHDISVIDSVCKEIWVSEQG 723
Cdd:COG1123 408 GQRQRVAIArALALE-PKLLILDEP-----TSALDVSVQAqilnlLRDlqreLGLTYLFISHDLAVVRYIADRVAVMYDG 481
|
..
gi 14318531 724 TV 725
Cdd:COG1123 482 RI 483
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
199-441 |
1.05e-37 |
|
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: 137.58 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 199 IHIDTFDLYVGDGQrILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRR------ELNVPKHVSILHVEQelrgddtka 272
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGElepdegIVTWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 273 lqsvldadvwrkqllseeakinerlkemdvlrqefeedslevkkldneredldnhliqisdklvdmesdkaearaasily 352
Cdd:cd03221 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 353 glgfsteaqqqptnsFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVSHDRAFLNEVAT 432
Cdd:cd03221 71 ---------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVAT 135
|
....*....
gi 14318531 433 DIIYQHNER 441
Cdd:cd03221 136 KIIELEDGK 144
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
528-717 |
1.54e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.53 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 528 SPPIIQLQDVSFGYDeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS------RNPRLRIGYFT 601
Cdd:COG1121 3 MMPAIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 602 QHHvdsmdlttsAVDWmskSFP---------GktdeeYRRHLGSFGI---------------TGTLGLQKMQL--LSGGQ 655
Cdd:COG1121 82 QRA---------EVDW---DFPitvrdvvlmG-----RYGRRGLFRRpsradreavdealerVGLEDLADRPIgeLSGGQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 656 KSRVAFA-ALClNNPHILVLDEPSNHLDTTGLDALVEALKNFNG---GVLMVSHDISVIDSVCKEI 717
Cdd:COG1121 145 QQRVLLArALA-QDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRV 209
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
140-451 |
5.12e-35 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 140.20 E-value: 5.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 140 KKLAKAEQKIAKKVAK----RNNKFVKYEASKLINDQKEEDYDSFFLQINPlefGSSAGKskDIhIDTFDLYVG-DGQRI 214
Cdd:COG0488 257 KKIAKEEEFIRRFRAKarkaKQAQSRIKALEKLEREEPPRRDKTVEIRFPP---PERLGK--KV-LELEGLSKSyGDKTL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 215 LSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRElnvpkhvsilhveqelrgddtkalqsvldadvwrkQLLSEEAKIN 294
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGEL-----------------------------------EPDSGTVKLG 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 295 ERLKeMDVLRQEFEEdslevkkLDNEREDLDnHLIQISDklvdmesDKAEARAASILYGLGFSTEAQQQPTNSFSGGWRM 374
Cdd:COG0488 376 ETVK-IGYFDQHQEE-------LDPDKTVLD-ELRDGAP-------GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKA 439
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 375 RLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVSHDRAFLNEVATDIIYQHNERLDYYRGqDFD 451
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPG-GYD 515
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
533-708 |
1.98e-30 |
|
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: 119.18 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 533 QLQDVSFGYDeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNP------RLRIGYFTQHH-- 604
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekeRKRIGYVPQRRsi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 605 -----VDSMDLTTSAVDWMSKSFPGKTDEEYRRHLGSFGITGTLGLQKMQL--LSGGQKSRVAFAALCLNNPHILVLDEP 677
Cdd:cd03235 80 drdfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIgeLSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190
....*....|....*....|....*....|....
gi 14318531 678 SNHLDTTGLDALVEALKNFNG---GVLMVSHDIS 708
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRRegmTILVVTHDLG 193
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
532-731 |
6.49e-30 |
|
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: 118.20 E-value: 6.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVsrnprlrigyftqhHVDSMDLT 611
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEV--------------LVDGKDIT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 612 TSAVDWMSKS------FP--------------------GKTDEEYRRH----LGSFGITGtLGLQKMQLLSGGQKSRVAF 661
Cdd:COG1122 67 KKNLRELRRKvglvfqNPddqlfaptveedvafgpenlGLPREEIRERveeaLELVGLEH-LADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 662 AALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNG---GVLMVSHDISVIDSVCKEIWVSEQGTVkRFEGT 731
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRI-VADGT 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
531-725 |
8.96e-30 |
|
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: 118.61 E-value: 8.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENNLLlKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV--------SRNPR---LRIGY 599
Cdd:COG1120 1 MLEAENLSVGYGGRPVL-DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaSLSRRelaRRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 600 FTQHHVDSMDLT---------TSAVDWMSKsfPGKTDEEY-RRHLGSFGITGtLGLQKMQLLSGGQKSRVAFA-ALClNN 668
Cdd:COG1120 80 VPQEPPAPFGLTvrelvalgrYPHLGLFGR--PSAEDREAvEEALERTGLEH-LADRPVDELSGGERQRVLIArALA-QE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 669 PHILVLDEPSNHLD---TTGLDALVEALKNFNG-GVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:COG1120 156 PPLLLLDEPTSHLDlahQLEVLELLRRLARERGrTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
489-725 |
8.05e-29 |
|
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: 121.79 E-value: 8.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 489 AAKSQEAQSRIKKLEKLPVLEPPEQDKTIDFKfpecdklSPPIIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANG 568
Cdd:COG4988 301 RANGIAAAEKIFALLDAPEPAAPAGTAPLPAA-------GPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 569 CGKTTLLKIMMEQLRPLKGfvsrnpRLRIGyftQHHVDSMDLTT--SAVDWMSKS---FPG------------KTDEEYR 631
Cdd:COG4988 374 AGKSTLLNLLLGFLPPYSG------SILIN---GVDLSDLDPASwrRQIAWVPQNpylFAGtirenlrlgrpdASDEELE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 632 R-----HLGSFGITGTLGLQKM-----QLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGG-- 699
Cdd:COG4988 445 AaleaaGLDEFVAALPDGLDTPlgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGrt 524
|
250 260
....*....|....*....|....*.
gi 14318531 700 VLMVSHDISVIDSvCKEIWVSEQGTV 725
Cdd:COG4988 525 VILITHRLALLAQ-ADRILVLDDGRI 549
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
532-723 |
1.26e-28 |
|
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: 112.48 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGY-DENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGfvsrnpRLRIGyftQHHVDSMDL 610
Cdd:cd03228 1 IEFKNVSFSYpGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSG------EILID---GVDLRDLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 611 ttsavdwmsksfpgktdEEYRRHLGsfgitgtLGLQKMQL---------LSGGQKSRVAFA-ALcLNNPHILVLDEPSNH 680
Cdd:cd03228 72 -----------------ESLRKNIA-------YVPQDPFLfsgtireniLSGGQRQRIAIArAL-LRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 14318531 681 LDTTGLDALVEALKNFNGG--VLMVSHDISVIDSvCKEIWVSEQG 723
Cdd:cd03228 127 LDPETEALILEALRALAKGktVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
532-725 |
1.87e-28 |
|
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: 112.11 E-value: 1.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSrnprlrigyftqhhVDSMDlt 611
Cdd:cd03230 1 IEVRNLSKRYG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK--------------VLGKD-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 612 tsavdwmsksfPGKTDEEYRRHLG----SFGITGTLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPsnhldTTGLD 687
Cdd:cd03230 64 -----------IKKEPEEVKRRIGylpeEPSLYENLTVRENLKLSGGMKQRLALAQALLHDPELLILDEP-----TSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14318531 688 A--------LVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:cd03230 128 PesrrefweLLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
493-725 |
3.29e-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: 121.09 E-value: 3.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 493 QEAQSRIKKLEKLpVLEPPEQDKtiDFKFPECDKLSPPIiQLQDVSFGYDENN-LLLKDVNLDVQMDSRIALVGANGCGK 571
Cdd:COG2274 439 QDAKIALERLDDI-LDLPPEREE--GRSKLSLPRLKGDI-ELENVSFRYPGDSpPVLDNISLTIKPGERVAIVGRSGSGK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 572 TTLLKIMMEQLRPLKGFV--------SRNPR-LR--IGYFTQH------------HVDSMDLTTSAVDWMSK-------- 620
Cdd:COG2274 515 STLLKLLLGLYEPTSGRIlidgidlrQIDPAsLRrqIGVVLQDvflfsgtireniTLGDPDATDEEIIEAARlaglhdfi 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 621 -SFPGKtdeeYRRHLGSFGITgtlglqkmqlLSGGQKSRVAFA-ALcLNNPHILVLDEPSNHLDTTGLDALVEALKNFNG 698
Cdd:COG2274 595 eALPMG----YDTVVGEGGSN----------LSGGQRQRLAIArAL-LRNPRILILDEATSALDAETEAIILENLRRLLK 659
|
250 260
....*....|....*....|....*....
gi 14318531 699 G--VLMVSHDISVIDSvCKEIWVSEQGTV 725
Cdd:COG2274 660 GrtVIIIAHRLSTIRL-ADRIIVLDKGRI 687
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
530-721 |
7.13e-28 |
|
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: 111.42 E-value: 7.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 530 PIIQLQDVSFGYDENnLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRN----------PRLRIGY 599
Cdd:COG4133 1 MMLEAENLSCRRGER-LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgepirdaredYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 600 FTqhHVDSMDLTTSA---VDWMSKSFPGKTDEEY-RRHLGSFGITGtLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLD 675
Cdd:COG4133 80 LG--HADGLKPELTVrenLRFWAALYGLRADREAiDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14318531 676 EPSNHLDTTGLDALVEALKNF--NGG-VLMVSHDISVIDSvCKEIWVSE 721
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHlaRGGaVLLTTHQPLELAA-ARVLDLGD 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
533-724 |
2.65e-27 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 110.25 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 533 QLQDVSFGY-DENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNP-----------RLRIGYF 600
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 601 TQHhVDSMDLTTSAVDWMS---KSFPGKTDEEYRRHLGSFGITGTLGLQK--MQLLSGGQKSRVAFAALCLNNPHILVLD 675
Cdd:cd03225 81 FQN-PDDQFFGPTVEEEVAfglENLGLPEEEIEERVEEALELVGLEGLRDrsPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 14318531 676 EPSNHLDTTGLDALVEALKNFNG---GVLMVSHDISVIDSVCKEIWVSEQGT 724
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
532-725 |
5.93e-27 |
|
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: 107.69 E-value: 5.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGY-DENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGfvsrnpRLRIgyftqhhvDSMDL 610
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSG------RVRL--------DGADI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 611 TTsaVDWmsksfpgktdEEYRRHLGSFgitgtlgLQKMQL---------LSGGQKSRVAFAALCLNNPHILVLDEPSNHL 681
Cdd:cd03246 67 SQ--WDP----------NELGDHVGYL-------PQDDELfsgsiaeniLSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 14318531 682 DTTGLDALVEALKNFNGG---VLMVSHDISVIDSVCKeIWVSEQGTV 725
Cdd:cd03246 128 DVEGERALNQAIAALKAAgatRIVIAHRPETLASADR-ILVLEDGRV 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
533-725 |
1.05e-26 |
|
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: 107.52 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 533 QLQDVSFGYDeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVsrnprlrigyftqhHVDSMDLtt 612
Cdd:cd03214 1 EVENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI--------------LLDGKDL-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 613 savdwmsKSFPGKtdeEYRRHLG-------SFGITGtLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTG 685
Cdd:cd03214 64 -------ASLSPK---ELARKIAyvpqaleLLGLAH-LADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 14318531 686 LDALVEALKNF----NGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:cd03214 133 QIELLELLRRLarerGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
533-724 |
1.60e-26 |
|
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: 106.18 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 533 QLQDVSFGYDENnLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVsrnprlrigyftqhHVDSMDLTT 612
Cdd:cd00267 1 EIENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI--------------LIDGKDIAK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 613 savdwmsksfpgKTDEEYRRHLGSFgitgtlglqkMQLlSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEA 692
Cdd:cd00267 66 ------------LPLEELRRRIGYV----------PQL-SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|....*
gi 14318531 693 LKNFNGG---VLMVSHDISVIDSVCKEIWVSEQGT 724
Cdd:cd00267 123 LRELAEEgrtVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
532-740 |
2.67e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 107.84 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV----------SRNPRLRIGYFT 601
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedvardPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 602 QHHVDSMDLT-TSAVDWMSKSFpGKTDEEYRRH----LGSFGITGTLGlQKMQLLSGGQKSRVAFA-ALcLNNPHILVLD 675
Cdd:COG1131 80 QEPALYPDLTvRENLRFFARLY-GLPRKEARERidelLELFGLTDAAD-RKVGTLSGGMKQRLGLAlAL-LHDPELLILD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 676 EPsnhldTTGLD--------ALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVkRFEGTIYDYRDYIL 740
Cdd:COG1131 157 EP-----TSGLDpearrelwELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI-VADGTPDELKARLL 223
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
210-442 |
3.94e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.82 E-value: 3.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDtkalQSVLDADVWRKQLLse 289
Cdd:COG4619 11 GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALAD--LDPPTSGEIY-----LDGKP----LSAMPPPEWRRQVA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 290 eakinerlkemdVLRQE--FEEDSLEvkklDNEREDLdnhliQISDKLVDMEsdkaeaRAASILYGLGFSTEAQQQPTNS 367
Cdd:COG4619 78 ------------YVPQEpaLWGGTVR----DNLPFPF-----QLRERKFDRE------RALELLERLGLPPDILDKPVER 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 368 FSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS----IAYLAEYLKTYPNTVLTVSHDRAFLNEVATDIIYQHNERL 442
Cdd:COG4619 131 LSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
438-521 |
7.26e-26 |
|
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: 101.50 E-value: 7.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 438 HNERLDYYRGqDFDTFYTTKEERRKNAQREYDNQMVYRKHLQEFIDKYRYNAAKSQEAQSRIKKLEKLPVLEPPEQDKtI 517
Cdd:pfam12848 4 ERGKLTTYKG-NYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEKPERDK-P 81
|
....
gi 14318531 518 DFKF 521
Cdd:pfam12848 82 KLRF 85
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
530-706 |
3.04e-25 |
|
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: 110.53 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 530 PIIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRN-----------PRLRIG 598
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDgvpvssldqdeVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 599 YFTQH-HVdsmdLTTSAVDWMSKSFPGKTDEEYRRHLGSFGITGTL-----GLQKM-----QLLSGGQKSRVAFAALCLN 667
Cdd:TIGR02868 413 VCAQDaHL----FDTTVRENLRLARPDATDEELWAALERVGLADWLralpdGLDTVlgeggARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 14318531 668 NPHILVLDEPSNHLDTTGLDALVEALKNFNGG--VLMVSHD 706
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAALSGrtVVLITHH 529
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
532-744 |
3.61e-25 |
|
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: 104.51 E-value: 3.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLlKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS--------------RNPRLRI 597
Cdd:cd03261 1 IELRGLTKSFGGRTVL-KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgedisglseaelYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 598 GYFTQHHV--DSMdlttSAVDWMskSFP-----GKTDEEYRR----HLGSFGITGTLGLQKMQlLSGGQKSRVAFA-ALC 665
Cdd:cd03261 80 GMLFQSGAlfDSL----TVFENV--AFPlrehtRLSEEEIREivleKLEAVGLRGAEDLYPAE-LSGGMKKRVALArALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 666 LnNPHILVLDEPSNHLD---TTGLDALVEALKN-FNGGVLMVSHDISVIDSVCKEIWVSEQGTVkRFEGTIydyrDYILQ 741
Cdd:cd03261 153 L-DPELLLYDEPTAGLDpiaSGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKI-VAEGTP----EELRA 226
|
...
gi 14318531 742 SAD 744
Cdd:cd03261 227 SDD 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
528-744 |
4.81e-25 |
|
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: 104.29 E-value: 4.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 528 SPPIIQLQDVSFGYDENnLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS--------------RNP 593
Cdd:COG1127 2 SEPMIEVRNLTKSFGDR-VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvdgqditglsekelYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 594 RLRIGYFTQHhvdsmdlttSAV-DWMS---------KSFPGKTDEEYRRH----LGSFGITGTlgLQKM--QlLSGGQKS 657
Cdd:COG1127 81 RRRIGMLFQG---------GALfDSLTvfenvafplREHTDLSEAEIRELvlekLELVGLPGA--ADKMpsE-LSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 658 RVAFA-ALCLnNPHILVLDEPsnhldTTGLD----ALVEAL-----KNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVkR 727
Cdd:COG1127 149 RVALArALAL-DPEILLYDEP-----TAGLDpitsAVIDELirelrDELGLTSVVVTHDLDSAFAIADRVAVLADGKI-I 221
|
250
....*....|....*..
gi 14318531 728 FEGTiydyRDYILQSAD 744
Cdd:COG1127 222 AEGT----PEELLASDD 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
531-727 |
5.85e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 103.59 E-value: 5.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV----------SRN--PRLR-- 596
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlvngqdlsrlKRReiPYLRrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 597 IGYFTQhhvDS---MDLTTSA-VdwmskSFP----GKTDEEYRRH----LGSFGITGtlglqKMQL----LSGGQKSRVA 660
Cdd:COG2884 81 IGVVFQ---DFrllPDRTVYEnV-----ALPlrvtGKSRKEIRRRvrevLDLVGLSD-----KAKAlpheLSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 661 FA-ALcLNNPHILVLDEPSNHLDTTGLDALVEALKNFN-GG--VLMVSHDISVIDSVCKEIWVSEQGTVKR 727
Cdd:COG2884 148 IArAL-VNRPELLLADEPTGNLDPETSWEIMELLEEINrRGttVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
548-679 |
4.77e-24 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 98.87 E-value: 4.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 548 LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRN-----------PRLRIGYFTQHHVDSMDLTTSAVD 616
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 617 WMSKSFPGKTD-------EEYRRHLGSFGITGTLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSN 679
Cdd:pfam00005 81 RLGLLLKGLSKrekdaraEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
532-742 |
5.59e-24 |
|
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: 101.47 E-value: 5.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDeNNLLLKDVNLDVQmDSRI-ALVGANGCGKTTLLKIMMEQLRPLKGFVSrnprlrigyftqhhVDSMDL 610
Cdd:COG4555 2 IEVENLSKKYG-KVPALKDVSFTAK-DGEItGLLGPNGAGKTTLLRMLAGLLKPDSGSIL--------------IDGEDV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 611 TTSAVDWMSK---------SFPGKTDEEYRRHLGSF-GITGTLG-------LQKMQL----------LSGGQKSRVAFAA 663
Cdd:COG4555 66 RKEPREARRQigvlpdergLYDRLTVRENIRYFAELyGLFDEELkkrieelIELLGLeefldrrvgeLSTGMKKKVALAR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 664 LCLNNPHILVLDEPSNHLD---TTGLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVkRFEGTIYDYRDYIL 740
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDvmaRRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV-VAQGSLDELREEIG 224
|
..
gi 14318531 741 QS 742
Cdd:COG4555 225 EE 226
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
490-725 |
7.39e-24 |
|
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: 106.39 E-value: 7.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 490 AKSQEAQSRIKKL--EKLPVLEPPEQDKTidfkfpecdkLSPPIIQLQDVSFGYDENN-LLLKDVNLDVQMDSRIALVGA 566
Cdd:COG4987 300 GRVRAAARRLNELldAPPAVTEPAEPAPA----------PGGPSLELEDVSFRYPGAGrPVLDGLSLTLPPGERVAIVGP 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 567 NGCGKTTLLKIMMEQLRPLKGFVS---------RNPRLR--IGYFTQH-HVdsmdlttsavdwmsksF------------ 622
Cdd:COG4987 370 SGSGKSTLLALLLRFLDPQSGSITlggvdlrdlDEDDLRrrIAVVPQRpHL----------------Fdttlrenlrlar 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 623 PGKTDEEYRR-----HLGSFGITGTLGLQKM-----QLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDT-TG---LDA 688
Cdd:COG4987 434 PDATDEELWAalervGLGDWLAALPDGLDTWlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAaTEqalLAD 513
|
250 260 270
....*....|....*....|....*....|....*..
gi 14318531 689 LVEALKnfNGGVLMVSHDISVIDSVCkEIWVSEQGTV 725
Cdd:COG4987 514 LLEALA--GRTVLLITHRLAGLERMD-RILVLEDGRI 547
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
486-725 |
1.66e-23 |
|
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: 106.10 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 486 RYNAAKSqeAQSRIKKLEKLPVlEPPEQDKTIDFkfpecdklsPPI---IQLQDVSFGY-DENNLLLKDVNLDVQMDSRI 561
Cdd:TIGR03375 427 RYQQAKT--ALQSLDELMQLPV-ERPEGTRFLHR---------PRLqgeIEFRNVSFAYpGQETPALDNVSLTIRPGEKV 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 562 ALVGANGCGKTTLLKIMMEQLRPLKGFVSR--------NP---RLRIGYFTQHHV-------DSMDLTTSAVDwmsksfp 623
Cdd:TIGR03375 495 AIIGRIGSGKSTLLKLLLGLYQPTEGSVLLdgvdirqiDPadlRRNIGYVPQDPRlfygtlrDNIALGAPYAD------- 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 624 gktDEEYRRHLGSFGITGTL-----GLQKM-----QLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEAL 693
Cdd:TIGR03375 568 ---DEEILRAAELAGVTEFVrrhpdGLDMQigergRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRL 644
|
250 260 270
....*....|....*....|....*....|....
gi 14318531 694 KNFNGG--VLMVSHDISVIDSVCKEIwVSEQGTV 725
Cdd:TIGR03375 645 KRWLAGktLVLVTHRTSLLDLVDRII-VMDNGRI 677
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
532-713 |
1.67e-23 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 99.59 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDEN-NLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS-----------RNPRLRIGY 599
Cdd:cd03245 3 IEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLldgtdirqldpADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 600 FTQhhvDSMDLTTSAVDWMSKSFPGKTDEEYRRHLGSFGITGTLGLQK----MQL------LSGGQKSRVAFAALCLNNP 669
Cdd:cd03245 83 VPQ---DVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPngldLQIgergrgLSGGQRQAVALARALLNDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14318531 670 HILVLDEPSNHLDTTGLDALVEALKNFNGG--VLMVSHDISVIDSV 713
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITHRPSLLDLV 205
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
533-714 |
2.33e-23 |
|
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: 98.48 E-value: 2.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 533 QLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV-------SRNPRLRIGYFTQHHV 605
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpiKAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 606 DSMDLTTSAVDWMSKSFPGKTDEEYRRHlgsfGITGTLGLQKMQL-----LSGGQKSRVAFAALCLNNPHILVLDEPSNH 680
Cdd:cd03226 81 DYQLFTDSVREELLLGLKELDAGNEQAE----TVLKDLDLYALKErhplsLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 14318531 681 LDTTGLDALVEALKNFNG---GVLMVSHDISVIDSVC 714
Cdd:cd03226 157 LDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVC 193
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
541-710 |
8.05e-23 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 96.72 E-value: 8.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 541 YDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNP-------------RLRIGYFTQhhvDS 607
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGepldysrkgllerRQRVGLVFQ---DP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 608 MDLTTSAVDWMSKSFP----GKTDEEYRRHLG-SFGITGTLGLQK--MQLLSGGQKSRVAFAALCLNNPHILVLDEPSNH 680
Cdd:TIGR01166 78 DDQLFAADVDQDVAFGplnlGLSEAEVERRVReALTAVGASGLRErpTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAG 157
|
170 180 190
....*....|....*....|....*....|...
gi 14318531 681 LDTTGLDALVEALKNFNG---GVLMVSHDISVI 710
Cdd:TIGR01166 158 LDPAGREQMLAILRRLRAegmTVVISTHDVDLA 190
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
547-710 |
9.69e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.15 E-value: 9.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 547 LLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRLRIGYFTQHhvdsmdlttSAVDWmskSFPgKT 626
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQR---------SEVPD---SLP-LT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 627 DEE------------YRRH-----------LGSFGITGTLGLQkMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDT 683
Cdd:NF040873 74 VRDlvamgrwarrglWRRLtrddraavddaLERVGLADLAGRQ-LGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|
gi 14318531 684 TGLDALVEALKNFNG---GVLMVSHDISVI 710
Cdd:NF040873 153 ESRERIIALLAEEHArgaTVVVVTHDLELV 182
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
215-396 |
1.20e-22 |
|
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: 94.64 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 215 LSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELNVPKHVSILHveQELRGDDTKALQsvldadvwrkqllseeakin 294
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDG--QDLTDDERKSLR-------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 295 erlKEMDVLRQEFEedslevkkLDNEREDLDNhlIQISDKLVDMESDKAEARAASILYGLG---FSTEAQQQPTNSFSGG 371
Cdd:pfam00005 59 ---KEIGYVFQDPQ--------LFPRLTVREN--LRLGLLLKGLSKREKDARAEEALEKLGlgdLADRPVGERPGTLSGG 125
|
170 180
....*....|....*....|....*
gi 14318531 372 WRMRLSLARALFCQPDLLLLDEPSN 396
Cdd:pfam00005 126 QRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
531-725 |
1.46e-22 |
|
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: 96.81 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENNL---LLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS--------------RNP 593
Cdd:cd03257 1 LLEVKNLSVSFPTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIfdgkdllklsrrlrKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 594 RLRIGYFTQhhvDSMdlttSAVD-WMS----------KSFPGKTDEEYRRHLGSFGITGTLGLQKMQL----LSGGQKSR 658
Cdd:cd03257 81 RKEIQMVFQ---DPM----SSLNpRMTigeqiaeplrIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRypheLSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 659 VAFA-ALCLnNPHILVLDEPsnhldTTGLDALVEAL---------KNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:cd03257 154 VAIArALAL-NPKLLIADEP-----TSALDVSVQAQildllkklqEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
537-710 |
9.02e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 95.18 E-value: 9.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 537 VSFGydeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRLRIGYFTQH-HVD-SMDLTTSA 614
Cdd:PRK09544 12 VSFG---QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKlYLDtTLPLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 615 VDWMSksfPGKTDEEYRRHLGSFGiTGTLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTG---LDALVE 691
Cdd:PRK09544 89 FLRLR---PGTKKEDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGqvaLYDLID 164
|
170 180
....*....|....*....|
gi 14318531 692 ALKN-FNGGVLMVSHDISVI 710
Cdd:PRK09544 165 QLRReLDCAVLMVSHDLHLV 184
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
532-725 |
9.37e-22 |
|
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: 95.26 E-value: 9.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYD---ENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS-----------RNPRLRI 597
Cdd:COG1124 2 LEVRNLSVSYGqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTfdgrpvtrrrrKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 598 GYFTQHHVDSMD--LTtsaVDWmSKSFP----GKTDEEYR--RHLGSFGITGTLGLQKMQLLSGGQKSRVAFA-ALCLnN 668
Cdd:COG1124 82 QMVFQDPYASLHprHT---VDR-ILAEPlrihGLPDREERiaELLEQVGLPPSFLDRYPHQLSGGQRQRVAIArALIL-E 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 669 PHILVLDEPsnhldTTGLDALVEAL---------KNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:COG1124 157 PELLLLDEP-----TSALDVSVQAEilnllkdlrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
532-724 |
2.66e-21 |
|
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: 91.86 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENnLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS-------------RNPRLRIG 598
Cdd:cd03229 1 LELKNVSKRYGQK-TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILidgedltdledelPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 599 YFTQHHVdsmdlttsavdwmskSFPGKTDEEYRRHLgsfgitgtlglqkmqlLSGGQKSRVAFA-ALClNNPHILVLDEP 677
Cdd:cd03229 80 MVFQDFA---------------LFPHLTVLENIALG----------------LSGGQQQRVALArALA-MDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 14318531 678 SNHLD---TTGLDALVEALK-NFNGGVLMVSHDISVIDSVCKEIWVSEQGT 724
Cdd:cd03229 128 TSALDpitRREVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
548-725 |
3.43e-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: 92.74 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 548 LKDVNLDVQMD---SRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRL---------------RIGYFTQH-----H 604
Cdd:cd03297 10 LPDFTLKIDFDlneEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLVFQQyalfpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 605 vdsMDLTTSAVDWMSKSFPGKTDEEYRRHLGSFGITGtLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTT 684
Cdd:cd03297 90 ---LNVRENLAFGLKRKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 14318531 685 GLDALV----EALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:cd03297 166 LRLQLLpelkQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
532-725 |
7.91e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 91.42 E-value: 7.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLlKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRP------LKGfVSRNP------RLRIGY 599
Cdd:COG4619 1 LELEGLSFRVGGKPIL-SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPtsgeiyLDG-KPLSAmpppewRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 600 FTQ----------HHVDsmdlttsavDWMSKSFPGKTDEEYRRHLGSFGITGTLGLQKMQLLSGGQKSRVAFAALCLNNP 669
Cdd:COG4619 79 VPQepalwggtvrDNLP---------FPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 670 HILVLDEPsnhldTTGLDA----LVEAL-----KNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:COG4619 150 DVLLLDEP-----TSALDPentrRVEELlreylAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
532-710 |
8.29e-21 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 97.16 E-value: 8.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGfvsrnpRLRIGyftQHHVDSMDLT 611
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSG------RILID---GVDIRDLTLE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 612 tsavDWMSK-------SF--------------PGKTDEEYRR--------------------HLGSFGITgtlglqkmql 650
Cdd:COG1132 411 ----SLRRQigvvpqdTFlfsgtirenirygrPDATDEEVEEaakaaqahefiealpdgydtVVGERGVN---------- 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 651 LSGGQKSRVAFA-ALcLNNPHILVLDEPSNHLDT-TglDALV-EALKNFNGG--VLMVSHDISVI 710
Cdd:COG1132 477 LSGGQRQRIAIArAL-LKDPPILILDEATSALDTeT--EALIqEALERLMKGrtTIVIAHRLSTI 538
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
530-725 |
1.33e-20 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 96.13 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 530 PIIQLQDVSFGY-DENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMeQLRPLKGFVS------------RNPRLR 596
Cdd:COG1123 3 PLLEVRDLSVRYpGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALM-GLLPHGGRISgevlldgrdlleLSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 597 ---IGYFTQHHVDSMDLTTSAVD--------WMSKSfpgKTDEEYRRHLGSFGITGTLGlQKMQLLSGGQKSRVAFAALC 665
Cdd:COG1123 82 grrIGMVFQDPMTQLNPVTVGDQiaealenlGLSRA---EARARVLELLEAVGLERRLD-RYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318531 666 LNNPHILVLDEPSNHLDTTG----LDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTqaeiLDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
532-708 |
1.56e-20 |
|
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: 90.99 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENN---LLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRN------PRLRIGYFTQ 602
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDgepvtgPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 603 HHvdsmdlttSAVDWMSK----SFP----GKTDEEYRRH----LGSFGITGTLGLQKMQlLSGGQKSRVAFA-ALcLNNP 669
Cdd:cd03293 81 QD--------ALLPWLTVldnvALGlelqGVPKAEARERaeelLELVGLSGFENAYPHQ-LSGGMRQRVALArAL-AVDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14318531 670 HILVLDEPSNHLD--TTGL--DALVEALKNFNGGVLMVSHDIS 708
Cdd:cd03293 151 DVLLLDEPFSALDalTREQlqEELLDIWRETGKTVLLVTHDID 193
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
528-707 |
5.09e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 90.53 E-value: 5.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 528 SPPIIQLQDVSFGYDENN---LLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRN------PRLRIG 598
Cdd:COG1116 4 AAPALELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDgkpvtgPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 599 YFTQHHvdsmdlttSAVDWMS-----------KSFPGKTDEEY-RRHLGSFGITGTLGL---QkmqlLSGGQKSRVAFA- 662
Cdd:COG1116 84 VVFQEP--------ALLPWLTvldnvalglelRGVPKAERRERaRELLELVGLAGFEDAyphQ----LSGGMRQRVAIAr 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14318531 663 ALcLNNPHILVLDEPSNHLD--TTGL--DALVEALKNFNGGVLMVSHDI 707
Cdd:COG1116 152 AL-ANDPEVLLMDEPFGALDalTRERlqDELLRLWQETGKTVLFVTHDV 199
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
529-710 |
8.46e-20 |
|
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: 89.37 E-value: 8.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 529 PPIIQLQDVSFGYDENNLLlKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPL-----------KGFVS-RNPRLR 596
Cdd:COG1119 1 DPLLELRNVTVRRGGKTIL-DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTygndvrlfgerRGGEDvWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 597 IGYFTQHHVDSMDLTTSAVD------------WMSksfPGKTDEEY-RRHLGSFGITGtLGLQKMQLLSGGQKSRVAFA- 662
Cdd:COG1119 80 IGLVSPALQLRFPRDETVLDvvlsgffdsiglYRE---PTDEQRERaRELLELLGLAH-LADRPFGTLSQGEQRRVLIAr 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 14318531 663 ALcLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGG----VLMVSHDISVI 710
Cdd:COG1119 156 AL-VKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaptLVLVTHHVEEI 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
532-709 |
1.56e-19 |
|
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: 87.93 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGY---DENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS---RNP------------ 593
Cdd:cd03255 1 IELKNLSKTYgggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgTDIsklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 594 RLRIGY-FTQHHVdsmdLTT-SAVD--WMSKSFPGKTDEEYRRH----LGSFGITGTLGLQKMQlLSGGQKSRVAFA-AL 664
Cdd:cd03255 81 RRHIGFvFQSFNL----LPDlTALEnvELPLLLAGVPKKERRERaeelLERVGLGDRLNHYPSE-LSGGQQQRVAIArAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14318531 665 cLNNPHILVLDEPSNHLDT-TG---LDALVEALKNFNGGVLMVSHDISV 709
Cdd:cd03255 156 -ANDPKIILADEPTGNLDSeTGkevMELLRELNKEAGTTIVVVTHDPEL 203
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
502-719 |
1.88e-19 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 92.35 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 502 LEKLPVLEPPEQDKTIDfkfpecdklSPPIIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQ 581
Cdd:TIGR02857 301 LDAAPRPLAGKAPVTAA---------PASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 582 LRPLKGFVSRN-----------PRLRIGYFTQH-HVdsmdLTTSAVDWMSKSFPGKTDEEYRRHLGSFGITGTL-----G 644
Cdd:TIGR02857 372 VDPTEGSIAVNgvpladadadsWRDQIAWVPQHpFL----FAGTIAENIRLARPDASDAEIREALERAGLDEFVaalpqG 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 645 LQKM-----QLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGG--VLMVSHDISVIdSVCKEI 717
Cdd:TIGR02857 448 LDTPigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHRLALA-ALADRI 526
|
..
gi 14318531 718 WV 719
Cdd:TIGR02857 527 VV 528
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
529-706 |
1.94e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 87.79 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 529 PPIIQLQDVSFGYDENNL---LLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV----------SRNPR- 594
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlidgqdisslSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 595 -LR---IGY-FTQHH-VDSMdlttSAVD--WMSKSFPGKTDEEYRRH----LGSFGITGTLGlQKMQLLSGGQKSRVAFA 662
Cdd:COG1136 82 rLRrrhIGFvFQFFNlLPEL----TALEnvALPLLLAGVSRKERRERarelLERVGLGDRLD-HRPSQLSGGQQQRVAIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14318531 663 -ALcLNNPHILVLDEPSNHLDT-TG---LDALVEALKNFNGGVLMVSHD 706
Cdd:COG1136 157 rAL-VNRPKLILADEPTGNLDSkTGeevLELLRELNRELGTTIVMVTHD 204
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
532-724 |
2.02e-19 |
|
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: 88.06 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS------RN---PRLR--IGYF 600
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdiREvtlDSLRraIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 601 TQhhvDSMDLTTSAVDWMSKSFPGKTDEEYRR-----HLG------SFG---ITGTLGLQkmqlLSGGQKSRVAFAALCL 666
Cdd:cd03253 81 PQ---DTVLFNDTIGYNIRYGRPDATDEEVIEaakaaQIHdkimrfPDGydtIVGERGLK----LSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 667 NNPHILVLDEPSNHLDTTGLDALVEALKNFNGG--VLMVSHDIS-VIDS----VCKEIWVSEQGT 724
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSKGrtTIVIAHRLStIVNAdkiiVLKDGRIVERGT 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
532-730 |
2.52e-19 |
|
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: 87.25 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDeNNLLLKDVNLDVQmDSRIALVGANGCGKTTLLKIMMEQLRPLKGF-------VSRNP---RLRIGYFT 601
Cdd:cd03264 1 LQLENLTKRYG-KKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTiridgqdVLKQPqklRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 602 QHHVDSMDLTTS-AVD---WMSKSFPGKTDEEYRRHLGSFGITGTLGlQKMQLLSGGQKSRVAFAALCLNNPHILVLDEP 677
Cdd:cd03264 79 QEFGVYPNFTVReFLDyiaWLKGIPSKEVKARVDEVLELVNLGDRAK-KKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 678 snhldTTGLDA---------LVEALKNfngGVLMVS-HDISVIDSVCKEIWVSEQGTVKrFEG 730
Cdd:cd03264 158 -----TAGLDPeerirfrnlLSELGED---RIVILStHIVEDVESLCNQVAVLNKGKLV-FEG 211
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
532-730 |
2.90e-19 |
|
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: 85.83 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENN-LLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVsrnprlrigYFTQHHVDSM-D 609
Cdd:cd03247 1 LSINNVSFSYPEQEqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGVPVSDLeK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 610 LTTSAVDWMSKsfpgktdeeyRRHLGSFGITGTLGLQkmqlLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTG---- 685
Cdd:cd03247 72 ALSSLISVLNQ----------RPYLFDTTLRNNLGRR----FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITerql 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 14318531 686 LDALVEALKnfNGGVLMVSHDISVIDSVcKEIWVSEQGTVKrFEG 730
Cdd:cd03247 138 LSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKII-MQG 178
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
532-730 |
3.09e-19 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 86.89 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLlKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV---------SRNPRLRIG---- 598
Cdd:cd03268 1 LKTNDLTKTYGKKRVL-DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItfdgksyqkNIEALRRIGalie 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 599 ------YFTQHHvdsmDLTTSAVdwmsksFPGKTDEEYRRHLGSFGITGTlGLQKMQLLSGGQKSRVAFAALCLNNPHIL 672
Cdd:cd03268 80 apgfypNLTARE----NLRLLAR------LLGIRKKRIDEVLDVVGLKDS-AKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 673 VLDEPSNHLDTTG---LDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVkRFEG 730
Cdd:cd03268 149 ILDEPTNGLDPDGikeLRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL-IEEG 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
532-731 |
3.83e-19 |
|
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: 86.90 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKG--FVSRNP---------RLRIGYF 600
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGqiLIDGIDirdisrkslRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 601 TQhhvDSMDLTTSAVDWMSKSFPGKTDEEYRR-----HLGSFGITGTLGLQKM-----QLLSGGQKSRVAFAALCLNNPH 670
Cdd:cd03254 83 LQ---DTFLFSGTIMENIRLGRPNATDEEVIEaakeaGAHDFIMKLPNGYDTVlgengGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 671 ILVLDEPSNHLDTTGLDALVEALKNFNGG--VLMVSHDISVIDSVCKeIWVSEQGTVKRfEGT 731
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGrtSIIIAHRLSTIKNADK-ILVLDDGKIIE-EGT 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
532-725 |
5.58e-19 |
|
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: 86.52 E-value: 5.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYD-ENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRP-----------LKGFVSRNPRLRIGY 599
Cdd:cd03251 1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVdsgrilidghdVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 600 FTQhhvDSMDLTTSAVDWMSKSFPGKTDEEYRR-----HLGSFGITGTLGLQKM-----QLLSGGQKSRVAFAALCLNNP 669
Cdd:cd03251 81 VSQ---DVFLFNDTVAENIAYGRPGATREEVEEaaraaNAHEFIMELPEGYDTVigergVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 670 HILVLDEPSNHLDTTGLDALVEALKNF--NGGVLMVSHDISVIDSVcKEIWVSEQGTV 725
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLmkNRTTFVIAHRLSTIENA-DRIVVLEDGKI 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
207-439 |
1.95e-18 |
|
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: 84.44 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 207 YVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILHVEQELRGDDTKALQ----SVL-DADV 281
Cdd:cd03225 9 YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNG--LLGPTSGEVLVDGKDLTKLSLKELRrkvgLVFqNPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 282 wrkQLLseeakinerlkeMDVLRQE--FeedSLEVKKLDNEredldnhliqisdklvdmesdKAEARAASILYGLGFStE 359
Cdd:cd03225 87 ---QFF------------GPTVEEEvaF---GLENLGLPEE---------------------EIEERVEEALELVGLE-G 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 360 AQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN---TVLTVSHDRAFLNEVATDIIY 436
Cdd:cd03225 127 LRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIV 206
|
...
gi 14318531 437 QHN 439
Cdd:cd03225 207 LED 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
203-435 |
2.14e-18 |
|
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: 89.19 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 203 TFDLYVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDTKALQSVLDADVW 282
Cdd:COG1123 269 RYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG--LLRPTSGSIL-----FDGKDLTKLSRRSLRELR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 283 RK-QLL--SEEAKINERLKemdvLRQEFEEdSLEVKKLDNEREdldnhliqisdklvdmesdkAEARAASILYGLGFSTE 359
Cdd:COG1123 342 RRvQMVfqDPYSSLNPRMT----VGDIIAE-PLRLHGLLSRAE--------------------RRERVAELLERVGLPPD 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 360 AQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN----TVLTVSHDRAFLNEVATDII 435
Cdd:COG1123 397 LADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelglTYLFISHDLAVVRYIADRVA 476
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
210-714 |
3.01e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 88.71 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELNVPK------HVSI----LHVE-QELRGDDTKALQSVL- 277
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTsgriiyHVALcekcGYVErPSKVGEPCPVCGGTLe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 278 --DADVWRkqlLSEEAKINERLKEMDVLRQEF---EEDSLevkkLDNEREDLDNhliqisdklVDMESDKAEARAASILY 352
Cdd:TIGR03269 91 peEVDFWN---LSDKLRRRIRKRIAIMLQRTFalyGDDTV----LDNVLEALEE---------IGYEGKEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 353 GLGFSTEAQQQpTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDvPSIAYLA-----EYLKTYPNTVLTVSHDRAFL 427
Cdd:TIGR03269 155 MVQLSHRITHI-ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD-PQTAKLVhnaleEAVKASGISMVLTSHWPEVI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 428 NEVATDIIYQHNERLdyyrgqdfdtfyttkeerrknaQREYDNQMVYRKHLQEFidkyrynaaksqeaqsrikkleklpv 507
Cdd:TIGR03269 233 EDLSDKAIWLENGEI----------------------KEEGTPDEVVAVFMEGV-------------------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 508 lEPPEQDKTIDfkfpecdkLSPPIIQLQDVSFGY---DENNLLLKD-VNLDVQMDSRIALVGANGCGKTTLLKIMMEQLR 583
Cdd:TIGR03269 265 -SEVEKECEVE--------VGEPIIKVRNVSKRYisvDRGVVKAVDnVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 584 PLKGFV------------SRNPRLR------IGYFTQH-----HVDSMDLTTSAVdwmSKSFPgktDEEYRRH----LGS 636
Cdd:TIGR03269 336 PTSGEVnvrvgdewvdmtKPGPDGRgrakryIGILHQEydlypHRTVLDNLTEAI---GLELP---DELARMKavitLKM 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 637 FGITGTLG---LQKM-QLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLD----TTGLDALVEALKNFNGGVLMVSHDIS 708
Cdd:TIGR03269 410 VGFDEEKAeeiLDKYpDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMD 489
|
....*.
gi 14318531 709 VIDSVC 714
Cdd:TIGR03269 490 FVLDVC 495
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
209-427 |
4.90e-18 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 84.08 E-value: 4.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 209 GDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILHVEQELRGDDTKALQsvldADVwrkQLLS 288
Cdd:COG1124 15 GRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAG--LERPWSGEVTFDGRPVTRRRRKAFR----RRV---QMVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 289 EEAkinerlkemdvlrqefeEDSLevkkldNEREDLDNHLiqiSDKLVDMESDKAEARAASILYGLGFSTEAQQQPTNSF 368
Cdd:COG1124 86 QDP-----------------YASL------HPRHTVDRIL---AEPLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS----IAYLAEYLKTYPNTVLTVSHDRAFL 427
Cdd:COG1124 140 SGGQRQRVAIARALILEPELLLLDEPTSALDVSVqaeiLNLLKDLREERGLTYLFVSHDLAVV 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
531-721 |
7.44e-18 |
|
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: 87.68 E-value: 7.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRLRIGYFTQ-------- 602
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQepqldptk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 603 -----------HHVDSMDlttsAVDWMSKSFpGKTDEEYRR-------------HLGSFGITGTL-----------GLQK 647
Cdd:TIGR03719 84 tvrenveegvaEIKDALD----RFNEISAKY-AEPDADFDKlaaeqaelqeiidAADAWDLDSQLeiamdalrcppWDAD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318531 648 MQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGGVLMVSHDISVIDSVCKeiWVSE 721
Cdd:TIGR03719 159 VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAG--WILE 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
209-436 |
1.12e-17 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 82.30 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 209 GDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDTKAlqsvldadvwrkqlls 288
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG--LIKESSGSIL-----LNGKPIKA---------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 289 eeakiNERLKEM-----DVLRQEFEEDSlevkkldneREDLDnhliqisdkLVDMESDKAEARAASILYGLGFSTEAQQQ 363
Cdd:cd03226 67 -----KERRKSIgyvmqDVDYQLFTDSV---------REELL---------LGLKELDAGNEQAETVLKDLDLYALKERH 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 364 PTnSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN---TVLTVSHDRAFLNEVATDIIY 436
Cdd:cd03226 124 PL-SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLL 198
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
210-432 |
1.16e-17 |
|
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: 82.14 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrrELNVPKHVSILHVEQELRgddtkalqsvLDADVWRKQL--L 287
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILA--GLLPPSAGEVLWNGEPIR----------DAREDYRRRLayL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 288 SEEAKINERLKEMDVLRqeFeedSLEVKKLDNEREDLDNHLIQIsdklvdmesdkaearaasilyGLgfsTEAQQQPTNS 367
Cdd:COG4133 81 GHADGLKPELTVRENLR--F---WAALYGLRADREAIDEALEAV---------------------GL---AGLADLPVRQ 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 368 FSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN---TVLTVSHDRAFLNEVAT 432
Cdd:COG4133 132 LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLArggAVLLTTHQPLELAAARV 199
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
210-435 |
1.88e-17 |
|
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: 82.00 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDTKALQSvldADVWRK----- 284
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG--LLKPTSGEVL-----VDGKDITKKNL---RELRRKvglvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 285 -----QLLSEeakinerlkemDVlrqefEED---SLEVKKLDNEredldnhliqisdklvdmesdKAEARAASIL--YGL 354
Cdd:COG1122 82 qnpddQLFAP-----------TV-----EEDvafGPENLGLPRE---------------------EIRERVEEALelVGL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 355 gfsTEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN---TVLTVSHDRAFLNEVA 431
Cdd:COG1122 125 ---EHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELA 201
|
....
gi 14318531 432 TDII 435
Cdd:COG1122 202 DRVI 205
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
531-732 |
3.54e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.59 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNP-------------RLRI 597
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysrkglmklRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 598 GYFTQhhvDSMDLTTSAVDWMSKSFPG-----KTDEEYRRHLGSFGITGTLGLQK--MQLLSGGQKSRVAFAALCLNNPH 670
Cdd:PRK13636 85 GMVFQ---DPDNQLFSASVYQDVSFGAvnlklPEDEVRKRVDNALKRTGIEHLKDkpTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 671 ILVLDEPSNHLDTTG----LDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVKrFEGTI 732
Cdd:PRK13636 162 VLVLDEPTAGLDPMGvseiMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGNP 226
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
546-725 |
3.83e-17 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 81.78 E-value: 3.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 546 LLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV----------SRNPR-LRIGYFTQHHVDSMDLTTSA 614
Cdd:TIGR03873 15 LIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVdlagvdlhglSRRARaRRVALVEQDSDTAVPLTVRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 615 VDWMSKS-----FPGKTDEEY---RRHLGSFGITgTLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTT-- 684
Cdd:TIGR03873 95 VVALGRIphrslWAGDSPHDAavvDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRaq 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 14318531 685 -GLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:TIGR03873 174 lETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGGRV 215
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
532-731 |
4.80e-17 |
|
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: 81.71 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLL-LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSrnprlrigyftqhhVDSMDL 610
Cdd:TIGR04520 1 IEVENVSFSYPESEKPaLKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVT--------------VDGLDT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 611 TTSAVDWmsksfpgktdeEYRRHLG-------------------SFG--------------ITGTLGLQKMQ-------- 649
Cdd:TIGR04520 67 LDEENLW-----------EIRKKVGmvfqnpdnqfvgatveddvAFGlenlgvpreemrkrVDEALKLVGMEdfrdreph 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 650 LLSGGQKSRVAFA-ALCLnNPHILVLDEPSNHLDTTGLDALVEALKNFNG----GVLMVSHDIS-VIDSvcKEIWVSEQG 723
Cdd:TIGR04520 136 LLSGGQKQRVAIAgVLAM-RPDIIILDEATSMLDPKGRKEVLETIRKLNKeegiTVISITHDMEeAVLA--DRVIVMNKG 212
|
....*...
gi 14318531 724 TVkRFEGT 731
Cdd:TIGR04520 213 KI-VAEGT 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
210-442 |
8.64e-17 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 80.49 E-value: 8.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRelnvpkhvsilhveqeLRGDDTKAlqSVLDADVWRKqllSE 289
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGL----------------LRPTSGEV--RVLGEDVARD---PA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 290 EAKinerlKEMDVLRQEFEedslevkkldneredLDNHL-----IQISDKLVDMESDKAEARAASILYGLGFsTEAQQQP 364
Cdd:COG1131 70 EVR-----RRIGYVPQEPA---------------LYPDLtvrenLRFFARLYGLPRKEARERIDELLELFGL-TDAADRK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 365 TNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN---TVLTVSHDrafLNEV---ATDIIYQH 438
Cdd:COG1131 129 VGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAegkTVLLSTHY---LEEAerlCDRVAIID 205
|
....
gi 14318531 439 NERL 442
Cdd:COG1131 206 KGRI 209
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
531-751 |
1.14e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 81.31 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDV--SFGydeNNLLLKDVNLDVQmDSRI-ALVGANGCGKTTLLKIMMEQLRP------LKGF-VSRNPRLRIGY- 599
Cdd:COG4152 1 MLELKGLtkRFG---DKTAVDDVSFTVP-KGEIfGLLGPNGAGKTTTIRIILGILAPdsgevlWDGEpLDPEDRRRIGYl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 600 ------------------FTQ-HHVDSMDLTTSAVDWMSKsfpgktdeeyrrhlgsFGITGTLGlQKMQLLSGGQKSRVA 660
Cdd:COG4152 77 peerglypkmkvgeqlvyLARlKGLSKAEAKRRADEWLER----------------LGLGDRAN-KKVEELSKGNQQKVQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 661 FAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNF--NG-GVLMVSHDISVIDSVCKEIWVSEQGTvKRFEGTI----- 732
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaaKGtTVIFSSHQMELVEELCDRIVIINKGR-KVLSGSVdeirr 218
|
250 260
....*....|....*....|
gi 14318531 733 -YDYRDYILQSADAAGVVKK 751
Cdd:COG4152 219 qFGRNTLRLEADGDAGWLRA 238
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
532-725 |
1.81e-16 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 78.72 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENnLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRN--------PRLR-IGYFTQ 602
Cdd:cd03259 1 LELKGLSKTYGSV-RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdvtgvpPERRnIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 603 HHvdsmdlttSAVDWMS---------KSFPGKTDEEYRRH---LGSFGITGTLGLQKMQlLSGGQKSRVAFA-ALcLNNP 669
Cdd:cd03259 80 DY--------ALFPHLTvaeniafglKLRGVPKAEIRARVrelLELVGLEGLLNRYPHE-LSGGQQQRVALArAL-AREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 670 HILVLDEPSNHLDT---TGL-DALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:cd03259 150 SLLLLDEPLSALDAklrEELrEELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
210-444 |
1.98e-16 |
|
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: 79.52 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDTKAlqsvldadvwrkqllse 289
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAG--LLKPDSGSIL-----IDGEDVRK----------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 290 eaKINERLKEMDVLRQEFE-EDSLEVKKLdneredldnhlIQISDKLVDMESDKAEARAASILYGLGFStEAQQQPTNSF 368
Cdd:COG4555 68 --EPREARRQIGVLPDERGlYDRLTVREN-----------IRYFAELYGLFDEELKKRIEELIELLGLE-EFLDRRVGEL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTY---PNTVLTVSHDRAFLNEVATDIIYQHNERLDY 444
Cdd:COG4555 134 STGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKVVA 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
531-734 |
2.02e-16 |
|
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: 79.16 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENNL---LLKDVNLDVQMDSRIALVGANGCGKTTLLKI--MMEqlRPLKGFVS--------------R 591
Cdd:cd03258 1 MIELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCinGLE--RPTSGSVLvdgtdltllsgkelR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 592 NPRLRIGYFTQHhvdsMDLTTSAVDWMSKSFP---GKTDEEYR----RHLGSFgitgtLGL-QKMQL----LSGGQKSRV 659
Cdd:cd03258 79 KARRRIGMIFQH----FNLLSSRTVFENVALPleiAGVPKAEIeervLELLEL-----VGLeDKADAypaqLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 660 AFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNG----GVLMVSHDISVIDSVCKEIWVSEQGTVKRfEGTIYD 734
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelglTIVLITHEMEVVKRICDRVAVMEKGEVVE-EGTVEE 227
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
204-514 |
2.48e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 83.08 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 204 FDL----YVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALsrrelnvpkhvsilhveqelrgddtkalqsvLDa 279
Cdd:PRK11147 320 FEMenvnYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM-------------------------------LG- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 280 dvwrkQLLSEEAKINERLKemdvlrqefeedsLEVKKLDNEREDLDnhliqiSDKLVdmESDKAEARAASILYG-----L 354
Cdd:PRK11147 368 -----QLQADSGRIHCGTK-------------LEVAYFDQHRAELD------PEKTV--MDNLAEGKQEVMVNGrprhvL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 355 G------FSTEAQQQPTNSFSGGWRMRLSLARaLFCQP-DLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVSHDRAFL 427
Cdd:PRK11147 422 GylqdflFHPKRAMTPVKALSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFV 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 428 -NEVATDIIYQHNERLDYYRGQDFD------TFYTTKEERRKNAQREydnqmvyrkhlqefidkyryNAAKSQEAQSRIK 500
Cdd:PRK11147 501 dNTVTECWIFEGNGKIGRYVGGYHDarqqqaQYLALKQPAVKKKEEA--------------------AAPKAETVKRSSK 560
|
330 340
....*....|....*....|...
gi 14318531 501 K--------LEKLP-VLEPPEQD 514
Cdd:PRK11147 561 KlsyklqreLEQLPqLLEDLEAE 583
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
532-725 |
2.60e-16 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 80.96 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLlKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKG---------FVSRNPRLR-IGYFT 601
Cdd:COG1118 3 IEVRNISKRFGSFTLL-DDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGrivlngrdlFTNLPPRERrVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 602 QH-----HvdsmdlttsavdwMS----------KSFPGKTDEEYR-RHLgsfgitgtlgLQKMQL----------LSGGQ 655
Cdd:COG1118 82 QHyalfpH-------------MTvaeniafglrVRPPSKAEIRARvEEL----------LELVQLegladrypsqLSGGQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 656 KSRVAFA-ALClNNPHILVLDEPSNHLDT---TGLDA-LVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:COG1118 139 RQRVALArALA-VEPEVLLLDEPFGALDAkvrKELRRwLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
212-435 |
3.72e-16 |
|
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: 78.32 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 212 QRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSIlhveqELRGDDTKALQSVLDADVWRK-QLLSEE 290
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILG--LLKPTSGSI-----IFDGKDLLKLSRRLRKIRRKEiQMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 291 A--KINERLKemdVLRQeFEEdSLEVKKLDNEREDLdnhLIQISDKLVDMESDKAEARAasilyglgFSTEaqqqptnsF 368
Cdd:cd03257 91 PmsSLNPRMT---IGEQ-IAE-PLRIHGKLSKKEAR---KEAVLLLLVGVGLPEEVLNR--------YPHE--------L 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKT----YPNTVLTVSHDRAFLNEVATDII 435
Cdd:cd03257 147 SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHDLGVVAKIADRVA 217
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
532-731 |
4.52e-16 |
|
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: 79.03 E-value: 4.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLL----LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVsrnprlrigyftqhHVDS 607
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFekkaLDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTV--------------TIDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 608 MDLTTSavdwmsksfPGKTDEEYRRHLG------------------------SFGITG------------TLGLQKMQL- 650
Cdd:TIGR04521 67 RDITAK---------KKKKLKDLRKKVGlvfqfpehqlfeetvykdiafgpkNLGLSEeeaeervkealeLVGLDEEYLe 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 651 -----LSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNG----GVLMVSHDISVIDSVCKEIWVSE 721
Cdd:TIGR04521 138 rspfeLSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKekglTVILVTHSMEDVAEYADRVIVMH 217
|
250
....*....|
gi 14318531 722 QGTVKrFEGT 731
Cdd:TIGR04521 218 KGKIV-LDGT 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
531-725 |
4.83e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.08 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV-----------SRNPRLRIGY 599
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgepitkenIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 600 FTQHHVDSMDLTTSAVDWMSKSFPGKTDEEYRRHLGSFGITgTLGLQKMQL-----LSGGQKSRVAFAALCLNNPHILVL 674
Cdd:PRK13652 83 VFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALH-MLGLEELRDrvphhLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 675 DEPSNHLDTTGLDALVEAL----KNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLndlpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
532-725 |
6.57e-16 |
|
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: 77.06 E-value: 6.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV-------SRNPRLRIGYFTQH- 603
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqdvSDLRGRAIPYLRRKi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 604 ---HVDSMDLTTSAVdWMSKSFP----GKTDEEYRRH----LGSFGITGTLGLQKMQLlSGGQKSRVAFAALCLNNPHIL 672
Cdd:cd03292 81 gvvFQDFRLLPDRNV-YENVAFAlevtGVPPREIRKRvpaaLELVGLSHKHRALPAEL-SGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 673 VLDEPSNHLDTTGLDALVEALKNFNGG---VLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAgttVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
532-705 |
7.56e-16 |
|
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: 75.65 E-value: 7.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEqLRPL-KGFVSRNPRLRIGYFTQHhvdsmdl 610
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWgSGRIGMPEGEDLLFLPQR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 611 ttsavdwmsksfpgktdeeyrrhlgSFGITGTLglqKMQL-------LSGGQKSRVAFAALCLNNPHILVLDEPSNHLDT 683
Cdd:cd03223 73 -------------------------PYLPLGTL---REQLiypwddvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180
....*....|....*....|..
gi 14318531 684 TGLDALVEALKNFNGGVLMVSH 705
Cdd:cd03223 125 ESEDRLYQLLKELGITVISVGH 146
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
548-725 |
9.41e-16 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 77.48 E-value: 9.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 548 LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKG---F-----------------VSR---NPRL--------- 595
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGsvlFdgeditglppheiarlgIGRtfqIPRLfpeltvlen 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 596 -RIGYftQHHVDSMDLTTSAVDWMSKsfpgkTDEEYRRHLGSFGITGTLGlQKMQLLSGGQKSRVAFA-ALCLNnPHILV 673
Cdd:cd03219 96 vMVAA--QARTGSGLLLARARREERE-----ARERAEELLERVGLADLAD-RPAGELSYGQQRRLEIArALATD-PKLLL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 674 LDEPS---NHLDTTGLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:cd03219 167 LDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
211-442 |
1.10e-15 |
|
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: 76.49 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 211 GQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrrelnvpkhvsilhveqelrgddtkalqSVLDADVWRKQLLSEE 290
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIL----------------------------GLIKPDSGEITFDGKS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 291 AKIN-ERLKEMDVLrqefeedsLEVKKLDNE---REDLDNH--LIQISDKLVDmesdkaearaaSILYGLGFSTEAQQqP 364
Cdd:cd03268 64 YQKNiEALRRIGAL--------IEAPGFYPNltaRENLRLLarLLGIRKKRID-----------EVLDVVGLKDSAKK-K 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 365 TNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN---TVLTVSHDRAFLNEVATDIIYQHNER 441
Cdd:cd03268 124 VKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDqgiTVLISSHLLSEIQKVADRIGIINKGK 203
|
.
gi 14318531 442 L 442
Cdd:cd03268 204 L 204
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
207-436 |
1.11e-15 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 81.03 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 207 YVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILHVEQELRGddtkalqsvLDADVWRKQl 286
Cdd:COG2274 483 YPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG--LYEPTSGRILIDGIDLRQ---------IDPASLRRQ- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 287 lseeakinerlkeMDVLRQEFE--EDSLevkkldneredLDNhlIQISDKLVDMEsdkaEARAASILYGL---------G 355
Cdd:COG2274 551 -------------IGVVLQDVFlfSGTI-----------REN--ITLGDPDATDE----EIIEAARLAGLhdfiealpmG 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 356 FSTEAQQQPTNsFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN--TVLTVSHDRAFLNEVatD 433
Cdd:COG2274 601 YDTVVGEGGSN-LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRLA--D 677
|
...
gi 14318531 434 IIY 436
Cdd:COG2274 678 RII 680
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
548-732 |
1.19e-15 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 76.77 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 548 LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKG-------FVSRNP---RLRIGYFTQHhvDSMDLTTSAVD- 616
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGtayingySIRTDRkaaRQSLGYCPQF--DALFDELTVREh 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 617 -WMSKSFPGKTDEEYRRHLGsfGITGTLGLQKMQL-----LSGGQKSRVAFAALCLNNPHILVLDEPsnhldTTGLD--- 687
Cdd:cd03263 96 lRFYARLKGLPKSEIKEEVE--LLLRVLGLTDKANkrartLSGGMKRKLSLAIALIGGPSVLLLDEP-----TSGLDpas 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14318531 688 -----ALVEALKNfNGGVLMVSHDISVIDSVCKEIWVSEQGTVkRFEGTI 732
Cdd:cd03263 169 rraiwDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKL-RCIGSP 216
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
548-743 |
2.22e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.27 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 548 LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPR------LRIGYftqhhvdSMDLTtsAVD--WMS 619
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsalleLGAGF-------HPELT--GREniYLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 620 KSFPGKTDEEYRRH---------LGSFgITgtlglQKMQLLSGGQKSRVAFA-ALCLnNPHILVLDEpsnhldttGL--- 686
Cdd:COG1134 113 GRLLGLSRKEIDEKfdeivefaeLGDF-ID-----QPVKTYSSGMRARLAFAvATAV-DPDILLVDE--------VLavg 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 687 DA--------LVEALKNFNGGVLMVSHDISVIDSVCKE-IWVsEQGTVkRFEGTIYD----YRDYILQSA 743
Cdd:COG1134 178 DAafqkkclaRIRELRESGRTVIFVSHSMGAVRRLCDRaIWL-EKGRL-VMDGDPEEviaaYEALLAGRE 245
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
548-741 |
2.30e-15 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 79.70 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 548 LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVsrnpRL---------------RIGYFTQ---------- 602
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV----RLdgadlkqwdretfgkHIGYLPQdvelfpgtva 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 603 -------HHVDSMDLTTSA----VDWMSKSFPGKTDEEyrrhLGSFGITgtlglqkmqlLSGGQKSRVAFAALCLNNPHI 671
Cdd:TIGR01842 410 eniarfgENADPEKIIEAAklagVHELILRLPDGYDTV----IGPGGAT----------LSGGQRQRIALARALYGDPKL 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 672 LVLDEPSNHLDTTGLDALVEALKNFN---GGVLMVSHDISVIDSVCKeIWVSEQGTVKRFeGTiydyRDYILQ 741
Cdd:TIGR01842 476 VVLDEPNSNLDEEGEQALANAIKALKargITVVVITHRPSLLGCVDK-ILVLQDGRIARF-GE----RDEVLA 542
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
512-705 |
4.23e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.10 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 512 EQDKTIDFKFPECDKLSPPIIQLQDVSFGY-DENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS 590
Cdd:PRK11160 319 EQKPEVTFPTTSTAAADQVSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 591 RNPRLRIGYFTQHHVDSMDLTTSAVDWMSKSF--------PGKTDEEYRRHLGSFGI-------------TGTLGLQkmq 649
Cdd:PRK11160 399 LNGQPIADYSEAALRQAISVVSQRVHLFSATLrdnlllaaPNASDEALIEVLQQVGLeklleddkglnawLGEGGRQ--- 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 650 lLSGGQKSRVAFAALCLNNPHILVLDEPsnhldTTGLDALVE-----ALKNFNGG--VLMVSH 705
Cdd:PRK11160 476 -LSGGEQRRLGIARALLHDAPLLLLDEP-----TEGLDAETErqileLLAEHAQNktVLMITH 532
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
547-725 |
5.57e-15 |
|
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: 74.12 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 547 LLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRP--LKGFV--------SRNPRLRIGYFTQHHVdsmdlttsavd 616
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVlingrpldKRSFRKIIGYVPQDDI----------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 617 wmsksfpgktdeeyrrHLGSFGITGTLGLQ-KMQLLSGGQKSRVAFAALCLNNPHILVLDEPsnhldTTGLDA-----LV 690
Cdd:cd03213 93 ----------------LHPTLTVRETLMFAaKLRGLSGGERKRVSIALELVSNPSLLFLDEP-----TSGLDSssalqVM 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 14318531 691 EALKNF-NGG--VLMVSHDIS-VIDSVCKEIWVSEQGTV 725
Cdd:cd03213 152 SLLRRLaDTGrtIICSIHQPSsEIFELFDKLLLLSQGRV 190
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
532-731 |
6.11e-15 |
|
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: 74.39 E-value: 6.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLlKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRN------------PRLRIGY 599
Cdd:cd03224 1 LEVENLNAGYGKSQIL-FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditglppherARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 600 -------FTQHHVD----------SMDLTTSAVDWMSKSFPgktDEEYRRHlgsfgitgtlglQKMQLLSGGQKSRVAFA 662
Cdd:cd03224 80 vpegrriFPELTVEenlllgayarRRAKRKARLERVYELFP---RLKERRK------------QLAGTLSGGEQQMLAIA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 663 -ALcLNNPHILVLDEPsnhldTTGL-----DALVEALKNFNGG---VLMVSHDISVIDSVCKEIWVSEQGTVkRFEGT 731
Cdd:cd03224 145 rAL-MSRPKLLLLDEP-----SEGLapkivEEIFEAIRELRDEgvtILLVEQNARFALEIADRAYVLERGRV-VLEGT 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
205-423 |
6.40e-15 |
|
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: 73.24 E-value: 6.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 205 DLYVGDGQR-ILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDTKALQSVldadvwr 283
Cdd:cd03214 4 NLSVGYGGRtVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAG--LLKPSSGEIL-----LDGKDLASLSPK------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 284 kqllseeakinERLKEMDVLRQefeedSLEvkkldneredldnhliqisdkLVDMEsDKAEaraasilyglgfsteaqqQ 363
Cdd:cd03214 70 -----------ELARKIAYVPQ-----ALE---------------------LLGLA-HLAD------------------R 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318531 364 PTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS----IAYLAEYLKTYPNTVLTVSHD 423
Cdd:cd03214 94 PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHqielLELLRRLARERGKTVVMVLHD 157
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
532-724 |
7.00e-15 |
|
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: 74.88 E-value: 7.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDE--NNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIM----------------------MEQLRPLKG 587
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptsgeilldgvdirdlnLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 588 FVSRNPRL---------RIGYFTQHHVDSMDLTTSA-VDWMSKSFPGKTDEEyrrhlgsfgiTGTLGLQkmqlLSGGQKS 657
Cdd:cd03249 81 LVSQEPVLfdgtiaeniRYGKPDATDEEVEEAAKKAnIHDFIMSLPDGYDTL----------VGERGSQ----LSGGQKQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318531 658 RVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGG--VLMVSHDISVID-----SVCKEIWVSEQGT 724
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGrtTIVIAHRLSTIRnadliAVLQNGQVVEQGT 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
209-436 |
1.16e-14 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 77.49 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 209 GDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDTKALqsvlDADVWRKQLLs 288
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG--FLPPYSGSIL-----INGVDLSDL----DPASWRRQIA- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 289 eeakinerlkemdVLRQE---FEeDSLevkkldneREDLDNHLIQISDKlvDMESDKAEARAASILYGL--GFSTEAQQQ 363
Cdd:COG4988 415 -------------WVPQNpylFA-GTI--------RENLRLGRPDASDE--ELEAALEAAGLDEFVAALpdGLDTPLGEG 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 364 PTNsFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS----IAYLAEYLKTYpnTVLTVSHDRAFLNEVatDIIY 436
Cdd:COG4988 471 GRG-LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETeaeiLQALRRLAKGR--TVILITHRLALLAQA--DRIL 542
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
205-423 |
1.39e-14 |
|
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: 74.31 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 205 DLYVG-DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDTKALqsvldadvwr 283
Cdd:COG1120 6 NLSVGyGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAG--LLKPSSGEVL-----LDGRDLASL---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 284 kqllseeaKINERLKEMDVLRQEFE-EDSLEVkkldneREdldnhliqisdkLVDM-------------ESDKAEARAAS 349
Cdd:COG1120 69 --------SRRELARRIAYVPQEPPaPFGLTV------RE------------LVALgryphlglfgrpsAEDREAVEEAL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 350 ILYGLgfsTEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDvpsIAY-------LAEYLKTYPNTVLTVSH 422
Cdd:COG1120 123 ERTGL---EHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLD---LAHqlevlelLRRLARERGRTVVMVLH 196
|
.
gi 14318531 423 D 423
Cdd:COG1120 197 D 197
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
229-731 |
1.75e-14 |
|
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: 77.13 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 229 GLVGQNGIGKSTLLRALSRrEL-----NVPKHVSILHVEQELRGddtKALQSVLdadvwrKQLLSEEAKINERLKEMDVL 303
Cdd:COG1245 103 GILGPNGIGKSTALKILSG-ELkpnlgDYDEEPSWDEVLKRFRG---TELQDYF------KKLANGEIKVAHKPQYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 304 RQEFEEDSLEV-KKLDnEREDLDnhliQISDKLvDMESdkaearaasILyglgfsteaqQQPTNSFSGGWRMRLSLARAL 382
Cdd:COG1245 173 PKVFKGTVRELlEKVD-ERGKLD----ELAEKL-GLEN---------IL----------DRDISELSGGELQRVAIAAAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 383 FCQPDLLLLDEPSNMLDV-------PSIAYLAEYLKTypntVLTVSHDRAFLNEVAtD---IIYqhnerldyyrGQdfdt 452
Cdd:COG1245 228 LRDADFYFFDEPSSYLDIyqrlnvaRLIRELAEEGKY----VLVVEHDLAILDYLA-DyvhILY----------GE---- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 453 fyttkeerrknaqreydnQMVY---------RKHLQEFIDKYRynaaksQEAQSRIKkleklpvleppeqDKTIDF--KF 521
Cdd:COG1245 289 ------------------PGVYgvvskpksvRVGINQYLDGYL------PEENVRIR-------------DEPIEFevHA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 522 PECDKLSPPIIQLQDVSFGYDENNLllkDVNL-DVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVsrNPRLRIGYF 600
Cdd:COG1245 332 PRREKEEETLVEYPDLTKSYGGFSL---EVEGgEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 601 TQHHVDSMDLTTSAVdwMSKSFPGKTDEEYRRHLgsfgITGTLGLQKM---QL--LSGGQKSRVAFAAlCLNNP-HILVL 674
Cdd:COG1245 407 PQYISPDYDGTVEEF--LRSANTDDFGSSYYKTE----IIKPLGLEKLldkNVkdLSGGELQRVAIAA-CLSRDaDLYLL 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 675 DEPSNHLDttgldalVE-------ALKNF----NGGVLMVSHDISVIDSVCKEIWVseqgtvkrFEGT 731
Cdd:COG1245 480 DEPSAHLD-------VEqrlavakAIRRFaenrGKTAMVVDHDIYLIDYISDRLMV--------FEGE 532
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
550-717 |
2.04e-14 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 75.09 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 550 DVNLDVQMDSRIALVGANGCGKTTLLKIMM-------------------------EQLRPLKG----------FVSRNPR 594
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILgllpppgitsgeilfdgedllklseKELRKIRGreiqmifqdpMTSLNPV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 595 LRIGY-----FTQHHVdsmdlttsavdwMSKSfpgKTDEEYRRHLGSFGITGTLGLQKM---QLlSGGQKSRVAFA-ALC 665
Cdd:COG0444 103 MTVGDqiaepLRIHGG------------LSKA---EARERAIELLERVGLPDPERRLDRyphEL-SGGMRQRVMIArALA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 666 LNnPHILVLDEPsnhldTTGLDALVEA-----LKN----FNGGVLMVSHDISVIDSVCKEI 717
Cdd:COG0444 167 LE-PKLLIADEP-----TTALDVTIQAqilnlLKDlqreLGLAILFITHDLGVVAEIADRV 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
536-725 |
3.17e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.50 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 536 DVSFGYdENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKG------------------------FVSR 591
Cdd:PRK13638 6 DLWFRY-QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGavlwqgkpldyskrgllalrqqvaTVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 592 NPRLRIGYftqHHVDSmDLTTSAvdwmsKSFPGKTDEEYRRHLGSFGITGTLGL--QKMQLLSGGQKSRVAFAALCLNNP 669
Cdd:PRK13638 85 DPEQQIFY---TDIDS-DIAFSL-----RNLGVPEAEITRRVDEALTLVDAQHFrhQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 670 HILVLDEPSNHLDTTGLDALVEALKNFNGG---VLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
531-730 |
4.73e-14 |
|
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: 72.02 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENN---LLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGF-------VSRNP---RLRI 597
Cdd:cd03266 1 MITADALTKRFRDVKktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFatvdgfdVVKEPaeaRRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 598 G-------------------YFTQHHVDSMDLTTSAVDWMSKSFpgkTDEEYR-RHLGSFgitgtlglqkmqllSGGQKS 657
Cdd:cd03266 81 GfvsdstglydrltarenleYFAGLYGLKGDELTARLEELADRL---GMEELLdRRVGGF--------------STGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 658 RVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGG---VLMVSHDISVIDSVCKEIWVSEQGTVkRFEG 730
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgkcILFSTHIMQEVERLCDRVVVLHRGRV-VYEG 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
211-435 |
4.81e-14 |
|
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: 70.35 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 211 GQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSIlhveqELRGDDTKALQSVLdadvWRKQLlsee 290
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAG--LLKPTSGEI-----LIDGKDIAKLPLEE----LRRRI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 291 akinerlkemdvlrqefeedslevkkldneredldnhliqisdklvdmesdkaearaaSILYGLgfsteaqqqptnsfSG 370
Cdd:cd00267 76 ----------------------------------------------------------GYVPQL--------------SG 83
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 371 GWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN---TVLTVSHDRAFLNEVATDII 435
Cdd:cd00267 84 GQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVI 151
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
532-710 |
5.86e-14 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 72.22 E-value: 5.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS--------------RNPRLRI 597
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtdinklkgkalRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 598 GYFTQHH--VDSMD----LTTSAVDWMS--KSFPGK-TDEEYRRH---LGSFGITgTLGLQKMQLLSGGQKSRVAFAALC 665
Cdd:cd03256 81 GMIFQQFnlIERLSvlenVLSGRLGRRStwRSLFGLfPKEEKQRAlaaLERVGLL-DKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14318531 666 LNNPHILVLDEPSNHLD----TTGLDALVEALKNFNGGVLMVSHDISVI 710
Cdd:cd03256 160 MQQPKLILADEPVASLDpassRQVMDLLKRINREEGITVIVSLHQVDLA 208
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
531-707 |
7.67e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 72.46 E-value: 7.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS-----------RNPRLRIGY 599
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvmgrevnaeneKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 600 FTQhhvDSMDLTTSAVDWMSKSF-P---GKTDEEYRRHLGSfgitgTLGLQKMQ--------LLSGGQKSRVAFAALCLN 667
Cdd:PRK13647 84 VFQ---DPDDQVFSSTVWDDVAFgPvnmGLDKDEVERRVEE-----ALKAVRMWdfrdkppyHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14318531 668 NPHILVLDEPSNHLDTTGLDALVEALKNFN--GGVLMVS-HDI 707
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHnqGKTVIVAtHDV 198
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
205-445 |
8.21e-14 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 71.03 E-value: 8.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 205 DLYVG-DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrrELNVPKHVSILHVEQELRGDDTK----ALQSVLDA 279
Cdd:cd03235 4 DLTVSyGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL--GLLKPTSGSIRVFGKPLEKERKRigyvPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 280 D----VWRKQLLSeeakineRLKEMDVLRQefeedsleVKKLDneREDLDNHLiqisdKLVDMeSDKAEARaasilygLG 355
Cdd:cd03235 82 DfpisVRDVVLMG-------LYGHKGLFRR--------LSKAD--KAKVDEAL-----ERVGL-SELADRQ-------IG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 356 fsteaqqqptnSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKT---YPNTVLTVSHDrafLNEV-- 430
Cdd:cd03235 132 -----------ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElrrEGMTILVVTHD---LGLVle 197
|
250
....*....|....*
gi 14318531 431 ATDIIYQHNERLDYY 445
Cdd:cd03235 198 YFDRVLLLNRTVVAS 212
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
550-732 |
8.36e-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: 73.61 E-value: 8.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 550 DVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRL---------------RIGY-------FTQHHVDS 607
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrRIGYvfqearlFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 608 mdlttSAVDWMSKSFPGKTDEEYRRHLGSFGITGTLGlQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLD 687
Cdd:TIGR02142 95 -----NLRYGMKRARPSERRISFERVIELLGIGHLLG-RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14318531 688 ALVEALKN----FNGGVLMVSHDISVIDSVCKEIWVSEQGTVKRFeGTI 732
Cdd:TIGR02142 169 EILPYLERlhaeFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA-GPI 216
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
532-707 |
9.44e-14 |
|
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: 71.06 E-value: 9.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLlKDVNLDVQMDSRIALVGANGCGKTTLLKIM--MEQLRP---------LKGFVSRNP------- 593
Cdd:cd03260 1 IELRDLNVYYGDKHAL-KDISLDIPKGEITALIGPSGCGKSTLLRLLnrLNDLIPgapdegevlLDGKDIYDLdvdvlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 594 RLRIGYFTQHHV-------DSMDLTTSAVDWMSKSFPGKTDEEyrrhlgsfgitgtlGLQKMQL------------LSGG 654
Cdd:cd03260 80 RRRVGMVFQKPNpfpgsiyDNVAYGLRLHGIKLKEELDERVEE--------------ALRKAALwdevkdrlhalgLSGG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 655 QKSRVAFAALCLNNPHILVLDEPSNHLD---TTGLDALVEALKNfNGGVLMVSHDI 707
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDpisTAKIEELIAELKK-EYTIVIVTHNM 200
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
531-706 |
9.58e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 74.77 E-value: 9.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRLRIGYFTQ-------H 603
Cdd:PRK11819 6 IYTMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQepqldpeK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 604 HV-----DSMDLTTSAVD-----WMSKSFPG----KTDEEYRR------HLGSFGITGTL-----------GLQKMQLLS 652
Cdd:PRK11819 86 TVrenveEGVAEVKAALDrfneiYAAYAEPDadfdALAAEQGElqeiidAADAWDLDSQLeiamdalrcppWDAKVTKLS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 14318531 653 GGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGGVLMVSHD 706
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
560-745 |
1.08e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 74.16 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 560 RIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRLRIGYFTQHHVDSMDLttSAVD---------WMSK-------SFP 623
Cdd:PRK15064 29 RYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEF--TVLDtvimghtelWEVKqerdriyALP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 624 GKTDEEYRRH----------------------LGSFGITGTLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHL 681
Cdd:PRK15064 107 EMSEEDGMKVadlevkfaemdgytaearagelLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318531 682 DTTGLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVKRFEGtiyDYRDYILQSADA 745
Cdd:PRK15064 187 DINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPG---NYDEYMTAATQA 247
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
532-725 |
1.12e-13 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 69.38 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDV--SFGydeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGfvsrnpRLRIGyftqhhvdsmd 609
Cdd:cd03216 1 LELRGItkRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSG------EILVD----------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 610 lttsavdwmSKSFPGKTDEEYRRHlgsfGItGTLglqkMQLlSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDAL 689
Cdd:cd03216 61 ---------GKEVSFASPRDARRA----GI-AMV----YQL-SVGERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
|
170 180 190
....*....|....*....|....*....|....*....
gi 14318531 690 VEALKNF--NG-GVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:cd03216 122 FKVIRRLraQGvAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
532-710 |
1.21e-13 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 70.19 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDEN----NLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPrlRIGYFTQhhvds 607
Cdd:cd03250 1 ISVEDASFTWDSGeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQ----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 608 mdlttsaVDW-MSKS------FpGKT-DEE-YRR--------------------HLGSFGITgtlglqkmqlLSGGQKSR 658
Cdd:cd03250 74 -------EPWiQNGTirenilF-GKPfDEErYEKvikacalepdleilpdgdltEIGEKGIN----------LSGGQKQR 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 659 VAFAALCLNNPHILVLDEP--------SNHLDTtglDALVEALKNfNGGVLMVSHDISVI 710
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPlsavdahvGRHIFE---NCILGLLLN-NKTRILVTHQLQLL 191
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
215-425 |
1.30e-13 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 74.25 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 215 LSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILHVEQELRGddtkalqsvLDADVWRKQL--LSEEAK 292
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG--FVDPTEGSIAVNGVPLAD---------ADADSWRDQIawVPQHPF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 293 InerlkemdvlrqeFEeDSLevkkldneredLDNhlIQISDKlvdmESDKAEARAASILYGLGFSTEAQQQPTNS----- 367
Cdd:TIGR02857 407 L-------------FA-GTI-----------AEN--IRLARP----DASDAEIREALERAGLDEFVAALPQGLDTpigeg 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 368 ---FSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN--TVLTVSHDRA 425
Cdd:TIGR02857 456 gagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLA 518
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
538-745 |
1.67e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.83 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 538 SFGYdenNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMM-EQL----------------------RPLKG----FVS 590
Cdd:PRK11147 12 SFSD---APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgEVLlddgriiyeqdlivarlqqdppRNVEGtvydFVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 591 RNPRLRIGYFTQHHVDSMDLTTSAVDWMSKSFpgKTDEEYRRHLGSF-------GITGTLGL---QKMQLLSGGQKSRVA 660
Cdd:PRK11147 89 EGIEEQAEYLKRYHDISHLVETDPSEKNLNEL--AKLQEQLDHHNLWqlenrinEVLAQLGLdpdAALSSLSGGWLRKAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 661 FAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVKRFEGtiyDYRDYIL 740
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPG---NYDQYLL 243
|
....*
gi 14318531 741 QSADA 745
Cdd:PRK11147 244 EKEEA 248
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
211-442 |
1.77e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 70.81 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 211 GQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHvSILHVeqelrgddtkalqsvldADvwrkQLLSEE 290
Cdd:COG4161 14 SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNL--LETPDS-GQLNI-----------------AG----HQFDFS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 291 AKINErlKEMDVLRQE----FEEDSL--EVKKLDNeredldnhLIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQP 364
Cdd:COG4161 70 QKPSE--KAIRLLRQKvgmvFQQYNLwpHLTVMEN--------LIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 365 tNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDvPSI-AYLAEYLKTYPNTVLT---VSHDRAFLNEVATDIIYQHNE 440
Cdd:COG4161 140 -LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD-PEItAQVVEIIRELSQTGITqviVTHEVEFARKVASQVVYMEKG 217
|
..
gi 14318531 441 RL 442
Cdd:COG4161 218 RI 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
546-705 |
1.85e-13 |
|
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: 70.38 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 546 LLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGF--------VSRNPRL---RIGYFTQHH--VDSMD--- 609
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTsgqilfngQPRKPDQfqkCVAYVRQDDilLPGLTvre 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 610 -LTTSAVDWMSKSFPG----KTDEEYR-RHLGsfgiTGTLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPsnhldT 683
Cdd:cd03234 101 tLTYTAILRLPRKSSDairkKRVEDVLlRDLA----LTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP-----T 171
|
170 180 190
....*....|....*....|....*....|
gi 14318531 684 TGLDA-----LVEALKNF---NGGVLMVSH 705
Cdd:cd03234 172 SGLDSftalnLVSTLSQLarrNRIVILTIH 201
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
531-725 |
1.92e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 70.81 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENNLLlKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKG-----------FVSRNPRLRIGY 599
Cdd:PRK11231 2 TLRTENLTVGYGTKRIL-NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGtvflgdkpismLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 600 FTQHHVDSMDLTTSAV------DWMskSFPGKTDEEYRRHLG-SFGITGTLGL--QKMQLLSGGQKSRVAFAALCLNNPH 670
Cdd:PRK11231 81 LPQHHLTPEGITVRELvaygrsPWL--SLWGRLSAEDNARVNqAMEQTRINHLadRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 671 ILVLDEPSNHLDTT---GLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:PRK11231 159 VVLLDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
548-730 |
2.14e-13 |
|
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: 70.25 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 548 LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRN----PRLRIGYFTQhhvdsMDLTtsAVD--WMSKS 621
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRgrvsSLLGLGGGFN-----PELT--GREniYLNGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 622 FPGKTDEEYRRH---------LGSFgITgtlglQKMQLLSGGQKSRVAFA-ALCLnNPHILVLDEPSNHLDTTGLDALVE 691
Cdd:cd03220 111 LLGLSRKEIDEKideiiefseLGDF-ID-----LPVKTYSSGMKARLAFAiATAL-EPDILLIDEVLAVGDAAFQEKCQR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 14318531 692 ALKNF---NGGVLMVSHDISVIDSVCKEIWVSEQGTVkRFEG 730
Cdd:cd03220 184 RLRELlkqGKTVILVSHDPSSIKRLCDRALVLEKGKI-RFDG 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
548-734 |
3.02e-13 |
|
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: 70.05 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 548 LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS--------RNPRL--RIGY-FTQHHVDSMDLttSAVD 616
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglvpwkRRKKFlrRIGVvFGQKTQLWWDL--PVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 617 --WMSKSFPGKTDEEYRRHLGsfGITGTLGLQKM-----QLLSGGQKSRVAFAALCLNNPHILVLDEPsnhldTTGLDAL 689
Cdd:cd03267 115 sfYLLAAIYDLPPARFKKRLD--ELSELLDLEELldtpvRQLSLGQRMRAEIAAALLHEPEILFLDEP-----TIGLDVV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 14318531 690 V-EALKNF--------NGGVLMVSHDISVIDSVCKEIWVSEQGTVkrfegtIYD 734
Cdd:cd03267 188 AqENIRNFlkeynrerGTTVLLTSHYMKDIEALARRVLVIDKGRL------LYD 235
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
544-705 |
3.27e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.13 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 544 NNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRN--------PRLRIGYFTqhHVDSMDLTTSAV 615
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDggdiddpdVAEACHYLG--HRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 616 D----WmsKSFPGKTDEEYRRHLGSFGITGTLGLqKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGlDALVE 691
Cdd:PRK13539 92 EnlefW--AAFLGGEELDIAAALEAVGLAPLAHL-PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA-VALFA 167
|
170
....*....|....*...
gi 14318531 692 AL----KNFNGGVLMVSH 705
Cdd:PRK13539 168 ELirahLAQGGIVIAATH 185
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
532-726 |
4.36e-13 |
|
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: 72.85 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNP-----------RLRIGYF 600
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkdidrhtlRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 601 TQhhvDSMDLTTSAVD-WMSKSFPGKTDEEYRRHLGSFGITGTLglQKMQL------------LSGGQKSRVAFAALCLN 667
Cdd:TIGR01193 554 PQ---EPYIFSGSILEnLLLGAKENVSQDEIWAACEIAEIKDDI--ENMPLgyqtelseegssISGGQKQRIALARALLT 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 668 NPHILVLDEPSNHLDTTGLDALVEALKNFNGGVLM-VSHDISVIDSVCKEIWVSEQGTVK 726
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLLNLQDKTIIfVAHRLSVAKQSDKIIVLDHGKIIE 688
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
531-731 |
4.39e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 70.11 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKG--FVSRNP-----------RLRI 597
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGevLIKGEPikydkksllevRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 598 GYFTQHHVDSMDLTTSAVDW----MSKSFPgkTDEEYRRHLGSFGITGTLGLQKM--QLLSGGQKSRVAFAALCLNNPHI 671
Cdd:PRK13639 81 GIVFQNPDDQLFAPTVEEDVafgpLNLGLS--KEEVEKRVKEALKAVGMEGFENKppHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 672 LVLDEPSNHLDTTGLDALVEALKNFN--GGVLMVS-HDISVIDSVCKEIWVSEQGTVKRfEGT 731
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNkeGITIIIStHDVDLVPVYADKVYVMSDGKIIK-EGT 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
207-430 |
5.47e-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: 5.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 207 YVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDTKALqsvlDADVWRKQ- 285
Cdd:COG4987 343 YPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR--FLDPQSGSIT-----LGGVDLRDL----DEDDLRRRi 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 286 -LLSEEAKInerlkemdvlrqeFEeDSLevkkldneREDLdnhliqisdKLVDMESDKAEARAAsiLYGLGFSTEAQQQP 364
Cdd:COG4987 412 aVVPQRPHL-------------FD-TTL--------RENL---------RLARPDATDEELWAA--LERVGLGDWLAALP 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 365 ----TN------SFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSI-AYLAEYLKTYPN-TVLTVSHDRAFLNEV 430
Cdd:COG4987 459 dgldTWlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEqALLADLLEALAGrTVLLITHRLAGLERM 536
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
532-717 |
6.28e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 68.46 E-value: 6.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLlKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV-------SRNPRLRIGY----- 599
Cdd:cd03269 1 LEVENVTKRFGRVTAL-DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdgkplDIAARNRIGYlpeer 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 600 --FTQHHVDSMDLTTSAVDWMSKSfpgKTDEEYRRHLGSFGITGtLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEP 677
Cdd:cd03269 80 glYPKMKVIDQLVYLAQLKGLKKE---EARRRIDEWLERLELSE-YANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14318531 678 SNHLDTTGLDALVEA---LKNFNGGVLMVSHDISVIDSVCKEI 717
Cdd:cd03269 156 FSGLDPVNVELLKDVireLARAGKTVILSTHQMELVEELCDRV 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
210-447 |
6.82e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 71.85 E-value: 6.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrRELNvPKHVSIlhveqelrgddtkalqsvldadVWrkqllSE 289
Cdd:PRK15064 330 DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV-GELE-PDSGTV----------------------KW-----SE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 290 EAKINERLKEMDvlrQEFEEDSLEVKKLDNEREDLDNhliqisDKLVdmesdkaearaASILYGLGFSTEAQQQPTNSFS 369
Cdd:PRK15064 381 NANIGYYAQDHA---YDFENDLTLFDWMSQWRQEGDD------EQAV-----------RGTLGRLLFSQDDIKKSVKVLS 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 370 GGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVSHDRAFLNEVATDIIYQHNERLDYYRG 447
Cdd:PRK15064 441 GGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSG 518
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
229-711 |
8.29e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.76 E-value: 8.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 229 GLVGQNGIGKSTLLRALSRrEL-----NVPKHVSILHVEQELRGddtKALQSVLdadvwrKQLLSEEAKINERLKEMDVL 303
Cdd:PRK13409 103 GILGPNGIGKTTAVKILSG-ELipnlgDYEEEPSWDEVLKRFRG---TELQNYF------KKLYNGEIKVVHKPQYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 304 RQEFEEDSLEVKKLDNEREDLDnhliQISDKLvDMESdkaearaasILyglgfsteaqQQPTNSFSGGWRMRLSLARALF 383
Cdd:PRK13409 173 PKVFKGKVRELLKKVDERGKLD----EVVERL-GLEN---------IL----------DRDISELSGGELQRVAIAAALL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 384 CQPDLLLLDEPSNMLDV-------PSIAYLAEylktyPNTVLTVSHDRAFLNEVAtDIIYqhnerldyyrgqdfdtfytt 456
Cdd:PRK13409 229 RDADFYFFDEPTSYLDIrqrlnvaRLIRELAE-----GKYVLVVEHDLAVLDYLA-DNVH-------------------- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 457 keerrknaqreydnqMVY---------------RKHLQEFIDKYRynaaksQEAQSRIKkleklpvleppeqDKTIDFKF 521
Cdd:PRK13409 283 ---------------IAYgepgaygvvskpkgvRVGINEYLKGYL------PEENMRIR-------------PEPIEFEE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 522 --PECDKLSPPIIQLQDVSFGYDENNLllkDVNL-DVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNprLRIG 598
Cdd:PRK13409 329 rpPRDESERETLVEYPDLTKKLGDFSL---EVEGgEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--LKIS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 599 YFTQHHVDSMDLTtsaVDWMSKSFPGKTDEEYRRHLgsfgITGTLGLQKM---QL--LSGGQKSRVAFAALCLNNPHILV 673
Cdd:PRK13409 404 YKPQYIKPDYDGT---VEDLLRSITDDLGSSYYKSE----IIKPLQLERLldkNVkdLSGGELQRVAIAACLSRDADLYL 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 14318531 674 LDEPSNHLDttgldalVE-------ALK----NFNGGVLMVSHDISVID 711
Cdd:PRK13409 477 LDEPSAHLD-------VEqrlavakAIRriaeEREATALVVDHDIYMID 518
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
532-731 |
8.62e-13 |
|
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: 68.17 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENnLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKG--FV--------SRNPRLRIGYFT 601
Cdd:cd03265 1 IEVENLVKKYGDF-EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGraTVaghdvvrePREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 602 QHHVDSMDLT-TSAVDWMSK--SFPG-KTDEEYRRHLGSFGitgtLGLQKMQLL---SGGQKSRVAFAALCLNNPHILVL 674
Cdd:cd03265 80 QDLSVDDELTgWENLYIHARlyGVPGaERRERIDELLDFVG----LLEAADRLVktySGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 675 DEPsnhldTTGLDA--------LVEALK-NFNGGVLMVSHDISVIDSVCKEIWVSEQGTVkRFEGT 731
Cdd:cd03265 156 DEP-----TIGLDPqtrahvweYIEKLKeEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI-IAEGT 215
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
563-717 |
8.81e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 67.90 E-value: 8.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 563 LVGANGCGKTTLLKIMMEQLRPLKGFVSRNPR-------------LRIGyftqhHVDSMDLTTSAVDWMSKSFPGKTDEE 629
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiarglLYLG-----HAPGIKTTLSVLENLRFWHADHSDEQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 630 YRRHLGSFGITGtLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNF---NGGVLMVSH- 705
Cdd:cd03231 106 VEEALARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHcarGGMVVLTTHq 184
|
170
....*....|..
gi 14318531 706 DISVIDSVCKEI 717
Cdd:cd03231 185 DLGLSEAGAREL 196
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
532-707 |
8.85e-13 |
|
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: 68.87 E-value: 8.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV--------SRNP---RLRIGYF 600
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedirEQDPvelRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 601 TQH-----HV---DSMDLTTSAVDWMSKSFPGKTDEeyrrhlgsfgITGTLGLQKMQL-------LSGGQKSRVAFA-AL 664
Cdd:cd03295 81 IQQiglfpHMtveENIALVPKLLKWPKEKIRERADE----------LLALVGLDPAEFadrypheLSGGQQQRVGVArAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 14318531 665 CLnNPHILVLDEPSNHLDTTGLDALVEALKNFN----GGVLMVSHDI 707
Cdd:cd03295 151 AA-DPPLLLMDEPFGALDPITRDQLQEEFKRLQqelgKTIVFVTHDI 196
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
532-706 |
1.03e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.81 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGydeNNLLlkDVNLDVQMDSRIALVGANGCGKTTLLKiMMEQLRPLKGFVSRNPR-----------LRIGYF 600
Cdd:PRK03695 1 MQLNDVAVS---TRLG--PLSAEVRAGEILHLVGPNGAGKSTLLA-RMAGLLPGSGSIQFAGQpleawsaaelaRHRAYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 601 TQHhvdsmDLTTSAVD---WMSKSFPGKTDEEYRRHLGSFgITGTLGLQK-----MQLLSGGQKSRVAFAALCL-----N 667
Cdd:PRK03695 75 SQQ-----QTPPFAMPvfqYLTLHQPDKTRTEAVASALNE-VAEALGLDDklgrsVNQLSGGEWQRVRLAAVVLqvwpdI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 14318531 668 NPH--ILVLDEPSNHLDTT---GLDALVEALKNFNGGVLMVSHD 706
Cdd:PRK03695 149 NPAgqLLLLDEPMNSLDVAqqaALDRLLSELCQQGIAVVMSSHD 192
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
548-734 |
1.07e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.73 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 548 LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS---RNP-RLRIGY-------FTQHhvdSM---DLttS 613
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgYVPfKRRKEFarrigvvFGQR---SQlwwDL--P 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 614 AVDwmskSFP------GKTDEEYRRHLGSFgiTGTLGLQKmQL------LSGGQKSRVAFAALCLNNPHILVLDEPsnhl 681
Cdd:COG4586 113 AID----SFRllkaiyRIPDAEYKKRLDEL--VELLDLGE-LLdtpvrqLSLGQRMRCELAAALLHRPKILFLDEP---- 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318531 682 dTTGLDALV-EALKNF--------NGGVLMVSHDISVIDSVCKEIWVSEQGTVkrfegtIYD 734
Cdd:COG4586 182 -TIGLDVVSkEAIREFlkeynrerGTTILLTSHDMDDIEALCDRVIVIDHGRI------IYD 236
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
531-725 |
1.18e-12 |
|
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: 67.88 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDE--NNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKG--------------------- 587
Cdd:cd03248 11 IVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGqvlldgkpisqyehkylhskv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 588 -FVSRNPRL-------RIGYFTQHhVDSMDLTTSAVDWMSKSFPGKTDEEYRRHLGsfgitgtlglQKMQLLSGGQKSRV 659
Cdd:cd03248 91 sLVGQEPVLfarslqdNIAYGLQS-CSFECVKEAAQKAHAHSFISELASGYDTEVG----------EKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 660 AFAALCLNNPHILVLDEPSNHLDTTGLDALVEALK--NFNGGVLMVSHDISVIDSVcKEIWVSEQGTV 725
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYdwPERRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
528-706 |
1.21e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 69.74 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 528 SPPIIQLQDVSFGYDENnLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIM--MEqlRPLKGFV--------SRNPRLR- 596
Cdd:COG3842 2 AMPALELENVSKRYGDV-TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagFE--TPDSGRIlldgrdvtGLPPEKRn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 597 IGYFTQHHvdsmDLttsavdwmsksFP--------------GKTDEEYRRH-----LGSFGITGtLGLQKMQLLSGGQKS 657
Cdd:COG3842 79 VGMVFQDY----AL-----------FPhltvaenvafglrmRGVPKAEIRArvaelLELVGLEG-LADRYPHQLSGGQQQ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 658 RVAFA-ALcLNNPHILVLDEP-SNhldttgLDA---------LVEALKNFNGGVLMVSHD 706
Cdd:COG3842 143 RVALArAL-APEPRVLLLDEPlSA------LDAklreemreeLRRLQRELGITFIYVTHD 195
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
211-442 |
1.24e-12 |
|
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: 66.65 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 211 GQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPK--HVSILhveqelrGDDTKAlqsvlDADVWRKQL-- 286
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILG--LLKPDsgEIKVL-------GKDIKK-----EPEEVKRRIgy 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 287 LSEEAKINERLKEMDVLRqefeedslevkkldneredldnhliqisdklvdmesdkaearaasilyglgfsteaqqqptn 366
Cdd:cd03230 78 LPEEPSLYENLTVRENLK-------------------------------------------------------------- 95
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 367 sFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN---TVLTVSHDRAFLNEVATDIIYQHNERL 442
Cdd:cd03230 96 -LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKegkTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
563-711 |
1.31e-12 |
|
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: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 563 LVGANGCGKTTLLKIMMEQLRPLKGFVSRNP------------RLRIgYFTQHHVDSMDLTTSA--VDWMSKSFPGKTDE 628
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwdeildefrgsELQN-YFTKLLEGDVKVIVKPqyVDLIPKAVKGKVGE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 629 EYRR--HLGSFG-ITGTLGL-----QKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDT---TGLDALVEALKNFN 697
Cdd:cd03236 110 LLKKkdERGKLDeLVDQLELrhvldRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqrLNAARLIRELAEDD 189
|
170
....*....|....
gi 14318531 698 GGVLMVSHDISVID 711
Cdd:cd03236 190 NYVLVVEHDLAVLD 203
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
203-432 |
1.53e-12 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 67.80 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 203 TFDLYVGDGQRI--LSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELNVPKHVSILHveqelRGDDTKALQsvldad 280
Cdd:TIGR02324 10 TFTLHQQGGVRLpvLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRH-----EGAWVDLAQ------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 281 vwrkqlLSEEAKINERLKEMDVLRQeFeedsLEVKKLDNEREDLDNHLIQISdklvdMESDKAEARAASILYGLGFSTEA 360
Cdd:TIGR02324 79 ------ASPREVLEVRRKTIGYVSQ-F----LRVIPRVSALEVVAEPLLERG-----VPREAARARARELLARLNIPERL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 361 QQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYL---KTYPNTVLTVSHDRAFLNEVAT 432
Cdd:TIGR02324 143 WHLPPATFSGGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIaeaKARGAALIGIFHDEEVRELVAD 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
205-442 |
1.54e-12 |
|
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: 67.91 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 205 DLYVG-DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqelrgddtkalqsVLDADVWR 283
Cdd:cd03261 5 GLTKSfGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVG--LLRPDSGEVL----------------IDGEDISG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 284 kqlLSEEAKINERlKEMDVLRQE---FeeDSLEVkkLDN------EREDLDNHLIqisdklvdmesdkaEARAASILYGL 354
Cdd:cd03261 67 ---LSEAELYRLR-RRMGMLFQSgalF--DSLTV--FENvafplrEHTRLSEEEI--------------REIVLEKLEAV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 355 GFSTEAQQQPTNsFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYL----KTYPNTVLTVSHDRAFLNEV 430
Cdd:cd03261 125 GLRGAEDLYPAE-LSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIrslkKELGLTSIMVTHDLDTAFAI 203
|
250
....*....|..
gi 14318531 431 ATDIIYQHNERL 442
Cdd:cd03261 204 ADRIAVLYDGKI 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
205-442 |
1.67e-12 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 67.70 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 205 DLYVG-DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqelrgddtkalqsVLDADVWR 283
Cdd:COG1127 10 NLTKSfGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG--LLRPDSGEIL----------------VDGQDITG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 284 kqlLSEEAKINERlKEMDVLRQE---FeeDSLEVkkLDN------EREDLDNHLIqisDKLVDMesdKAEaraasiLYGL 354
Cdd:COG1127 72 ---LSEKELYELR-RRIGMLFQGgalF--DSLTV--FENvafplrEHTDLSEAEI---RELVLE---KLE------LVGL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 355 GfstEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDvP----SIAYL-AEYLKTYPNTVLTVSHDRAFLNE 429
Cdd:COG1127 132 P---GAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLD-PitsaVIDELiRELRDELGLTSVVVTHDLDSAFA 207
|
250
....*....|...
gi 14318531 430 VATDIIYQHNERL 442
Cdd:COG1127 208 IADRVAVLADGKI 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
529-731 |
1.81e-12 |
|
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: 67.70 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 529 PPIIQLQDVSFGYDENNLLlKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKG---F----VSRNP-----RLR 596
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVL-HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGsirFdgedITGLPphriaRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 597 IGY-------FTQ-----------HHVDSMDLTTSAVDWMSKSFPgkTDEEYRRHLGsfgitGTlglqkmqlLSGGQKSR 658
Cdd:COG0410 80 IGYvpegrriFPSltveenlllgaYARRDRAEVRADLERVYELFP--RLKERRRQRA-----GT--------LSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 659 VAFA-ALcLNNPHILVLDEPSnhldtTGL-----DALVEALKNFNG---GVLMVSHDISVIDSVCKEIWVSEQGTVkRFE 729
Cdd:COG0410 145 LAIGrAL-MSRPKLLLLDEPS-----LGLaplivEEIFEIIRRLNRegvTILLVEQNARFALEIADRAYVLERGRI-VLE 217
|
..
gi 14318531 730 GT 731
Cdd:COG0410 218 GT 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
531-682 |
2.47e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 67.33 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDV--SFGydeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMeQL-RPLKGFVsrnprlrigyftqhHVDS 607
Cdd:COG1126 1 MIEIENLhkSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCIN-LLeEPDSGTI--------------TVDG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 608 MDLTTSAVDWmsksfpgktdEEYRRHLG----SFG----------ITgtLGLQK-------------MQLL--------- 651
Cdd:COG1126 63 EDLTDSKKDI----------NKLRRKVGmvfqQFNlfphltvlenVT--LAPIKvkkmskaeaeeraMELLervgladka 130
|
170 180 190
....*....|....*....|....*....|....*....
gi 14318531 652 -------SGGQKSRVAFA-ALCLnNPHILVLDEPSNHLD 682
Cdd:COG1126 131 daypaqlSGGQQQRVAIArALAM-EPKVMLFDEPTSALD 168
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
531-723 |
2.78e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.82 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV------------SRNPRLR-- 596
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditrlknREVPFLRrq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 597 IGYFTQHHVDSMDLTTSAVDWMSKSFPGKTDEEYRRHLGSfgitgtlGLQKMQLL----------SGGQKSRVAFAALCL 666
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSA-------ALDKVGLLdkaknfpiqlSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 667 NNPHILVLDEPSNHLDTTGLDALVEALKNFNG---GVLMVSHDISVIDSVCKEIWVSEQG 723
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
526-725 |
2.93e-12 |
|
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: 69.85 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 526 KLSPPIIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMmeqLR---PLKGfvsrnpRLRIgyftq 602
Cdd:COG5265 352 VVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLL---FRfydVTSG------RILI----- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 603 hhvDSMDLTtsavDWMSKSF--------------------------PGKTDEEYRR-----HLGSFgITG------TL-- 643
Cdd:COG5265 418 ---DGQDIR----DVTQASLraaigivpqdtvlfndtiayniaygrPDASEEEVEAaaraaQIHDF-IESlpdgydTRvg 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 644 --GLQkmqlLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTG----LDALVEALKNFNggVLMVSHDIS-VIDsvCKE 716
Cdd:COG5265 490 erGLK----LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTeraiQAALREVARGRT--TLVIAHRLStIVD--ADE 561
|
....*....
gi 14318531 717 IWVSEQGTV 725
Cdd:COG5265 562 ILVLEAGRI 570
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
532-725 |
3.01e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.14 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDE--NNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV-------------------- 589
Cdd:TIGR00958 479 IEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlldgvplvqydhhylhrqva 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 590 ---------SRNPRLRIGYFTQHHVDSMdLTTSAVDWMSKSFPGKTDEEYRRHLGSFGitgtlglqkmQLLSGGQKSRVA 660
Cdd:TIGR00958 559 lvgqepvlfSGSVRENIAYGLTDTPDEE-IMAAAKAANAHDFIMEFPNGYDTEVGEKG----------SQLSGGQKQRIA 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 661 FAALCLNNPHILVLDEPSNHLDTTgLDALVEALKNFNG-GVLMVSHDISVIDSvCKEIWVSEQGTV 725
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAE-CEQLLQESRSRASrTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
203-435 |
3.16e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 66.69 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 203 TFDLYVGDGQRI--LSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELNVPKHVSILHVEQELrgddtkalqsvldaD 280
Cdd:COG4778 13 TFTLHLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWV--------------D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 281 VwrkqllseeAKINERlkEMDVLRQE-------FeedsLE----VKKLDneredldnhliQISDKLVDMESDKAEA--RA 347
Cdd:COG4778 79 L---------AQASPR--EILALRRRtigyvsqF----LRviprVSALD-----------VVAEPLLERGVDREEAraRA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 348 ASILYGLGFSTEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS----IAYLAEyLKTYPNTVLTVSHD 423
Cdd:COG4778 133 RELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEE-AKARGTAIIGIFHD 211
|
250
....*....|..
gi 14318531 424 RAFLNEVATDII 435
Cdd:COG4778 212 EEVREAVADRVV 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
532-692 |
3.44e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 69.60 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS-----------RNPRLRIGYF 600
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidgtdirtvtrASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 601 TQhhvDSMDLTTSAVDWMSKSFPGKTDEEYRRHLGS-----FGITGTLGLQKM-----QLLSGGQKSRVAFAALCLNNPH 670
Cdd:PRK13657 415 FQ---DAGLFNRSIEDNIRVGRPDATDEEMRAAAERaqahdFIERKPDGYDTVvgergRQLSGGERQRLAIARALLKDPP 491
|
170 180
....*....|....*....|..
gi 14318531 671 ILVLDEPsnhldTTGLDALVEA 692
Cdd:PRK13657 492 ILILDEA-----TSALDVETEA 508
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
530-707 |
3.50e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 67.73 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 530 PIIQLQDVSFGYDENN-LLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSrnprlrigyftqhhVDSM 608
Cdd:PRK13635 4 EIIRVEHISFRYPDAAtYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTIT--------------VGGM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 609 DLTTSAVdW-------M-----SKSFPGKT----------------DEEYRRhlgsfgITGTLGLQKMQ--------LLS 652
Cdd:PRK13635 70 VLSEETV-WdvrrqvgMvfqnpDNQFVGATvqddvafglenigvprEEMVER------VDQALRQVGMEdflnrephRLS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 653 GGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFN--GG--VLMVSHDI 707
Cdd:PRK13635 143 GGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeqKGitVLSITHDL 201
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
201-423 |
3.80e-12 |
|
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: 66.24 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 201 IDTFDL-YVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRelnvpkhvsilhveqeLRGDDTKALQSVLDA 279
Cdd:cd03265 1 IEVENLvKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTL----------------LKPTSGRATVAGHDV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 280 dvwrkqlLSEEAKINERLKEMdvlrqeFEEDSLevkklDNEREDLDNHLIQisDKLVDMESDKAEARAASILYGLGFsTE 359
Cdd:cd03265 65 -------VREPREVRRRIGIV------FQDLSV-----DDELTGWENLYIH--ARLYGVPGAERRERIDELLDFVGL-LE 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 360 AQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLK----TYPNTVLTVSHD 423
Cdd:cd03265 124 AADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEklkeEFGMTILLTTHY 191
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
530-709 |
4.27e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 66.38 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 530 PIIQLQDVSFGYDENNLL---LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS---------------- 590
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSVQtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIfngqpmsklssaakae 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 591 -RNPRLriGYFTQ-HHV--DSMDLTTSAVDWM-SKSFPGKTDEEYRRHLGSFGITGTlGLQKMQLLSGGQKSRVAFAALC 665
Cdd:PRK11629 84 lRNQKL--GFIYQfHHLlpDFTALENVAMPLLiGKKKPAEINSRALEMLAAVGLEHR-ANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 14318531 666 LNNPHILVLDEPSNHLDTTGLDALVEALKNFN----GGVLMVSHDISV 709
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNrlqgTAFLVVTHDLQL 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
530-706 |
4.32e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.10 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 530 PIIQLQDVSFGYDeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPR-----------LRIG 598
Cdd:PRK13548 1 AMLEARNLSVRLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwspaelaRRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 599 YFTQHHVDSMDLTTSAVDWMSKS----FPGKTDEEYRRHLGSFGITGtLGLQKMQLLSGGQKSRVAFA-ALC-----LNN 668
Cdd:PRK13548 80 VLPQHSSLSFPFTVEEVVAMGRAphglSRAEDDALVAAALAQVDLAH-LAGRDYPQLSGGEQQRVQLArVLAqlwepDGP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 14318531 669 PHILVLDEPsnhldTTGLD-----ALVEALKNF----NGGVLMVSHD 706
Cdd:PRK13548 159 PRWLLLDEP-----TSALDlahqhHVLRLARQLaherGLAVIVVLHD 200
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
531-697 |
4.47e-12 |
|
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: 66.55 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS--------------RNPRLR 596
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILlegtditklrgkklRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 597 IGYFTQHH--VDSMDL----------TTSAVDWMSKSFPGKTDEEYRRHLGSFGITGtLGLQKMQLLSGGQKSRVAFAAL 664
Cdd:TIGR02315 81 IGMIFQHYnlIERLTVlenvlhgrlgYKPTWRSLLGRFSEEDKERALSALERVGLAD-KAYQRADQLSGGQQQRVAIARA 159
|
170 180 190
....*....|....*....|....*....|...
gi 14318531 665 CLNNPHILVLDEPSNHLDTTGLDALVEALKNFN 697
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRIN 192
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
192-423 |
4.80e-12 |
|
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: 68.93 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 192 SAGKSKDIHIDTFDLYVG--DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSIL---HVEQELR 266
Cdd:TIGR02868 326 GAVGLGKPTLELRDLSAGypGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAG--LLDPLQGEVTldgVPVSSLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 267 GDDTKALQSVLDADVwrkQLLSEEAKINERLKEMDVLRQEFEeDSLEVKKLDNEREDLDNhliqisdklvdmesdkaear 346
Cdd:TIGR02868 404 QDEVRRRVSVCAQDA---HLFDTTVRENLRLARPDATDEELW-AALERVGLADWLRALPD-------------------- 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 347 aasilyglGFSTEAQQQPTnSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDV-PSIAYLAEYLKTYPN-TVLTVSHD 423
Cdd:TIGR02868 460 --------GLDTVLGEGGA-RLSGGERQRLALARALLADAPILLLDEPTEHLDAeTADELLEDLLAALSGrTVVLITHH 529
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
528-697 |
5.13e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.93 E-value: 5.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 528 SPPIIQLQDVSFGYDeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKG-----------FVSRNPRLR 596
Cdd:PRK10253 4 SVARLRGEQLTLGYG-KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGhvwldgehiqhYASKEVARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 597 IGYFTQHHVDSMDLTTSAVDWMSKsFPG--------KTDEE-YRRHLGSFGITgTLGLQKMQLLSGGQKSRVAFAALCLN 667
Cdd:PRK10253 83 IGLLAQNATTPGDITVQELVARGR-YPHqplftrwrKEDEEaVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190
....*....|....*....|....*....|
gi 14318531 668 NPHILVLDEPSNHLDTTGLDALVEALKNFN 697
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELN 190
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
561-705 |
5.66e-12 |
|
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: 65.46 E-value: 5.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 561 IALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPrlrigyftQHHVDSMDLTTSAVDWMSKSfPG-KTD---EE----YRR 632
Cdd:TIGR01189 29 LQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG--------TPLAEQRDEPHENILYLGHL-PGlKPElsaLEnlhfWAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 633 HLGSFGITGTLGLQKMQL----------LSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLD---ALVEALKNFNGG 699
Cdd:TIGR01189 100 IHGGAQRTIEDALAAVGLtgfedlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAllaGLLRAHLARGGI 179
|
....*.
gi 14318531 700 VLMVSH 705
Cdd:TIGR01189 180 VLLTTH 185
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
212-424 |
6.31e-12 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 65.59 E-value: 6.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 212 QRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrrELNVPkhvsilhVEQELRGDDTKALQsvldadvwrkqlLSEEA 291
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILG--GLDRP-------TSGEVRVDGTDISK------------LSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 292 KINERLKEMDVLRQEFeedslevkKLDNEREDLDNhlIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQPtNSFSGG 371
Cdd:cd03255 76 LAAFRRRHIGFVFQSF--------NLLPDLTALEN--VELPLLLAGVPKKERRERAEELLERVGLGDRLNHYP-SELSGG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 372 WRMRLSLARALFCQPDLLLLDEPSNMLDVPS----IAYLAEYLKTYPNTVLTVSHDR 424
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP 201
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
532-726 |
6.32e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.89 E-value: 6.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDE-NNLLLKDVNLDVQMDSRIALVGANGCGKTT---LL---------KIMME----------QLRPLKGF 588
Cdd:PRK11176 342 IEFRNVTFTYPGkEVPALRNINFKIPAGKTVALVGRSGSGKSTianLLtrfydidegEILLDghdlrdytlaSLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 589 VSRNPRL-------RIGYFTQHHVDSMDLTTSAVDWMSKSFPGKTDEEYRRHLGSFGItgtlglqkmqLLSGGQKSRVAF 661
Cdd:PRK11176 422 VSQNVHLfndtianNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGV----------LLSGGQRQRIAI 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 662 AALCLNNPHILVLDEPSNHLDTTGLDALVEALKNF--NGGVLMVSHDISVIDSVcKEIWVSEQGTVK 726
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAALDELqkNRTSLVIAHRLSTIEKA-DEILVVEDGEIV 557
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
525-706 |
9.52e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.17 E-value: 9.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 525 DKLSPPIIQLQDVSFGYDEN-NLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS-----------RN 592
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKidgitiskenlKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 593 PRLRIGYFTQHHvDSMDLTTSAVDWMSKSFPGK--TDEEYRRHLGSF----GITGTLGlQKMQLLSGGQKSRVAFAALCL 666
Cdd:PRK13632 81 IRKKIGIIFQNP-DNQFIGATVEDDIAFGLENKkvPPKKMKDIIDDLakkvGMEDYLD-KEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 14318531 667 NNPHILVLDEPSNHLDTTG----LDALVEALKNFNGGVLMVSHD 706
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGkreiKKIMVDLRKTRKKTLISITHD 202
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
509-723 |
1.01e-11 |
|
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: 68.20 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 509 EPPEQDKtidfkfpecDKLSPP----IIQLQDVSFGY-DENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIM----- 578
Cdd:TIGR02203 313 SPPEKDT---------GTRAIErargDVEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIprfye 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 579 -----------------MEQLRPLKGFVSRNPRL-------RIGYFTQHHVDSMDLTTSAVDWMSKSFPGKTDEEYRRHL 634
Cdd:TIGR02203 384 pdsgqilldghdladytLASLRRQVALVSQDVVLfndtianNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPI 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 635 GSFGItgtlglqkmqLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTG----LDALVEALKNFNGgvLMVSHDISVI 710
Cdd:TIGR02203 464 GENGV----------LLSGGQRQRLAIARALLKDAPILILDEATSALDNESerlvQAALERLMQGRTT--LVIAHRLSTI 531
|
250
....*....|...
gi 14318531 711 DSVcKEIWVSEQG 723
Cdd:TIGR02203 532 EKA-DRIVVMDDG 543
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
205-436 |
1.04e-11 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 65.50 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 205 DLYVG-DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRAlsrrelnvpkhvsILHVEQELRGddtkalqsvldadvwr 283
Cdd:COG1121 11 NLTVSyGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKA-------------ILGLLPPTSG---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 284 kqllseEAKINERLKEMDVLR-----QefeedslevkkldneREDLDNHL-IQISDkLVDM-------------ESDKAE 344
Cdd:COG1121 62 ------TVRLFGKPPRRARRRigyvpQ---------------RAEVDWDFpITVRD-VVLMgrygrrglfrrpsRADREA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 345 ARAASILYGLgfsTEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN---TVLTVS 421
Cdd:COG1121 120 VDEALERVGL---EDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVT 196
|
250
....*....|....*
gi 14318531 422 HDRAFLNEVATDIIY 436
Cdd:COG1121 197 HDLGAVREYFDRVLL 211
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
214-443 |
1.07e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.76 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 214 ILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILHVEQELR-GDDTKALQSVLDadvwRKQLLSEEAK 292
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINF--LEKPSEGSIVVNGQTINlVRDKDGQLKVAD----KNQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 293 INerlkemdVLRQEFEEDSlEVKKLDNEREdldnHLIQIsdklvdMESDKAEARAASILY--GLGFSTEAQQQPTNSFSG 370
Cdd:PRK10619 94 LT-------MVFQHFNLWS-HMTVLENVME----APIQV------LGLSKQEARERAVKYlaKVGIDERAQGKYPVHLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 371 GWRMRLSLARALFCQPDLLLLDEPSNMLD---VPSIAYLAEYLKTYPNTVLTVSHDRAFLNEVATDIIYQHNERLD 443
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
532-734 |
1.21e-11 |
|
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: 65.44 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVS--FGydeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV--------SRNPRLR-IGYF 600
Cdd:cd03296 3 IEVRNVSkrFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggedatDVPVQERnVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 601 TQHHVDSMDLTTSA-VDW---MSKSFPGKTDEEYRRHLGSFgitgtlgLQKMQL----------LSGGQKSRVAFA-ALC 665
Cdd:cd03296 80 FQHYALFRHMTVFDnVAFglrVKPRSERPPEAEIRAKVHEL-------LKLVQLdwladrypaqLSGGQRQRVALArALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 666 LnNPHILVLDEPSNHLDTTGLDALVEALKNFNGGV----LMVSHDISVIDSVCKEIWVSEQGTVKRFeGT---IYD 734
Cdd:cd03296 153 V-EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvttVFVTHDQEEALEVADRVVVMNKGRIEQV-GTpdeVYD 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
207-425 |
1.22e-11 |
|
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: 63.56 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 207 YVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILHVEQELRGddtkalqsvLDADVWRKQl 286
Cdd:cd03228 10 YPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR--LYDPTSGEILIDGVDLRD---------LDLESLRKN- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 287 lseeakinerlkeMDVLRQefeedslevkkldneredlDNHLiqisdklvdmesdkaeaRAASILYglgfsteaqqqptN 366
Cdd:cd03228 78 -------------IAYVPQ-------------------DPFL-----------------FSGTIRE-------------N 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 367 SFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN--TVLTVSHDRA 425
Cdd:cd03228 96 ILSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAHRLS 156
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
532-725 |
1.86e-11 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 64.81 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENN-LLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV-----------SRNPRLRIGY 599
Cdd:cd03252 1 ITFEHVRFRYKPDGpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 600 FTQHHV-------DSMDLTTSAVDwMSK-----------SFPGKTDEEYRRHLGSFGITgtlglqkmqlLSGGQKSRVAF 661
Cdd:cd03252 81 VLQENVlfnrsirDNIALADPGMS-MERvieaaklagahDFISELPEGYDTIVGEQGAG----------LSGGQRQRIAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 662 AALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGG--VLMVSHDISVIDSVCKeIWVSEQGTV 725
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGrtVIIIAHRLSTVKNADR-IIVMEKGRI 214
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
532-710 |
1.89e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.44 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMM--------EQL---RPLKGFVSRNPRLRIGYF 600
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMgyypltegEIRldgRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 601 TQHHV---DSM--------DLTTSAVdW----------MSKSFPGktdeeyrrhlgsfGITGTLGLQKmQLLSGGQKSRV 659
Cdd:PRK10790 421 QQDPVvlaDTFlanvtlgrDISEEQV-WqaletvqlaeLARSLPD-------------GLYTPLGEQG-NNLSVGQKQLL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 14318531 660 AFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNF--NGGVLMVSHDISVI 710
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHRLSTI 538
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
368-725 |
1.96e-11 |
|
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: 67.02 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 368 FSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVpSI-----AYLAEYLKTYPNTVLTVSHDrafLNEVatdiiyqhnerl 442
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVqaqilDLLKDLQRELGMALLLITHD---LGVV------------ 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 443 dyyrgqdfdtfyttkeerRKNAQREY---DNQMVYRKHLQEFIdkyrynaAKSQEAQSRiKKLEKLPVLEPPEQDKTidf 519
Cdd:COG4172 221 ------------------RRFADRVAvmrQGEIVEQGPTAELF-------AAPQHPYTR-KLLAAEPRGDPRPVPPD--- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 520 kfpecdklSPPIIQLQDVSFGYD-ENNLL---------LKDVNLDVQMDSRIALVGANGCGKTTLLKIMM---------- 579
Cdd:COG4172 272 --------APPLLEARDLKVWFPiKRGLFrrtvghvkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLrlipsegeir 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 580 -----------EQLRPLKG---------FVSRNPRLRIGyftQ--------HHvdsmdlttsavdwmsksfPGKTDEEYR 631
Cdd:COG4172 344 fdgqdldglsrRALRPLRRrmqvvfqdpFGSLSPRMTVG---QiiaeglrvHG------------------PGLSAAERR 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 632 RHLGSFgitgtlgLQKMQL-----------LSGGQKSRVAFA-ALCLNnPHILVLDEPsnhldTTGLDALVEA-----LK 694
Cdd:COG4172 403 ARVAEA-------LEEVGLdpaarhrypheFSGGQRQRIAIArALILE-PKLLVLDEP-----TSALDVSVQAqildlLR 469
|
410 420 430
....*....|....*....|....*....|....*
gi 14318531 695 N----FNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:COG4172 470 DlqreHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
369-725 |
2.19e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.19 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNT----VLTVSHDRAFLNEVATDIiyqhnerLDY 444
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmsmgVIFITHDMGVVAEIADRV-------LVM 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 445 YRGQDFDTfyTTKEERRKNAQREYDNQMVYRKHlqefidkyRYNAAKSQEAQSR--IKKLEKLPVLEPP-EQDKTIDfkf 521
Cdd:PRK10261 243 YQGEAVET--GSVEQIFHAPQHPYTRALLAAVP--------QLGAMKGLDYPRRfpLISLEHPAKQEPPiEQDTVVD--- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 522 pecdklSPPIIQLQDVSFGYDENNLLL----------KDVNLDVQMDSRIALVGANGCGKTT----LLKIMMEQ------ 581
Cdd:PRK10261 310 ------GEPILQVRNLVTRFPLRSGLLnrvtrevhavEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVESQggeiif 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 582 ------------LRPLK---------GFVSRNPRLRIGY-----FTQHHVDSMDLTTSAVDWMSKSFpGKTDEEYRRHLG 635
Cdd:PRK10261 384 ngqridtlspgkLQALRrdiqfifqdPYASLDPRQTVGDsimepLRVHGLLPGKAAAARVAWLLERV-GLLPEHAWRYPH 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 636 SFgitgtlglqkmqllSGGQKSRVAFA-ALCLnNPHILVLDEPSNHLDTTG----LDALVEALKNFNGGVLMVSHDISVI 710
Cdd:PRK10261 463 EF--------------SGGQRQRICIArALAL-NPKVIIADEAVSALDVSIrgqiINLLLDLQRDFGIAYLFISHDMAVV 527
|
410
....*....|....*
gi 14318531 711 DSVCKEIWVSEQGTV 725
Cdd:PRK10261 528 ERISHRVAVMYLGQI 542
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
532-727 |
3.14e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 65.04 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENN----LLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS----------RNPRLR- 596
Cdd:PRK13634 3 ITFQKVEHRYQYKTpferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigervitagkKNKKLKp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 597 ----IGY---FTQHHVDSmdlTTSAVD--WMSKSFpGKTDEEYRRH----LGSFGITGTLgLQKMQL-LSGGQKSRVAFA 662
Cdd:PRK13634 83 lrkkVGIvfqFPEHQLFE---ETVEKDicFGPMNF-GVSEEDAKQKaremIELVGLPEEL-LARSPFeLSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 663 ALCLNNPHILVLDEPSNHLDTTGLDALVEAL----KNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVKR 727
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFyklhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
211-439 |
3.20e-11 |
|
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: 62.59 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 211 GQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSIlhveqELRGDDTKALqsvldadvwRKQLLSEE 290
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG--LEEPDSGSI-----LIDGEDLTDL---------EDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 291 AKINerlkemdVLRQEFEedslevkkLDNEREDLDNhliqisdklvdmesdkaearaasILYGLgfsteaqqqptnsfSG 370
Cdd:cd03229 76 RRIG-------MVFQDFA--------LFPHLTVLEN-----------------------IALGL--------------SG 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 371 GWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKT----YPNTVLTVSHDRAFLNEVATDIIYQHN 439
Cdd:cd03229 104 GQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
525-723 |
3.45e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.83 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 525 DKLSPPIIQLQDVSFGYDENnLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS----------RNPR 594
Cdd:PRK13537 1 GPMSVAPIDFRNVEKRYGDK-LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsraRHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 595 LRIGYFTQHHVDSMDLTTSAVDWMSKSFPGKTDEEYRRH---LGSFGITGTLGLQKMQLLSGGQKSRVAFAALCLNNPHI 671
Cdd:PRK13537 80 QRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALvppLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 672 LVLDEPSNHLDTTGLDALVEALKNF---NGGVLMVSHDISVIDSVCKEIWVSEQG 723
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLlarGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
334-423 |
4.93e-11 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 63.96 E-value: 4.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 334 KLVDMESDKAEARAASIL--YGL-GFsteaqqqpTNSF----SGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYL 406
Cdd:COG1116 106 ELRGVPKAERRERARELLelVGLaGF--------EDAYphqlSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERL 177
|
90 100
....*....|....*....|.
gi 14318531 407 AEYL----KTYPNTVLTVSHD 423
Cdd:COG1116 178 QDELlrlwQETGKTVLFVTHD 198
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
201-429 |
5.71e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.49 E-value: 5.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 201 IDTFDLYVGDG-QRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILHVEQELRGDDTKALQSVLda 279
Cdd:PRK11231 3 LRTENLTVGYGtKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFAR--LLTPQSGTVFLGDKPISMLSSRQLARRL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 280 DVWRKQLLSEEA-KINE--------------RLKEMDvlrQEFEEDSLEvkkldneredlDNHLIQISDKLVDmesdkae 344
Cdd:PRK11231 79 ALLPQHHLTPEGiTVRElvaygrspwlslwgRLSAED---NARVNQAME-----------QTRINHLADRRLT------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 345 araasilyglgfsteaqqqptnSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDvpsIAYLAEY------LKTYPNTVL 418
Cdd:PRK11231 138 ----------------------DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD---INHQVELmrlmreLNTQGKTVV 192
|
250
....*....|.
gi 14318531 419 TVSHDrafLNE 429
Cdd:PRK11231 193 TVLHD---LNQ 200
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
199-442 |
5.94e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.11 E-value: 5.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 199 IHIDTFDLYVGDGQrILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHvsilhveqelrGDDTKAlQSVLD 278
Cdd:PRK11124 3 IQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNL--LEMPRS-----------GTLNIA-GNHFD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 279 advwrkqlLSEEAKInerlKEMDVLRQE----FEEDSL--EVKKLDNeredldnhLIQISDKLVDMESDKAEARAASILY 352
Cdd:PRK11124 68 --------FSKTPSD----KAIRELRRNvgmvFQQYNLwpHLTVQQN--------LIEAPCRVLGLSKDQALARAEKLLE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 353 GLGFSTEAQQQPTNsFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDvPSI-AYLAEYLKTYPNTVLT---VSHDRAFLN 428
Cdd:PRK11124 128 RLRLKPYADRFPLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALD-PEItAQIVSIIRELAETGITqviVTHEVEVAR 205
|
250
....*....|....
gi 14318531 429 EVATDIIYQHNERL 442
Cdd:PRK11124 206 KTASRVVYMENGHI 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
544-719 |
6.23e-11 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 63.12 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 544 NNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRN--------PRLR-IGYFTQHHVDSMDLTTS- 613
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlpPEKRdISYVPQNYALFPHMTVYk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 614 --AVDWMSKSFPGKTDEEYRRHLGSF-GITGTLGlQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALV 690
Cdd:cd03299 91 niAYGLKKRKVDKKEIERKVLEIAEMlGIDHLLN-RKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190
....*....|....*....|....*....|...
gi 14318531 691 EALK----NFNGGVLMVSHDISvidsvckEIWV 719
Cdd:cd03299 170 EELKkirkEFGVTVLHVTHDFE-------EAWA 195
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
531-705 |
7.05e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 63.57 E-value: 7.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENN-----LLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVsrnprlrigyftqhHV 605
Cdd:PRK13633 4 MIKCKNVSYKYESNEestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV--------------YV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 606 DSMDLTTSAVDWMSKSFPG-----------------------------------KTDE--------EYRRHlgsfgitgt 642
Cdd:PRK13633 70 DGLDTSDEENLWDIRNKAGmvfqnpdnqivativeedvafgpenlgippeeireRVDEslkkvgmyEYRRH--------- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 643 lglqKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTG----LDALVEALKNFNGGVLMVSH 705
Cdd:PRK13633 141 ----APHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGrrevVNTIKELNKKYGITIILITH 203
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
217-423 |
7.61e-11 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 62.31 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 217 NAQLTLSFGhRYGLVGQNGIGKSTLLRALSrrELNVPKHVSIlhveqelrgddtkalqsVLDADVWrkqllseeakiNER 296
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIA--GLEKPDGGTI-----------------VLNGTVL-----------FDS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 297 LKEMDVLRQE------FEEDSLeVKKLdNEREDLDNHLIQISDKlvdmeSDKAEARAASILYGLgfsTEAQQQPTNSFSG 370
Cdd:cd03297 65 RKKINLPPQQrkiglvFQQYAL-FPHL-NVRENLAFGLKRKRNR-----EDRISVDELLDLLGL---DHLLNRYPAQLSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 371 GWRMRLSLARALFCQPDLLLLDEPSNMLDVPS----IAYLAEYLKTYPNTVLTVSHD 423
Cdd:cd03297 135 GEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLPELKQIKKNLNIPVIFVTHD 191
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
548-707 |
7.84e-11 |
|
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: 62.87 E-value: 7.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 548 LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVsrnpRLRIGYFTQHHVDSMDL--TTSAVDWMS------ 619
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGV----ILEGKQITEPGPDRMVVfqNYSLLPWLTvrenia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 620 ----KSFPGKTDEEYRR----HLGSFGITGTLGLQKMQLlSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVE 691
Cdd:TIGR01184 77 lavdRVLPDLSKSERRAiveeHIALVGLTEAADKRPGQL-SGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180
....*....|....*....|
gi 14318531 692 ALKNF----NGGVLMVSHDI 707
Cdd:TIGR01184 156 ELMQIweehRVTVLMVTHDV 175
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
196-443 |
8.25e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.21 E-value: 8.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 196 SKDIHIDTFDLYVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALS------RRELNVPKHVSILHVEQE----- 264
Cdd:COG4178 360 DGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAglwpygSGRIARPAGARVLFLPQRpylpl 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 265 --LRGddtkalqsvldadvwrkQLL---SEEAKINERLKEmdVLRQefeedsleVKkLDNEREDLDnhliqisdklvdme 339
Cdd:COG4178 440 gtLRE-----------------ALLypaTAEAFSDAELRE--ALEA--------VG-LGHLAERLD-------------- 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 340 sdkAEARAASILyglgfsteaqqqptnsfSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLK-TYPN-TV 417
Cdd:COG4178 478 ---EEADWDQVL-----------------SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLReELPGtTV 537
|
250 260
....*....|....*....|....*.
gi 14318531 418 LTVSHdRAFLNEVatdiiyqHNERLD 443
Cdd:COG4178 538 ISVGH-RSTLAAF-------HDRVLE 555
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
222-447 |
8.81e-11 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 62.39 E-value: 8.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 222 LSF----GHRYGLVGQNGIGKSTLLRALSrrelnvpkhvsilhveQELRGDDTKALQSVLDAdvwrkqlLSEEAKINERL 297
Cdd:cd03266 24 VSFtvkpGEVTGLLGPNGAGKTTTLRMLA----------------GLLEPDAGFATVDGFDV-------VKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 298 KemdvlrqeFEEDSLEVKKLDNEREDLdnhliQISDKLVDMESDKAEARAASILYGLGFStEAQQQPTNSFSGGWRMRLS 377
Cdd:cd03266 81 G--------FVSDSTGLYDRLTARENL-----EYFAGLYGLKGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 378 LARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN---TVLTVSHDRAFLNEVATDIIYQHNERLdYYRG 447
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVLHRGRV-VYEG 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
201-442 |
9.84e-11 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 62.20 E-value: 9.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 201 IDTFDLYVGDGQR-ILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELNVPKhvsiLHVEQE--LRGDDtkalqsVL 277
Cdd:cd03260 1 IELRDLNVYYGDKhALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPG----APDEGEvlLDGKD------IY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 278 DADVwrkqllseeaKINERLKEMDVLRQE--------FEEDSLEVK----KLDNEREDLDNHLIQISDkLVDMESDKAEA 345
Cdd:cd03260 71 DLDV----------DVLELRRRVGMVFQKpnpfpgsiYDNVAYGLRlhgiKLKEELDERVEEALRKAA-LWDEVKDRLHA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 346 RaasilyglgfsteaqqqptnSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIA----YLAEYLKTYpnTVLTVS 421
Cdd:cd03260 140 L--------------------GLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAkieeLIAELKKEY--TIVIVT 197
|
250 260
....*....|....*....|.
gi 14318531 422 HDRAFLNEVATDIIYQHNERL 442
Cdd:cd03260 198 HNMQQAARVADRTAFLLNGRL 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
547-705 |
9.97e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.07 E-value: 9.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 547 LLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRP---------LKGFV--SRNPRLRIGYFTQHH--VDSM----D 609
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkgsgsvlLNGMPidAKEMRAISAYVQQDDlfIPTLtvreH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 610 LTTSAVDWMSKSFPGKTdeeyRRHLGSFGITgTLGLQK-----------MQLLSGGQKSRVAFAALCLNNPHILVLDEPs 678
Cdd:TIGR00955 120 LMFQAHLRMPRRVTKKE----KRERVDEVLQ-ALGLRKcantrigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEP- 193
|
170 180 190
....*....|....*....|....*....|....*
gi 14318531 679 nhldTTGLDA-----LVEALKNF-NGG--VLMVSH 705
Cdd:TIGR00955 194 ----TSGLDSfmaysVVQVLKGLaQKGktIICTIH 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
211-438 |
1.17e-10 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 61.78 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 211 GQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELnvpkhvsilHVEQELRGDDTKalqsvldadvwrkqLLSEE 290
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEE---------PDSGTIIIDGLK--------------LTDDK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 291 AKINERLKEMDVLRQEFEedslevkkLDNEREDLDN-HLIQIsdKLVDMESDKAEARAASILYGLGFSTEAQQQPtNSFS 369
Cdd:cd03262 69 KNINELRQKVGMVFQQFN--------LFPHLTVLENiTLAPI--KVKGMSKAEAEERALELLEKVGLADKADAYP-AQLS 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 370 GGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIaylAEYLKTYPN------TVLTVSHDRAFLNEVATDIIYQH 438
Cdd:cd03262 138 GGQQQRVAIARALAMNPKVMLFDEPTSALDPELV---GEVLDVMKDlaeegmTMVVVTHEMGFAREVADRVIFMD 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
532-725 |
1.25e-10 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 61.78 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDV--SFGydeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS-------------RNPRLR 596
Cdd:cd03262 1 IEIKNLhkSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIidglkltddkkniNELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 597 IGYFTQH-----HVDSMDLTTSAVDW---MSKSfpgKTDEEYRRHLGSFGITGtlglQKMQL---LSGGQKSRVAFA-AL 664
Cdd:cd03262 78 VGMVFQQfnlfpHLTVLENITLAPIKvkgMSKA---EAEERALELLEKVGLAD----KADAYpaqLSGGQQQRVAIArAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 665 CLnNPHILVLDEPSNHLD--TTG--LDALVEALKNfngGVLM--VSHDISVIDSVCKEIWVSEQGTV 725
Cdd:cd03262 151 AM-NPKVMLFDEPTSALDpeLVGevLDVMKDLAEE---GMTMvvVTHEMGFAREVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
530-708 |
2.11e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.08 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 530 PIIQLQDVSFGYDENN-LLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVsrnprlrigYFTQHHVDSM 608
Cdd:PRK13648 6 SIIVFKNVSFQYQSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI---------FYNNQAITDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 609 DLttsavdwmsksfpgktdEEYRRHLG-------------------SFGITG-TLGLQKM-------------------- 648
Cdd:PRK13648 77 NF-----------------EKLRKHIGivfqnpdnqfvgsivkydvAFGLENhAVPYDEMhrrvsealkqvdmleradye 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 649 -QLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTG---LDALVEALK-NFNGGVLMVSHDIS 708
Cdd:PRK13648 140 pNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDArqnLLDLVRKVKsEHNITIISITHDLS 204
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
522-706 |
2.21e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 63.32 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 522 PECDKLSPPIIQLQDVSFGYDeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGfvsrnprlrigyft 601
Cdd:PRK11607 10 AKTRKALTPLLEIRNLTKSFD-GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAG-------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 602 QHHVDSMDLTTSA-----VDWMSKS---FPGKTDEEYRrhlgSFG--------------ITGTLGLQKMQ--------LL 651
Cdd:PRK11607 75 QIMLDGVDLSHVPpyqrpINMMFQSyalFPHMTVEQNI----AFGlkqdklpkaeiasrVNEMLGLVHMQefakrkphQL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 652 SGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDAL----VEALKNFNGGVLMVSHD 706
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqlevVDILERVGVTCVMVTHD 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
548-752 |
2.48e-10 |
|
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: 61.40 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 548 LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKG-------FVSRNP-----RLRIGYFTQHHVDSMDLTT--- 612
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGkilldgqDITKLPmhkraRLGIGYLPQEASIFRKLTVeen 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 613 -SAVDWMSKsfpgkTDEEYRRH-----LGSFGITgTLGLQKMQLLSGGQKSRVAFA-ALCLNnPHILVLDEPsnhldTTG 685
Cdd:cd03218 96 iLAVLEIRG-----LSKKEREEkleelLEEFHIT-HLRKSKASSLSGGERRRVEIArALATN-PKFLLLDEP-----FAG 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 686 LD--------ALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVkRFEGTiydyRDYILQSADaagvVKKH 752
Cdd:cd03218 164 VDpiavqdiqKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV-LAEGT----PEEIAANEL----VRKV 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
538-732 |
2.48e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 62.79 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 538 SFGYDEnnlLLKDVNLDVQMDSRIALVGANGCGKTTLLKIM--MEQ-----LRpLKGF-VSR-NPRLR-IGYFTQHHVDS 607
Cdd:PRK10851 11 SFGRTQ---VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIagLEHqtsghIR-FHGTdVSRlHARDRkVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 608 MDLTTSAvdwmSKSFpGKTDEEYRRHLGSFGITG--TLGLQKMQL----------LSGGQKSRVAFA-ALCLnNPHILVL 674
Cdd:PRK10851 87 RHMTVFD----NIAF-GLTVLPRRERPNAAAIKAkvTQLLEMVQLahladrypaqLSGGQKQRVALArALAV-EPQILLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 675 DEPSNHLDTT-------GLDALVEALKnFNGgvLMVSHD----ISVIDSVC-------------KEIW-------VSE-Q 722
Cdd:PRK10851 161 DEPFGALDAQvrkelrrWLRQLHEELK-FTS--VFVTHDqeeaMEVADRVVvmsqgnieqagtpDQVWrepatrfVLEfM 237
|
250
....*....|
gi 14318531 723 GTVKRFEGTI 732
Cdd:PRK10851 238 GEVNRLQGTI 247
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
209-411 |
2.51e-10 |
|
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: 61.43 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 209 GDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILHVEQELRGDDTKALQSvldadvWRKQ--L 286
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNG--LVEPTSGSVLIDGTDINKLKGKALRQ------LRRQigM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 287 LSEEAKINERLKEMD-VLrqefeedsleVKKLDNEredldnHLIQISDKLVDmESDKAEARAAsiLYGLGFSTEAqQQPT 365
Cdd:cd03256 83 IFQQFNLIERLSVLEnVL----------SGRLGRR------STWRSLFGLFP-KEEKQRALAA--LERVGLLDKA-YQRA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14318531 366 NSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLK 411
Cdd:cd03256 143 DQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLK 188
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
532-734 |
2.72e-10 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 61.10 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKG--FVSRNP-------RLRIGYFTQ 602
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGeiLLDGKDitnlpphKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 603 H-----HVDSMD-----LTtsavdwMSKSFPGKTDEEYRRHLGSFGITGtLGLQKMQLLSGGQKSRVAFAALCLNNPHIL 672
Cdd:cd03300 80 NyalfpHLTVFEniafgLR------LKKLPKAEIKERVAEALDLVQLEG-YANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 673 VLDEPSNHLDTTGLDALVEALKNFNGGV----LMVSHDISVIDSVCKEIWVSEQGTVKRFeGT---IYD 734
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELgitfVFVTHDQEEALTMSDRIAVMNKGKIQQI-GTpeeIYE 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
531-707 |
2.77e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.12 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGY-DENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPlkgfvSRNPRLRIgyftqhHVDSMD 609
Cdd:PRK13640 5 IVEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLP-----DDNPNSKI------TVDGIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 610 LTTSAVdWMSK------------SFPGKTDEEYRrhlgSFGI--------------------TGTLGLQKM--QLLSGGQ 655
Cdd:PRK13640 74 LTAKTV-WDIRekvgivfqnpdnQFVGATVGDDV----AFGLenravprpemikivrdvladVGMLDYIDSepANLSGGQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 656 KSRVAFAALCLNNPHILVLDEPSNHLDTTG----LDALVEALKNFNGGVLMVSHDI 707
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGkeqiLKLIRKLKKKNNLTVISITHDI 204
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
528-724 |
2.78e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.54 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 528 SPPIIQLQDVS--FGydenNLLLKD-VNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVsrnpRLR---IGYFT 601
Cdd:PRK11300 2 SQPLLSVSGLMmrFG----GLLAVNnVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI----LLRgqhIEGLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 602 QHHVDSMDL--TTSAVdwmsKSFPGKTDEE-----YRRHLGSFGITGTLG------------------LQKMQL------ 650
Cdd:PRK11300 74 GHQIARMGVvrTFQHV----RLFREMTVIEnllvaQHQQLKTGLFSGLLKtpafrraesealdraatwLERVGLlehanr 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 651 ----LSGGQKSRVAFAALCLNNPHILVLDEPS---NHLDTTGLDALVEALKN-FNGGVLMVSHDISVIDSVCKEIWVSEQ 722
Cdd:PRK11300 150 qagnLAYGQQRRLEIARCMVTQPEILMLDEPAaglNPKETKELDELIAELRNeHNVTVLLIEHDMKLVMGISDRIYVVNQ 229
|
..
gi 14318531 723 GT 724
Cdd:PRK11300 230 GT 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
547-725 |
2.88e-10 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 61.74 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 547 LLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSrnprLRIGYFTQHHVDSM-----DLTTSAVDWMSKS 621
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVS----FRGQDLYQLDRKQRrafrrDVQLVFQDSPSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 622 FPGKTDE----EYRRHLGSFGITG----TLGLQKM------------QLLSGGQKSRVAFAALCLNNPHILVLDEPSNHL 681
Cdd:TIGR02769 102 NPRMTVRqiigEPLRHLTSLDESEqkarIAELLDMvglrsedadklpRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 14318531 682 D---TTGLDALVEALKN-FNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:TIGR02769 182 DmvlQAVILELLRKLQQaFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
550-728 |
2.94e-10 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 62.43 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 550 DVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRL---------------RIGYFTQHHvdsmdlttsa 614
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrRIGYVFQEA---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 615 vdwmsKSFP----------GKTDEEYRRHLGSF-GITGTLGL-----QKMQLLSGGQKSRVAFA-ALcLNNPHILVLDEP 677
Cdd:COG4148 87 -----RLFPhlsvrgnllyGRKRAPRAERRISFdEVVELLGIghlldRRPATLSGGERQRVAIGrAL-LSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 678 snhldttgLDALVEALKN------------FNGGVLMVSHDISVIDSVCKEIWVSEQGTVKRF 728
Cdd:COG4148 161 --------LAALDLARKAeilpylerlrdeLDIPILYVSHSLDEVARLADHVVLLEQGRVVAS 215
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
531-725 |
4.00e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.67 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENNLL----LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS---------------R 591
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdivvsstskqkeiK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 592 NPRLRIGYFTQHHVDSM--DLTTSAVDWMSKSFpGKTDEEYRR----HLGSFGITGTLGLQKMQLLSGGQKSRVAFAALC 665
Cdd:PRK13643 81 PVRKKVGVVFQFPESQLfeETVLKDVAFGPQNF-GIPKEKAEKiaaeKLEMVGLADEFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 666 LNNPHILVLDEPSNHLDTTG---LDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
207-430 |
4.13e-10 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 60.30 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 207 YVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILHveqelrgDDTKALQsvLDADVWRKQL 286
Cdd:cd03245 12 YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAG--LYKPTSGSVLL-------DGTDIRQ--LDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 287 --LSEEAK-INERLKEMDVLRQEFEEDS--LEVKKLDNEREDLDNHliqisdklvdmesdkaearaasilyGLGFSTEAQ 361
Cdd:cd03245 81 gyVPQDVTlFYGTLRDNITLGAPLADDEriLRAAELAGVTDFVNKH-------------------------PNGLDLQIG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 362 QQPTNsFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTY--PNTVLTVSHDRAFLNEV 430
Cdd:cd03245 136 ERGRG-LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSLLDLV 205
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
532-725 |
4.62e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 61.30 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLL----LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSrnprlrigyftqhhVDS 607
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVR--------------VDD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 608 MDLTTSAVDWMSKS----------FP--------------------GKTDEEY----RRHLGSFGITGTLGLQKMQLLSG 653
Cdd:PRK13649 69 TLITSTSKNKDIKQirkkvglvfqFPesqlfeetvlkdvafgpqnfGVSQEEAealaREKLALVGISESLFEKNPFELSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 654 GQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGG---VLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:PRK13649 149 GQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgmtIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
561-721 |
5.11e-10 |
|
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: 60.50 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 561 IALVGANGCGKTTLLKIMMEQLRPLKGFVSRnPRLRIGYFTQHHvdSMDLTTSAVDWMSKSFPGKTDEEYRRHlgsfGIT 640
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYI--KADYEGTVRDLLSSITKDFYTHPYFKT----EIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 641 GTLGLQKM---QL--LSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNF----NGGVLMVSHDISVID 711
Cdd:cd03237 101 KPLQIEQIldrEVpeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMID 180
|
170
....*....|
gi 14318531 712 SVCKEIWVSE 721
Cdd:cd03237 181 YLADRLIVFE 190
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
532-725 |
5.90e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 60.83 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLL----LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNP-------------R 594
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdiR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 595 LRIGYFTQHHVDSMDLTTSAVD-WMSKSFPGKTDEE-YRRHLGSFGITGtLGLQKMQ-----LLSGGQKSRVAFAALCLN 667
Cdd:PRK13637 83 KKVGLVFQYPEYQLFEETIEKDiAFGPINLGLSEEEiENRVKRAMNIVG-LDYEDYKdkspfELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318531 668 NPHILVLDEPSNHLDTTGLDALVEALKN----FNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKElhkeYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
210-423 |
6.73e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.42 E-value: 6.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRelnVPKHVSILHVEQELRGDDTKALQSVLDadvwRKQLLSE 289
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL---INSQGEIWFDGQPLHNLNRRQLLPVRH----RIQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 290 E--AKINERLKEMDVLrqefeEDSLEVkkldneredldnHLIQISdklvdmeSDKAEARAASILYGLGFSTEAQQQPTNS 367
Cdd:PRK15134 370 DpnSSLNPRLNVLQII-----EEGLRV------------HQPTLS-------AAQREQQVIAVMEEVGLDPETRHRYPAE 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 368 FSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNT----VLTVSHD 423
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhqlaYLFISHD 485
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
211-436 |
6.74e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 60.15 E-value: 6.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 211 GQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELNVPKHVSIlhveqelrGDDTkalqsvLDADvwrKQLLSEE 290
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV--------GDIT------IDTA---RSLSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 291 AKINERLKEMDVLRQEFeedslevkKLDNEREDLDNhLIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQPtNSFSG 370
Cdd:PRK11264 78 GLIRQLRQHVGFVFQNF--------NLFPHRTVLEN-IIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYP-RRLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 371 GWRMRLSLARALFCQPDLLLLDEPSNMLD-------VPSIAYLAEYLKtypnTVLTVSHDRAFLNEVATDIIY 436
Cdd:PRK11264 148 GQQQRVAIARALAMRPEVILFDEPTSALDpelvgevLNTIRQLAQEKR----TMVIVTHEMSFARDVADRAIF 216
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
532-705 |
7.04e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 62.13 E-value: 7.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLK------------IMM-EQLRPLkgFVSRNPRLRIG 598
Cdd:COG4178 363 LALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRaiaglwpygsgrIARpAGARVL--FLPQRPYLPLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 599 yftqhhvdsmDLTtSAVdwmskSFPGK----TDEEYRRHLGSfgitgtLGLQKM-----------QLLSGGQKSRVAFAA 663
Cdd:COG4178 441 ----------TLR-EAL-----LYPATaeafSDAELREALEA------VGLGHLaerldeeadwdQVLSLGEQQRLAFAR 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 14318531 664 LCLNNPHILVLDEPSNHLDTTGLDALVEALKN--FNGGVLMVSH 705
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH 542
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
530-723 |
8.44e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.09 E-value: 8.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 530 PIIQLQDVSFGYDENNLL--------LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS----------- 590
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGLSgkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwrgeplaklnr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 591 -------R-------------NPRLRIGYFTQH---HVDSMDlttsavdwmsksfpgKTDEEYRRH--LGSFGITGTLGL 645
Cdd:PRK10419 82 aqrkafrRdiqmvfqdsisavNPRKTVREIIREplrHLLSLD---------------KAERLARASemLRAVDLDDSVLD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 646 QKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLD---TTGLDALVEALKN-FNGGVLMVSHDISVIDSVCKEIWVSE 721
Cdd:PRK10419 147 KRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlQAGVIRLLKKLQQqFGTACLFITHDLRLVERFCQRVMVMD 226
|
..
gi 14318531 722 QG 723
Cdd:PRK10419 227 NG 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
532-723 |
9.01e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 60.61 E-value: 9.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLL----LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS---------------RN 592
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagyhitpetgnknlKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 593 PRLRIGYFTQHHVDSMDLTTSAVDWM--SKSFpGKTDEEYR----RHLGSFGITGTLGLQKMQLLSGGQKSRVAFAALCL 666
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLFENTVLKDVEfgPKNF-GFSEDEAKekalKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 667 NNPHILVLDEPSNHLDTTGLDALVEALKNFNGG---VLMVSHDISVIDSVCKEIWVSEQG 723
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
213-431 |
9.54e-10 |
|
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: 61.62 E-value: 9.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 213 RILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLnVPKHVSILHVEQELRGDDTKALQSvldadvWRKQL------ 286
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR--L-IPSEGEIRFDGQDLDGLSRRALRP------LRRRMqvvfqd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 287 ----LseeakiNERlkeMDVlrqefeEDSLEvkkldnerEDLDNHLIQISDKLVdmesdkaEARAASILYGLGFSTEAQQ 362
Cdd:COG4172 371 pfgsL------SPR---MTV------GQIIA--------EGLRVHGPGLSAAER-------RARVAEALEEVGLDPAARH 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 363 QPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVpSI-----AYLAEYLKTYPNTVLTVSHD----RAFLNEVA 431
Cdd:COG4172 421 RYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV-SVqaqilDLLRDLQREHGLAYLFISHDlavvRALAHRVM 497
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
209-725 |
1.02e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.64 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 209 GDGQRILSNAQLTLSFGHRYGLVGQNGIGKStlLRALS-RRELNVPKHVSilhveqeLRGDDTKALQSVLDADvwrkqll 287
Cdd:PRK15134 19 QTVRTVVNDVSLQIEAGETLALVGESGSGKS--VTALSiLRLLPSPPVVY-------PSGDIRFHGESLLHAS------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 288 sEEAKINERLKEMDVLrqeFEEDSLEVKKLDNeredLDNHLIQISDKLVDMESDKAEARAASILYGLGFSTEAQQqpTNS 367
Cdd:PRK15134 83 -EQTLRGVRGNKIAMI---FQEPMVSLNPLHT----LEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKR--LTD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 368 F----SGGWRMRLSLARALFCQPDLLLLDEPSNMLDV---PSIAYLAEYLKTYPN-TVLTVSHDRAFLNEVATDI-IYQH 438
Cdd:PRK15134 153 YphqlSGGERQRVMIAMALLTRPELLIADEPTTALDVsvqAQILQLLRELQQELNmGLLFITHNLSIVRKLADRVaVMQN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 439 NERLDYYRGQdfdTFYTTkeerrknAQREYDNQMVyrkhlqefidkyryNAAKSQEAqsrikkleklpvlEPPEQDktid 518
Cdd:PRK15134 233 GRCVEQNRAA---TLFSA-------PTHPYTQKLL--------------NSEPSGDP-------------VPLPEP---- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 519 fkfpecdklSPPIIQLQD--VSFGYDE--------NNLLLKDVNLDVQMDSRIALVGANGCGKTT----LLKIMMEQ--- 581
Cdd:PRK15134 272 ---------ASPLLDVEQlqVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQgei 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 582 ---LRPLKGFVSR--------------------NPRLRI------GYFTQH-HVDSMDLTTSAVDWMSKSfpGKTDEEYR 631
Cdd:PRK15134 343 wfdGQPLHNLNRRqllpvrhriqvvfqdpnsslNPRLNVlqiieeGLRVHQpTLSAAQREQQVIAVMEEV--GLDPETRH 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 632 RHLGSFgitgtlglqkmqllSGGQKSRVAFA-ALCLnNPHILVLDEPSNHLDTTGLDALVEALKNFNG----GVLMVSHD 706
Cdd:PRK15134 421 RYPAEF--------------SGGQRQRIAIArALIL-KPSLIILDEPTSSLDKTVQAQILALLKSLQQkhqlAYLFISHD 485
|
570
....*....|....*....
gi 14318531 707 ISVIDSVCKEIWVSEQGTV 725
Cdd:PRK15134 486 LHVVRALCHQVIVLRQGEV 504
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
230-423 |
1.11e-09 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 59.02 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 230 LVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGddtkalqsvldadvwrkqllseeAKINERLKEMDVLrqeFEE 309
Cdd:cd03293 35 LVGPSGCGKSTLLRIIAG--LERPTSGEVL-----VDG-----------------------EPVTGPGPDRGYV---FQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 310 DSL----EVkkldneredLDNhlIQISDKLVDMESDKAEARAASIL--YGL-GFsteAQQQPtNSFSGGWRMRLSLARAL 382
Cdd:cd03293 82 DALlpwlTV---------LDN--VALGLELQGVPKAEARERAEELLelVGLsGF---ENAYP-HQLSGGMRQRVALARAL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 14318531 383 FCQPDLLLLDEPSNMLDVPSIAYLAEYL----KTYPNTVLTVSHD 423
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELldiwRETGKTVLLVTHD 191
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
530-707 |
1.12e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 59.88 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 530 PIIQLQDVSFGYDENN---LLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRN------PRLRIGYF 600
Cdd:COG4525 2 SMLTVRHVSVRYPGGGqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDgvpvtgPGADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 601 TQHHvdsmdlttSAVDWMSK----SFPGK-----TDEEYRRHLGSFGITGTLGLQKMQL--LSGGQKSRVAFA-ALClNN 668
Cdd:COG4525 82 FQKD--------ALLPWLNVldnvAFGLRlrgvpKAERRARAEELLALVGLADFARRRIwqLSGGMRQRVGIArALA-AD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 14318531 669 PHILVLDEPsnhldTTGLDA---------LVEALKNFNGGVLMVSHDI 707
Cdd:COG4525 153 PRFLLMDEP-----FGALDAltreqmqelLLDVWQRTGKGVFLITHSV 195
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
532-725 |
1.25e-09 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 58.66 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLllkDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGfvsrnpRLRIGYFTQHHVDSMDLT 611
Cdd:cd03298 1 VRLDKIRFSYGEQPM---HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSG------RVLINGVDVTAAPPADRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 612 TSAVDWMSKSFPGKTDEEY-------RRHLGSF------GITGTLGLQKMQL-----LSGGQKSRVAFAALCLNNPHILV 673
Cdd:cd03298 72 VSMLFQENNLFAHLTVEQNvglglspGLKLTAEdrqaieVALARVGLAGLEKrlpgeLSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 674 LDEPSNHLDTT---GLDALVEALKNFNG-GVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:cd03298 152 LDEPFAALDPAlraEMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
211-423 |
1.50e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 59.31 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 211 GQR-ILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrrelnvpkhvsilHVEQELRGddtkalqsvldadvwrkQLLSE 289
Cdd:PRK11247 23 GERtVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLA-------------GLETPSAG-----------------ELLAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 290 EAKINErlkEMDVLRQEFEEDSLEVKK--LDNEREDLDNHLiqisdklvdmesdKAEARAAsiLYGLGFSTEAQQQPTnS 367
Cdd:PRK11247 73 TAPLAE---AREDTRLMFQDARLLPWKkvIDNVGLGLKGQW-------------RDAALQA--LAAVGLADRANEWPA-A 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 368 FSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS---IAYLAEYL-KTYPNTVLTVSHD 423
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTrieMQDLIESLwQQHGFTVLLVTHD 193
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
210-425 |
1.72e-09 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 58.30 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGddtkalQSVLDADVWRKqllse 289
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAG--LERPDSGEIL-----IDG------RDVTGVPPERR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 290 eakinerlkemDVlRQEFEEDSL----EVkkldneredLDNhlIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQPT 365
Cdd:cd03259 73 -----------NI-GMVFQDYALfphlTV---------AEN--IAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPH 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 366 nSFSGGWRMRLSLARALFCQPDLLLLDEP-SNmLDVPSIAYLAEYLKTYPN----TVLTVSHDRA 425
Cdd:cd03259 130 -ELSGGQQQRVALARALAREPSLLLLDEPlSA-LDAKLREELREELKELQRelgiTTIYVTHDQE 192
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
490-723 |
2.08e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.63 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 490 AKSQ---EAQSrIKKLEKLPVLEPPEQDKTIDFKfpecdklSPPIIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGA 566
Cdd:PRK11174 313 AKAQavgAAES-LVTFLETPLAHPQQGEKELASN-------DPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGP 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 567 NGCGKTTL-------------LKIMMEQLRPLK--------GFVSRNPRLRIGyftqhhvdsmdlttSAVDWMSKSFPGK 625
Cdd:PRK11174 385 SGAGKTSLlnallgflpyqgsLKINGIELRELDpeswrkhlSWVGQNPQLPHG--------------TLRDNVLLGNPDA 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 626 TDEEY-----RRHLGSFGITGTLGLQ-----KMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKN 695
Cdd:PRK11174 451 SDEQLqqaleNAWVSEFLPLLPQGLDtpigdQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA 530
|
250 260 270
....*....|....*....|....*....|
gi 14318531 696 FNGG--VLMVSHDISVIDSvCKEIWVSEQG 723
Cdd:PRK11174 531 ASRRqtTLMVTHQLEDLAQ-WDQIWVMQDG 559
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
215-399 |
2.13e-09 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 58.36 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 215 LSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDTKALQsvldadvwrkqllseEAKIN 294
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING--LERPTSGSVL-----VDGTDLTLLS---------------GKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 295 ERLKEMDVLRQEFeedslevkKLDNEREDLDNhlIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQPTNsFSGGWRM 374
Cdd:cd03258 79 KARRRIGMIFQHF--------NLLSSRTVFEN--VALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQ-LSGGQKQ 147
|
170 180
....*....|....*....|....*
gi 14318531 375 RLSLARALFCQPDLLLLDEPSNMLD 399
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALD 172
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
651-734 |
2.20e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 59.71 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 651 LSGGQKSRVAFA-ALClNNPHILVLDEPSNHLD--TTG--LDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:COG1135 141 LSGGQKQRVGIArALA-NNPKVLLCDEATSALDpeTTRsiLDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
....*....
gi 14318531 726 KrFEGTIYD 734
Cdd:COG1135 220 V-EQGPVLD 227
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
536-705 |
2.23e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 536 DVSFGYdENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVsrnprlrigYFTQHHVDSmDLTTSA- 614
Cdd:PRK13540 6 ELDFDY-HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEI---------LFERQSIKK-DLCTYQk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 615 ----VDWMSKSFPGKTDEE---YRRHL--GSFGITGTLGLQKMQ--------LLSGGQKSRVAFAALCLNNPHILVLDEP 677
Cdd:PRK13540 75 qlcfVGHRSGINPYLTLREnclYDIHFspGAVGITELCRLFSLEhlidypcgLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 14318531 678 SNHLDTTGLDAL---VEALKNFNGGVLMVSH 705
Cdd:PRK13540 155 LVALDELSLLTIitkIQEHRAKGGAVLLTSH 185
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
547-705 |
2.45e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 57.54 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 547 LLKDVNLDVQMDSRIALVGANGCGKTTLLKIMM--EQLRPLKGFV----------SRNPRLRIGYFT--QHHVDsmdltt 612
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEIlfkgeditdlPPEERARLGIFLafQYPPE------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 613 savdwmsksFPGKTDEEYRRHLGsfgitgtLGLqkmqllSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEA 692
Cdd:cd03217 89 ---------IPGVKNADFLRYVN-------EGF------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEV 146
|
170
....*....|....*.
gi 14318531 693 LKNF---NGGVLMVSH 705
Cdd:cd03217 147 INKLreeGKSVLIITH 162
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
201-400 |
2.88e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 59.86 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 201 IDTFDLYVGDG-QRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALsrRELNVPKHVSILhveqeLRGDDTKALqsvlDA 279
Cdd:PRK09536 4 IDVSDLSVEFGdTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAI--NGTLTPTAGTVL-----VAGDDVEAL----SA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 280 DVWRKQLLS--EEAKINerlKEMDVlRQEFEED-SLEVKKLDNEREDldnhliqiSDKLVDMESDKAEARAasilyglgF 356
Cdd:PRK09536 73 RAASRRVASvpQDTSLS---FEFDV-RQVVEMGrTPHRSRFDTWTET--------DRAAVERAMERTGVAQ--------F 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 14318531 357 SteaqQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDV 400
Cdd:PRK09536 133 A----DRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
215-423 |
3.18e-09 |
|
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: 58.11 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 215 LSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrrelnvpkhvSILHveqelrgdDTKALQSVLDADVWRKQllseeakiN 294
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILS----------GLLQ--------PTSGEVRVAGLVPWKRR--------K 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 295 ERLKEMDVLRQEFEEDSLEVKKLDNERedLDNHLIQIS--------DKLVDMesdkaeARAASILYglgfsteaqqQPTN 366
Cdd:cd03267 91 KFLRRIGVVFGQKTQLWWDLPVIDSFY--LLAAIYDLPparfkkrlDELSEL------LDLEELLD----------TPVR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 367 SFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTY----PNTVLTVSHD 423
Cdd:cd03267 153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHY 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
214-436 |
3.71e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.80 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 214 ILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRrelnvpkhvsilhVEQELRGDDTKALQSVLDAdvwrkqllseeaKI 293
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINK-------------LEEITSGDLIVDGLKVNDP------------KV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 294 NERLkemdvLRQE----FEEDSL--EVKKLDNeredldnhlIQISDKLV-DMESDKAEARAASILYGLGFSTEAQQQPtN 366
Cdd:PRK09493 71 DERL-----IRQEagmvFQQFYLfpHLTALEN---------VMFGPLRVrGASKEEAEKQARELLAKVGLAERAHHYP-S 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 367 SFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDvPSIAYlaEYLKTYPN------TVLTVSHDRAFLNEVATDIIY 436
Cdd:PRK09493 136 ELSGGQQQRVAIARALAVKPKLMLFDEPTSALD-PELRH--EVLKVMQDlaeegmTMVIVTHEIGFAEKVASRLIF 208
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
210-422 |
3.90e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.86 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRrelNVPKHVSILHVEQELRgddtkalqsVLDADVWRKQL--L 287
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG---FLPYQGSLKINGIELR---------ELDPESWRKHLswV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 288 SEEAkinerlkemdvlrQEFEEdSLevkkldneredLDNHL---IQISDKLVDMESDKAEAraASILYGL--GFSTEAQQ 362
Cdd:PRK11174 429 GQNP-------------QLPHG-TL-----------RDNVLlgnPDASDEQLQQALENAWV--SEFLPLLpqGLDTPIGD 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318531 363 QpTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN--TVLTVSH 422
Cdd:PRK11174 482 Q-AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRrqTTLMVTH 542
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
532-725 |
6.26e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.87 E-value: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENN----LLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS---------------RN 592
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTvdditithktkdkyiRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 593 PRLRIGYFTQHHVDSM--DLTTSAVDWMSKSFPGKTDEEYRRhlgSFGITGTLGLQK--MQL----LSGGQKSRVAFAAL 664
Cdd:PRK13646 83 VRKRIGMVFQFPESQLfeDTVEREIIFGPKNFKMNLDEVKNY---AHRLLMDLGFSRdvMSQspfqMSGGQMRKIAIVSI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 665 CLNNPHILVLDEPSNHLDTTGLDALVEALKNF----NGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqtdeNKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
527-730 |
6.31e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 58.30 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 527 LSPPIIQLQDVSFGYdENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS----------RNPRLR 596
Cdd:PRK13536 37 MSTVAIDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 597 IGYFTQhhVDSMDLTTSAVDWM---SKSFPGKTD--EEYRRHLGSFGITGTLGLQKMQLLSGGQKSRVAFAALCLNNPHI 671
Cdd:PRK13536 116 IGVVPQ--FDNLDLEFTVRENLlvfGRYFGMSTReiEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318531 672 LVLDEPSNHLDTTGLDALVEALKNF---NGGVLMVSHDISVIDSVCKEIWVSEQGtVKRFEG 730
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLlarGKTILLTTHFMEEAERLCDRLCVLEAG-RKIAEG 254
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
210-410 |
6.76e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 56.21 E-value: 6.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrrELNVPkhvsilhVEQELRGDDTKALQSvldADVWRKQLLSe 289
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILA--GLLRP-------DSGEVRWNGTPLAEQ---RDEPHENILY- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 290 eakinerLKEMDVLRQEfeedsLEV-KKLDNEREDLDNHLIQISDKLVDMesdkaearaasilyGLgfsTEAQQQPTNSF 368
Cdd:TIGR01189 78 -------LGHLPGLKPE-----LSAlENLHFWAAIHGGAQRTIEDALAAV--------------GL---TGFEDLPAAQL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYL 410
Cdd:TIGR01189 129 SAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
527-682 |
7.23e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.09 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 527 LSPPIIQLQDVSFGYDENNLLlKDVNLDVQMDSRIALVGANGCGKTTLLKIM--MEQLRP---LKGFVSRN------PR- 594
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKAL-NSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNghniysPRt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 595 ----LR--IGY-FTQHHVDSMDLTTSAV---------------DWMSKSFPGKT--DE-EYRRHLGSFGitgtlglqkmq 649
Cdd:PRK14239 80 dtvdLRkeIGMvFQQPNPFPMSIYENVVyglrlkgikdkqvldEAVEKSLKGASiwDEvKDRLHDSALG----------- 148
|
170 180 190
....*....|....*....|....*....|...
gi 14318531 650 lLSGGQKSRVAFAALCLNNPHILVLDEPSNHLD 682
Cdd:PRK14239 149 -LSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
561-711 |
7.59e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 561 IALVGANGCGKTTLLKIMMEQLRPLKGFVSRNP-------RLRiG-----YFTQhhVDSMDLTTS----AVDWMSKSFPG 624
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswdevlkRFR-GtelqnYFKK--LYNGEIKVVhkpqYVDLIPKVFKG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 625 KTDEEYRR--HLGSFG-ITGTLGL-----QKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLD----TTGLDALVEA 692
Cdd:PRK13409 179 KVRELLKKvdERGKLDeVVERLGLenildRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqrLNVARLIREL 258
|
170
....*....|....*....
gi 14318531 693 LKNFNggVLMVSHDISVID 711
Cdd:PRK13409 259 AEGKY--VLVVEHDLAVLD 275
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
210-422 |
8.24e-09 |
|
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: 57.02 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRelNVP---KHVSILhvEQELRGddtkalqsvldADVW--RK 284
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGD--LPPtygNDVRLF--GERRGG-----------EDVWelRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 285 Q--LLSEE--AKINERLKEMDVLRQEFEeDSLevkkldnereDLDNHLiqisdklvdmeSDKAEARAASILYGLGFSTEA 360
Cdd:COG1119 79 RigLVSPAlqLRFPRDETVLDVVLSGFF-DSI----------GLYREP-----------TDEQRERARELLELLGLAHLA 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 361 QQqPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS----IAYLAEYLKTYPNTVLTVSH 422
Cdd:COG1119 137 DR-PFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
210-399 |
9.09e-09 |
|
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: 56.05 E-value: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGhRYGLVGQNGIGKSTLLRALSrrELNVPKHVSILHVEQELRGDDTKALQSV--LDADV-WRKQL 286
Cdd:cd03264 11 GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILA--TLTPPSSGTIRIDGQDVLKQPQKLRRRIgyLPQEFgVYPNF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 287 LSEEAkinerLKEMDVLRqefeedslevkkldneredldnhliqisdklvDMESDKAEARAASILYGLGFSTEAQQqPTN 366
Cdd:cd03264 88 TVREF-----LDYIAWLK--------------------------------GIPSKEVKARVDEVLELVNLGDRAKK-KIG 129
|
170 180 190
....*....|....*....|....*....|...
gi 14318531 367 SFSGGWRMRLSLARALFCQPDLLLLDEPSNMLD 399
Cdd:cd03264 130 SLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
528-705 |
9.17e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.40 E-value: 9.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 528 SPPIIQLQDVSFGYDENNLLLKdvnLDVQMDSRIALV--GANGCGKTTLLKIMMEQLRPLKGFV-------SRNPRLR-I 597
Cdd:PRK13543 8 APPLLAAHALAFSRNEEPVFGP---LDFHVDAGEALLvqGDNGAGKTTLLRVLAGLLHVESGQIqidgktaTRGDRSRfM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 598 GYFTqhHVDSMDLTTSAVDWM----------SKSFPGKTdeeyrrhLGSFGITG---TLGLQkmqlLSGGQKSRVAFAAL 664
Cdd:PRK13543 85 AYLG--HLPGLKADLSTLENLhflcglhgrrAKQMPGSA-------LAIVGLAGyedTLVRQ----LSAGQKKRLALARL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 14318531 665 CLNNPHILVLDEPSNHLDTTG---LDALVEALKNFNGGVLMVSH 705
Cdd:PRK13543 152 WLSPAPLWLLDEPYANLDLEGitlVNRMISAHLRGGGAALVTTH 195
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
561-721 |
9.29e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 55.66 E-value: 9.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 561 IALVGANGCGKTTLLKIMMEQLRPLKGfvsrnprlrigyftqhhVDSMDLTTSAVDwmsksfPGKTDeeyrrhlgsfgit 640
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGD-----------------NDEWDGITPVYK------PQYID------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 641 gtlglqkmqlLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNF----NGGVLMVSHDISVIDSVCKE 716
Cdd:cd03222 72 ----------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYLSDR 141
|
....*
gi 14318531 717 IWVSE 721
Cdd:cd03222 142 IHVFE 146
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
193-459 |
1.02e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.98 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 193 AGKSKD--IHIDTFDLYVGDgQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRrelnvpkhvsILHVEQELRGDDT 270
Cdd:PRK14246 3 AGKSAEdvFNISRLYLYIND-KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNR----------LIEIYDSKIKVDG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 271 KALqsVLDADVWRKQLLSEEAKINErlkemdVLRQEFEEDSLEVkkLDNEREDLDNHLIQisdklvdmesDKAEAR--AA 348
Cdd:PRK14246 72 KVL--YFGKDIFQIDAIKLRKEVGM------VFQQPNPFPHLSI--YDNIAYPLKSHGIK----------EKREIKkiVE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 349 SILYGLGFSTEAQQQ---PTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN--TVLTVSHD 423
Cdd:PRK14246 132 ECLRKVGLWKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
250 260 270
....*....|....*....|....*....|....*.
gi 14318531 424 RAFLNEVATDIIYQHNERLDYYrGQDFDTFYTTKEE 459
Cdd:PRK14246 212 PQQVARVADYVAFLYNGELVEW-GSSNEIFTSPKNE 246
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
231-435 |
1.02e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 57.67 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 231 VGQNGIGKSTLLRALSRRElnVPkhvsilhVEQELRGDDtkalQSVLDADVWRKQLLSEEAKI---------NERLKEMD 301
Cdd:PRK11308 47 VGESGCGKSTLARLLTMIE--TP-------TGGELYYQG----QDLLKADPEAQKLLRQKIQIvfqnpygslNPRKKVGQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 302 VLrqefeEDSLevkkldneredldnhliQISDKLvdmesDKAE--ARAASILYGLGFSTEAQQQPTNSFSGGWRMRLSLA 379
Cdd:PRK11308 114 IL-----EEPL-----------------LINTSL-----SAAErrEKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318531 380 RALFCQPDLLLLDEPSNMLDVpSI--------AYLAEYLKTypnTVLTVSHDRAFLNEVATDII 435
Cdd:PRK11308 167 RALMLDPDVVVADEPVSALDV-SVqaqvlnlmMDLQQELGL---SYVFISHDLSVVEHIADEVM 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
532-725 |
1.14e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 56.30 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDEnnlLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGfvsrnpRLRIgyftqhhvDSMDLT 611
Cdd:COG3840 2 LRLDDLTYRYGD---FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSG------RILW--------NGQDLT 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 612 TSAVDW--MSKSF--------------------PG-KTDEEYRRH----LGSFGITGtLGLQKMQLLSGGQKSRVAFA-A 663
Cdd:COG3840 65 ALPPAErpVSMLFqennlfphltvaqniglglrPGlKLTAEQRAQveqaLERVGLAG-LLDRLPGQLSGGQRQRVALArC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318531 664 LCLNNPhILVLDEP-SNhldttgLD--------ALVEAL-KNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:COG3840 144 LVRKRP-ILLLDEPfSA------LDpalrqemlDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRI 208
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
534-708 |
1.20e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.61 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 534 LQDVSFGYDENNLLlKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGfvsrnpRLRIGYFTQHHV-------- 605
Cdd:PRK11247 15 LNAVSKRYGERTVL-NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG------ELLAGTAPLAEAredtrlmf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 606 -DSMDLT-TSAVDWMSKSFPGKTDEEYRRHLGSFGITGTLGlQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDT 683
Cdd:PRK11247 88 qDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRAN-EWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180
....*....|....*....|....*....
gi 14318531 684 -TGLD--ALVEALKNFNG-GVLMVSHDIS 708
Cdd:PRK11247 167 lTRIEmqDLIESLWQQHGfTVLLVTHDVS 195
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
531-710 |
1.21e-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: 58.61 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEqLRPLK-GFVSRNPRLRIGYFTQHhvDSMD 609
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGE-LWPVYgGRLTKPAKGKLFYVPQR--PYMT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 610 LTT---------SAVDWMSKSFPGKTDEEYRR--HLGSFgITGTLGLQKMQ----LLSGGQKSRVAFAALCLNNPHILVL 674
Cdd:TIGR00954 528 LGTlrdqiiypdSSEDMKRRGLSDKDLEQILDnvQLTHI-LEREGGWSAVQdwmdVLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....*.
gi 14318531 675 DEPSNHLDTTGLDALVEALKNFNGGVLMVSHDISVI 710
Cdd:TIGR00954 607 DECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLW 642
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
565-718 |
1.32e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.58 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 565 GANGCGKTTLLKIMMEQLRPLKGFVSRN----PRLRIGYFTQ-----HH--VDSmDLTtsAV---DWMSKSFPGKTDEEY 630
Cdd:PRK13538 34 GPNGAGKTSLLRILAGLARPDAGEVLWQgepiRRQRDEYHQDllylgHQpgIKT-ELT--ALenlRFYQRLHGPGDDEAL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 631 RRHLGSFGITGTLGLQKMQLlSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLdALVEALknF-----NGG-VLMVS 704
Cdd:PRK13538 111 WEALAQVGLAGFEDVPVRQL-SAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV-ARLEAL--LaqhaeQGGmVILTT 186
|
170
....*....|....*
gi 14318531 705 H-DISVIDSVCKEIW 718
Cdd:PRK13538 187 HqDLPVASDKVRKLR 201
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
362-431 |
1.41e-08 |
|
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: 57.43 E-value: 1.41e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318531 362 QQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNT----VLTVSHDrafLNEVA 431
Cdd:TIGR02142 126 GRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEfgipILYVSHS---LQEVL 196
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
366-430 |
1.48e-08 |
|
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: 54.92 E-value: 1.48e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 366 NSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAE---YLKTYPNTVLTVSHDRAFLNEV 430
Cdd:cd03246 95 NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQaiaALKAAGATRIVIAHRPETLASA 162
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
210-425 |
1.55e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 55.32 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALS--RR----ELNVPKHVSILHVEQELRGDDTKALqSVLDA---D 280
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAgvLRptsgTVRRAGGARVAYVPQRSEVPDSLPL-TVRDLvamG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 281 VWRKQLLSEeakineRLKemdvlrqefeedslevkkldneREDldnhliqisdklvdmesdkaEARAASILYGLGFsTEA 360
Cdd:NF040873 82 RWARRGLWR------RLT----------------------RDD--------------------RAAVDDALERVGL-ADL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 361 QQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN---TVLTVSHDRA 425
Cdd:NF040873 113 AGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLE 180
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
215-431 |
1.61e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 56.71 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 215 LSNAQLTLSFGHRYGLVGQNGIGKSTLlralsrrelnvpkhvsILHVEQELRgdDTKALQSVLDADVWRKqllSEEAKIN 294
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTL----------------IQNINALLK--PTTGTVTVDDITITHK---TKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 295 ERLKEMDVLRQEFEEDSLEvkklDN-EREdldnhlIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQPTNSFSGGWR 373
Cdd:PRK13646 82 PVRKRIGMVFQFPESQLFE----DTvERE------IIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318531 374 MRLSLARALFCQPDLLLLDEPSNMLDVPS---IAYLAEYLKTYPN-TVLTVSHDrafLNEVA 431
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSkrqVMRLLKSLQTDENkTIILVSHD---MNEVA 210
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
561-711 |
1.64e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 561 IALVGANGCGKTTLLKIMMEQLRPLKGFVSRNP-------RLRiG-----YFTQhhVDSMDLTTS----AVDWMSKSFPG 624
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDEEPswdevlkRFR-GtelqdYFKK--LANGEIKVAhkpqYVDLIPKVFKG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 625 -------KTDEEyrrhlGSF-GITGTLGLQKM-----QLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVE 691
Cdd:COG1245 179 tvrelleKVDER-----GKLdELAEKLGLENIldrdiSELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVAR 253
|
170 180
....*....|....*....|...
gi 14318531 692 ALKNF---NGGVLMVSHDISVID 711
Cdd:COG1245 254 LIRELaeeGKYVLVVEHDLAILD 276
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
531-731 |
1.67e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 56.53 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV----------SRNPRLR--IG 598
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgdfSKLQGIRklVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 599 YFTQHHvdsmdlttsavdwmSKSFPGKTDEEYRrhlgSFG-----------------ITGTLGLQKM-----QLLSGGQK 656
Cdd:PRK13644 81 IVFQNP--------------ETQFVGRTVEEDL----AFGpenlclppieirkrvdrALAEIGLEKYrhrspKTLSGGQG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 657 SRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFN---GGVLMVSHDISVIdSVCKEIWVSEQGTVkRFEGT 731
Cdd:PRK13644 143 QCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHekgKTIVYITHNLEEL-HDADRIIVMDRGKI-VLEGE 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
528-705 |
1.91e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.34 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 528 SPPIIQLQDVS--FGydeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRP------LKG--FVSRNPR--- 594
Cdd:COG1129 1 AEPLLEMRGISksFG---GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPdsgeilLDGepVRFRSPRdaq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 595 -LRIGYFTQH--HVDSMD-----------LTTSAVDWmsksfpGKTDEEYRRHLGSFGIT-------GTLGLQKMQLlsg 653
Cdd:COG1129 78 aAGIAIIHQElnLVPNLSvaeniflgrepRRGGLIDW------RAMRRRARELLARLGLDidpdtpvGDLSVAQQQL--- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 654 gqksrVAFA-ALcLNNPHILVLDEPsnhldTTGLD--------ALVEALKNFNGGVLMVSH 705
Cdd:COG1129 149 -----VEIArAL-SRDARVLILDEP-----TASLTereverlfRIIRRLKAQGVAIIYISH 198
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
528-706 |
1.91e-08 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 55.52 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 528 SPPIIQLQDV--SFGYDENNL-LLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVsrnprlrigyftqhH 604
Cdd:COG4181 5 SAPIIELRGLtkTVGTGAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTV--------------R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 605 VDSMDLTTsavdwmsksfpgkTDEEYR-----RHLG----SFGITGTL------------------------GLQKMQL- 650
Cdd:COG4181 71 LAGQDLFA-------------LDEDARarlraRHVGfvfqSFQLLPTLtalenvmlplelagrrdarararaLLERVGLg 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 651 ---------LSGGQKSRVAFA-ALcLNNPHILVLDEPSNHLDT-TG---LDALvEALKNFNGGVL-MVSHD 706
Cdd:COG4181 138 hrldhypaqLSGGEQQRVALArAF-ATEPAILFADEPTGNLDAaTGeqiIDLL-FELNRERGTTLvLVTHD 206
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
533-706 |
1.98e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 55.18 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 533 QLQDVSFGYDeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPlkGFvSRNPRLRIgyftqhhvDSMDLTT 612
Cdd:COG4136 3 SLENLTITLG-GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSP--AF-SASGEVLL--------NGRRLTA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 613 SAVdwmsksfpgktdeeYRRHLG------------------SFGITGTLG-----------LQKMQL----------LSG 653
Cdd:COG4136 71 LPA--------------EQRRIGilfqddllfphlsvgenlAFALPPTIGraqrrarveqaLEEAGLagfadrdpatLSG 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 654 GQKSRVAFAALCLNNPHILVLDEPSNHLDTT---GLDALV-EALKNFNGGVLMVSHD 706
Cdd:COG4136 137 GQRARVALLRALLAEPRALLLDEPFSKLDAAlraQFREFVfEQIRQRGIPALLVTHD 193
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
530-725 |
2.06e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 57.16 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 530 PIIQLQD--VSFGydeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV-----------SRNPRLR 596
Cdd:PRK09536 2 PMIDVSDlsVEFG---DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVlvagddvealsARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 597 IGYFTQHHVDSMDLTTSAVDWMSKS-----FPGKTDEEYRRHLGSFGITGTLGL--QKMQLLSGGQKSRVAFA-ALCLNN 668
Cdd:PRK09536 79 VASVPQDTSLSFEFDVRQVVEMGRTphrsrFDTWTETDRAAVERAMERTGVAQFadRPVTSLSGGERQRVLLArALAQAT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 669 PhILVLDEPSNHLD------TTgldALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:PRK09536 159 P-VLLLDEPTASLDinhqvrTL---ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
369-435 |
2.08e-08 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 56.69 E-value: 2.08e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEPSNMLDvpsiAYLA--------EYLKTYPNTVLTVSHDR--AFlnEVATDII 435
Cdd:COG1118 135 SGGQRQRVALARALAVEPEVLLLDEPFGALD----AKVRkelrrwlrRLHDELGGTTVFVTHDQeeAL--ELADRVV 205
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
531-707 |
2.13e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 55.86 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVS--F--GYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGfvsrnprlRIgyftqhHVD 606
Cdd:COG1101 1 MLELKNLSktFnpGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSG--------SI------LID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 607 SMDLTTSAVD----WMSKSF--------PGKTDEE-----YRRHLG---SFGITG-----------TLGL-------QKM 648
Cdd:COG1101 67 GKDVTKLPEYkrakYIGRVFqdpmmgtaPSMTIEEnlalaYRRGKRrglRRGLTKkrrelfrellaTLGLglenrldTKV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 649 QLLSGGQKSRVAFAALCLNNPHILVLDEpsnHldTTGLD----ALVEAL-----KNFNGGVLMVSHDI 707
Cdd:COG1101 147 GLLSGGQRQALSLLMATLTKPKLLLLDE---H--TAALDpktaALVLELtekivEENNLTTLMVTHNM 209
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
212-423 |
2.35e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.85 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 212 QRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALsrrelnvpkhvsiLHVEQELRGDDTkalqsvldadvWRKQLLSEEA 291
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLL-------------VGLESPSQGNVS-----------WRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 292 KINERLKEMDVlrQEFEEDSLEVKkldNEREDLDNHLIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQPTNSFSGG 371
Cdd:PRK10419 81 RAQRKAFRRDI--QMVFQDSISAV---NPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 372 WRMRLSLARALFCQPDLLLLDEP-SN---MLDVPSIAYLAEYLKTYPNTVLTVSHD 423
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAvSNldlVLQAGVIRLLKKLQQQFGTACLFITHD 211
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
214-422 |
2.46e-08 |
|
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: 55.17 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 214 ILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILHVEQELRGDDTKALQSVLdadvwrkQLLSEEAKI 293
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLEN--FYQPQGGQVLLDGKPISQYEHKYLHSKV-------SLVGQEPVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 294 NERlkemdvlrqefeedSLevkkldneREDLDNHLIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQpTNSFSGGWR 373
Cdd:cd03248 100 FAR--------------SL--------QDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEK-GSQLSGGQK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 14318531 374 MRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN--TVLTVSH 422
Cdd:cd03248 157 QRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
207-402 |
2.66e-08 |
|
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: 55.18 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 207 YVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDTkalqSVLDADVWRKQL 286
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQR--FYVPENGRVL-----VDGHDL----ALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 287 lseeakinerlkemDVLRQEfeedslevKKLDNeREDLDNhlIQISDKLVDMESDKAEARAAS----IL-YGLGFSTEAQ 361
Cdd:cd03252 79 --------------GVVLQE--------NVLFN-RSIRDN--IALADPGMSMERVIEAAKLAGahdfISeLPEGYDTIVG 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 14318531 362 QQPTnSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS 402
Cdd:cd03252 134 EQGA-GLSGGQRQRIAIARALIHNPRILIFDEATSALDYES 173
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
532-706 |
2.71e-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: 54.95 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGfvsrnpRLRIGYFTQHHVDSMDLT 611
Cdd:cd03301 1 VELENVTKRFG-NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSG------RIYIGGRDVTDLPPKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 612 TSAV-------------DWMS------KSFPGKTDEEYRRHLGSFGITGTLGlQKMQLLSGGQKSRVAFAALCLNNPHIL 672
Cdd:cd03301 74 IAMVfqnyalyphmtvyDNIAfglklrKVPKDEIDERVREVAELLQIEHLLD-RKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 14318531 673 VLDEP-SNhldttgLDA---------LVEALKNFNGGVLMVSHD 706
Cdd:cd03301 153 LMDEPlSN------LDAklrvqmraeLKRLQQRLGTTTIYVTHD 190
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
215-423 |
2.80e-08 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 55.16 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 215 LSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrrELNVPKHVSILHVEQELR--GDDTKALQSVLDADVWRKqllseeAK 292
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLIS--GLAQPTSGGVILEGKQITepGPDRMVVFQNYSLLPWLT------VR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 293 INERLKEMDVLRQEFEEdslevkkldnEREDLDNHLIQisdklvdmesdkaearaasiLYGLgfsTEAQQQPTNSFSGGW 372
Cdd:TIGR01184 73 ENIALAVDRVLPDLSKS----------ERRAIVEEHIA--------------------LVGL---TEAADKRPGQLSGGM 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 373 RMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN----TVLTVSHD 423
Cdd:TIGR01184 120 KQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEehrvTVLMVTHD 174
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
212-442 |
2.90e-08 |
|
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: 55.58 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 212 QRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELNVPKHVSILHVE-QELRGDDTKALQSVLdadvwrkQLLSEE 290
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDlYQLDRKQRRAFRRDV-------QLVFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 291 A--KINERLKEMDVLRQEFEEdslevkkldneredldnhliqisdkLVDMESDKAEARAASILYGLGFSTEAQQQPTNSF 368
Cdd:TIGR02769 97 SpsAVNPRMTVRQIIGEPLRH-------------------------LTSLDESEQKARIAELLDMVGLRSEDADKLPRQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEPSNMLDV---PSIAYLAEYLKTYPNTV-LTVSHDRAFLNEVATDIIYQHNERL 442
Cdd:TIGR02769 152 SGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqAVILELLRKLQQAFGTAyLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
530-731 |
2.95e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.68 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 530 PIIQLQDVSFGYDE--NNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRP-------LKGFVSRNPRLR---- 596
Cdd:PLN03232 613 PAISIKNGYFSWDSktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaetssvvIRGSVAYVPQVSwifn 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 597 ----------IGYFTQHHVDSMDLTTSAVDWmsKSFPGKTdeeyRRHLGSFGITgtlglqkmqlLSGGQKSRVAFAALCL 666
Cdd:PLN03232 693 atvrenilfgSDFESERYWRAIDVTALQHDL--DLLPGRD----LTEIGERGVN----------ISGGQKQRVSMARAVY 756
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318531 667 NNPHILVLDEPsnhldTTGLDALVeALKNFNGGV---------LMVSHDISVIDSVCKEIWVSEqGTVKRfEGT 731
Cdd:PLN03232 757 SNSDIYIFDDP-----LSALDAHV-AHQVFDSCMkdelkgktrVLVTNQLHFLPLMDRIILVSE-GMIKE-EGT 822
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
215-435 |
3.52e-08 |
|
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: 54.75 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 215 LSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRElnVPKHVSILhveqeLRGDDTKALQSvldADVWRK------QLLS 288
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFL--RPTSGSVL-----FDGEDITGLPP---HEIARLgigrtfQIPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 289 EeakinerLKEMDVLrqefeeDSLEVKKLDNEREDLdnhliqISDKLVDMESDkAEARAASIL--YGLGfstEAQQQPTN 366
Cdd:cd03219 86 L-------FPELTVL------ENVMVAAQARTGSGL------LLARARREERE-ARERAEELLerVGLA---DLADRPAG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318531 367 SFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN---TVLTVSHDRAFLNEVATDII 435
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRErgiTVLLVEHDMDVVMSLADRVT 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
529-682 |
3.99e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.11 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 529 PPIIQLQDVSFGYDeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLlkimmeqLRPLKGFVSRNpRLRIgyftqhHVDSM 608
Cdd:PRK09452 12 SPLVELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTV-------LRLIAGFETPD-SGRI------MLDGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 609 DLT-TSA----VDWMSKS---FPGKT----------------DEEYRR--------HLGSFgitgtlGLQKMQLLSGGQK 656
Cdd:PRK09452 77 DIThVPAenrhVNTVFQSyalFPHMTvfenvafglrmqktpaAEITPRvmealrmvQLEEF------AQRKPHQLSGGQQ 150
|
170 180
....*....|....*....|....*.
gi 14318531 657 SRVAFAALCLNNPHILVLDEPSNHLD 682
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
210-399 |
4.15e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 56.00 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrrelnvpkhvsilHVEQELRGddtkalQSVLDAdvwrkQLLSE 289
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLA-------------GFEQPTAG------QIMLDG-----VDLSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 290 EAKINERLKEMDVLRQEFEEDSLEvkkldnerEDLDNHLIQisDKLvdmESDKAEARAASILYGLGFSTEAQQQPtNSFS 369
Cdd:PRK11607 86 VPPYQRPINMMFQSYALFPHMTVE--------QNIAFGLKQ--DKL---PKAEIASRVNEMLGLVHMQEFAKRKP-HQLS 151
|
170 180 190
....*....|....*....|....*....|
gi 14318531 370 GGWRMRLSLARALFCQPDLLLLDEPSNMLD 399
Cdd:PRK11607 152 GGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
201-422 |
4.25e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.92 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 201 IDTFDLYVGDGQ-RILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRrelnvpkhVSILHVEQELRGDDTKALQSVLDA 279
Cdd:PRK14247 4 IEIRDLKVSFGQvEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNR--------LIELYPEARVSGEVYLDGQDIFKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 280 DVW----RKQLLSEeakINERLKEMDVlrqeFEEDSLEVK--KLDNEREDLDNHLIQISDK--LVDMESDKAEAraasil 351
Cdd:PRK14247 76 DVIelrrRVQMVFQ---IPNPIPNLSI----FENVALGLKlnRLVKSKKELQERVRWALEKaqLWDEVKDRLDA------ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 352 yglgfsteaqqqPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAE-YLKTYPN-TVLTVSH 422
Cdd:PRK14247 143 ------------PAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESlFLELKKDmTIVLVTH 203
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
212-425 |
4.40e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.93 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 212 QRILSNAQLTLSFGHRYGL---------------VGQNGIGKSTLLRALSRRElnVPKHVSILHveqELRGDDTKALQSV 276
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCrdvsfdlypgevlgiVGESGSGKTTLLNALSARL--APDAGEVHY---RMRDGQLRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 277 LDADvwRKQLLSEE-------------------AKINERLkeMDV-------LRQEfEEDSLEVKKLDNERedldnhliq 330
Cdd:PRK11701 79 SEAE--RRRLLRTEwgfvhqhprdglrmqvsagGNIGERL--MAVgarhygdIRAT-AGDWLERVEIDAAR--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 331 ISDklvdmesdkaearaasilyglgfsteaqqQPTnSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYL 410
Cdd:PRK11701 145 IDD-----------------------------LPT-TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLL 194
|
250
....*....|....*....
gi 14318531 411 KTYPNT----VLTVSHDRA 425
Cdd:PRK11701 195 RGLVRElglaVVIVTHDLA 213
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
369-430 |
4.57e-08 |
|
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: 56.30 E-value: 4.57e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEP-SNmLDVPSIAYLAE---YLKTYPNTVLTVSHDRAFLNEV 430
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPnSN-LDDEGEAALAAairALKARGATVVVITHRPSLLAAV 533
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
213-682 |
4.97e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 213 RILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRrELNVPK--------HVSILHVEQelrgddtkaLQSVLDaDVWRK 284
Cdd:PRK10938 17 KTLQLPSLTLNAGDSWAFVGANGSGKSALARALAG-ELPLLSgerqsqfsHITRLSFEQ---------LQKLVS-DEWQR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 285 Q---LLSEEakinerlkEMDVLRQEFEEDSLEVKklDNEREDLDNHLIQISDKLvdmesdkaearaasilyglgfsteaq 361
Cdd:PRK10938 86 NntdMLSPG--------EDDTGRTTAEIIQDEVK--DPARCEQLAQQFGITALL-------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 362 QQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVShdrAFLNEVaTDI--IYQHN 439
Cdd:PRK10938 130 DRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLV---LVLNRF-DEIpdFVQFA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 440 ERLDyyrgqdfDTFYTTKEERRKNAQReydnqmvyrkhlqefidkyrynAAKSQEAQSriKKLEKLPVLEPpeQDKTIDF 519
Cdd:PRK10938 206 GVLA-------DCTLAETGEREEILQQ----------------------ALVAQLAHS--EQLEGVQLPEP--DEPSARH 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 520 KFPEcdklSPPIIQLQDVSFGYDENNlLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMM-------------------- 579
Cdd:PRK10938 253 ALPA----NEPRIVLNNGVVSYNDRP-ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysndltlfgrrrgs 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 580 -EQLRPLK---GFVSRNPRL--RI----------GYFtqhhvDSMDLTTSAVDWMSKsfpgKTDEeyrrHLGSFGITGTL 643
Cdd:PRK10938 328 gETIWDIKkhiGYVSSSLHLdyRVstsvrnvilsGFF-----DSIGIYQAVSDRQQK----LAQQ----WLDILGIDKRT 394
|
490 500 510
....*....|....*....|....*....|....*....
gi 14318531 644 GLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLD 682
Cdd:PRK10938 395 ADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
528-728 |
5.28e-08 |
|
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: 56.23 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 528 SPPIIQLQD--VSFG-YDENNLLLKDVNLDVQMDSRIALVGANGCGKT-TLLKIM------------------------- 578
Cdd:COG4172 3 SMPLLSVEDlsVAFGqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpdpaahpsgsilfdgqdllgls 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 579 MEQLRPLKG------F----VSRNPRLRIGyfTQ------HH--VDSMDLTTSAVDWMSKSfpGKTDEEYRrhLGSFgit 640
Cdd:COG4172 83 ERELRRIRGnriamiFqepmTSLNPLHTIG--KQiaevlrLHrgLSGAAARARALELLERV--GIPDPERR--LDAY--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 641 gtlglqKMQLlSGGQKSRVAFAALCLNNPHILVLDEPsnhldTTGLDALVEA-----LKN----FNGGVLMVSHDISVI- 710
Cdd:COG4172 154 ------PHQL-SGGQRQRVMIAMALANEPDLLIADEP-----TTALDVTVQAqildlLKDlqreLGMALLLITHDLGVVr 221
|
250 260
....*....|....*....|...
gi 14318531 711 ---DSVC--KEIWVSEQGTVKRF 728
Cdd:COG4172 222 rfaDRVAvmRQGEIVEQGPTAEL 244
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
527-725 |
5.50e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.89 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 527 LSPPIIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS-----RNPRLR---IG 598
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgqpTRQALQknlVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 599 YFTQhhvdsmdltTSAVDWmskSFPGKTDEEYRrhLGSFGITGTL-------------GLQKMQL----------LSGGQ 655
Cdd:PRK15056 82 YVPQ---------SEEVDW---SFPVLVEDVVM--MGRYGHMGWLrrakkrdrqivtaALARVDMvefrhrqigeLSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 656 KSRVAFAALCLNNPHILVLDEPsnhldTTGLDALVEA--------LKNFNGGVLMVSHDISVIDSVCkEIWVSEQGTV 725
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEP-----FTGVDVKTEAriisllreLRDEGKTMLVSTHNLGSVTEFC-DYTVMVKGTV 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
207-423 |
5.87e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.01 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 207 YVGDGQR---ILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELNVPKHVSILhveqelrGDDTKALqsvldadvwr 283
Cdd:PRK10584 15 SVGQGEHelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLV-------GQPLHQM---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 284 kqllSEEAKINERLKEMDVLRQEFeedsLEVKKLdNEREDldnhlIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQ 363
Cdd:PRK10584 78 ----DEEARAKLRAKHVGFVFQSF----MLIPTL-NALEN-----VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318531 364 PTNsFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYL----KTYPNTVLTVSHD 423
Cdd:PRK10584 144 PAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
189-429 |
7.79e-08 |
|
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: 54.19 E-value: 7.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 189 FGSSAGKSKDIHIDTFD---LYVGDGQRI-LSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILHVEQE 264
Cdd:cd03294 10 FGKNPQKAFKLLAKGKSkeeILKKTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINR--LIEPTSGKVLIDGQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 265 LRGDDTKALQSVldadvwrkqllseeakineRLKEMDVLRQEFeedslevkKLDNEREDLDNhlIQISDKLVDMESDKAE 344
Cdd:cd03294 88 IAAMSRKELREL-------------------RRKKISMVFQSF--------ALLPHRTVLEN--VAFGLEVQGVPRAERE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 345 ARAASILYGLGFSTEAQQQPtNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDvPSI-----AYLAEYLKTYPNTVLT 419
Cdd:cd03294 139 ERAAEALELVGLEGWEHKYP-DELSGGMQQRVGLARALAVDPDILLMDEAFSALD-PLIrremqDELLRLQAELQKTIVF 216
|
250
....*....|
gi 14318531 420 VSHDrafLNE 429
Cdd:cd03294 217 ITHD---LDE 223
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
229-435 |
8.12e-08 |
|
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: 54.29 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 229 GLVGQNGIGKSTLLRALSRREL-NVPKHVS------ILhveQELRGDdtkALQSVLdadvwrKQLLSEEAKINERLKEMD 301
Cdd:cd03236 30 GLVGPNGIGKSTALKILAGKLKpNLGKFDDppdwdeIL---DEFRGS---ELQNYF------TKLLEGDVKVIVKPQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 302 VLRQEFEEDSLEVKKLDNEREDLDNHLIQIS-DKLVDMESDkaearaasilyglgfsteaqqqptnSFSGGWRMRLSLAR 380
Cdd:cd03236 98 LIPKAVKGKVGELLKKKDERGKLDELVDQLElRHVLDRNID-------------------------QLSGGELQRVAIAA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 381 ALFCQPDLLLLDEPSNMLDVP---SIAYLAEYLKTYPNTVLTVSHDRAFLNEVAtDII 435
Cdd:cd03236 153 ALARDADFYFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLS-DYI 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
369-431 |
8.28e-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: 53.88 E-value: 8.28e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS----IAYLAEYLKTYPNTVLTVSHD----RAFLNEVA 431
Cdd:cd03299 131 SGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHDfeeaWALADKVA 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
210-410 |
1.05e-07 |
|
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: 52.88 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrrELNVPKHVSILhveQELRGDDTKAlqsvldaDVWRKQLL-- 287
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILA--GLSPPLAGRVL---LNGGPLDFQR-------DSIARGLLyl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 288 SEEAKINERLKEMDVLRqeFEEDslevkklDNEREdldnhliQISDKLVDMEsdkaearaasiLYGLGfsteaqQQPTNS 367
Cdd:cd03231 79 GHAPGIKTTLSVLENLR--FWHA-------DHSDE-------QVEEALARVG-----------LNGFE------DRPVAQ 125
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14318531 368 FSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYL 410
Cdd:cd03231 126 LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
368-435 |
1.06e-07 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 54.29 E-value: 1.06e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 368 FSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVpSI-----AYLAEYLKTYPNTVLTVSHDRAFLNEVATDII 435
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDV-TIqaqilNLLKDLQRELGLAILFITHDLGVVAEIADRVA 222
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
204-436 |
1.16e-07 |
|
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: 53.42 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 204 FDLYVG-DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRElnvpkHVSILHVEQELRGDDTKALqsvldadvw 282
Cdd:TIGR01978 4 KDLHVSvEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHP-----SYEVTSGTILFKGQDLLEL--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 283 rkqllseeaKINERLKEMDVLRQEFEEDSLEVKKLDNEREDLDNHLIQISDKLVDMESDKAEARAASILYGLGFSTeAQQ 362
Cdd:TIGR01978 70 ---------EPDERARAGLFLAFQYPEEIPGVSNLEFLRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEF-LNR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 363 QPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS---IAYLAEYLKTYPNTVLTVSHDRAFLNEVATDIIY 436
Cdd:TIGR01978 140 SVNEGFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDAlkiVAEGINRLREPDRSFLIITHYQRLLNYIKPDYVH 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
368-422 |
1.51e-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: 51.77 E-value: 1.51e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 368 FSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVSH 422
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH 146
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
651-707 |
1.60e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.55 E-value: 1.60e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 651 LSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGG---VLMVSHDI 707
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgktIILVTHDL 225
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
368-423 |
1.76e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.96 E-value: 1.76e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 368 FSGGWRMRLSLARALFCQPDLLLLDEPSNMLDV---PSIAYLAEYLKTYPNT-VLTVSHD 423
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvqAQIMTLLNELKREFNTaIIMITHD 221
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
561-710 |
1.92e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.22 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 561 IALVGANGCGKTTLLKIMMEQLRPLKGFVsrnprlrigyftqhHVDSMDLTTSAVDWMSKSFPGKTDEEYrrhlgsfgit 640
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGV--------------IYIDGEDILEEVLDQLLLIIVGGKKAS---------- 60
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 641 gtlglqkmqlLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGGVLMVSHDISVI 710
Cdd:smart00382 61 ----------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
652-719 |
2.08e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.57 E-value: 2.08e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 652 SGGQKSRV--AFAALClnNPHILVLDEPsnhldTTGLDALVEA--------LKN-FNGGVLMVSHDISVIDSVCKEIWV 719
Cdd:PRK09473 163 SGGMRQRVmiAMALLC--RPKLLIADEP-----TTALDVTVQAqimtllneLKReFNTAIIMITHDLGVVAGICDKVLV 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
528-578 |
2.08e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 52.73 E-value: 2.08e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 14318531 528 SPPIIQLQDVSFGYDeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIM 578
Cdd:COG1117 8 LEPKIEVRNLNVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL 57
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
191-399 |
2.17e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 53.68 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 191 SSAGKSKDIHIDTFDLYVGDGQRILSNA-QLTLSFGHRYGLVGQNGIGKSTLLRAlsrrelnvpkhvsILHVEQELRGDD 269
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSYGDKAVVNGlSFTVASGECFGLLGPNGAGKSTIARM-------------ILGMTSPDAGKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 270 TkalqsVLDADVWRKQLLSEeAKINErLKEMDVLRQEFeedslevkkldNEREDLdnhliQISDKLVDMESDKAEARAAS 349
Cdd:PRK13536 99 T-----VLGVPVPARARLAR-ARIGV-VPQFDNLDLEF-----------TVRENL-----LVFGRYFGMSTREIEAVIPS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14318531 350 ILYGLGFSTEAQQqPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLD 399
Cdd:PRK13536 156 LLEFARLESKADA-RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
532-728 |
2.32e-07 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 52.11 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDEN-NLLLKDVNLDVQMDSRIALVGANGCGKTTLL----------------------KIMMEQLRPLKGF 588
Cdd:cd03244 3 IEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLlalfrlvelssgsilidgvdisKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 589 VSRNP-------RLRIGYFTQHhvdsmdlttsavdwmsksfpgkTDEEYRR-----HLGSFGITGTLGLQKMQL-----L 651
Cdd:cd03244 83 IPQDPvlfsgtiRSNLDPFGEY----------------------SDEELWQalervGLKEFVESLPGGLDTVVEeggenL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 652 SGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNF--NGGVLMVSHDI-SVIDsvCKEIWVSEQGTVKRF 728
Cdd:cd03244 141 SVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAHRLdTIID--SDRILVLDKGRVVEF 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
526-706 |
2.36e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 52.41 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 526 KLSPPIIQLQDVSFGYDENnLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFV--------SRNP---R 594
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDA-KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegedisTLKPeiyR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 595 LRIGYFTQHHVDSMDlttSAVDWMskSFP----GKTDEE--YRRHLGSFGITGTLGLQKMQLLSGGQKSRVAFaalcLNN 668
Cdd:PRK10247 81 QQVSYCAQTPTLFGD---TVYDNL--IFPwqirNQQPDPaiFLDDLERFALPDTILTKNIAELSGGEKQRISL----IRN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14318531 669 ----PHILVLDEPSNHLDTTGLDALVEALKNFNG----GVLMVSHD 706
Cdd:PRK10247 152 lqfmPKVLLLDEITSALDESNKHNVNEIIHRYVReqniAVLWVTHD 197
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
538-725 |
2.46e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 53.57 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 538 SFGydeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGfvsrnprlrigyftQHHVDSMDLTTSAVD- 616
Cdd:PRK11432 15 RFG---SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEG--------------QIFIDGEDVTHRSIQq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 617 ------WMSKS-FPgktdeeyrrHLgSFGITGTLGLqKMQ-----------------------------LLSGGQKSRVA 660
Cdd:PRK11432 78 rdicmvFQSYAlFP---------HM-SLGENVGYGL-KMLgvpkeerkqrvkealelvdlagfedryvdQISGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 661 FA-ALCLnNPHILVLDEPSNHLDT----TGLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:PRK11432 147 LArALIL-KPKVLLFDEPLSNLDAnlrrSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
201-428 |
3.35e-07 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 52.43 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 201 IDTFDLYVGDGQR-ILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRrelnvpkhvsilhveqELRGD------DTKAL 273
Cdd:COG4559 2 LEAENLSVRLGGRtLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG----------------ELTPSsgevrlNGRPL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 274 QSvldadvWRKQLLSeeakinerlKEMDVLRQE------FEedSLEVKKLDneredLDNHLIQISDklvdmesDKAEARA 347
Cdd:COG4559 66 AA------WSPWELA---------RRRAVLPQHsslafpFT--VEEVVALG-----RAPHGSSAAQ-------DRQIVRE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 348 ASILYGL-GFSteaqQQPTNSFSGGWRMRLSLARALfCQ--------PDLLLLDEPSNMLDvpsIAY---LAEYLKTY-- 413
Cdd:COG4559 117 ALALVGLaHLA----GRSYQTLSGGEQQRVQLARVL-AQlwepvdggPRWLFLDEPTSALD---LAHqhaVLRLARQLar 188
|
250
....*....|....*.
gi 14318531 414 -PNTVLTVSHDrafLN 428
Cdd:COG4559 189 rGGGVVAVLHD---LN 201
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
212-423 |
3.38e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 52.04 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 212 QRILSNAQLTLSFGHRYGLVGQNGIGKSTLLR------ALSRRELNVPKHVSILHVEQELRGDDTKALQsvldadVWRKQ 285
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRvvlglvAPDEGVIKRNGKLRIGYVPQKLYLDTTLPLT------VNRFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 286 LLSEEAKinerlkemdvlrqefEEDSLEVKKldneredldnhliqisdklvdmesdkaEARAASILyglgfsteaqQQPT 365
Cdd:PRK09544 91 RLRPGTK---------------KEDILPALK---------------------------RVQAGHLI----------DAPM 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318531 366 NSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVP---SIAYLAEYLKTYPN-TVLTVSHD 423
Cdd:PRK09544 119 QKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNgqvALYDLIDQLRRELDcAVLMVSHD 180
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
341-399 |
3.47e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 52.17 E-value: 3.47e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 341 DKAE--ARAASILYGLGFStEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLD 399
Cdd:COG4525 107 PKAErrARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
211-435 |
3.60e-07 |
|
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: 51.96 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 211 GQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRElnVPKHVSILhveqeLRGDDTKALQSvldADVWRK------ 284
Cdd:COG0411 16 GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFY--RPTSGRIL-----FDGRDITGLPP---HRIARLgiartf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 285 QLLSEeakinerLKEMDVLrqefeeDSLEVKKLDNEREDLDNHLIQIsdKLVDMESDKAEARAASILYGLGFSTEAQQqP 364
Cdd:COG0411 86 QNPRL-------FPELTVL------ENVLVAAHARLGRGLLAALLRL--PRARREEREARERAEELLERVGLADRADE-P 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 365 TNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN----TVLTVSHDRAFLNEVATDII 435
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDergiTILLIEHDMDLVMGLADRIV 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
651-725 |
3.74e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 52.32 E-value: 3.74e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 651 LSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEAL----KNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFerlnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
531-707 |
3.79e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.43 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDEN--NLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGfvsrnprlrigyftQHHVDSM 608
Cdd:PRK13650 4 IIEVKNLTFKYKEDqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESG--------------QIIIDGD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 609 DLTTSAVdWmsksfpgktdeEYRRHLG-------------------SFGITGT-LGLQKMQ------------------- 649
Cdd:PRK13650 70 LLTEENV-W-----------DIRHKIGmvfqnpdnqfvgatveddvAFGLENKgIPHEEMKervnealelvgmqdfkere 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318531 650 --LLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKN----FNGGVLMVSHDI 707
Cdd:PRK13650 138 paRLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGirddYQMTVISITHDL 201
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
532-725 |
3.91e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 51.94 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLlKDVNLDVQMDSRIALVGANGCGKTTLLKIM--ME-----QL----------RPLKGFVSRNPR 594
Cdd:COG4161 3 IQLKNINCFYGSHQAL-FDINLECPSGETLVLLGPSGAGKSSLLRVLnlLEtpdsgQLniaghqfdfsQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 595 LRIGY-FTQH----HVDSMDLTTSA---VDWMSKSfpgKTDEEYRRHLGsfgitgTLGLQKM-----QLLSGGQKSRVAF 661
Cdd:COG4161 82 QKVGMvFQQYnlwpHLTVMENLIEApckVLGLSKE---QAREKAMKLLA------RLRLTDKadrfpLHLSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 662 AALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNG-GV--LMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGItqVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
200-424 |
4.16e-07 |
|
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: 53.76 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 200 HIDTFDL---YVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRrelnvpkhvsILHVEQELRGD----DTKA 272
Cdd:TIGR01271 1217 QMDVQGLtakYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLR----------LLSTEGEIQIDgvswNSVT 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 273 LQSvldadvWRKQLLSEEAKI----NERLKEMDVLRQEFEEDSLEVKkldnEREDLDNHLIQISDKLvdmesDKAEARAA 348
Cdd:TIGR01271 1287 LQT------WRKAFGVIPQKVfifsGTFRKNLDPYEQWSDEEIWKVA----EEVGLKSVIEQFPDKL-----DFVLVDGG 1351
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 349 SILyglgfsteaqqqptnsfSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLK-TYPNTVLTVSHDR 424
Cdd:TIGR01271 1352 YVL-----------------SNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKqSFSNCTVILSEHR 1411
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
210-726 |
4.18e-07 |
|
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: 53.29 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrrelNVPKHVS----ILHVEQELRGddtkalQSVLDADVWRKQ 285
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILS----GVYPHGTwdgeIYWSGSPLKA------SNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 286 LLSEEAKInerLKEMDVLRQEFeedslevkkLDNEredldnhliqISDKLVDMESDKAEARAASILYGLGFSTEAQQQPT 365
Cdd:TIGR02633 82 IIHQELTL---VPELSVAENIF---------LGNE----------ITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 366 NSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEY---LKTYPNTVLTVSHDrafLNEVA--TDIIYQHNE 440
Cdd:TIGR02633 140 GDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIirdLKAHGVACVYISHK---LNEVKavCDTICVIRD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 441 rldyyrGQDFDTfyttkEERRKNAQREYDNQMVYRKhlqefidkyrynaaksqeaqsrikkLEKLPVLEPPE-QDKTIDF 519
Cdd:TIGR02633 217 ------GQHVAT-----KDMSTMSEDDIITMMVGRE-------------------------ITSLYPHEPHEiGDVILEA 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 520 KFPEC-DKLSPPIIQLQDVSFGYDENNLLlkdvnldvqmdsriALVGANGCGKTTLL-------------KIMMEQlRPL 585
Cdd:TIGR02633 261 RNLTCwDVINPHRKRVDDVSFSLRRGEIL--------------GVAGLVGAGRTELVqalfgaypgkfegNVFING-KPV 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 586 KgfvSRNP--------------RLRIGYFTQHHVdSMDLTTSAVDwmskSFPGKTDEEYRRHLGSFGitgtLGLQKMQL- 650
Cdd:TIGR02633 326 D---IRNPaqairagiamvpedRKRHGIVPILGV-GKNITLSVLK----SFCFKMRIDAAAELQIIG----SAIQRLKVk 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 651 ----------LSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTG---LDALVEALKNFNGGVLMVSHDISVIDSVCKEI 717
Cdd:TIGR02633 394 taspflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRV 473
|
....*....
gi 14318531 718 WVSEQGTVK 726
Cdd:TIGR02633 474 LVIGEGKLK 482
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
532-734 |
4.61e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 52.50 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVS--FGYDENNLL-LKDVNLDVQMDSRIALVGANGCGKTTLLKI--MMEqlRPLKGFVS--------------RN 592
Cdd:PRK11153 2 IELKNISkvFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCinLLE--RPTSGRVLvdgqdltalsekelRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 593 PRLRIGYFTQHhvdsMDLTTSAVDWMSKSFP----GKTDEEYRRHlgsfgITGTL---GLQ-KMQL----LSGGQKSRVA 660
Cdd:PRK11153 80 ARRQIGMIFQH----FNLLSSRTVFDNVALPlelaGTPKAEIKAR-----VTELLelvGLSdKADRypaqLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 661 FA-ALClNNPHILVLDEPSNHLDTTGLDALVEALKNFNG----GVLMVSHDISVIDSVCKEIWVSEQGTVKRfEGTIYD 734
Cdd:PRK11153 151 IArALA-SNPKVLLCDEATSALDPATTRSILELLKDINRelglTIVLITHEMDVVKRICDRVAVIDAGRLVE-QGTVSE 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
209-429 |
4.76e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 51.21 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 209 GDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELnvPKHVSILhveqelrgddtkalqsVLDADVwrkqlls 288
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEER--PTSGQVL----------------VNGQDL------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 289 eeAKINERlkEMDVLR-------QEFeedslevkKLDNEREDLDNhlIQISDKLVDMESDKAEARAASILYGLGFSTEAQ 361
Cdd:COG2884 67 --SRLKRR--EIPYLRrrigvvfQDF--------RLLPDRTVYEN--VALPLRVTGKSRKEIRRRVREVLDLVGLSDKAK 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 362 QQPtNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDvPSIAY-LAEYLKTYpN----TVLTVSHDRAFLNE 429
Cdd:COG2884 133 ALP-HELSGGEQQRVAIARALVNRPELLLADEPTGNLD-PETSWeIMELLEEI-NrrgtTVLIATHDLELVDR 202
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
531-731 |
5.02e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.69 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKG---FVSRN-PRL-RIGYFTQHHV 605
Cdd:PRK11831 7 LVDMRGVSFTRG-NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGeilFDGENiPAMsRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 606 DSM-----DLTTSAVDWMSKSFPgktdeeYRRH---------------LGSFGITGTLGLQKMQlLSGGQKSRVAFAALC 665
Cdd:PRK11831 86 MSMlfqsgALFTDMNVFDNVAYP------LREHtqlpapllhstvmmkLEAVGLRGAAKLMPSE-LSGGMARRAALARAI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 666 LNNPHILVLDEPSNHLDTTGLDALVEALKNFNG--GV--LMVSHDISVIDSVCKEIW-VSEQGTVKrfEGT 731
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVtcVVVSHDVPEVLSIADHAYiVADKKIVA--HGS 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
214-423 |
5.09e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 51.36 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 214 ILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrrELNVPKHVSILHVEQELRGddtkalqsvldadvwrkqlLSEEAKI 293
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLG--GLDTPTSGDVIFNGQPMSK-------------------LSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 294 NERLKEMDVLRQeFEEDSLEVKKLDNEREDLdnhLIQisdklvDMESDKAEARAASILYGLGFSTEAQQQPTnSFSGGWR 373
Cdd:PRK11629 83 ELRNQKLGFIYQ-FHHLLPDFTALENVAMPL---LIG------KKKPAEINSRALEMLAAVGLEHRANHRPS-ELSGGER 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 14318531 374 MRLSLARALFCQPDLLLLDEPSNMLD---VPSIAYLAEYLKTYPNTV-LTVSHD 423
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGTAfLVVTHD 205
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
369-431 |
5.88e-07 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 52.41 E-value: 5.88e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNT----VLTVSHDrafLNEVA 431
Cdd:COG4148 135 SGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDEldipILYVSHS---LDEVA 198
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
530-709 |
5.93e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.80 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 530 PIIQLQDVSFGY---DENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGF---------------VSR 591
Cdd:PRK10535 3 ALLELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdvatldadaLAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 592 NPRLRIGY-FTQHHVDSmDLTTSAVDWMSKSFPGKTDEEYRRH----LGSFGITGTLGLQKMQlLSGGQKSRVAFAALCL 666
Cdd:PRK10535 83 LRREHFGFiFQRYHLLS-HLTAAQNVEVPAVYAGLERKQRLLRaqelLQRLGLEDRVEYQPSQ-LSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14318531 667 NNPHILVLDEPSNHLDT-TGLD--ALVEALKNFNGGVLMVSHDISV 709
Cdd:PRK10535 161 NGGQVILADEPTGALDShSGEEvmAILHQLRDRGHTVIIVTHDPQV 206
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
563-706 |
6.28e-07 |
|
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: 52.11 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 563 LVGANGCGKTTLLKIMMEQLRPLKGFV--------SRNPRLR-IGYFTQHHVDSMDLTTSAvdwmSKSFPGKTDEEYR-- 631
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSImldgedvtNVPPHLRhINMVFQSYALFPHMTVEE----NVAFGLKMRKVPRae 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 632 ---RHLGSFGIT--GTLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNG----GVLM 702
Cdd:TIGR01187 77 ikpRVLEALRLVqlEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEqlgiTFVF 156
|
....
gi 14318531 703 VSHD 706
Cdd:TIGR01187 157 VTHD 160
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
215-428 |
6.65e-07 |
|
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: 50.87 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 215 LSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELNVPKHVSILHVE-QELRGDDTKALQsvldadvwrkqllseeaki 293
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvSDLRGRAIPYLR------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 294 nerlKEMDVLRQEFeedslevkKLDNEREDLDNhlIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQPtNSFSGGWR 373
Cdd:cd03292 78 ----RKIGVVFQDF--------RLLPDRNVYEN--VAFALEVTGVPPREIRKRVPAALELVGLSHKHRALP-AELSGGEQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 374 MRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN---TVLTVSHDRAFLN 428
Cdd:cd03292 143 QRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKagtTVVVATHAKELVD 200
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
548-727 |
7.07e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.89 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 548 LKDVNLDVQMDSRIALVGANGCGKTTL--LKIMMEQlrPLKG-------------------------------FVSRNPR 594
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLarLLTMIET--PTGGelyyqgqdllkadpeaqkllrqkiqivfqnpYGSLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 595 LRIGYFTQhhvDSMDLTTS---------AVDWMSKSfpGKTDEEYRRHLGSFgitgtlglqkmqllSGGQKSRVAFA-AL 664
Cdd:PRK11308 109 KKVGQILE---EPLLINTSlsaaerrekALAMMAKV--GLRPEHYDRYPHMF--------------SGGQRQRIAIArAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 665 CLnNPHILVLDEPSNHLDTT----GLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWV------SEQGTVKR 727
Cdd:PRK11308 170 ML-DPDVVVADEPVSALDVSvqaqVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVmylgrcVEKGTKEQ 241
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
532-726 |
7.08e-07 |
|
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: 50.63 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDEnnlLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRLRIGYFTQHHVDSMDLT 611
Cdd:TIGR01277 1 LALDKVRYEYEH---LPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 612 TSAVdwmsksFPGKTdeeYRRHLGsFGITGTLGL---QKMQL-------------------LSGGQKSRVAFAALCLNNP 669
Cdd:TIGR01277 78 ENNL------FAHLT---VRQNIG-LGLHPGLKLnaeQQEKVvdaaqqvgiadyldrlpeqLSGGQRQRVALARCLVRPN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 670 HILVLDEPSNHLDT---TGLDALVEAL-KNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVK 726
Cdd:TIGR01277 148 PILLLDEPFSALDPllrEEMLALVKQLcSERQRTLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
530-710 |
7.35e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 51.19 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 530 PIIQLQDVSFGYDENNLLlKDVNLDVQMDSRIALVGANGCGKTTLLKiMMEQLRPLKGFVSRNPRLRigYFTQH------ 603
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKIL-EGVSMEIYQSKVTAIIGPSGCGKSTFLK-CLNRMNELESEVRVEGRVE--FFNQNiyerrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 604 HVDSMDLTTSAVDWMSKSFPGKTDEE---------YRRHLGSFGITGTL------------GLQKMQL-LSGGQKSRVAF 661
Cdd:PRK14258 82 NLNRLRRQVSMVHPKPNLFPMSVYDNvaygvkivgWRPKLEIDDIVESAlkdadlwdeikhKIHKSALdLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 14318531 662 AALCLNNPHILVLDEPSNHLD---TTGLDALVEALK-NFNGGVLMVSHDISVI 710
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDpiaSMKVESLIQSLRlRSELTMVIVSHNLHQV 214
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
531-746 |
7.75e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.17 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENNLLlKDVNLDVQMDSRIALVGANGCGKTTLL----------KIMMEQLRPLKGFVSRNPRL----- 595
Cdd:PRK09984 4 IIRVEKLAKTFNQHQAL-HAVDLNIHHGEMVALLGPSGSGKSTLLrhlsglitgdKSAGSHIELLGRTVQREGRLardir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 596 ----RIGYFTQHH----------------VDSMDLTTSAVDWMSKsfpgktdEEYRRHLGSFGITGT--LGLQKMQLLSG 653
Cdd:PRK09984 83 ksraNTGYIFQQFnlvnrlsvlenvligaLGSTPFWRTCFSWFTR-------EQKQRALQALTRVGMvhFAHQRVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 654 GQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGG----VLMVSHDISVIDSVCKEIWVSEQGTV---- 725
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgitVVVTLHQVDYALRYCERIVALRQGHVfydg 235
|
250 260
....*....|....*....|....*..
gi 14318531 726 --KRFEGTIYD--YR--DYILQSADAA 746
Cdd:PRK09984 236 ssQQFDNERFDhlYRsiNRVEENAKAA 262
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
547-723 |
9.60e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 50.66 E-value: 9.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 547 LLKDVNLDVQMDSRIALVGANGCGKTTLL------------KIMMEQ----LRPLKGFVSRNprlrIGYFTQHHvdSMDL 610
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFymvvgivprdagNIIIDDedisLLPLHARARRG----IGYLPQEA--SIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 611 TTSAVDWMSKSFPGKTD--EEYRRH-----LGSFGIT---GTLGlqkmQLLSGGQKSRVAFAALCLNNPHILVLDEPSNH 680
Cdd:PRK10895 92 RLSVYDNLMAVLQIRDDlsAEQREDranelMEEFHIEhlrDSMG----QSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14318531 681 LDTTG---LDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQG 723
Cdd:PRK10895 168 VDPISvidIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQG 213
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
495-676 |
1.33e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.51 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 495 AQSRIKKLEKLPvLEPPEQDKTIDFKFPECDKLSppiiqLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTL 574
Cdd:PRK10522 292 AQVAFNKLNKLA-LAPYKAEFPRPQAFPDWQTLE-----LRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 575 LKIMMEQLRPLKGfvsrnprlrigyftQHHVDSMDLTtsavdwmsksfpGKTDEEYRRH--------------LGSFGIT 640
Cdd:PRK10522 366 AMLLTGLYQPQSG--------------EILLDGKPVT------------AEQPEDYRKLfsavftdfhlfdqlLGPEGKP 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 641 G----------TLGLQ-KMQL---------LSGGQKSRVAFAALCLNNPHILVLDE 676
Cdd:PRK10522 420 AnpalvekwleRLKMAhKLELedgrisnlkLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
651-731 |
1.42e-06 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 51.73 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 651 LSGGQKSRVAFAALCLNNPHILVLDEPSNHLD--TTGL--DALVEALKNFNGGVLMVSHDISVI-DSVCKEIWVsEQGTV 725
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqTAKLvhNALEEAVKASGISMVLTSHWPEVIeDLSDKAIWL-ENGEI 247
|
....*.
gi 14318531 726 KRfEGT 731
Cdd:TIGR03269 248 KE-EGT 252
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
526-711 |
1.50e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.96 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 526 KLSPPIIQLQDvSFGYDENNL---LLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQL--RPLKGFVsrnpRLRIGYF 600
Cdd:COG2401 22 DLSERVAIVLE-AFGVELRVVeryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV----DVPDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 601 TQHH--VDSMDLTTSAVDwmsksfpgktdeeyrrhlgSFGITGTLGLQKMQL-------LSGGQKSRVAFAALCLNNPHI 671
Cdd:COG2401 97 GREAslIDAIGRKGDFKD-------------------AVELLNAVGLSDAVLwlrrfkeLSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 14318531 672 LVLDEPSNHLDTT----GLDALVEALKNFNGGVLMVSHDISVID 711
Cdd:COG2401 158 LVIDEFCSHLDRQtakrVARNLQKLARRAGITLVVATHHYDVID 201
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
201-428 |
1.84e-06 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 50.16 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 201 IDTFDLYVGDGQR-ILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrrelnvpkhvsilhveQELRGD------DTKAL 273
Cdd:PRK13548 3 LEARNLSVRLGGRtLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS----------------GELSPDsgevrlNGRPL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 274 QSvldadvWRKQLLseeAKineRLKemdVLRQEFeedSL-------EVKKLDneREDLDNHLIQisdklvdmesDKAEAR 346
Cdd:PRK13548 67 AD------WSPAEL---AR---RRA---VLPQHS---SLsfpftveEVVAMG--RAPHGLSRAE----------DDALVA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 347 AASILYGL-GFSTEAQQQptnsFSGGWRMRLSLARALfCQ-------PDLLLLDEPSNMLDvpsIAY-------LAEYLK 411
Cdd:PRK13548 117 AALAQVDLaHLAGRDYPQ----LSGGEQQRVQLARVL-AQlwepdgpPRWLLLDEPTSALD---LAHqhhvlrlARQLAH 188
|
250
....*....|....*..
gi 14318531 412 TYPNTVLTVSHDrafLN 428
Cdd:PRK13548 189 ERGLAVIVVLHD---LN 202
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
154-399 |
1.86e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 51.36 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 154 AKRNNKFVKYEASKLINDQKEEDYDSFFLQINPLEFGssagkskdihidtfdlYVGDGQRILSNAQLTLSFGHRYGLVGQ 233
Cdd:PRK11160 311 ARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFT----------------YPDQPQPVLKGLSLQIKAGEKVALLGR 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 234 NGIGKSTLLRALSRrELNvPKHVSIL--------HVEQELRGDDTKALQSV-LDADVWRKQLLSEEAKIN-ERLKEmdVL 303
Cdd:PRK11160 375 TGCGKSTLLQLLTR-AWD-PQQGEILlngqpiadYSEAALRQAISVVSQRVhLFSATLRDNLLLAAPNASdEALIE--VL 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 304 RQefeedsLEVKKLDNEREDLDNHLiqisdklvdmesdkaearaasilyglGfstEAQQQptnsFSGGWRMRLSLARALF 383
Cdd:PRK11160 451 QQ------VGLEKLLEDDKGLNAWL--------------------------G---EGGRQ----LSGGEQRRLGIARALL 491
|
250
....*....|....*.
gi 14318531 384 CQPDLLLLDEPSNMLD 399
Cdd:PRK11160 492 HDAPLLLLDEPTEGLD 507
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
211-423 |
1.88e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.89 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 211 GQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRelnVPKHVSILHVEQE---LRGDDTKALQSVldadvwrkQLL 287
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGI---VPRDAGNIIIDDEdisLLPLHARARRGI--------GYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 288 SEEAKINERLKEMDVLRQefeedSLEVKKldneredldnhliqisdklvDMESDKAEARAASILYGLGFStEAQQQPTNS 367
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMA-----VLQIRD--------------------DLSAEQREDRANELMEEFHIE-HLRDSMGQS 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 368 FSGGWRMRLSLARALFCQPDLLLLDEPSNMLD---VPSIAYLAEYLKTYPNTVLTVSHD 423
Cdd:PRK10895 138 LSGGERRRVEIARALAANPKFILLDEPFAGVDpisVIDIKRIIEHLRDSGLGVLITDHN 196
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
215-423 |
2.65e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 50.08 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 215 LSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrrELNVPKHVSILHV-EQELRGDDTKALQSVLDADVWRKQLLSEEAKI 293
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLN--ALLLPDTGTIEWIfKDEKNKKKTKEKEKVLEKLVIQKTRFKKIKKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 294 NERLKEMDVLRQeFEEDSLEVKKLDNEredldnhliqISDKLVDMESDKAEA--RAASILYGLGFSTEAQQQPTNSFSGG 371
Cdd:PRK13651 101 KEIRRRVGVVFQ-FAEYQLFEQTIEKD----------IIFGPVSMGVSKEEAkkRAAKYIELVGLDESYLQRSPFELSGG 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 372 WRMRLSLARALFCQPDLLLLDEPSNMLD---VPSIAYLAEYLKTYPNTVLTVSHD 423
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
532-707 |
2.73e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 49.20 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDenNLLLKdVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGfvsrnpRLRIGyfTQHHVDsmdlT 611
Cdd:PRK10771 2 LKLTDITWLYH--HLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASG------SLTLN--GQDHTT----T 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 612 TSAVDWMSKSF--------------------PG-KTDEEYRRHLGSfgITGTLGLQKM--QL---LSGGQKSRVAFAALC 665
Cdd:PRK10771 67 PPSRRPVSMLFqennlfshltvaqniglglnPGlKLNAAQREKLHA--IARQMGIEDLlaRLpgqLSGGQRQRVALARCL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14318531 666 LNNPHILVLDEPSNHLDTT----GLDALVEALKNFNGGVLMVSHDI 707
Cdd:PRK10771 145 VREQPILLLDEPFSALDPAlrqeMLTLVSQVCQERQLTLLMVSHSL 190
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
334-468 |
2.76e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 49.31 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 334 KLVDMESDKAEARAASILYGLGFStEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAE-YLKT 412
Cdd:PRK11248 96 QLAGVEKMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTlLLKL 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 413 YPNT---VLTVSHD---RAFLnevATDIIY------QHNERLDYYRGQDF---DTFYTTKEERRKNAQREY 468
Cdd:PRK11248 175 WQETgkqVLLITHDieeAVFM---ATELVLlspgpgRVVERLPLNFARRFvagESSRSIKSDPQFIAMREY 242
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
222-429 |
2.98e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 49.80 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 222 LSF----GHRYGLVGQNGIGKSTLLRALsrRELNVPKHVSILHVEQELRGDDTKALQSVldadvwrkqllseeakinERL 297
Cdd:PRK13537 26 LSFhvqrGECFGLLGPNGAGKTTTLRML--LGLTHPDAGSISLCGEPVPSRARHARQRV------------------GVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 298 KEMDVLRQEFeedslevkkldNEREDLdnhliQISDKLVDMESDKAEARAASILYGLGFSTEAQQqPTNSFSGGWRMRLS 377
Cdd:PRK13537 86 PQFDNLDPDF-----------TVRENL-----LVFGRYFGLSAAAARALVPPLLEFAKLENKADA-KVGELSGGMKRRLT 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 378 LARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTY---PNTVLTVSHdraFLNE 429
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLlarGKTILLTTH---FMEE 200
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
368-436 |
3.11e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 48.68 E-value: 3.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318531 368 FSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAE---YLKTYPNTVLTVSHDRAFLNEVATDIIY 436
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEvinKLREEGKSVLIITHYQRLLDYIKPDRVH 176
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
532-578 |
3.13e-06 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 50.07 E-value: 3.13e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 14318531 532 IQLQDVSFGYDENNLLlKDVNLDVQMDSRIALVGANGCGKTTLLKIM 578
Cdd:COG3839 4 LELENVSKSYGGVEAL-KDIDLDIEDGEFLVLLGPSGCGKSTLLRMI 49
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
529-725 |
3.36e-06 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 48.20 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 529 PPIIQLQDVSFGydennLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS--------RNPR----LR 596
Cdd:cd03215 2 EPVLEVRGLSVK-----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITldgkpvtrRSPRdairAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 597 IGYFTqhhvdsmdlttsavdwmsksfpgktdEEYRRH--LGSFGITGTLGLQkmQLLSGG--QKsrVAFAALCLNNPHIL 672
Cdd:cd03215 77 IAYVP--------------------------EDRKREglVLDLSVAENIALS--SLLSGGnqQK--VVLARWLARDPRVL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 673 VLDEPsnhldTTGLD--------ALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:cd03215 127 ILDEP-----TRGVDvgakaeiyRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
548-728 |
3.49e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.43 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 548 LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRLRI--------GYFTQhhVDSMDLTTSAVDWMS 619
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSViaisaglsGQLTG--IENIEFKMLCMGFKR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 620 KSFPGKTDEeyrrhLGSFGITGTLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTT----GLDALVEaLKN 695
Cdd:PRK13546 118 KEIKAMTPK-----IIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTfaqkCLDKIYE-FKE 191
|
170 180 190
....*....|....*....|....*....|...
gi 14318531 696 FNGGVLMVSHDISVIDSVCKEIWVSEQGTVKRF 728
Cdd:PRK13546 192 QNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDY 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
651-734 |
3.83e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 49.46 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 651 LSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTG----LDALVEALKNfNGGVLMVSHDISVIDSVCKEIWVSEQGTVK 726
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGehemMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
....*...
gi 14318531 727 RfEGTIYD 734
Cdd:PRK13631 256 K-TGTPYE 262
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
198-393 |
4.11e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.10 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 198 DIHIDTFDlYVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLrALSRRELNVpkhvsilhVEQELRGDDTKALQSVL 277
Cdd:PRK10789 315 DVNIRQFT-YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLL-SLIQRHFDV--------SEGDIRFHDIPLTKLQL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 278 DAdvWRKQ---------LLSEEAKINERLKEMDVLRQEFEedslEVKKLDNEREDLDNhLIQisdklvdmesdkaearaa 348
Cdd:PRK10789 385 DS--WRSRlavvsqtpfLFSDTVANNIALGRPDATQQEIE----HVARLASVHDDILR-LPQ------------------ 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 14318531 349 silyglGFSTEAQQQPTnSFSGGWRMRLSLARALFCQPDLLLLDE 393
Cdd:PRK10789 440 ------GYDTEVGERGV-MLSGGQKQRISIARALLLNAEILILDD 477
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
562-723 |
4.40e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.40 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 562 ALVGANGCGKTTLLKIMMEQLRPLKGFV---SRN-------PRLRIGYFTQHHVDSMDLTTSAVDWMSKSFPGKTDEEYR 631
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVlvgGKDietnldaVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQ 1039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 632 RHLGSfgITGTLGL-----QKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGG--VLMVS 704
Cdd:TIGR01257 1040 LEMEA--MLEDTGLhhkrnEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGrtIIMST 1117
|
170
....*....|....*....
gi 14318531 705 HDISVIDSVCKEIWVSEQG 723
Cdd:TIGR01257 1118 HHMDEADLLGDRIAIISQG 1136
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
223-403 |
4.81e-06 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 49.34 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 223 SF----GHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDTkalqSVLDADVWRK-----QLLSEE--A 291
Cdd:COG4608 38 SFdirrGETLGLVGESGCGKSTLGRLLLR--LEEPTSGEIL-----FDGQDI----TGLSGRELRPlrrrmQMVFQDpyA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 292 KINERLKEMDVLRqefeedslevkkldnerEDLDNHliqisdKLVDmeSDKAEARAASILYGLGFSTE-AQQQPtNSFSG 370
Cdd:COG4608 107 SLNPRMTVGDIIA-----------------EPLRIH------GLAS--KAERRERVAELLELVGLRPEhADRYP-HEFSG 160
|
170 180 190
....*....|....*....|....*....|...
gi 14318531 371 GWRMRLSLARALFCQPDLLLLDEPSNMLDVpSI 403
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDV-SI 192
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
199-460 |
5.36e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.49 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 199 IHIDTFDLYVgDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRrelnvpkhVSILHVEQELRGDDTKALQSVLD 278
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR--------MNELESEVRVEGRVEFFNQNIYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 279 ADV----WRKQLLSEEAKINerLKEMDVlrqeFEEDSLEVKKLD-NEREDLDNhLIQISDKLVDMESDKAEARAASILyg 353
Cdd:PRK14258 79 RRVnlnrLRRQVSMVHPKPN--LFPMSV----YDNVAYGVKIVGwRPKLEIDD-IVESALKDADLWDEIKHKIHKSAL-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 354 lgfsteaqqqptnSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDvPSIAYLAEYLktypntvltvSHDRAFLNEVaTD 433
Cdd:PRK14258 150 -------------DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLD-PIASMKVESL----------IQSLRLRSEL-TM 204
|
250 260
....*....|....*....|....*..
gi 14318531 434 IIYQHNERlDYYRGQDFDTFYTTKEER 460
Cdd:PRK14258 205 VIVSHNLH-QVSRLSDFTAFFKGNENR 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
369-424 |
5.46e-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: 49.33 E-value: 5.46e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEP-SNmLDVPS----IAYLAEYLKTYPNTVLTVSHDR 424
Cdd:COG3842 137 SGGQQQRVALARALAPEPRVLLLDEPlSA-LDAKLreemREELRRLQRELGITFIYVTHDQ 196
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
340-443 |
5.61e-06 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 48.49 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 340 SDKAEARAASILYGLGFSTEAQQQPtNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN---- 415
Cdd:cd03296 110 EAEIRAKVHELLKLVQLDWLADRYP-AQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelhv 188
|
90 100
....*....|....*....|....*...
gi 14318531 416 TVLTVSHDRAFLNEVATDIIYQHNERLD 443
Cdd:cd03296 189 TTVFVTHDQEEALEVADRVVVMNKGRIE 216
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
367-457 |
5.71e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 48.62 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 367 SFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTypntvltvshdrafLNEVATDIIYQHNERlDYYR 446
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHE--------------LKEQYTIIIVTHNMQ-QAAR 215
|
90
....*....|.
gi 14318531 447 GQDFDTFYTTK 457
Cdd:PRK14243 216 VSDMTAFFNVE 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
209-422 |
5.78e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 49.78 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 209 GDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDTKALqsvlDADVWRKQLLs 288
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLR--FYDPTSGRIL-----IDGVDIRDL----TLESLRRQIG- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 289 eeakinerlkemdVLRQEFE--EDSLEvkkldneredlDNhlIQISDKLVDMESDKAEARAASI---LYGL--GFSTEAQ 361
Cdd:COG1132 418 -------------VVPQDTFlfSGTIR-----------EN--IRYGRPDATDEEVEEAAKAAQAhefIEALpdGYDTVVG 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 362 QQPTNsFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS----IAYLAEYLKTYpnTVLTVSH 422
Cdd:COG1132 472 ERGVN-LSGGQRQRIAIARALLKDPPILILDEATSALDTETealiQEALERLMKGR--TTIVIAH 533
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
213-422 |
6.01e-06 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 48.04 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 213 RILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELNVP-KHVSILHVEQELRGDDTKALQS-VLDADVWRKQLLSEE 290
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGtTSGQILFNGQPRKPDQFQKCVAyVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 291 AkinerLKEMDVLRQEFEEDSLEVKKLDNEREDLDNHLIQISDKLVdmesdkaearaasilyglgfsteaqqqptNSFSG 370
Cdd:cd03234 101 T-----LTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLV-----------------------------KGISG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 14318531 371 GWRMRLSLARALFCQPDLLLLDEPSNMLDvPSIAYlaeylktypNTVLTVSH 422
Cdd:cd03234 147 GERRRVSIAVQLLWDPKVLILDEPTSGLD-SFTAL---------NLVSTLSQ 188
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
220-444 |
6.72e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 48.46 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 220 LTLSFGHR--YGLVGQNGIGKSTLLRALSrrELNVPKHVSILHVEQELrgddtkalqsvldaDVWRKQLLSEEAKINERL 297
Cdd:PRK13638 20 LNLDFSLSpvTGLVGANGCGKSTLFMNLS--GLLRPQKGAVLWQGKPL--------------DYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 298 KEMDvlRQEFEEDslevkkLDNEredldnhliqISDKLVDMESDKAE-ARAASILYGLGFSTEAQQQPTNSFSGGWRMRL 376
Cdd:PRK13638 84 QDPE--QQIFYTD------IDSD----------IAFSLRNLGVPEAEiTRRVDEALTLVDAQHFRHQPIQCLSHGQKKRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 377 SLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLK---TYPNTVLTVSHDRAFLNEVaTDIIY--QHNERLDY 444
Cdd:PRK13638 146 AIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRrivAQGNHVIISSHDIDLIYEI-SDAVYvlRQGQILTH 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
334-423 |
6.72e-06 |
|
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: 48.07 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 334 KLVDMESDKAEARAASI--LYGLGFSTEAQQQPtNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLK 411
Cdd:cd03295 101 KLLKWPKEKIRERADELlaLVGLDPAEFADRYP-HELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFK 179
|
90
....*....|....*.
gi 14318531 412 TYPN----TVLTVSHD 423
Cdd:cd03295 180 RLQQelgkTIVFVTHD 195
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
343-425 |
7.17e-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: 47.81 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 343 AEARAASILYGLGFSTEAQQQPtNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYL----KTYPNTVL 418
Cdd:COG4181 123 ARARARALLERVGLGHRLDHYP-AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfelnRERGTTLV 201
|
....*..
gi 14318531 419 TVSHDRA 425
Cdd:COG4181 202 LVTHDPA 208
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
201-425 |
7.87e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.91 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 201 IDTFDLYVGDGQ-RILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRR-ELNvpkhvSILHVEQELRgddtkalqsvld 278
Cdd:PRK14267 5 IETVNLRVYYGSnHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlELN-----EEARVEGEVR------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 279 adVWRKQLLSEEAKINERLKEMDVLRQE---------FEEDSLEVK--KLDNEREDLDNHLIQISDKLVDMESDKaeara 347
Cdd:PRK14267 68 --LFGRNIYSPDVDPIEVRREVGMVFQYpnpfphltiYDNVAIGVKlnGLVKSKKELDERVEWALKKAALWDEVK----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 348 asilyglgfsTEAQQQPTNsFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN--TVLTVSHDRA 425
Cdd:PRK14267 141 ----------DRLNDYPSN-LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTHSPA 209
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
543-712 |
8.02e-06 |
|
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: 46.93 E-value: 8.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 543 ENNLllKDVNLDVQMDSRIALVGANGCGKTTLLK--IMMEQLRPLKGFVSRNPRLRIGYftqhhVDSMdlttsavdwmsk 620
Cdd:cd03238 8 VHNL--QNLDVSIPLNVLVVVTGVSGSGKSTLVNegLYASGKARLISFLPKFSRNKLIF-----IDQL------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 621 SFPGKTDEEYRrhlgsfgitgTLGlQKMQLLSGGQKSRVAFAA-LCLNNPHIL-VLDEPSNHLDTTGLDALVEALK---N 695
Cdd:cd03238 69 QFLIDVGLGYL----------TLG-QKLSTLSGGELQRVKLASeLFSEPPGTLfILDEPSTGLHQQDINQLLEVIKgliD 137
|
170
....*....|....*..
gi 14318531 696 FNGGVLMVSHDISVIDS 712
Cdd:cd03238 138 LGNTVILIEHNLDVLSS 154
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
213-425 |
8.07e-06 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 47.73 E-value: 8.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 213 RILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqelrgddtkalqsVLDADVWRkqlLSEeak 292
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG--LDRPTSGEVL----------------IDGQDISS---LSE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 293 inerlKEMDVLRQE-----FEE----DSLEVkkldneredLDNhlIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQ 363
Cdd:COG1136 78 -----RELARLRRRhigfvFQFfnllPELTA---------LEN--VALPLLLAGVSRKERRERARELLERVGLGDRLDHR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 364 PtNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS----IAYLAEYLKTYPNTVLTVSHDRA 425
Cdd:COG1136 142 P-SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPE 206
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
534-729 |
8.36e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.52 E-value: 8.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 534 LQDVSFGYDEN-NLLLKDVNLDVQMDSRIALVGANGCGKTTLLK---------------------IMMEQLR------PL 585
Cdd:TIGR01271 1220 VQGLTAKYTEAgRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSallrllstegeiqidgvswnsVTLQTWRkafgviPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 586 KGFV-SRNPRLRIGYFTQHHVDSMDLTTSAVDWMS--KSFPGKTDeeYRRHLGSFgitgtlglqkmqLLSGGQKSRVAFA 662
Cdd:TIGR01271 1300 KVFIfSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSviEQFPDKLD--FVLVDGGY------------VLSNGHKQLMCLA 1365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 663 ALCLNNPHILVLDEPSNHLDTTGLDALVEALKNF--NGGVLMVSHDISVIDSvCKEIWVSEQGTVKRFE 729
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSfsNCTVILSEHRVEALLE-CQQFLVIEGSSVKQYD 1433
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
345-401 |
8.98e-06 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 47.48 E-value: 8.98e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 345 ARAASILYGLGFSTEAQQQPtNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVP 401
Cdd:COG4136 112 ARVEQALEEAGLAGFADRDP-ATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAA 167
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
550-728 |
9.01e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.72 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 550 DVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRL---------------RIGYFTQ------HHVDSM 608
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrRIGYVFQdarlfpHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 609 DLTTSavdwMSKSFPGKTDEeyrrhlgsfgITGTLGLQKMqL------LSGGQKSRVAFAALCLNNPHILVLDEPSNHLD 682
Cdd:PRK11144 96 NLRYG----MAKSMVAQFDK----------IVALLGIEPL-LdrypgsLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14318531 683 ---TTGLDALVEAL-KNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVKRF 728
Cdd:PRK11144 161 lprKRELLPYLERLaREINIPILYVSHSLDEILRLADRVVVLEQGKVKAF 210
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
442-711 |
9.23e-06 |
|
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: 48.15 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 442 LDYYRGQDFDTFYTTKEERRKNA-------QREYDNQMVYRKHLQEFIDK---YRYNAAKSQEAQSRIKKLEKLPVLEPP 511
Cdd:pfam13304 19 LRFLADFDALVIGLTDERSRNGGiggipslLNGIDPKEPIEFEISEFLEDgvrYRYGLDLEREDVEEKLSSKPTLLEKRL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 512 EQDKTIDFKFPecdKLSPPIIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSR 591
Cdd:pfam13304 99 LLREDSEEREP---KFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 592 NPRLRIGYFTQHHVDSMDLTTSAVDwMSKSFPGKTDEEYRRHLGSFGIT---GTLGLQKMQLLSGGQKSRVAFAALCLNN 668
Cdd:pfam13304 176 ALFPDLKELLQRLVRGLKLADLNLS-DLGEGIEKSLLVDDRLRERGLILlenGGGGELPAFELSDGTKRLLALLAALLSA 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 14318531 669 PH---ILVLDEPSNHLDTTGLDALVEALKNF---NGGVLMVSHDISVID 711
Cdd:pfam13304 255 LPkggLLLIDEPESGLHPKLLRRLLELLKELsrnGAQLILTTHSPLLLD 303
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
194-423 |
9.94e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 48.49 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 194 GKSKDIHIDTFDLYVGdgqriLSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDTKAL 273
Cdd:PRK10070 28 GLSKEQILEKTGLSLG-----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNR--LIEPTRGQVL-----IDGVDIAKI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 274 QsvldadvwrkqllseEAKINE-RLKEMDVLRQEFeedslevkKLDNEREDLDNHLIQIsdKLVDMESDKAEARAASILY 352
Cdd:PRK10070 96 S---------------DAELREvRRKKIAMVFQSF--------ALMPHMTVLDNTAFGM--ELAGINAEERREKALDALR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 353 GLGFSTEAQQQPtNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDvPSIAY-----LAEYLKTYPNTVLTVSHD 423
Cdd:PRK10070 151 QVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEAFSALD-PLIRTemqdeLVKLQAKHQRTIVFISHD 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
491-710 |
9.99e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.26 E-value: 9.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 491 KSQEAQSRIKKL-EKLPVLEPPEQDKtidfKFPECDKlsppiIQLQDVSFGYD--ENNLLLKDVNLDVQMDSRIALVGAN 567
Cdd:PTZ00265 350 KSLEATNSLYEIiNRKPLVENNDDGK----KLKDIKK-----IQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGES 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 568 GCGKTTLLKIMMEQLRPLKG-----------------------FVSRNPRL---------------------------RI 597
Cdd:PTZ00265 421 GCGKSTILKLIERLYDPTEGdiiindshnlkdinlkwwrskigVVSQDPLLfsnsiknnikyslyslkdlealsnyynED 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 598 GYFTQHHVDSMDLTTSA----VDWMSKSFPGKTDEEYRRHLGSFGITGTLGLQKMQL----------------------L 651
Cdd:PTZ00265 501 GNDSQENKNKRNSCRAKcagdLNDMSNTTDSNELIEMRKNYQTIKDSEVVDVSKKVLihdfvsalpdkyetlvgsnaskL 580
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 652 SGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGG----VLMVSHDISVI 710
Cdd:PTZ00265 581 SGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNenriTIIIAHRLSTI 643
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
547-682 |
1.05e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 47.93 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 547 LLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPrlRIGYFTQhhvdsmdlttsaVDWMsksFPGKT 626
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--RISFSSQ------------FSWI---MPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 627 DE---------EYRRH----------------------LGSFGITgtlglqkmqlLSGGQKSRVAFAALCLNNPHILVLD 675
Cdd:cd03291 115 KEniifgvsydEYRYKsvvkacqleeditkfpekdntvLGEGGIT----------LSGGQRARISLARAVYKDADLYLLD 184
|
....*..
gi 14318531 676 EPSNHLD 682
Cdd:cd03291 185 SPFGYLD 191
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
362-423 |
1.11e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 48.16 E-value: 1.11e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 362 QQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS----IAYLAEYLKTYPNTVLTVSHD 423
Cdd:COG4586 149 DTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSkeaiREFLKEYNRERGTTILLTSHD 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
339-423 |
1.16e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 48.95 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 339 ESDKAEARAASILYGLGFSTEAQQQPtNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS----IAYLAEyLKTYP 414
Cdd:PRK10535 117 ERKQRLLRAQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSgeevMAILHQ-LRDRG 194
|
....*....
gi 14318531 415 NTVLTVSHD 423
Cdd:PRK10535 195 HTVIIVTHD 203
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
548-707 |
1.18e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 47.39 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 548 LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRP------LKGFVSRNPRLRIGYFTQHHV-----DSMD-----LT 611
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYqhgsitLDGKPVEGPGAERGVVFQNEGllpwrNVQDnvafgLQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 612 TSAVDWMSKsfpgktDEEYRRHLGSFGITGtLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVE 691
Cdd:PRK11248 97 LAGVEKMQR------LEIAHQMLKKVGLEG-AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169
|
170 180
....*....|....*....|
gi 14318531 692 AL----KNFNGGVLMVSHDI 707
Cdd:PRK11248 170 LLlklwQETGKQVLLITHDI 189
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
550-719 |
1.28e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 47.80 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 550 DVNLDVQMDSRIALVGANGCGKTTLLKIMM----------------------EQLRPLKG---------FVSRNPRLRIG 598
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLrleeptsgeilfdgqditglsgRELRPLRRrmqmvfqdpYASLNPRMTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 599 Y-----FTQHHV-DSMDLTTSAVDWMSKSfpGKTDEEYRRHLGSFgitgtlglqkmqllSGGQKSRVAFA-ALCLNnPHI 671
Cdd:COG4608 116 DiiaepLRIHGLaSKAERRERVAELLELV--GLRPEHADRYPHEF--------------SGGQRQRIGIArALALN-PKL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 672 LVLDEPsnhldTTGLDALVEA--------LKN-FNGGVLMVSHDISVIDSVCKEIWV 719
Cdd:COG4608 179 IVCDEP-----VSALDVSIQAqvlnlledLQDeLGLTYLFISHDLSVVRHISDRVAV 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
205-395 |
1.61e-05 |
|
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: 46.66 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 205 DLYVGDGQ-RILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDTKALQSvldADVWR 283
Cdd:cd03224 5 NLNAGYGKsQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMG--LLPPRSGSIR-----FDGRDITGLPP---HERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 284 K--QLLSEEAKInerLKEMDVlrqefeEDSLEV----KKLDNEREDLDnhliqisdKLVDMESDKAEARaasilyglgfs 357
Cdd:cd03224 75 AgiGYVPEGRRI---FPELTV------EENLLLgayaRRRAKRKARLE--------RVYELFPRLKERR----------- 126
|
170 180 190
....*....|....*....|....*....|....*...
gi 14318531 358 teaqQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPS 395
Cdd:cd03224 127 ----KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
367-422 |
1.83e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.56 E-value: 1.83e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 367 SFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTV----LTVSH 422
Cdd:PRK11144 128 SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREInipiLYVSH 187
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
532-682 |
1.90e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 47.72 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENnLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIM-----------------MEQLRPLKgfvsRNpr 594
Cdd:PRK11000 4 VTLRNVTKAYGDV-VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIagleditsgdlfigekrMNDVPPAE----RG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 595 lrIGYFTQHHVDSMDLttSAVDWMS---KSFPGKTDEEYRR--HLGSFGITGTLGLQKMQLLSGGQKSRVAFAALCLNNP 669
Cdd:PRK11000 77 --VGMVFQSYALYPHL--SVAENMSfglKLAGAKKEEINQRvnQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEP 152
|
170
....*....|...
gi 14318531 670 HILVLDEPSNHLD 682
Cdd:PRK11000 153 SVFLLDEPLSNLD 165
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
531-707 |
1.92e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 47.01 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDENNLL--LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS-----------RNPRLRI 597
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKidgelltaenvWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 598 GYFTQHHvDSMDLTTSAVDWMSKSFPGK---TDEEYRRHLGSFGITGTLGLQKMQ--LLSGGQKSRVAFAALCLNNPHIL 672
Cdd:PRK13642 84 GMVFQNP-DNQFVGATVEDDVAFGMENQgipREEMIKRVDEALLAVNMLDFKTREpaRLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 14318531 673 VLDEPSNHLDTTGLDALVEAL----KNFNGGVLMVSHDI 707
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIheikEKYQLTVLSITHDL 201
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
528-705 |
1.92e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.71 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 528 SPPIIQLQDVS--FGydeNNLLLKDVNLDVQmDSRI-ALVGANGCGKTTLLKIMMEQLRPLKG--FVS------RNPR-- 594
Cdd:COG3845 2 MPPALELRGITkrFG---GVVANDDVSLTVR-PGEIhALLGENGAGKSTLMKILYGLYQPDSGeiLIDgkpvriRSPRda 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 595 --LRIGYFTQHH--VDSMdlttSAVD----WMSKSFPGKTD-EEYRRHLGSfgITGTLGLQ-----KMQLLSGGQKSRVA 660
Cdd:COG3845 78 iaLGIGMVHQHFmlVPNL----TVAEnivlGLEPTKGGRLDrKAARARIRE--LSERYGLDvdpdaKVEDLSVGEQQRVE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 14318531 661 FA-ALcLNNPHILVLDEPsnhldTTGL-----DALVEALKNF--NG-GVLMVSH 705
Cdd:COG3845 152 ILkAL-YRGARILILDEP-----TAVLtpqeaDELFEILRRLaaEGkSIIFITH 199
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
369-423 |
2.30e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 46.29 E-value: 2.30e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEP---------SNMLDVpsiayLAEYLKTYPNTVLTVSHD 423
Cdd:COG3840 131 SGGQRQRVALARCLVRKRPILLLDEPfsaldpalrQEMLDL-----VDELCRERGLTVLMVTHD 189
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
530-731 |
2.30e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.20 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 530 PIIQLQDVSFGYDENN--LLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKG--FVSRNprlRIGYFTQhhv 605
Cdd:PLN03130 613 PAISIKNGYFSWDSKAerPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDasVVIRG---TVAYVPQ--- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 606 dsmdlttsaVDWMSKS-------FPGKTD-EEYRRHLGSFGITGTLGL----------QKMQLLSGGQKSRVAFAALCLN 667
Cdd:PLN03130 687 ---------VSWIFNAtvrdnilFGSPFDpERYERAIDVTALQHDLDLlpggdlteigERGVNISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 668 NPHILVLDEPSNHLDT-TGLDALVEALKNFNGGV--LMVSHDISVIDSVCKEIWVSEqGTVKRfEGT 731
Cdd:PLN03130 758 NSDVYIFDDPLSALDAhVGRQVFDKCIKDELRGKtrVLVTNQLHFLSQVDRIILVHE-GMIKE-EGT 822
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
548-724 |
2.61e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.47 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 548 LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRlriGYFTQHHVDSMDL-------TTSAVDWMS- 619
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI---NYNKLDHKLAAQLgigiiyqELSVIDELTv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 620 --KSFPGK-----------TDEEYRRHLGSFgITGTLGLQ-----KMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHL 681
Cdd:PRK09700 98 leNLYIGRhltkkvcgvniIDWREMRVRAAM-MLLRVGLKvdldeKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14318531 682 DTTGLD---ALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGT 724
Cdd:PRK09700 177 TNKEVDylfLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGS 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
219-425 |
2.92e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.63 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 219 QLTLSFGHR--YGLVGQNGIGKSTLLRALSRRELNVPKHvsilhveqELRGDDTKALQSVLDadvWRKQLlseeakinER 296
Cdd:PRK14271 39 QVSMGFPARavTSLMGPTGSGKTTFLRTLNRMNDKVSGY--------RYSGDVLLGGRSIFN---YRDVL--------EF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 297 LKEMDVLRQEfeEDSLEVKKLDNEREDLDNHliqisdKLVDMESDKAEARAAsiLYGLGFSTEAQQQPTNS---FSGGWR 373
Cdd:PRK14271 100 RRRVGMLFQR--PNPFPMSIMDNVLAGVRAH------KLVPRKEFRGVAQAR--LTEVGLWDAVKDRLSDSpfrLSGGQQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 14318531 374 MRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN--TVLTVSHDRA 425
Cdd:PRK14271 170 QLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLA 223
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
369-422 |
3.20e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 47.41 E-value: 3.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVSH 422
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
532-729 |
3.48e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 45.78 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGYDENNLLLkDVNLDVQMDSRIALVGANGCGKTTLLKI--MMEQlrPLKG--------F-VSRNP------- 593
Cdd:PRK11124 3 IQLNGINCFYGAHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVlnLLEM--PRSGtlniagnhFdFSKTPsdkaire 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 594 -RLRIGY-FTQH----HVDSMDLTTSA---VDWMSKSfpgKTDEEYRRHLGSFGITGTLGLQKMQLlSGGQKSRVAFAAL 664
Cdd:PRK11124 80 lRRNVGMvFQQYnlwpHLTVQQNLIEApcrVLGLSKD---QALARAEKLLERLRLKPYADRFPLHL-SGGQQQRVAIARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318531 665 CLNNPHILVLDEPSNHLD---TTGLDALVEALKNFNGGVLMVSHDISVIDSVCKEI------WVSEQGTVKRFE 729
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDpeiTAQIVSIIRELAETGITQVIVTHEVEVARKTASRVvymengHIVEQGDASCFT 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
207-402 |
3.62e-05 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 47.02 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 207 YVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELnvPKHVSIL---HVEQELRGDDTKALQSVLDADVwr 283
Cdd:TIGR02203 340 YPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE--PDSGQILldgHDLADYTLASLRRQVALVSQDV-- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 284 kQLLSEEAKINERLKEMDVLRQEFEEDSLEvkkldneredlDNHLIQISDKLvdmesdkaearaasilyGLGFSTEAQQQ 363
Cdd:TIGR02203 416 -VLFNDTIANNIAYGRTEQADRAEIERALA-----------AAYAQDFVDKL-----------------PLGLDTPIGEN 466
|
170 180 190
....*....|....*....|....*....|....*....
gi 14318531 364 PTNsFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS 402
Cdd:TIGR02203 467 GVL-LSGGQRQRLAIARALLKDAPILILDEATSALDNES 504
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
360-435 |
3.86e-05 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 46.62 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 360 AQQQPTNsFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN----TVLTVSHDRAFLNEVATDII 435
Cdd:PRK10851 130 ADRYPAQ-LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEelkfTSVFVTHDQEEAMEVADRVV 208
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
189-442 |
4.11e-05 |
|
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: 45.60 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 189 FGSSAGKSKDIHIDTFDLYVGDgQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELnvPKHVSIlhveqELRGD 268
Cdd:cd03220 13 YKGGSSSLKKLGILGRKGEVGE-FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYP--PDSGTV-----TVRGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 269 DTK--ALQSVLDADvwrkqlLS--EEAKINERLKEMDvlrqefeedslevkkldneREDLDNHLIQISDklvdmesdkae 344
Cdd:cd03220 85 VSSllGLGGGFNPE------LTgrENIYLNGRLLGLS-------------------RKEIDEKIDEIIE----------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 345 araasiLYGLGfstEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEpsnMLDV-------PSIAYLAEYLKTyPNTV 417
Cdd:cd03220 129 ------FSELG---DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE---VLAVgdaafqeKCQRRLRELLKQ-GKTV 195
|
250 260
....*....|....*....|....*
gi 14318531 418 LTVSHDRAFLNEVATDIIYQHNERL 442
Cdd:cd03220 196 ILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
207-422 |
4.12e-05 |
|
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: 45.00 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 207 YVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLrALSRRELnVPKHVSILhveqeLRGDDTKALQsvldadvwrkql 286
Cdd:cd03247 10 YPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLL-QLLTGDL-KPQQGEIT-----LDGVPVSDLE------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 287 lseeakiNERLKEMDVLRQEFeedslevkkldneredldnHLIqisdklvdmesdkaearAASILYGLGfsteaqqqptN 366
Cdd:cd03247 71 -------KALSSLISVLNQRP-------------------YLF-----------------DTTLRNNLG----------R 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 367 SFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS----IAYLAEYLKTypNTVLTVSH 422
Cdd:cd03247 98 RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITerqlLSLIFEVLKD--KTLIWITH 155
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
211-436 |
5.48e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 45.88 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 211 GQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrrelnvpkhvSILHVEQ-ELRGDDTKALQSvldadvwrkqllSE 289
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLN----------GLLQPTEgKVTVGDIVVSST------------SK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 290 EAKINERLKEMDVLRQEFEEDSLEVKKLDNeredldnhlIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQPTNSFS 369
Cdd:PRK13643 76 QKEIKPVRKKVGVVFQFPESQLFEETVLKD---------VAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318531 370 GGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS---IAYLAEYLKTYPNTVLTVSHdraFLNEVA--TDIIY 436
Cdd:PRK13643 147 GGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH---LMDDVAdyADYVY 215
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
334-399 |
5.48e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.27 E-value: 5.48e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 334 KLVDMESDKAEARAASILYGLGFsTEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLD 399
Cdd:NF000106 112 R*LDLSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
361-394 |
5.77e-05 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 45.23 E-value: 5.77e-05
10 20 30
....*....|....*....|....*....|....
gi 14318531 361 QQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEP 394
Cdd:cd03218 127 RKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
561-693 |
6.03e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.41 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 561 IALVGANGCGKTTLLKIMMEQLRP--LKGFVSRNPR-------LRIGYFTQHHVDSMDLTT-SAVDWMSKSFPGKTDEEY 630
Cdd:PLN03211 97 LAVLGPSGSGKSTLLNALAGRIQGnnFTGTILANNRkptkqilKRTGFVTQDDILYPHLTVrETLVFCSLLRLPKSLTKQ 176
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 631 RRHLGSFGITGTLGLQK----------MQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEAL 693
Cdd:PLN03211 177 EKILVAESVISELGLTKcentiignsfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
369-435 |
6.26e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.89 E-value: 6.26e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEY---LKTYPNTVLT-VSHDRAFLNEVATDII 435
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELlleLQQKENMALVlITHDLALVAEAAHKII 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
341-400 |
6.50e-05 |
|
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: 44.92 E-value: 6.50e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318531 341 DKAE--ARAASILYGLGFSTEAQQQPtNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDV 400
Cdd:cd03300 103 PKAEikERVAEALDLVQLEGYANRKP-SQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
363-395 |
6.61e-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: 44.97 E-value: 6.61e-05
10 20 30
....*....|....*....|....*....|...
gi 14318531 363 QPTNSFSGGWRMRLSLARALFCQPDLLLLDEPS 395
Cdd:COG0410 132 QRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
214-402 |
7.29e-05 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 44.84 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 214 ILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDTKALQsvldadvwrkqllseeakI 293
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLER--FYDPTSGEIL-----LDGVDIRDLN------------------L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 294 NERLKEMDVLRQE---FEEDSLEVKKL-DNEREDldnhliqisdklVDMESDKAEARAASILYGL--GFSTEAQQQPTnS 367
Cdd:cd03249 73 RWLRSQIGLVSQEpvlFDGTIAENIRYgKPDATD------------EEVEEAAKKANIHDFIMSLpdGYDTLVGERGS-Q 139
|
170 180 190
....*....|....*....|....*....|....*
gi 14318531 368 FSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS 402
Cdd:cd03249 140 LSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
213-247 |
8.24e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 44.69 E-value: 8.24e-05
10 20 30
....*....|....*....|....*....|....*
gi 14318531 213 RILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSR 247
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG 74
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
532-577 |
1.01e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.22 E-value: 1.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 14318531 532 IQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKI 577
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRM 49
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
369-423 |
1.16e-04 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 45.06 E-value: 1.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEP-SNmLDVPS----IAYLAEYLKTYPNTVLTVSHD 423
Cdd:COG3839 135 SGGQRQRVALGRALVREPKVFLLDEPlSN-LDAKLrvemRAEIKRLHRRLGTTTIYVTHD 193
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
199-399 |
1.19e-04 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 44.64 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 199 IHIDTFDLYVGDgQRILSNaqLTLSFGHR--YGLVGQNGIGKSTLLRALSRreLNvpKHVSILHVEQELRGDDtkalQSV 276
Cdd:COG1117 12 IEVRNLNVYYGD-KQALKD--INLDIPENkvTALIGPSGCGKSTLLRCLNR--MN--DLIPGARVEGEILLDG----EDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 277 LDADV----WRKQL-----------LS-EE-----AKINERL--KEMDvlrqEFEEDSL-------EVKkldneredldn 326
Cdd:COG1117 81 YDPDVdvveLRRRVgmvfqkpnpfpKSiYDnvaygLRLHGIKskSELD----EIVEESLrkaalwdEVK----------- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 327 hliqisDKLvdmesdkaearaasilyglgfsteaqQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLD 399
Cdd:COG1117 146 ------DRL--------------------------KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
532-729 |
1.43e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 44.46 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 532 IQLQDVSFGY-DENNLLLKDVNLDVQMDSRIALVGANGCGKTTLL---------------------KIMMEQLR------ 583
Cdd:cd03289 3 MTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflrllntegdiqidgvswnSVPLQKWRkafgvi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 584 PLKGFVSRNP-RLRIGYFTQHHVDSMDLTTSAVDWMS--KSFPGKTDeeYRRHLGSFgitgtlglqkmqLLSGGQKSRVA 660
Cdd:cd03289 83 PQKVFIFSGTfRKNLDPYGKWSDEEIWKVAEEVGLKSviEQFPGQLD--FVLVDGGC------------VLSHGHKQLMC 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318531 661 FAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGG--VLMVSHDISVIDSvCKEIWVSEQGTVKRFE 729
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADctVILSEHRIEAMLE-CQRFLVIEENKVRQYD 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
540-752 |
1.44e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 540 GYDENNLLLKDVN---LDVQMDSRIALVGANGCGKTTLLKI-----MMEQLRPLKGFVSRNPRL-RIGYFTQHHVDSMDL 610
Cdd:PTZ00265 1244 GDEEQNVGMKNVNefsLTKEGGSGEDSTVFKNSGKILLDGVdicdyNLKDLRNLFSIVSQEPMLfNMSIYENIKFGKEDA 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 611 TT---------SAVDWMSKSFPGKtdeeYRRHLGSFGitgtlglqkmQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHL 681
Cdd:PTZ00265 1324 TRedvkrackfAAIDEFIESLPNK----YDTNVGPYG----------KSLSGGQKQRIAIARALLREPKILLLDEATSSL 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 682 DTTG----LDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVS---EQGTVKRFEGTiydyRDYILQSADaaGVVKKH 752
Cdd:PTZ00265 1390 DSNSekliEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNnpdRTGSFVQAHGT----HEELLSVQD--GVYKKY 1461
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
538-706 |
1.51e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 44.00 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 538 SFGYDENNL-LLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS------------RNPRLR---IGYFT 601
Cdd:PRK10584 15 SVGQGEHELsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlvgqplhqmdeeARAKLRakhVGFVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 602 QHHVDSMDLTTSAVDWMSKSFPGKTDEEYRRH----LGSFGITGTLGLQKMQLlSGGQKSRVAFAALCLNNPHILVLDEP 677
Cdd:PRK10584 95 QSFMLIPTLNALENVELPALLRGESSRQSRNGakalLEQLGLGKRLDHLPAQL-SGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|...
gi 14318531 678 SNHLD-TTG---LDALVEALKNFNGGVLMVSHD 706
Cdd:PRK10584 174 TGNLDrQTGdkiADLLFSLNREHGTTLILVTHD 206
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
341-442 |
1.65e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 44.43 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 341 DKAEARAASILYGLGFSTEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYP---NTV 417
Cdd:PRK13641 119 DEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQkagHTV 198
|
90 100
....*....|....*....|....*
gi 14318531 418 LTVSHDRAFLNEVATDIIYQHNERL 442
Cdd:PRK13641 199 ILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
360-431 |
1.76e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 44.24 E-value: 1.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 360 AQQQPtNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLD-------VPSIAYLAEYLKTypnTVLTVSHDrafLNEVA 431
Cdd:PRK13635 134 LNREP-HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrrevLETVRQLKEQKGI---TVLSITHD---LDEAA 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
369-423 |
1.78e-04 |
|
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: 43.40 E-value: 1.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEP-SN---MLDVPSIAYLAEYLKTYPNTVLTVSHD 423
Cdd:cd03301 132 SGGQRQRVALGRAIVREPKVFLMDEPlSNldaKLRVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
363-394 |
1.86e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 43.86 E-value: 1.86e-04
10 20 30
....*....|....*....|....*....|..
gi 14318531 363 QPTNSFSGGWRMRLSLARALFCQPDLLLLDEP 394
Cdd:COG1137 132 SKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
338-431 |
2.15e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.85 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 338 MESDKAEARAASILYGLGFSTEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS----IAYLAEYLKTY 413
Cdd:PRK10261 434 LPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIrgqiINLLLDLQRDF 513
|
90
....*....|....*...
gi 14318531 414 PNTVLTVSHDRAFLNEVA 431
Cdd:PRK10261 514 GIAYLFISHDMAVVERIS 531
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
522-737 |
2.24e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.66 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 522 PECDKLSPPIIQLQDVSFGYDENNLLlKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGfvsrnpRLRIGYFT 601
Cdd:PRK15439 2 QTSDTTAPPLLCARSISKQYSGVEVL-KGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSG------TLEIGGNP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 602 QHH---VDSMDLTTSAVDWMSKSFPGKTDEEYRrhlgSFGITGTLGL-----QKMQLLSGGQKSRVAFAAL--------- 664
Cdd:PRK15439 75 CARltpAKAHQLGIYLVPQEPLLFPNLSVKENI----LFGLPKRQASmqkmkQLLAALGCQLDLDSSAGSLevadrqive 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 665 ----CLNNPHILVLDEPSNHL---DTTGLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVKrFEGTIYDYRD 737
Cdd:PRK15439 151 ilrgLMRDSRILILDEPTASLtpaETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIA-LSGKTADLST 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
220-403 |
2.40e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 43.93 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 220 LTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILHVEQELRGDDTKALQSVldadvwRK--QLLSEE--AKINE 295
Cdd:PRK15079 42 LRLYEGETLGVVGESGCGKSTFARAIIG--LVKATDGEVAWLGKDLLGMKDDEWRAV------RSdiQMIFQDplASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 296 RLKEMDVLRqefeedslevkkldnerEDLDNHLIQISDKLVdmesdKAEARAASILYGLgFSTEAQQQPtNSFSGGWRMR 375
Cdd:PRK15079 114 RMTIGEIIA-----------------EPLRTYHPKLSRQEV-----KDRVKAMMLKVGL-LPNLINRYP-HEFSGGQCQR 169
|
170 180
....*....|....*....|....*...
gi 14318531 376 LSLARALFCQPDLLLLDEPSNMLDVpSI 403
Cdd:PRK15079 170 IGIARALILEPKLIICDEPVSALDV-SI 196
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
162-400 |
2.46e-04 |
|
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: 44.35 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 162 KYEASKLINDQKEEDY--DSFFlqINPLEFGSSAGKSKDIHIDTFDLYVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKS 239
Cdd:TIGR01193 437 KLQAARVANNRLNEVYlvDSEF--INKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKS 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 240 TLLRALSRreLNVPKHVSILhveqelrgddtkaLQSVLDADVWRKQLlseEAKINerlkemdVLRQEFEEDSLEVkkldn 319
Cdd:TIGR01193 515 TLAKLLVG--FFQARSGEIL-------------LNGFSLKDIDRHTL---RQFIN-------YLPQEPYIFSGSI----- 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 320 eredLDNHLIQISDKLVDMESDKA----EARAASILYGLGFSTEAQQQPTNsFSGGWRMRLSLARALFCQPDLLLLDEPS 395
Cdd:TIGR01193 565 ----LENLLLGAKENVSQDEIWAAceiaEIKDDIENMPLGYQTELSEEGSS-ISGGQKQRIALARALLTDSKVLILDEST 639
|
....*
gi 14318531 396 NMLDV 400
Cdd:TIGR01193 640 SNLDT 644
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
211-423 |
2.72e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 43.62 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 211 GQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRElnVPKHVSILHVEQELRGDDTKALQsvldadvwrkqllsee 290
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQ--PPSEGEILLDAQPLESWSSKAFA---------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 291 akinerlKEMDVLRQEF-EEDSLEVKKLDN-EREDLDNHLIQISdklvdmESDKAEARAASILYGLgfsTEAQQQPTNSF 368
Cdd:PRK10575 85 -------RKVAYLPQQLpAAEGMTVRELVAiGRYPWHGALGRFG------AADREKVEEAISLVGL---KPLAHRLVDSL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEPSNMLDvpsIAYLAEYLKTYPN-------TVLTVSHD 423
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALD---IAHQVDVLALVHRlsqerglTVIAVLHD 207
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
207-435 |
2.79e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 43.16 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 207 YVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrrELNVPKHVSILhveqeLRGDDTkalqSVLDADVWRKQL 286
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVA--SLISPTSGTLL-----FEGEDI----STLKPEIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 287 lSEEAkinerlkEMDVLRQEFEEDSLEVKkldneredldnhlIQISDKLVDMesdkaeARAASILYGLGFSTEAQQQPTN 366
Cdd:PRK10247 84 -SYCA-------QTPTLFGDTVYDNLIFP-------------WQIRNQQPDP------AIFLDDLERFALPDTILTKNIA 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 367 SFSGGWRMRLSLARALFCQPDLLLLDEPSNMLD------VPSIayLAEYLKTYPNTVLTVSHDRaflNEV--ATDII 435
Cdd:PRK10247 137 ELSGGEKQRISLIRNLQFMPKVLLLDEITSALDesnkhnVNEI--IHRYVREQNIAVLWVTHDK---DEInhADKVI 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
346-444 |
3.20e-04 |
|
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: 42.87 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 346 RAASILYGLGFSTEAQQQPtNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDvPSI-----AYLAEYLKTYPNTVLTV 420
Cdd:cd03298 108 AIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALD-PALraemlDLVLDLHAETKMTVLMV 185
|
90 100
....*....|....*....|....
gi 14318531 421 SHDRAFLNEVATDIIYQHNERLDY 444
Cdd:cd03298 186 THQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
358-431 |
3.67e-04 |
|
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: 43.19 E-value: 3.67e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 358 TEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDvPS-----IAYLAEYLKTYPNTVLTVSHDrafLNEVA 431
Cdd:TIGR04520 127 EDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLD-PKgrkevLETIRKLNKEEGITVISITHD---MEEAV 201
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
207-427 |
3.74e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 42.55 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 207 YVGdGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELNVPKHVSilhveqeLRGDDTKALQSvldadvwrkql 286
Cdd:PRK10908 11 YLG-GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIW-------FSGHDITRLKN----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 287 lseeakinerlKEMDVLRQE----FEEDSLEVkkldnEREDLDNhlIQISDKLVDMESDKAEARAASILYGLGFSTEAQQ 362
Cdd:PRK10908 72 -----------REVPFLRRQigmiFQDHHLLM-----DRTVYDN--VAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKN 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 363 QPTNsFSGGWRMRLSLARALFCQPDLLLLDEPSNMLD---VPSIAYLAEYLKTYPNTVLTVSHDRAFL 427
Cdd:PRK10908 134 FPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
367-422 |
4.03e-04 |
|
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: 42.15 E-value: 4.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 367 SFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN---TVLTVSH 422
Cdd:cd03213 111 GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtgrTIICSIH 169
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
210-402 |
4.08e-04 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILHVEQELRGDDTKALQS---VLDADVwrkQL 286
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFR--FYDVSSGSILIDGQDIREVTLDSLRRaigVVPQDT---VL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 287 LSEEAKINERLKEMDVLrqefEEDSLEVKKLdneredldnhlIQISDKLVDMESdkaearaasilyglGFSTEAQQQPTn 366
Cdd:cd03253 87 FNDTIGYNIRYGRPDAT----DEEVIEAAKA-----------AQIHDKIMRFPD--------------GYDTIVGERGL- 136
|
170 180 190
....*....|....*....|....*....|....*.
gi 14318531 367 SFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS 402
Cdd:cd03253 137 KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHT 172
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
347-422 |
4.18e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 43.71 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 347 AASILYGLGFSTEAQQQPTNSF----SGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN---TVLT 419
Cdd:PLN03211 182 AESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQkgkTIVT 261
|
...
gi 14318531 420 VSH 422
Cdd:PLN03211 262 SMH 264
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
366-424 |
5.12e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 43.41 E-value: 5.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 366 NSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKtypntvlTVSHDR 424
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALD-------ELMKGR 521
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
530-723 |
6.23e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.12 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 530 PIIQLQDVSF-GYdennlllKDVNLDVQMDSRIALVGANGCGKTTLLKIMMeQLRPLKG---------FVSRNP--RLRI 597
Cdd:PRK15439 267 PVLTVEDLTGeGF-------RNISLEVRAGEILGLAGVVGAGRTELAETLY-GLRPARGgrimlngkeINALSTaqRLAR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 598 G--YFTQH------HVDS-MDLTTSAVDWMSKSF---PGK---TDEEYRRHLGsfgITGTLGLQKMQLLSGGQKSRVAFA 662
Cdd:PRK15439 339 GlvYLPEDrqssglYLDApLAWNVCALTHNRRGFwikPARenaVLERYRRALN---IKFNHAEQAARTLSGGNQQKVLIA 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 663 AlCLN-NPHILVLDEPsnhldTTGLDA--------LVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQG 723
Cdd:PRK15439 416 K-CLEaSPQLLIVDEP-----TRGVDVsarndiyqLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
651-723 |
6.34e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.31 E-value: 6.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 651 LSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTT---GLDALVEAL-KNFNGGVLMVSHDISVIDSVCKEIWVSEQG 723
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQG 245
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
359-395 |
6.40e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 42.17 E-value: 6.40e-04
10 20 30
....*....|....*....|....*....|....*..
gi 14318531 359 EAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPS 395
Cdd:PRK11614 129 ERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
355-427 |
6.48e-04 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 41.93 E-value: 6.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 355 GFSTEAQQQPTNsFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLA-----EYLKTYPNTVLTVSHDRAFL 427
Cdd:cd03290 129 GDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqegilKFLQDDKRTLVLVTHKLQYL 205
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
207-411 |
6.56e-04 |
|
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: 42.15 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 207 YVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRReLNVPKHVSILHVEQelrgdDTKALQSvldadvWRKQL 286
Cdd:cd03289 12 YTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSW-----NSVPLQK------WRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 287 LSEEAKI----NERLKEMDVLRQEFEEDSLEVKkldnEREDLDNHLIQISDKLvdmesdkaearAASILYGlGFsteaqq 362
Cdd:cd03289 80 GVIPQKVfifsGTFRKNLDPYGKWSDEEIWKVA----EEVGLKSVIEQFPGQL-----------DFVLVDG-GC------ 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14318531 363 qptnSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLK 411
Cdd:cd03289 138 ----VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK 182
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
537-705 |
6.61e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 42.21 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 537 VSFGYDEnnlLLKDVNLDVQMDSRIALVGANGCGKTTLLKImmeqlrpLKGFVSRNPRLRIG---YFTQHHVDSMDLT-- 611
Cdd:PRK14247 11 VSFGQVE---VLDGVNLEIPDNTITALMGPSGSGKSTLLRV-------FNRLIELYPEARVSgevYLDGQDIFKMDVIel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 612 ---TSAVDWMSKSFPG-----------------KTDEEYRRHLgsfgitgTLGLQKMQL--------------LSGGQKS 657
Cdd:PRK14247 81 rrrVQMVFQIPNPIPNlsifenvalglklnrlvKSKKELQERV-------RWALEKAQLwdevkdrldapagkLSGGQQQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 14318531 658 RVAFAALCLNNPHILVLDEPSNHLD---TTGLDALVEALKNfNGGVLMVSH 705
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDpenTAKIESLFLELKK-DMTIVLVTH 203
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
369-431 |
7.40e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 42.03 E-value: 7.40e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEPSNMLD----VPSIAYLAEYLKTYPNTVLTVSHDrafLNEVA 431
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD---LDEVA 205
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
490-676 |
7.92e-04 |
|
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: 42.86 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 490 AKSQEAQSRIKKLE-KLPVLEPPEQDKTIDFKFPECDKlsppiIQLQDVSFGY----DENNLLLKDVNLDVQMDSRIALV 564
Cdd:COG4615 290 SRANVALRKIEELElALAAAEPAAADAAAPPAPADFQT-----LELRGVTYRYpgedGDEGFTLGPIDLTIRRGELVFIV 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 565 GANGCGKTTLLKIMMEQLRPLKGfvsrnpRLRigyftqhhVDSMDLTTSAVDWmsksfpgktdeeYRR---------HLg 635
Cdd:COG4615 365 GGNGSGKSTLAKLLTGLYRPESG------EIL--------LDGQPVTADNREA------------YRQlfsavfsdfHL- 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 636 sF----GITGTLG-------LQKMQL---------------LSGGQKSRVAFAALCLNNPHILVLDE 676
Cdd:COG4615 418 -FdrllGLDGEADpararelLERLELdhkvsvedgrfsttdLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
651-725 |
8.02e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.42 E-value: 8.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 651 LSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTT----GLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTV 725
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTiqaqIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
321-394 |
8.04e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 8.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 321 REDLDNHLiqisdKLVDMESDKAEARAASIL--YGLGfstEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEP 394
Cdd:NF033858 357 RQNLELHA-----RLFHLPAAEIAARVAEMLerFDLA---DVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
230-436 |
9.24e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 42.30 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 230 LVGQNGIGKSTLLRALSRreLNVPKHVSILHVEQELRGDDTKALQSVLDADVWR--KQLLSEEAKINER---LKEMDVLR 304
Cdd:COG3593 28 LVGENNSGKSSILEALRL--LLGPSSSRKFDEEDFYLGDDPDLPEIEIELTFGSllSRLLRLLLKEEDKeelEEALEELN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 305 QEFEEdslEVKKLdneREDLDNHLIQISDKL-VDMESDKAE----ARAASILYGLGFSTeaqqqPTNSFSGG--WRMRLS 377
Cdd:COG3593 106 EELKE---ALKAL---NELLSEYLKELLDGLdLELELSLDEledlLKSLSLRIEDGKEL-----PLDRLGSGfqRLILLA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318531 378 LARALF-----CQPDLLLLDEPSNMLDVPSIAYLAEYLKTY---PNTVLTVSHDRAFLNEVATDIIY 436
Cdd:COG3593 175 LLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELsekPNQVIITTHSPHLLSEVPLENIR 241
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
550-712 |
9.77e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.05 E-value: 9.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 550 DVNLDVQMDSRIAL-VGANGCGKTTLLkimmEQLR-PLKGFVSRNPRLRigyftqHHVDSMDLTTSAVDWMSKSFPGKTD 627
Cdd:cd03240 13 HERSEIEFFSPLTLiVGQNGAGKTTII----EALKyALTGELPPNSKGG------AHDPKLIREGEVRAQVKLAFENANG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 628 EEY--RRHLGSF--------GITGTLGLQKMQLLSGGQKS------RVAFA-ALCLNNPhILVLDEPSNHLDTTGLD-AL 689
Cdd:cd03240 83 KKYtiTRSLAILenvifchqGESNWPLLDMRGRCSGGEKVlasliiRLALAeTFGSNCG-ILALDEPTTNLDEENIEeSL 161
|
170 180
....*....|....*....|....*..
gi 14318531 690 VEALKNFNGG----VLMVSHDISVIDS 712
Cdd:cd03240 162 AEIIEERKSQknfqLIVITHDEELVDA 188
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
367-400 |
1.06e-03 |
|
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: 1.06e-03
10 20 30
....*....|....*....|....*....|....
gi 14318531 367 SFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDV 400
Cdd:TIGR01271 548 TLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
338-436 |
1.07e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 41.71 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 338 MESDKAEARAASILYGLGFSTEAQQQPtNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPS----IAYLAEYLKTY 413
Cdd:PRK13652 109 LDEETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGvkelIDFLNDLPETY 187
|
90 100
....*....|....*....|...
gi 14318531 414 PNTVLTVSHDRAFLNEVAtDIIY 436
Cdd:PRK13652 188 GMTVIFSTHQLDLVPEMA-DYIY 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
367-441 |
1.27e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.32 E-value: 1.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 367 SFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN----TVLTVSHDRAFLNEVATDIIYQHNER 441
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAHRIASIKRSDKIVVFNNPDR 1436
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
207-422 |
1.32e-03 |
|
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: 41.06 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 207 YVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDTKalqsvldadvwrkql 286
Cdd:cd03251 10 YPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPR--FYDVDSGRIL-----IDGHDVR--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 287 lseEAKINERLKEMDVLRQE---FEedslevkklDNEREDldnhlIQISDKLVDMESDKAEARAASIL-----YGLGFST 358
Cdd:cd03251 68 ---DYTLASLRRQIGLVSQDvflFN---------DTVAEN-----IAYGRPGATREEVEEAARAANAHefimeLPEGYDT 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 359 EAQQQPTNsFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYL-KTYPN-TVLTVSH 422
Cdd:cd03251 131 VIGERGVK-LSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALeRLMKNrTTFVIAH 195
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
211-408 |
1.53e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 40.63 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 211 GQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILHVEQElrGDDTKALQSV-----LDAdvwrkq 285
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAG--LLPPAAGTIKLDGGD--IDDPDVAEAChylghRNA------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 286 llseeakinerLKemdvlrqefeeDSLEVKK-LDNEREDLDNHLIQISDKLVDMEsdkaearaasiLYGLGfsteaqQQP 364
Cdd:PRK13539 84 -----------MK-----------PALTVAEnLEFWAAFLGGEELDIAAALEAVG-----------LAPLA------HLP 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 14318531 365 TNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAE 408
Cdd:PRK13539 125 FGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAE 168
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
367-422 |
1.56e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 40.91 E-value: 1.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 367 SFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN--TVLTVSH 422
Cdd:PRK14239 148 GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTR 205
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
213-399 |
1.62e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 41.27 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 213 RILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrrELNVPKHVSILHVEQELRGDD-TKALQSVldadvwRKQL----- 286
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLN--GLHVPTQGSVRVDDTLITSTSkNKDIKQI------RKKVglvfq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 287 LSEEAKINER-LKEMDVLRQEFEEDSLEVKKLdnEREDLdnHLIQISDKLVDmesdkaearaasilyglgfsteaqqqpT 365
Cdd:PRK13649 93 FPESQLFEETvLKDVAFGPQNFGVSQEEAEAL--AREKL--ALVGISESLFE---------------------------K 141
|
170 180 190
....*....|....*....|....*....|....*.
gi 14318531 366 NSF--SGGWRMRLSLARALFCQPDLLLLDEPSNMLD 399
Cdd:PRK13649 142 NPFelSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
528-723 |
1.77e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 40.84 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 528 SPPIIQLQDVSFGYDEnnLLLKDVNLDVQMDSRIALVGANGCGKT----TLLKIMMEQLRPLKG---------------- 587
Cdd:PRK10418 1 MPQQIELRNIALQAAQ--PLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGrvlldgkpvapcalrg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 588 ----FVSRNPR-----LRIgyFTQHHVDSMDLT--TSAVDWMSKSFPGKTDEEYRRHLGSFGITgtlglqkmqlLSGG-- 654
Cdd:PRK10418 79 rkiaTIMQNPRsafnpLHT--MHTHARETCLALgkPADDATLTAALEAVGLENAARVLKLYPFE----------MSGGml 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 655 QKSRVAFAALClNNPhILVLDEPsnhldTTGLDALVEA---------LKNFNGGVLMVSHDISVIDSVCKEIWVSEQG 723
Cdd:PRK10418 147 QRMMIALALLC-EAP-FIIADEP-----TTDLDVVAQArildllesiVQKRALGMLLVTHDMGVVARLADDVAVMSHG 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
529-704 |
1.91e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 41.54 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 529 PPIIQLQDVSFGYdennlLLKDVNLDVqmdsR------IA-LVGAngcGKTTLLKIMMEQLRPLKGFVS--------RNP 593
Cdd:COG1129 254 EVVLEVEGLSVGG-----VVRDVSFSV----RageilgIAgLVGA---GRTELARALFGADPADSGEIRldgkpvriRSP 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 594 R----LRIGYFT---QHH--VDSMD----LTTSAVDWMSKSF---PGKTDEEYRRHLGSFGI-TGTLGlQKMQLLSGG-- 654
Cdd:COG1129 322 RdairAGIAYVPedrKGEglVLDLSirenITLASLDRLSRGGlldRRRERALAEEYIKRLRIkTPSPE-QPVGNLSGGnq 400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 14318531 655 QKsrVAFAALCLNNPHILVLDEPsnhldTTGLD--------ALVEALKNFNGGVLMVS 704
Cdd:COG1129 401 QK--VVLAKWLATDPKVLILDEP-----TRGIDvgakaeiyRLIRELAAEGKAVIVIS 451
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
531-707 |
1.98e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.92 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 531 IIQLQDVSFGYDeNNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIM--MEQLRP---LKG---FVSRN-------P-- 593
Cdd:PRK14243 10 VLRTENLNVYYG-SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPgfrVEGkvtFHGKNlyapdvdPve 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 594 -RLRIGYFTQHhvdSMDLTTSAVDWMS-----KSFPGKTDEEYRRHLGSFGITGTLG---LQKMQLLSGGQKSRVAFAAL 664
Cdd:PRK14243 89 vRRRIGMVFQK---PNPFPKSIYDNIAygariNGYKGDMDELVERSLRQAALWDEVKdklKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14318531 665 CLNNPHILVLDEPSNHLD---TTGLDALVEALKNfNGGVLMVSHDI 707
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDpisTLRIEELMHELKE-QYTIIIVTHNM 210
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
530-739 |
2.07e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.41 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 530 PIIQLQDVSF--GYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVS-RNPRLRIGYFTQHHVD 606
Cdd:PRK13545 20 PFDKLKDLFFrsKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDiKGSAALIAISSGLNGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 607 SMDLTTSAVDWMSKSFPGKTDEEYRRHLGSFGITGTLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGL 686
Cdd:PRK13545 100 LTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318531 687 DALVEALKNF--NGG-VLMVSHDISVIDSVC-KEIW-----VSEQGTVKRfegTIYDYRDYI 739
Cdd:PRK13545 180 KKCLDKMNEFkeQGKtIFFISHSLSQVKSFCtKALWlhygqVKEYGDIKE---VVDHYDEFL 238
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
211-246 |
2.16e-03 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 39.33 E-value: 2.16e-03
10 20 30
....*....|....*....|....*....|....*.
gi 14318531 211 GQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALS 246
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILS 47
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
548-706 |
2.21e-03 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 40.70 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 548 LKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSrnprlrigyftqhhVDSMDLTTsavdwMSKS------ 621
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVL--------------IDGQDIAA-----MSRKelrelr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 622 -------------FPGKT----------------DEEYRRHLGSFGITGTLGL--QKMQLLSGGQKSRVAFAALCLNNPH 670
Cdd:cd03294 101 rkkismvfqsfalLPHRTvlenvafglevqgvprAEREERAAEALELVGLEGWehKYPDELSGGMQQRVGLARALAVDPD 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 14318531 671 ILVLDEPSNHLD----TTGLDALVEALKNFNGGVLMVSHD 706
Cdd:cd03294 181 ILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHD 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
369-430 |
2.22e-03 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 39.33 E-value: 2.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPN---TVLTVSHdraFLNEV 430
Cdd:cd03216 84 SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH---RLDEV 145
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
361-423 |
2.23e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 41.17 E-value: 2.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 361 QQQPtNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVP-------SIAYLAEYLKTypnTVLTVSHD 423
Cdd:PRK11000 128 DRKP-KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAlrvqmriEISRLHKRLGR---TMIYVTHD 193
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
369-399 |
2.25e-03 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 40.86 E-value: 2.25e-03
10 20 30
....*....|....*....|....*....|.
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEPSNMLD 399
Cdd:PRK11432 138 SGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
369-422 |
2.51e-03 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 40.34 E-value: 2.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEPSNMLDvPS-----IAYLAEYLKTYPNTVLTVSH 422
Cdd:PRK10771 131 SGGQRQRVALARCLVREQPILLLDEPFSALD-PAlrqemLTLVSQVCQERQLTLLMVSH 188
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
338-399 |
2.55e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 40.39 E-value: 2.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318531 338 MESDKAEARAASILYGLGFSTEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLD 399
Cdd:PRK13634 116 VSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
353-427 |
2.65e-03 |
|
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: 39.61 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 353 GLGFSTeaQQQPTNSFSGGWRMRLSLARALF--CQPDLLLLDEPSNMLDVPSIAYLAEYLKTY---PNTVLTVSHDRAFL 427
Cdd:cd03238 75 GLGYLT--LGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVILIEHNLDVL 152
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
367-435 |
2.72e-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: 2.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318531 367 SFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTY----PNTVLTVSHDRAFLNEVATDII 435
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYLSDRIH 143
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
324-423 |
2.80e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 40.50 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 324 LDNHLIqisdklvdmESDKAEARAASILYGLGFSTEAQQQPtNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDvP-- 401
Cdd:PRK13648 109 LENHAV---------PYDEMHRRVSEALKQVDMLERADYEP-NALSGGQKQRVAIAGVLALNPSVIILDEATSMLD-Pda 177
|
90 100
....*....|....*....|....*
gi 14318531 402 --SIAYLAEYLKTYPN-TVLTVSHD 423
Cdd:PRK13648 178 rqNLLDLVRKVKSEHNiTIISITHD 202
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
215-399 |
2.80e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 40.55 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 215 LSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDTKALQsvldadvwRKQLLSEEAKIN 294
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINL--LERPTSGRVL-----VDGQDLTALS--------EKELRKARRQIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 295 erlkeMdvLRQEFeedslevkKLDNEREDLDNhlIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQPTNsFSGGWRM 374
Cdd:PRK11153 86 -----M--IFQHF--------NLLSSRTVFDN--VALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQ-LSGGQKQ 147
|
170 180
....*....|....*....|....*
gi 14318531 375 RLSLARALFCQPDLLLLDEPSNMLD 399
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALD 172
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
344-399 |
3.17e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 3.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 14318531 344 EARAASIlyGLGFSTEAQQQPTNsFSGGWRMRLSLARALFCQPDLLLLDEPSNMLD 399
Cdd:PTZ00243 762 EADLAQL--GGGLETEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
369-394 |
3.21e-03 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 39.37 E-value: 3.21e-03
10 20
....*....|....*....|....*.
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEP 394
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDP 154
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
651-708 |
3.32e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 40.08 E-value: 3.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 651 LSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNG--GVLMVSHDIS 708
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLA 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
214-400 |
3.72e-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: 39.52 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 214 ILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILHVEQELRGDDTKALQS----VLDaDVWrkqLLSE 289
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMR--FYDPQKGQILIDGIDIRDISRKSLRSmigvVLQ-DTF---LFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 290 EAKINERLKEMDVlRQEFEEDSLEVKKLDNEREDLDNhliqisdklvdmesdkaearaasilyglGFSTEAQQQPTNsFS 369
Cdd:cd03254 92 TIMENIRLGRPNA-TDEEVIEAAKEAGAHDFIMKLPN----------------------------GYDTVLGENGGN-LS 141
|
170 180 190
....*....|....*....|....*....|.
gi 14318531 370 GGWRMRLSLARALFCQPDLLLLDEPSNMLDV 400
Cdd:cd03254 142 QGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
198-422 |
3.99e-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: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 198 DIHIDTFDL-YVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRreLNVPKHVSILhveqeLRGDDTkalqSV 276
Cdd:cd03244 2 DIEFKNVSLrYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFR--LVELSSGSIL-----IDGVDI----SK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 277 LDADVWRKQllseeakinerlkeMDVLRQE---FEeDSLevkkldneREDLDNHLIQISDKLVD-MESDKAEARAASILY 352
Cdd:cd03244 71 IGLHDLRSR--------------ISIIPQDpvlFS-GTI--------RSNLDPFGEYSDEELWQaLERVGLKEFVESLPG 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318531 353 GLGFSTEAQQqptNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTY-PN-TVLTVSH 422
Cdd:cd03244 128 GLDTVVEEGG---ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAfKDcTVLTIAH 196
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
360-399 |
4.20e-03 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 40.32 E-value: 4.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 14318531 360 AQQQPTNsFSGGWRMRLSLARALFCQPDLLLLDEPSNMLD 399
Cdd:PRK09452 138 AQRKPHQ-LSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
210-423 |
4.47e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 39.83 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 210 DGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSrrelNVPKHVSilhvEQELRGDDTkalqsvldADVWRKQLLSE 289
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLN----GILKPSS----GRILFDGKP--------IDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 290 EAKINERLKEMDvlRQEFEEDSLEvkkldneredldnhliQISDKLVDME--SDKAEARAASILYGLGFStEAQQQPTNS 367
Cdd:PRK13636 81 RESVGMVFQDPD--NQLFSASVYQ----------------DVSFGAVNLKlpEDEVRKRVDNALKRTGIE-HLKDKPTHC 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 368 FSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIA----YLAEYLKTYPNTVLTVSHD 423
Cdd:PRK13636 142 LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSeimkLLVEMQKELGLTIIIATHD 201
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
367-400 |
4.59e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 39.84 E-value: 4.59e-03
10 20 30
....*....|....*....|....*....|....
gi 14318531 367 SFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDV 400
Cdd:cd03291 159 TLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
362-435 |
4.70e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.18 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 362 QQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVP-------SIAYLAEYLKTypnTVLTVSHDRAFLNEVATDI 434
Cdd:PRK13409 448 DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlavakAIRRIAEEREA---TALVVDHDIYMIDYISDRL 524
|
.
gi 14318531 435 I 435
Cdd:PRK13409 525 M 525
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
346-441 |
4.89e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 39.65 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 346 RAASILYGLGFSTEAQQQPTNsFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDvPS-----IAYLAEYLKTYPNTVLTV 420
Cdd:PRK13637 124 KRAMNIVGLDYEDYKDKSPFE-LSGGQKRRVAIAGVVAMEPKILILDEPTAGLD-PKgrdeiLNKIKELHKEYNMTIILV 201
|
90 100
....*....|....*....|.
gi 14318531 421 SHDRAFLNEVATDIIYQHNER 441
Cdd:PRK13637 202 SHSMEDVAKLADRIIVMNKGK 222
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
341-399 |
5.04e-03 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 39.21 E-value: 5.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 14318531 341 DKAEARAASILYGLGFSTEAQQQPtNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLD 399
Cdd:COG1126 111 AEAEERAMELLERVGLADKADAYP-AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
211-265 |
5.35e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.99 E-value: 5.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14318531 211 GQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALS---------------RRELNVPKH-----VSILHveQEL 265
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTgiytrdagsilylgkEVTFNGPKSsqeagIGIIH--QEL 88
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
560-586 |
6.18e-03 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 37.86 E-value: 6.18e-03
10 20
....*....|....*....|....*..
gi 14318531 560 RIALVGANGCGKTTLLKIMMEQLRPLK 586
Cdd:COG4917 3 RIMLIGRSGAGKTTLTQALNGEELEYR 29
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
537-583 |
7.76e-03 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 39.59 E-value: 7.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 14318531 537 VSFGYDENNLllKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLR 583
Cdd:TIGR03925 344 VPLGLGESDL--APVYVDFAESPHLLIFGDSESGKTTLLRTIARGIV 388
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
221-349 |
8.21e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 39.72 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 221 TLSFGHRYGLV-GQNGIGKSTLLRALsrRELNVPKHVSILHVEQELRGDDTKALQSVL--DADvWRKQLLSEEAKIN--- 294
Cdd:COG4694 19 WLAFFKKLNLIyGENGSGKSTLSRIL--RSLELGDTSSEVIAEFEIEAGGSAPNPSVRvfNRD-FVEENLRSGEEIKgif 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318531 295 -------ERLKEMDVLRQEFEEDSLEVKKLDNEREDLDNHLIQISDKLVDMESDKAEARAAS 349
Cdd:COG4694 96 tlgeeniELEEEIEELEKEIEDLKKELDKLEKELKEAKKALEKLLEDLAKSIKDDLKKLFAS 157
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
212-399 |
9.01e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 38.40 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 212 QRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELNVPkhvsilhveqelrgddtkalqsvlDADVWRkqllseea 291
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTP------------------------VAGCVD-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318531 292 kinerlkemdvlrqefeedsLEVKKLDNEREDLDNhliqisdklVDMESDKAEarAASILYGLGFStEAQ--QQPTNSFS 369
Cdd:COG2401 91 --------------------VPDNQFGREASLIDA---------IGRKGDFKD--AVELLNAVGLS-DAVlwLRRFKELS 138
|
170 180 190
....*....|....*....|....*....|
gi 14318531 370 GGWRMRLSLARALFCQPDLLLLDEPSNMLD 399
Cdd:COG2401 139 TGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
369-406 |
9.71e-03 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 37.80 E-value: 9.71e-03
10 20 30
....*....|....*....|....*....|....*...
gi 14318531 369 SGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYL 406
Cdd:cd03215 106 SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEI 143
|
|
| |
