|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-636 |
0e+00 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 784.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSIASVKQETPALAITA 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 81 LEYVLQGNPDYYALRCQLKQAEQQGDGETQAQVHQQLELMKGYSIEAKAGELLHGLGFSNTQIDYAVSDFSGGWRMRLNL 160
Cdd:PRK10636 81 LEYVIDGDREYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 161 AQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAGTLVLISHDREFLDAVVGEIWHIDQQQINVYKGNYSQFERQKAE 240
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 241 RLAQQQAQFDKQQEQIAHLEKFITRFKAKASKAKQAQSRVKALERMEKLAPAHVDSPFDFSFAEPDALPNPLIALDGAQA 320
Cdd:PRK10636 241 RLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFHFSFRAPESLPNPLLKMEKVSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 321 GYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGLKVGYFAQHQLEALDLQASPVTHLQR 400
Cdd:PRK10636 321 GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHLAR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 401 LNPQASEQSLRDFLGGFAFIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSFDGAM 480
Cdd:PRK10636 401 LAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 481 VTVSHDRHLLKNTADEFYLVDSGEVRQFGYDLDAYYQWLTKANQEQKQTQVEPDK--ANSSANRKEQKRKEAEFRKHVQP 558
Cdd:PRK10636 481 VVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQENQTDEAPKEnnANSAQARKDQKRREAELRTQTQP 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 559 LKKAIDKLEKQLDTLAPKLADIESQLSDNSVYEEQHKERLKQLLAQQSDYAQQQEAAEEQLLEHMDELEQQEQAFYES 636
Cdd:PRK10636 561 LRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQMLLEGQSN 638
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-518 |
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: 651.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 4 ITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSIASVKQETPALA-ITALE 82
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDdLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 83 YVLQGNPDYYALRCQLKQAEQQG-----DGETQAQVHQQLELMKGYSIEAKAGELLHGLGFSNTQIDYAVSDFSGGWRMR 157
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLaepdeDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 158 LNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAGTLVLISHDREFLDAVVGEIWHIDQQQINVYKGNYSQFERQ 237
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 238 KAERLAQQQAQFDKQQEQIAHLEKFITRFKAKASKAKQAQSRVKALERMEKLAPAHVDSPFDFSFAEPDALPNPLIALDG 317
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLGKKVLELEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 318 AQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGLKVGYFAQHQlEALDLQASPVTH 397
Cdd:COG0488 321 LSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EELDPDKTVLDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 398 LQRLNPQASEQSLRDFLGGFAFIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSFD 477
Cdd:COG0488 400 LRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 800951443 478 GAMVTVSHDRHLLKNTADEFYLVDSGEVRQFGYDLDAYYQW 518
Cdd:COG0488 480 GTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-508 |
8.90e-115 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 359.56 E-value: 8.90e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLfallkgeLQLDAGNA--KVPKEWSIASVKQETPALAIT 79
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTF-------LRYMAMHAidGIPKNCQILHVEQEVVGDDTT 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 80 ALEYVLQGNPDyyalRCQLKQAE-----QQGDGETQ-----------------------AQVHQQLELMKGYSIEAKAGE 131
Cdd:PLN03073 251 ALQCVLNTDIE----RTQLLEEEaqlvaQQRELEFEtetgkgkgankdgvdkdavsqrlEEIYKRLELIDAYTAEARAAS 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 132 LLHGLGFSNTQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAGTLVLISHDREFLDA 211
Cdd:PLN03073 327 ILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNT 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 212 VVGEIWHIDQQQINVYKGNYSQFERQKAERLAQQQAQFDKQQEQIAHLEKFITRFKAKASKAKQAQSRVKALERMEKLAP 291
Cdd:PLN03073 407 VVTDILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLGHVDA 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 292 AHVDSPFDFSFAEPDALPN-PLIALDGAQAGY-GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDV 369
Cdd:PLN03073 487 VVNDPDYKFEFPTPDDRPGpPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 370 FFHQGLKVGYFAQHQLEALDLQASPVTHLQRLNPQASEQSLRDFLGGFAFIGDKALDPVAPFSGGEKARLVLAMLVYQKP 449
Cdd:PLN03073 567 FRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKP 646
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 800951443 450 NLLLLDEPTNHLDLEMRHALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQF 508
Cdd:PLN03073 647 HILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPF 705
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-487 |
3.34e-89 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 286.79 E-value: 3.34e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSIASVKQETPAL-AIT 79
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFeEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 80 ALEYVLQGNPDYYALRCQ------LKQAEQQgDGETQAQVHQQLELMKGYSIEAKAGELLHGLGFSNTQIDYAVSDFSGG 153
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQErdriyaLPEMSEE-DGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 154 WRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAGTLVLISHDREFLDAVVGEIWHIDQQQINVYKGNYSQ 233
Cdd:PRK15064 160 WKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 234 F---ERQKAERLAqqqAQFDKQQEQIAHLEKFITRFKAKASKAKQAQSRVKALER--MEKLAPAHVDSPFdFSFAEPDAL 308
Cdd:PRK15064 240 YmtaATQARERLL---ADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKikLEEVKPSSRQNPF-IRFEQDKKL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 309 PNPLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGLKVGYFAQHQLEAL 388
Cdd:PRK15064 316 HRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 389 DlqaSPVTHL----QRLNPQASEQSLRDFLGGFAFIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLE 464
Cdd:PRK15064 396 E---NDLTLFdwmsQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME 472
|
490 500
....*....|....*....|...
gi 800951443 465 MRHALVMALQSFDGAMVTVSHDR 487
Cdd:PRK15064 473 SIESLNMALEKYEGTLIFVSHDR 495
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-604 |
1.28e-79 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 264.51 E-value: 1.28e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 16 LLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSIASVKQETP-ALAITALEYVLQGN------ 88
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPrNVEGTVYDFVAEGIeeqaey 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 89 -PDYYALRCQLKQAEQQGDGETQAQVHQQLELMKGYSIEAKAGELLHGLGFSNtqiDYAVSDFSGGWRMRLNLAQALIRD 167
Cdd:PRK11147 98 lKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDP---DAALSSLSGGWLRKAALGRALVSN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 168 ADLLLLDEPTNHLDLDAVYWLERFLRSYAGTLVLISHDREFLDAVVGEIWHIDQQQINVYKGNYSQFERQKAERLAQQQA 247
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALRVEEL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 248 QFDKQQEQIAHLEKFI--------TRfkakaskakqAQSRVKAL-----ERMEKL-----APAHVDspfdfsfaepDALP 309
Cdd:PRK11147 255 QNAEFDRKLAQEEVWIrqgikarrTR----------NEGRVRALkalrrERSERRevmgtAKMQVE----------EASR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 310 NPLIALDGAQAGY--GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGLKVGYFAQHQlEA 387
Cdd:PRK11147 315 SGKIVFEMENVNYqiDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHR-AE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 388 LDLQASPVTHL----QRLNPQASEQSLRDFLGGFAFIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDL 463
Cdd:PRK11147 394 LDPEKTVMDNLaegkQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 464 EMRHALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVD-SGEVRQF--GYDlDAYYQwltKAN-QEQKQTQVEPDKANSS 539
Cdd:PRK11147 474 ETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEgNGKIGRYvgGYH-DARQQ---QAQyLALKQPAVKKKEEAAA 549
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 540 ANRKEQKRKEAEFRKHVQplkKAIDKLEKQLDTLAPKLADIESQLSDNSVYEEQHKERLKQL--LAQ 604
Cdd:PRK11147 550 PKAETVKRSSKKLSYKLQ---RELEQLPQLLEDLEAEIEALQAQVADADFFSQPHEQTQKVLadLAD 613
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-490 |
1.39e-65 |
|
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: 224.81 E-value: 1.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 14 KCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSIASVKQEtPAL--AITALEYVLQGNPDY 91
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQE-PQLdpTKTVRENVEEGVAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 92 YALRCQLKQ-----AEQQGD----GETQAQVHQQLELMKGYSIEAKAGELLHGLGFSNTqiDYAVSDFSGGWRMRLNLAQ 162
Cdd:TIGR03719 97 KDALDRFNEisakyAEPDADfdklAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPW--DADVTKLSGGERRRVALCR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 163 ALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAGTLVLISHDREFLDAVVGEIWHIDQQQINVYKGNYSQFERQKAERL 242
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 243 AQQQAQFDKQQEQIAHLEKFItrfkakASKAKQAQSRVKA-LERMEKLAPAHVDSPFDFS--FAEP-DALPNPLIALDGA 318
Cdd:TIGR03719 255 EQEEKEESARQKTLKRELEWV------RQSPKGRQAKSKArLARYEELLSQEFQKRNETAeiYIPPgPRLGDKVIEAENL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 319 QAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGLKVGYFAQHQlEALD------LQA 392
Cdd:TIGR03719 329 TKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSR-DALDpnktvwEEI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 393 SPVTHLQRLNpqASEQSLRDFLGGFAFIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMA 472
Cdd:TIGR03719 408 SGGLDIIKLG--KREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEA 485
|
490
....*....|....*...
gi 800951443 473 LQSFDGAMVTVSHDRHLL 490
Cdd:TIGR03719 486 LLNFAGCAVVISHDRWFL 503
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-487 |
1.75e-55 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 197.65 E-value: 1.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 14 KCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSIASVKQEtPAL--AITALEYVLQGNPDY 91
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQE-PQLdpEKTVRENVEEGVAEV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 92 YALRCQLKQ-----AEQQGD----GETQAQVHQQLELMKGYSIEAK---AGELLH---GlgfsntqiDYAVSDFSGGWRM 156
Cdd:PRK11819 99 KAALDRFNEiyaayAEPDADfdalAAEQGELQEIIDAADAWDLDSQleiAMDALRcppW--------DAKVTKLSGGERR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 157 RLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAGTLVLISHDREFLDAVVGEIWHIDQQQINVYKGNYSQFER 236
Cdd:PRK11819 171 RVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 237 QKAERLAQQQAQFDKQQEQIAH-LE-----------KfitrfkakaskakqaqsrVKA-LERMEKLAPAHVDSPFDfsFA 303
Cdd:PRK11819 251 QKAKRLAQEEKQEAARQKALKReLEwvrqspkarqaK------------------SKArLARYEELLSEEYQKRNE--TN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 304 E-----PDALPNPLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGLKVG 378
Cdd:PRK11819 311 EifippGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 379 YFAQHQlEALDlqaspvthlqrlnPQAS-----------------EQSLRDFLGGFAFIGDKALDPVAPFSGGEKARLVL 441
Cdd:PRK11819 391 YVDQSR-DALD-------------PNKTvweeisggldiikvgnrEIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHL 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 800951443 442 AMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSFDGAMVTVSHDR 487
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDR 502
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
313-504 |
4.29e-50 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 170.32 E-value: 4.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGLKVGYFAQhqlealdlqa 392
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 393 spvthlqrlnpqaseqslrdflggfafigdkaldpvapFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMA 472
Cdd:cd03221 71 --------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEA 112
|
170 180 190
....*....|....*....|....*....|..
gi 800951443 473 LQSFDGAMVTVSHDRHLLKNTADEFYLVDSGE 504
Cdd:cd03221 113 LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
322-569 |
1.09e-49 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 180.65 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGLKVGYFAQHQ--------LEAL----- 388
Cdd:COG0488 8 FGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPpldddltvLDTVldgda 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 389 ----------DLQASPVTHLQRLNPQASEQSLRDFLGGFAF------------IGDKALD-PVAPFSGGEKARLVLAMLV 445
Cdd:COG0488 88 elraleaeleELEAKLAEPDEDLERLAELQEEFEALGGWEAearaeeilsglgFPEEDLDrPVSELSGGWRRRVALARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 446 YQKPNLLLLDEPTNHLDLEMRHALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFGYDLDAYYQWLTKANQE 525
Cdd:COG0488 168 LSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQRAERLEQ 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 800951443 526 QKQTQvepdkanssANRKEQKRKEAEF--------RKHVQP--LKKAIDKLEKQ 569
Cdd:COG0488 248 EAAAY---------AKQQKKIAKEEEFirrfrakaRKAKQAqsRIKALEKLERE 292
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-237 |
2.53e-47 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 174.10 E-value: 2.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSIASVKQETPAL--AI 78
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELdpDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 79 TALEYVLQGNPdyyalrcqlkqaeqqgdGETQAQVHQQLELMkgysieakagellhglGFSNTQIDYAVSDFSGGWRMRL 158
Cdd:COG0488 395 TVLDELRDGAP-----------------GGTEQEVRGYLGRF----------------LFSGDDAFKPVGVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 800951443 159 NLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAGTLVLISHDREFLDAVVGEIWHIDQQQINVYKGNYSQFERQ 237
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-223 |
1.01e-44 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 156.07 E-value: 1.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSIAsvkqetpalaital 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 82 eYVLQgnpdyyalrcqlkqaeqqgdgetqaqvhqqlelmkgysieakagellhglgfsntqidyavsdFSGGWRMRLNLA 161
Cdd:cd03221 67 -YFEQ---------------------------------------------------------------LSGGEKMRLALA 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800951443 162 QALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAGTLVLISHDREFLDAVVGEIWHIDQQQ 223
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
312-509 |
4.37e-32 |
|
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: 124.77 E-value: 4.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 312 LIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH----QGL-------KVGYF 380
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgrdlASLsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 381 AQHQLEALDLQA--------SP-VTHLQRLNP---QASEQSLRDfLGgfafIGDKALDPVAPFSGGEKARLVLAMLVYQK 448
Cdd:COG1120 81 PQEPPAPFGLTVrelvalgrYPhLGLFGRPSAedrEAVEEALER-TG----LEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 449 PNLLLLDEPTNHLDLemRHAL-VMAL-----QSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:COG1120 156 PPLLLLDEPTSHLDL--AHQLeVLELlrrlaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQG 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
321-509 |
2.60e-30 |
|
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: 117.15 E-value: 2.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 321 GYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHqGLKVGYFAQHQLealdlqASPVTHLqr 400
Cdd:cd03214 8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD-GKDLASLSPKEL------ARKIAYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 401 lnPQASEQslrdfLGgfafIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLemRHAL-VMAL-----Q 474
Cdd:cd03214 79 --PQALEL-----LG----LAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI--AHQIeLLELlrrlaR 145
|
170 180 190
....*....|....*....|....*....|....*
gi 800951443 475 SFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:cd03214 146 ERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-505 |
7.16e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 123.86 E-value: 7.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITD--IELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGelqLDAGNAKVPKEWSIA--SVKQETPAL 76
Cdd:COG1123 4 LLEVRDlsVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG---LLPHGGRISGEVLLDgrDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 77 AITALEYVLQgnpdyyalrcqlkQAEQQGDGET-QAQVHQQLEL--MKGYSIEAKAGELLHGLGFSnTQIDYAVSDFSGG 153
Cdd:COG1123 81 RGRRIGMVFQ-------------DPMTQLNPVTvGDQIAEALENlgLSRAEARARVLELLEAVGLE-RRLDRYPHQLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 154 WRMRLNLAQALIRDADLLLLDEPTNHLDLDA---VYWLERFLRSYAG-TLVLISHDREFLDAVVGEIWHIDQQQInvykg 229
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRI----- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 230 nysqFERQKAERLaqqqaqfdkqqeqiahlekfitrfkakaskakqaqsrvkaLERMEKLAPAHVDSPFDFSFAEPDALP 309
Cdd:COG1123 222 ----VEDGPPEEI----------------------------------------LAAPQALAAVPRLGAARGRAAPAAAAA 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 310 NPLIALDGAQAGY-----GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVGYFAQHQ 384
Cdd:COG1123 258 EPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILF-DGKDLTKLSRRS 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 385 LEALDLQASPVthLQrlNPQAS-------EQSLRDFLgGFAFIGDKA--------------LDPVA----P--FSGGEKA 437
Cdd:COG1123 337 LRELRRRVQMV--FQ--DPYSSlnprmtvGDIIAEPL-RLHGLLSRAerrervaellervgLPPDLadryPheLSGGQRQ 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 800951443 438 RLVLA-MLVyQKPNLLLLDEPTNHLDLEMRhALVMAL-----QSFDGAMVTVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:COG1123 412 RVAIArALA-LEPKLLILDEPTSALDVSVQ-AQILNLlrdlqRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
327-547 |
6.62e-29 |
|
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: 121.20 E-value: 6.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 327 ILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGLKVGYFAQH-QL-EALDLQ-------ASPVTH 397
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEpQLdPTKTVRenveegvAEIKDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 398 LQRLNP------------------QASEQSLRDFLGGFAFigDKALD-------------PVAPFSGGEKARLVLAMLVY 446
Cdd:TIGR03719 100 LDRFNEisakyaepdadfdklaaeQAELQEIIDAADAWDL--DSQLEiamdalrcppwdaDVTKLSGGERRRVALCRLLL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 447 QKPNLLLLDEPTNHLDLEMRHALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEvrqfGYDLDA-YYQWLtkanqE 525
Cdd:TIGR03719 178 SKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGR----GIPWEGnYSSWL-----E 248
|
250 260
....*....|....*....|..
gi 800951443 526 QKQTQVEPDKANSSANRKEQKR 547
Cdd:TIGR03719 249 QKQKRLEQEEKEESARQKTLKR 270
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
309-503 |
4.50e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 112.88 E-value: 4.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 309 PNPLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH------QGLKVGYFAQ 382
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFgkpprrARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 383 HqlEALDLQaSPVT-----------H---LQRLNP---QASEQSLrDFLGgfafIGDKALDPVAPFSGGEKARLVLA-ML 444
Cdd:COG1121 83 R--AEVDWD-FPITvrdvvlmgrygRrglFRRPSRadrEAVDEAL-ERVG----LEDLADRPIGELSGGQQQRVLLArAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800951443 445 VyQKPNLLLLDEPTNHLDLEMRHA---LVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSG 503
Cdd:COG1121 155 A-QDPDLLLLDEPFAGVDAATEEAlyeLLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-240 |
8.60e-28 |
|
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: 112.26 E-value: 8.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEwsiasVKQETPALAITA 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE-----DVRKEPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 81 LEYVLQGNPDYYALRcqlkqaeqqgdGETQAQVHQQLELMKGYSIEAKAGELLHGLGFSNTqIDYAVSDFSGGWRMRLNL 160
Cdd:COG4555 76 IGVLPDERGLYDRLT-----------VRENIRYFAELYGLFDEELKKRIEELIELLGLEEF-LDRRVGELSTGMKKKVAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 161 AQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYA--GTLVLIS-HDREFLDAVVGEIWHIDQQQInVYKGNYSQFERQ 237
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKkeGKTVLFSsHIMQEVEALCDRVVILHKGKV-VAQGSLDELREE 222
|
...
gi 800951443 238 KAE 240
Cdd:COG4555 223 IGE 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
322-504 |
9.53e-27 |
|
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: 106.56 E-value: 9.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHqGLKVGYFAQHQLEAldlqaspvtHLQRL 401
Cdd:cd00267 9 YGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID-GKDIAKLPLEELRR---------RIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 402 nPQaseqslrdflggfafigdkaldpvapFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSF--DGA 479
Cdd:cd00267 79 -PQ--------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaeEGR 131
|
170 180
....*....|....*....|....*.
gi 800951443 480 MV-TVSHDRHLLKNTADEFYLVDSGE 504
Cdd:cd00267 132 TViIVTHDPELAELAADRVIVLKDGK 157
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
282-519 |
1.06e-26 |
|
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: 114.86 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 282 ALERMEKLAPAHVDSPFDfsfAEPDALPNPL-IALDGAQAGY--GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLL 358
Cdd:COG4987 305 AARRLNELLDAPPAVTEP---AEPAPAPGGPsLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 359 AQELAPQAGDVffhqglkvgYFAQHQLEALDLQA--------SPVTHL--------QRL-NPQASEQSLRDF-----LGG 416
Cdd:COG4987 382 LRFLDPQSGSI---------TLGGVDLRDLDEDDlrrriavvPQRPHLfdttlrenLRLaRPDATDEELWAAlervgLGD 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 417 FAFIGDKALD-PV----APFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSF--DGAMVTVSHDRHL 489
Cdd:COG4987 453 WLAALPDGLDtWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHRLAG 532
|
250 260 270
....*....|....*....|....*....|....*
gi 800951443 490 LkNTADEFYLVDSGEVRQFG-----YDLDAYYQWL 519
Cdd:COG4987 533 L-ERMDRILVLEDGRIVEQGtheelLAQNGRYRQL 566
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
328-459 |
2.56e-26 |
|
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: 105.04 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 328 LHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF-----------HQGLKVGYFAQH-----QLEALD-- 389
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdltdderkSLRKEIGYVFQDpqlfpRLTVREnl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 390 LQASPVTHLQRLNPQASEQSLRDFLGGFAFIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTN 459
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
323-550 |
2.95e-26 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 113.29 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGLKVGYFAQH-QL-------EALDLQASP 394
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEpQLdpektvrENVEEGVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 395 VTH-LQRLNP------------------QASEQSLRDFLGGFAFigDKALD-------------PVAPFSGGEKARLVLA 442
Cdd:PRK11819 98 VKAaLDRFNEiyaayaepdadfdalaaeQGELQEIIDAADAWDL--DSQLEiamdalrcppwdaKVTKLSGGERRRVALC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 443 MLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSFDGAMVTVSHDRHLLKNTAdEFYL-VDSGEvrqfGYDLDA-YYQWLt 520
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVA-GWILeLDRGR----GIPWEGnYSSWL- 249
|
250 260 270
....*....|....*....|....*....|
gi 800951443 521 kanqEQKQTQVEpdkansSANRKEQKRKEA 550
Cdd:PRK11819 250 ----EQKAKRLA------QEEKQEAARQKA 269
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
322-505 |
4.29e-26 |
|
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: 105.17 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHqglkvGYfaqhqlealDLQASPVTHLQRL 401
Cdd:cd03230 10 YGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL-----GK---------DIKKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 402 N--PQasEQSLRDFLGGFAFIGdkaldpvapFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSFDGA 479
Cdd:cd03230 76 GylPE--EPSLYENLTVRENLK---------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE 144
|
170 180
....*....|....*....|....*....
gi 800951443 480 MVTV---SHDRHLLKNTADEFYLVDSGEV 505
Cdd:cd03230 145 GKTIllsSHILEEAERLCDRVAILNNGRI 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
313-505 |
1.64e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 104.51 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH----QGL-------KVGYFA 381
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDgkplSAMpppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 382 QhqlEALDLQASPVTHLQR----LNPQASEQSLRDFLGGFAFiGDKALD-PVAPFSGGEKARLVLAMLVYQKPNLLLLDE 456
Cdd:COG4619 81 Q---EPALWGGTVRDNLPFpfqlRERKFDRERALELLERLGL-PPDILDkPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 800951443 457 PTNHLDLEMRHALVMALQSF----DGAMVTVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:COG4619 157 PTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-257 |
3.69e-25 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 110.43 E-value: 3.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 14 KCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSIASVKQETPALaitaleyvlqgNPDYYA 93
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAEL-----------DPEKTV 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 94 LrcqlkqaEQQGDGETQAQVHQQLELMKGYsieakagelLHGLGFSNTQIDYAVSDFSGGWRMRLNLAQALIRDADLLLL 173
Cdd:PRK11147 401 M-------DNLAEGKQEVMVNGRPRHVLGY---------LQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLIL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 174 DEPTNHLDLDAVYWLERFLRSYAGTLVLISHDREFLDAVVGEIWHID-QQQINVYKGNYSQFERQKAERLAQQQAQFDKQ 252
Cdd:PRK11147 465 DEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEgNGKIGRYVGGYHDARQQQAQYLALKQPAVKKK 544
|
....*
gi 800951443 253 QEQIA 257
Cdd:PRK11147 545 EEAAA 549
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-242 |
4.06e-25 |
|
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: 109.64 E-value: 4.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSIASVKQETPALAital 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALD---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 82 eyvlqGNPDYYalrcqlkqaEQQGDGetqaqvhqqLELMK--GYSIEAKAgeLLHGLGFSNTQIDYAVSDFSGGWRMRLN 159
Cdd:TIGR03719 399 -----PNKTVW---------EEISGG---------LDIIKlgKREIPSRA--YVGRFNFKGSDQQKKVGQLSGGERNRVH 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 160 LAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAGTLVLISHDREFLDAVVGeiwHI----DQQQINVYKGNYSQFE 235
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIAT---HIlafeGDSHVEWFEGNFSEYE 530
|
....*..
gi 800951443 236 RQKAERL 242
Cdd:TIGR03719 531 EDKKRRL 537
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
322-509 |
5.63e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 103.99 E-value: 5.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHqGL-----------KVGYFAQHQ------ 384
Cdd:COG1131 10 YGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVL-GEdvardpaevrrRIGYVPQEPalypdl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 385 --LEALDLQASpvthLQRLNPQASEQSLRDFLGGFAfIGDKALDPVAPFSGGEKARLVLAM-LVYQkPNLLLLDEPTNHL 461
Cdd:COG1131 89 tvRENLRFFAR----LYGLPRKEARERIDELLELFG-LTDAADRKVGTLSGGMKQRLGLALaLLHD-PELLILDEPTSGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 800951443 462 DLEMRHALVMALQSFDGAMVTV---SHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:COG1131 163 DPEARRELWELLRELAAEGKTVllsTHYLEEAERLCDRVAIIDKGRIVADG 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
282-509 |
1.84e-24 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 108.38 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 282 ALERMEKLAPAHVDSPFDFSFAEPDALpNPLIALDGAQAGYGDTT--ILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLA 359
Cdd:COG2274 444 ALERLDDILDLPPEREEGRSKLSLPRL-KGDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 360 QELAPQAGDVFF---------HQGL--KVGYFAQHQ-------LEALDLQASPVThLQRLNpQASEQS-LRDFL----GG 416
Cdd:COG2274 523 GLYEPTSGRILIdgidlrqidPASLrrQIGVVLQDVflfsgtiRENITLGDPDAT-DEEII-EAARLAgLHDFIealpMG 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 417 F-AFIGDKAldpvAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSFDG--AMVTVSHDRHLLKNt 493
Cdd:COG2274 601 YdTVVGEGG----SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL- 675
|
250
....*....|....*.
gi 800951443 494 ADEFYLVDSGEVRQFG 509
Cdd:COG2274 676 ADRIIVLDKGRIVEDG 691
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
313-509 |
2.23e-24 |
|
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: 102.03 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGY-GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHqGL------------KVGY 379
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD-GKditkknlrelrrKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 380 ---FAQHQL-------------EALDLqaSPVTHLQRLnpqasEQSLRDF-LGGFAfigDKAldpvaPF--SGGEKARL- 439
Cdd:COG1122 80 vfqNPDDQLfaptveedvafgpENLGL--PREEIRERV-----EEALELVgLEHLA---DRP-----PHelSGGQKQRVa 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 800951443 440 ---VLAMlvyqKPNLLLLDEPTNHLDLEMRHALVMALQSFDGA---MVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:COG1122 145 iagVLAM----EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHDLDLVAELADRVIVLDDGRIVADG 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
312-515 |
7.69e-24 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 106.19 E-value: 7.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 312 LIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGLKVG------------- 378
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVArlqqdpprnvegt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 379 ---YFA---QHQLEALDlQASPVTHL-------QRLNPQASEQSLRDFLGGFAF-------IGDKALDPVAP---FSGGE 435
Cdd:PRK11147 83 vydFVAegiEEQAEYLK-RYHDISHLvetdpseKNLNELAKLQEQLDHHNLWQLenrinevLAQLGLDPDAAlssLSGGW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 436 KARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFGYDLDAY 515
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQY 241
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
323-504 |
8.14e-24 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 99.85 E-value: 8.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF-----------HQGLKVGY---FAQHQLEAL 388
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdgkdltklslkELRRKVGLvfqNPDDQFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 389 D-----------LQASPVTHLQRLnpqasEQSLRDFLggfafIGDKALDPVAPFSGGEKARLVLA-MLVYQkPNLLLLDE 456
Cdd:cd03225 92 TveeevafglenLGLPEEEIEERV-----EEALELVG-----LEGLRDRSPFTLSGGQKQRVAIAgVLAMD-PDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 800951443 457 PTNHLDLEMRHALVMALQSFDGA---MVTVSHDRHLLKNTADEFYLVDSGE 504
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-242 |
8.22e-24 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 105.97 E-value: 8.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 12 GPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSIASVKQETPALA--ITALEYVLQGNp 89
Cdd:PRK11819 335 GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDpnKTVWEEISGGL- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 90 DY------------YALRCQLKQAEQQgdgetqaqvhqqlelmkgysieAKAGELlhglgfsntqidyavsdfSGGWRMR 157
Cdd:PRK11819 414 DIikvgnreipsraYVGRFNFKGGDQQ----------------------KKVGVL------------------SGGERNR 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 158 LNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAGTLVLISHDREFLDAVVGeiwHI----DQQQINVYKGNYSQ 233
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIAT---HIlafeGDSQVEWFEGNFQE 530
|
....*....
gi 800951443 234 FERQKAERL 242
Cdd:PRK11819 531 YEEDKKRRL 539
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
313-504 |
1.16e-23 |
|
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: 98.22 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTT--ILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQglkvgyfaqhqleaLDL 390
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG--------------VDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 391 QASPVTHLQRL------NPQASEQSLRDFLggfafigdkaldpvapFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLE 464
Cdd:cd03228 67 RDLDLESLRKNiayvpqDPFLFSGTIRENI----------------LSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 800951443 465 MRHALVMALQSFDG--AMVTVSHDRHLLKNtADEFYLVDSGE 504
Cdd:cd03228 131 TEALILEALRALAKgkTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
321-501 |
1.76e-23 |
|
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: 98.76 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 321 GYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF------HQGLKVGYFAQHQ---------- 384
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkpleKERKRIGYVPQRRsidrdfpisv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 385 ----LEALDLQASPVTHLQRLNPQASEQSLrDFLGgfafIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNH 460
Cdd:cd03235 88 rdvvLMGLYGHKGLFRRLSKADKAKVDEAL-ERVG----LSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 800951443 461 LDLEMRHA---LVMALQSFDGAMVTVSHDRHLLKNTADEFYLVD 501
Cdd:cd03235 163 VDPKTQEDiyeLLRELRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
280-509 |
2.30e-23 |
|
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: 104.45 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 280 VKALERMEKLAPAHVDSPFDFSFAEPDAlPNPLIALDGAQAGYGD-TTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLL 358
Cdd:COG4988 305 IAAAEKIFALLDAPEPAAPAGTAPLPAA-GPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 359 AQELAPQAGDVffhqglkvgyfaqhQLEALDLQASPVTHLQRL----------------------NPQASEQSLR----- 411
Cdd:COG4988 384 LGFLPPYSGSI--------------LINGVDLSDLDPASWRRQiawvpqnpylfagtirenlrlgRPDASDEELEaalea 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 412 ----DFL----GGFAF-IGDKAldpvAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQS-FDGAMV 481
Cdd:COG4988 450 agldEFVaalpDGLDTpLGEGG----RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlAKGRTV 525
|
250 260
....*....|....*....|....*....
gi 800951443 482 -TVSHDRHLLKNtADEFYLVDSGEVRQFG 509
Cdd:COG4988 526 iLITHRLALLAQ-ADRILVLDDGRIVEQG 553
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
321-490 |
6.35e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.53 E-value: 6.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 321 GYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGLKVGYFAQH------------QLEAL 388
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRsevpdslpltvrDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 389 DLQA--SPVTHLQRLNPQASEQSLrDFLGgfafIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMR 466
Cdd:NF040873 81 GRWArrGLWRRLTRDDRAAVDDAL-ERVG----LADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180
....*....|....*....|....*..
gi 800951443 467 HAL--VMALQSFDGA-MVTVSHDRHLL 490
Cdd:NF040873 156 ERIiaLLAEEHARGAtVVVVTHDLELV 182
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-224 |
7.51e-23 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 95.93 E-value: 7.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEwsiaSVKQEtPALAITAL 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK----DIKKE-PEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 82 EYVLQGNPDYYALRcqlkqaeqqgdgetqaqVHQQLELmkgysieakagellhglgfsntqidyavsdfSGGWRMRLNLA 161
Cdd:cd03230 76 GYLPEEPSLYENLT-----------------VRENLKL-------------------------------SGGMKQRLALA 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 800951443 162 QALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYA---GTLVLISHDREFLDAVVGEIWHIDQQQI 224
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-205 |
1.18e-22 |
|
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: 97.42 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKV---------PKEWS--IASV 69
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdgrdlaslsRRELArrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 70 KQETPA-LAITALEYVLQGnpdyyalRCQLKQAEQQGDGETQAQVHQQLELMkgySIEAKAGELLHGLgfsntqidyavs 148
Cdd:COG1120 81 PQEPPApFGLTVRELVALG-------RYPHLGLFGRPSAEDREAVEEALERT---GLEHLADRPVDEL------------ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 800951443 149 dfSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG----TLVLISHD 205
Cdd:COG1120 139 --SGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARergrTVVMVLHD 197
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-178 |
1.37e-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: 94.25 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAG----NAKVPKEWSIASVKQEtpalaitaLEYVLQGNPDYY 92
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGtillDGQDLTDDERKSLRKE--------IGYVFQDPQLFP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 93 ALRCQlkqaeqqgdgETQAQVHQQLELMKGYSiEAKAGELLHGLG---FSNTQIDYAVSDFSGGWRMRLNLAQALIRDAD 169
Cdd:pfam00005 73 RLTVR----------ENLRLGLLLKGLSKREK-DARAEEALEKLGlgdLADRPVGERPGTLSGGQRQRVAIARALLTKPK 141
|
....*....
gi 800951443 170 LLLLDEPTN 178
Cdd:pfam00005 142 LLLLDEPTA 150
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
16-239 |
3.02e-22 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 100.74 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 16 LLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKvpkeWSIASvkqetpalaitALEYVLQGNPDYYALR 95
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK----WSENA-----------NIGYYAQDHAYDFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 96 CQL----KQAEQQGDGETqaqvhqqlelmkgySIEAKAGELLhglgFSNTQIDYAVSDFSGGWRMRLNLAQALIRDADLL 171
Cdd:PRK15064 399 LTLfdwmSQWRQEGDDEQ--------------AVRGTLGRLL----FSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 172 LLDEPTNHLDLDAVYWLERFLRSYAGTLVLISHDREFLDAVVGEIWHIDQQQINVYKGNYSQFERQKA 239
Cdd:PRK15064 461 VMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQG 528
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-212 |
4.31e-22 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 94.47 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAkvpkEWSIASVKQETPALA--- 77
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEV----LWNGEPIRDAREDYRrrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 78 ------------ITALEYvlqgnpdyyaLRCQlkqAEQQGDGETQAQVHQQLELMKgysieakagelLHGLGfsntqiDY 145
Cdd:COG4133 78 aylghadglkpeLTVREN----------LRFW---AALYGLRADREAIDEALEAVG-----------LAGLA------DL 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 146 AVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYA---GTLVLISHDREFLDAV 212
Cdd:COG4133 128 PVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA 197
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
322-506 |
5.77e-22 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 95.31 E-value: 5.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAG--DVFFHQGLKVGYFAQHQL-------------- 385
Cdd:COG4555 11 YGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGsiLIDGEDVRKEPREARRQIgvlpderglydrlt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 386 --EALDLQASpvthLQRLNPQASEQSLRDFLGGFAFigDKALD-PVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLD 462
Cdd:COG4555 91 vrENIRYFAE----LYGLFDEELKKRIEELIELLGL--EEFLDrRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 800951443 463 LEMRHALVMALQSF--DGAMVTVS-HDRHLLKNTADEFYLVDSGEVR 506
Cdd:COG4555 165 VMARRLLREILRALkkEGKTVLFSsHIMQEVEALCDRVVILHKGKVV 211
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
323-505 |
6.19e-22 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 95.65 E-value: 6.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF-----------HQGLKVGYFAQHQLEALDLQ 391
Cdd:TIGR03873 12 GGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLagvdlhglsrrARARRVALVEQDSDTAVPLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 392 ASPVTHLQR--------LNPQASEQSLRDFLG--GFAFIGDKALDPVapfSGGEKARLVLAMLVYQKPNLLLLDEPTNHL 461
Cdd:TIGR03873 92 VRDVVALGRiphrslwaGDSPHDAAVVDRALArtELSHLADRDMSTL---SGGERQRVHVARALAQEPKLLLLDEPTNHL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 800951443 462 DLEMRHALVMALQSFDGAMVTVS---HDRHLLKNTADEFYLVDSGEV 505
Cdd:TIGR03873 169 DVRAQLETLALVRELAATGVTVVaalHDLNLAASYCDHVVVLDGGRV 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
311-486 |
8.52e-22 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 93.70 E-value: 8.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 311 PLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQG----LKVGYFAQ---- 382
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdAREDYRRRlayl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 383 -HQLeALDLQASPVTHL---QRLNP-QASEQSLRDFLGGFAfIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEP 457
Cdd:COG4133 81 gHAD-GLKPELTVRENLrfwAALYGlRADREAIDEALEAVG-LAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|..
gi 800951443 458 TNHLDLEMRHALVMALQSF---DGAMVTVSHD 486
Cdd:COG4133 159 FTALDAAGVALLAELIAAHlarGGAVLLTTHQ 190
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-223 |
1.01e-21 |
|
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: 93.69 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 11 RGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVP----KEWSIASVKQETpalaitalEYVLQ 86
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdlTKLSLKELRRKV--------GLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 87 gNPDY------------YALR-CQLKQAEqqgdgetqaqvhqqlelmkgysIEAKAGELLHGLGFSNTQiDYAVSDFSGG 153
Cdd:cd03225 83 -NPDDqffgptveeevaFGLEnLGLPEEE----------------------IEERVEEALELVGLEGLR-DRSPFTLSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 800951443 154 WRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG---TLVLISHDREFLDAVVGEIWHIDQQQ 223
Cdd:cd03225 139 QKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
319-486 |
2.33e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.93 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 319 QAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVfFHQGLKVGYFAQHQL------------- 385
Cdd:PRK11231 9 TVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTV-FLGDKPISMLSSRQLarrlallpqhhlt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 386 -EALDLQA------SP-VTHLQRLNP-------QASEQSLRDFLggfafigdkALDPVAPFSGGEKARLVLAMLVYQKPN 450
Cdd:PRK11231 88 pEGITVRElvaygrSPwLSLWGRLSAednarvnQAMEQTRINHL---------ADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 800951443 451 LLLLDEPTNHLDLE-----MRhaLVMALQSFDGAMVTVSHD 486
Cdd:PRK11231 159 VVLLDEPTTYLDINhqvelMR--LMRELNTQGKTVVTVLHD 197
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-224 |
3.48e-21 |
|
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: 97.52 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGP-KCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKV---------PKEWS--IASV 69
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIngvdlsdldPASWRrqIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 70 KQETPALAITALEYVLQGNPDYyalrcqlkqaeqqgdgeTQAQVHQQLELmkgysieAKAGELLHGL--GFsNTQIDYAV 147
Cdd:COG4988 417 PQNPYLFAGTIRENLRLGRPDA-----------------SDEELEAALEA-------AGLDEFVAALpdGL-DTPLGEGG 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 800951443 148 SDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG--TLVLISHDREFLDAvVGEIWHIDQQQI 224
Cdd:COG4988 472 RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALLAQ-ADRILVLDDGRI 549
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
30-203 |
3.52e-21 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 92.82 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 30 VGLVGSNGCGKSSLFALLKGELQLDAGNAKVpkeWSIASVKQETPALAITAleYVLQGNPDYYALRcqlkqaeqqgdget 109
Cdd:COG1131 29 FGLLGPNGAGKTTTIRMLLGLLRPTSGEVRV---LGEDVARDPAEVRRRIG--YVPQEPALYPDLT-------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 110 qaqVHQQLELMKGY------SIEAKAGELLHGLGFSNtQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLD 183
Cdd:COG1131 90 ---VRENLRFFARLyglprkEARERIDELLELFGLTD-AADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPE 165
|
170 180
....*....|....*....|..
gi 800951443 184 AVYWLERFLRSYA--GTLVLIS 203
Cdd:COG1131 166 ARRELWELLRELAaeGKTVLLS 187
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
322-509 |
4.20e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 93.26 E-value: 4.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVffhqglkvgYFAQHQLEALDLQAspvthLQRL 401
Cdd:COG4559 11 LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEV---------RLNGRPLAAWSPWE-----LARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 402 N---PQASEQSLrDF-------LGGFAFIGDKALDP-----------VAPF--------SGGEKARL----VLAML---V 445
Cdd:COG4559 77 RavlPQHSSLAF-PFtveevvaLGRAPHGSSAAQDRqivrealalvgLAHLagrsyqtlSGGEQQRVqlarVLAQLwepV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 446 YQKPNLLLLDEPTNHLDLEMRHALVMALQSF---DGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:COG4559 156 DGGPRWLFLDEPTSALDLAHQHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQG 222
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
282-486 |
5.97e-21 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 96.66 E-value: 5.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 282 ALERMEKLAPAHVDSPF-DFSFAEPDALPNPLIALDGAQAGY-GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLA 359
Cdd:TIGR02868 303 AAERIVEVLDAAGPVAEgSAPAAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 360 QELAPQAGDV---------FFHQGLK--VGYFAQ--HqlealdLQASPVTHLQRL-NPQASEQSLRDFLGGfAFIGD--- 422
Cdd:TIGR02868 383 GLLDPLQGEVtldgvpvssLDQDEVRrrVSVCAQdaH------LFDTTVRENLRLaRPDATDEELWAALER-VGLADwlr 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 800951443 423 ---KALDPV-----APFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALV-MALQSFDG-AMVTVSHD 486
Cdd:TIGR02868 456 alpDGLDTVlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLeDLLAALSGrTVVLITHH 529
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
311-496 |
8.76e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 92.10 E-value: 8.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 311 PLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGLKVGYFAQ--HQLEAL 388
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQklYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 389 DLQaspVTHLQRLNPQASEQslrDFLGGFAFIGDKAL--DPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMR 466
Cdd:PRK09544 83 PLT---VNRFLRLRPGTKKE---DILPALKRVQAGHLidAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180 190
....*....|....*....|....*....|....
gi 800951443 467 HALVMAL----QSFDGAMVTVSHDRHLLKNTADE 496
Cdd:PRK09544 157 VALYDLIdqlrRELDCAVLMVSHDLHLVMAKTDE 190
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-224 |
1.41e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 91.30 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKV-----PKEWS-IASVKQET- 73
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkppRRARRrIGYVPQRAe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 74 --PALAITALEYVLQGNPDYYALRCQLKQAEQQgdgetqaQVHQQLELMkgysieakagellhGL-GFSNTQIdyavSDF 150
Cdd:COG1121 86 vdWDFPITVRDVVLMGRYGRRGLFRRPSRADRE-------AVDEALERV--------------GLeDLADRPI----GEL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 151 SGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG---TLVLISHDREFLDAVVGEIWHIDQQQI 224
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
12-233 |
2.13e-20 |
|
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: 95.22 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 12 GPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKV----PKEWS-------IASVKQETPALAITA 80
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLggvdLRDLDeddlrrrIAVVPQRPHLFDTTL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 81 LEYVLQGNPDyyALRCQLKQAEQQgdgetqAQVHQQLElmkgysieakagELLHGLgfsNTQIDYAVSDFSGGWRMRLNL 160
Cdd:COG4987 426 RENLRLARPD--ATDEELWAALER------VGLGDWLA------------ALPDGL---DTWLGEGGRRLSGGERRRLAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 161 AQALIRDADLLLLDEPTNHLD-LDAVYWLERFLRSYAG-TLVLISHDREFLDAvVGEIWHIDQQQInVYKGNYSQ 233
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDaATEQALLADLLEALAGrTVLLITHRLAGLER-MDRILVLEDGRI-VEQGTHEE 555
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-223 |
2.51e-20 |
|
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: 88.07 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 3 QITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAkvpkEWSIASVKQETPALAITALE 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI----LIDGKDIAKLPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 83 YVLQgnpdyyalrcqlkqaeqqgdgetqaqvhqqlelmkgysieakagellhglgfsntqidyavsdFSGGWRMRLNLAQ 162
Cdd:cd00267 77 YVPQ---------------------------------------------------------------LSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 800951443 163 ALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG---TLVLISHDREFLDAVVGEIWHIDQQQ 223
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
310-485 |
4.21e-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: 90.14 E-value: 4.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 310 NPLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVF--FHQGL----------KV 377
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlFGERRggedvwelrkRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 378 GYFA---QHQLE----ALDLQAS----------PVTHLQRlnpQASEQSLrDFLGgfafIGDKALDPVAPFSGGEKaRLV 440
Cdd:COG1119 81 GLVSpalQLRFPrdetVLDVVLSgffdsiglyrEPTDEQR---ERARELL-ELLG----LAHLADRPFGTLSQGEQ-RRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 800951443 441 L---AMLvyQKPNLLLLDEPTNHLDLEMRHALVMALQSF--DG--AMVTVSH 485
Cdd:COG1119 152 LiarALV--KDPELLILDEPTAGLDLGARELLLALLDKLaaEGapTLVLVTH 201
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
322-506 |
1.76e-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: 87.27 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF--------HQGLKV--------GYF----A 381
Cdd:cd03268 10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdgksyqknIEALRRigalieapGFYpnltA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 382 QHQLEALDLQAspvthlqRLNPQASEQSLRdfLGGFAFIGDKaldPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHL 461
Cdd:cd03268 90 RENLRLLARLL-------GIRKKRIDEVLD--VVGLKDSAKK---KVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 800951443 462 D----LEMRhALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVR 506
Cdd:cd03268 158 DpdgiKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
313-504 |
6.10e-19 |
|
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: 84.55 E-value: 6.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH-------------QGLKVGY 379
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgedltdledelppLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 380 -FAQHQLealdlqaspVTHLQrlnpqaseqslrdflggfafigdkALDPVA-PFSGGEKARLVLAMLVYQKPNLLLLDEP 457
Cdd:cd03229 81 vFQDFAL---------FPHLT------------------------VLENIAlGLSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 800951443 458 TNHLDLEMRH---ALVMALQSFDG-AMVTVSHDRHLLKNTADEFYLVDSGE 504
Cdd:cd03229 128 TSALDPITRRevrALLKSLQAQLGiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-224 |
6.23e-19 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 85.64 E-value: 6.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAG---------NAKVPKEW--SIASVK 70
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGeiyldgkplSAMPPPEWrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 71 QETPALAITALEYVlqgnPDYYALRcqlkqaEQQGDGEtqaqvhqqlelmkgysieaKAGELLHGLGFSNTQIDYAVSDF 150
Cdd:COG4619 81 QEPALWGGTVRDNL----PFPFQLR------ERKFDRE-------------------RALELLERLGLPPDILDKPVERL 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 151 SGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYA----GTLVLISHDREFLDAVVGEIWHIDQQQI 224
Cdd:COG4619 132 SGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
322-486 |
1.24e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 85.98 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHqglkvgyfaQHQLEALDLQASpVTHLQRL 401
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLN---------GRPLADWSPAEL-ARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 402 nPQASeqSLrdflgGFAF----------------------IGDKALDPV--APF--------SGGEKARLVLAMLVYQ-- 447
Cdd:PRK13548 82 -PQHS--SL-----SFPFtveevvamgraphglsraeddaLVAAALAQVdlAHLagrdypqlSGGEQQRVQLARVLAQlw 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 800951443 448 ----KPNLLLLDEPTNHLDLEMRHALVMALQSF----DGAMVTVSHD 486
Cdd:PRK13548 154 epdgPPRWLLLDEPTSALDLAHQHHVLRLARQLaherGLAVIVVLHD 200
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
324-505 |
1.45e-18 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 83.52 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 324 DTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVffhqglkvgYFAQHQLEAL-DLQASPVTHLQRlN 402
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGVPVSDLeKALSSLISVLNQ-R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 403 PQASEQSLRDFLGgfafigdkaldpvAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSF--DGAM 480
Cdd:cd03247 84 PYLFDTTLRNNLG-------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVlkDKTL 150
|
170 180
....*....|....*....|....*.
gi 800951443 481 VTVSHdrHLLK-NTADEFYLVDSGEV 505
Cdd:cd03247 151 IWITH--HLTGiEHMDKILFLENGKI 174
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-504 |
1.69e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 89.48 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 30 VGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSiasvkqetpalaiTALEY----VLQgnpDYYA------LRCQLK 99
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWD-------------EVLKRfrgtELQ---NYFKklyngeIKVVHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 100 -----QAEQQGDGETQaqvhqqlELMKGYSIEAKAGELLHGLGFSNTqIDYAVSDFSGGWRMRLNLAQALIRDADLLLLD 174
Cdd:PRK13409 166 pqyvdLIPKVFKGKVR-------ELLKKVDERGKLDEVVERLGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 175 EPTNHLDldaVYwlERF-----LRSYAG--TLVLISHDREFLDAVVGEIwHIdqqqinVY--KGNYSQFERQKAERLAqq 245
Cdd:PRK13409 238 EPTSYLD---IR--QRLnvarlIRELAEgkYVLVVEHDLAVLDYLADNV-HI------AYgePGAYGVVSKPKGVRVG-- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 246 qaqfdkqqeqI-AHLEKFI----TRFkakaskakqaqsRVKALERMEKlapahvdSPFDFSFAEpdalpnPLIALDGAQA 320
Cdd:PRK13409 304 ----------InEYLKGYLpeenMRI------------RPEPIEFEER-------PPRDESERE------TLVEYPDLTK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 321 GYGDttilhsIKLNLVPGSR-----IALLGRNGAGKSTLIKLLAQELAPQAGDVFFhqGLKVGYfaqhqlealdlqaSPv 395
Cdd:PRK13409 349 KLGD------FSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--ELKISY-------------KP- 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 396 thlQRLNPqASEQSLRDFLggfAFIGDK--------------ALDP-----VAPFSGGEKARLVLAMLVYQKPNLLLLDE 456
Cdd:PRK13409 407 ---QYIKP-DYDGTVEDLL---RSITDDlgssyykseiikplQLERlldknVKDLSGGELQRVAIAACLSRDADLYLLDE 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 800951443 457 PTNHLDLEMRHALVMALQSF----DGAMVTVSHDRHLLKNTADEFyLVDSGE 504
Cdd:PRK13409 480 PSAHLDVEQRLAVAKAIRRIaeerEATALVVDHDIYMIDYISDRL-MVFEGE 530
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
322-505 |
1.72e-18 |
|
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: 84.23 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH-------QGLKVGYFA----QHQL----- 385
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNgkpikakERRKSIGYVmqdvDYQLftdsv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 386 -EALDLQASPVThlqrLNPQASEQSLRDFlggfafiGDKALDPVAPF--SGGEKARLVLAMLVYQKPNLLLLDEPTNHLD 462
Cdd:cd03226 90 rEELLLGLKELD----AGNEQAETVLKDL-------DLYALKERHPLslSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 800951443 463 LE-MRH--ALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:cd03226 159 YKnMERvgELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-504 |
2.27e-18 |
|
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: 89.07 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 30 VGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSiasvkqetpalaiTALEY----VLQgnpDYYA------LRCQLK 99
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWD-------------EVLKRfrgtELQ---DYFKklangeIKVAHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 100 -----QAEQQGDGETQaqvhqqlELMKGYSIEAKAGELLHGLGFSNTqIDYAVSDFSGGWRMRLNLAQALIRDADLLLLD 174
Cdd:COG1245 166 pqyvdLIPKVFKGTVR-------ELLEKVDERGKLDELAEKLGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 175 EPTNHLDldaVYwlERF-----LRSYAG---TLVLISHDREFLDAVVGEIwHIdqqqinVY--KGNYSQFERQKAERLAq 244
Cdd:COG1245 238 EPSSYLD---IY--QRLnvarlIRELAEegkYVLVVEHDLAILDYLADYV-HI------LYgePGVYGVVSKPKSVRVG- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 245 qqaqfdkqqeqI-AHLEKFIT----RFkakaskakqaqsRvkalermeklapahvDSPFDFSFAEPDALPN--PLIALDG 317
Cdd:COG1245 305 -----------InQYLDGYLPeenvRI------------R---------------DEPIEFEVHAPRREKEeeTLVEYPD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 318 AQAGYGDttilhsIKLNLVPGS-----RIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhqGLKVGYFAQHqLEAlDLQA 392
Cdd:COG1245 347 LTKSYGG------FSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE--DLKISYKPQY-ISP-DYDG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 393 SPVTHLQRLNPQASEQSL--RDFLGGFAFigDKALD-PVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHAL 469
Cdd:COG1245 417 TVEEFLRSANTDDFGSSYykTEIIKPLGL--EKLLDkNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 494
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 800951443 470 VMALQSF-----DGAMVtVSHDRHLLKNTADEFyLVDSGE 504
Cdd:COG1245 495 AKAIRRFaenrgKTAMV-VDHDIYLIDYISDRL-MVFEGE 532
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
313-505 |
2.33e-18 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 84.18 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTTI--LHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF---------HQGLK--VGY 379
Cdd:cd03245 3 IEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirqldPADLRrnIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 380 FAQHQ-----------------------LEALDLqaSPVTHLQRLNPQASEQSLRDflGGFAfigdkaldpvapFSGGEK 436
Cdd:cd03245 83 VPQDVtlfygtlrdnitlgapladderiLRAAEL--AGVTDFVNKHPNGLDLQIGE--RGRG------------LSGGQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 800951443 437 ARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSF--DGAMVTVSHDRHLLkNTADEFYLVDSGEV 505
Cdd:cd03245 147 QAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSLL-DLVDRIIVMDSGRI 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
17-207 |
2.66e-18 |
|
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: 88.50 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKV---------PKEW--SIASVKQeTPAL-AITALEYV 84
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpladadADSWrdQIAWVPQ-HPFLfAGTIAENI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 85 LQGNPDyyALRCQLKQAEQQgdgetqaqvhqqlelmkgysieAKAGELLHGLGFS-NTQIDYAVSDFSGGWRMRLNLAQA 163
Cdd:TIGR02857 417 RLARPD--ASDAEIREALER----------------------AGLDEFVAALPQGlDTPIGEGGAGLSGGQAQRLALARA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 800951443 164 LIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG--TLVLISHDRE 207
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLA 518
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
317-509 |
4.00e-18 |
|
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: 83.74 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 317 GAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQG----LKVGYFAQHQLEALD--- 389
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsslLGLGGGFNPELTGREniy 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 390 LQASpvthLQRLNPQASEQSLRDFLgGFAFIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMR--- 466
Cdd:cd03220 107 LNGR----LLGLSRKEIDEKIDEII-EFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQekc 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 800951443 467 HALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:cd03220 182 QRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-205 |
4.13e-18 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 82.48 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 3 QITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVpkewsiasvkQETPALAITALE 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL----------DGKDLASLSPKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 83 yvlqgnpdyyaLRCQLkqaeqqgdgetqAQVHQQLELMKgysIEAKAGELLHGLgfsntqidyavsdfSGGWRMRLNLAQ 162
Cdd:cd03214 71 -----------LARKI------------AYVPQALELLG---LAHLADRPFNEL--------------SGGERQRVLLAR 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 800951443 163 ALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG----TLVLISHD 205
Cdd:cd03214 111 ALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARergkTVVMVLHD 157
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
217-302 |
4.21e-18 |
|
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: 79.15 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 217 WHIDQQQINVYKGNYSQFERQKAERLAQQQAQFDKQQEQIAHLEKFITRFKAKASKAKQAQSRVKALERMEKLAPAHVDS 296
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEKPERDK 80
|
....*.
gi 800951443 297 PfDFSF 302
Cdd:pfam12848 81 P-KLRF 85
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
321-509 |
8.93e-18 |
|
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: 82.55 E-value: 8.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 321 GYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH--------------QGLKVGYFAQHQLE 386
Cdd:cd03257 14 GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDgkdllklsrrlrkiRRKEIQMVFQDPMS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 387 AL-------DLQASPVTHLQRLNPQAsEQSLRDFLGGFAFIGDKALDPVAP--FSGGEKARLVLAMLVYQKPNLLLLDEP 457
Cdd:cd03257 94 SLnprmtigEQIAEPLRIHGKLSKKE-ARKEAVLLLLVGVGLPEEVLNRYPheLSGGQRQRVAIARALALNPKLLIADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 458 TNHLDLEMRhALVMAL-----QSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:cd03257 173 TSALDVSVQ-AQILDLlkklqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
313-509 |
1.24e-17 |
|
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: 81.86 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTTILHSIKLNLVPGSrIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH--------QGL--KVGYFAQ 382
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDgqdvlkqpQKLrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 383 H--------QLEALDLQASpvthLQRLNPQASEQSLRDFLGGFAfIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLL 454
Cdd:cd03264 80 EfgvypnftVREFLDYIAW----LKGIPSKEVKARVDEVLELVN-LGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 455 DEPTNHLDLEMRHALVMALQSFdGAMVTV---SHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSEL-GEDRIVilsTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
322-505 |
1.76e-17 |
|
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: 82.10 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF--------------HQGL-----KVGYF-- 380
Cdd:cd03219 10 FGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFdgeditglppheiaRLGIgrtfqIPRLFpe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 381 ----------AQHQLEALDLQASPVTHLQRLNPQASEqsLRDFLGgfafIGDKALDPVAPFSGGEKARLVLAMLVYQKPN 450
Cdd:cd03219 90 ltvlenvmvaAQARTGSGLLLARARREEREARERAEE--LLERVG----LADLADRPAGELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 451 LLLLDEPTNHLDLEMRHA---LVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:cd03219 164 LLLLDEPAAGLNPEETEElaeLIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
17-230 |
2.06e-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: 81.61 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKV----PKEWSIASVKQEtpalaitaLEYVLQgNPDY- 91
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdgkdITKKNLRELRRK--------VGLVFQ-NPDDq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 92 -----------YALRcQLKQAEQqgdgETQAQVHQQLELMKgysIEAKAgellhglgfsntqiDYAVSDFSGGWRMRLNL 160
Cdd:COG1122 88 lfaptveedvaFGPE-NLGLPRE----EIRERVEEALELVG---LEHLA--------------DRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 800951443 161 AQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG---TLVLISHDREFLDAVVGEIWHIDQQQInVYKGN 230
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRI-VADGT 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
313-509 |
2.37e-17 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 81.78 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHqGLKVGYFAQHQLEALDLQ- 391
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-GEDISGLSEAELYRLRRRm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 392 -------------------ASPVTHLQRLNPQASEQSLRDFLGGFAFIGDKALDPvAPFSGGEKARLVLAMLVYQKPNLL 452
Cdd:cd03261 80 gmlfqsgalfdsltvfenvAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYP-AELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 800951443 453 LLDEPTNHLD---LEMRHALVMALQ-SFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:cd03261 159 LYDEPTAGLDpiaSGVIDDLIRSLKkELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-209 |
4.24e-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: 80.38 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 16 LLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSIASVKQETPAlaitaleYVLQgNPDYYALR 95
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIG-------YVMQ-DVDYQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 96 CQLKQAEQQGDGETQAQVHQQLELMKGYSIEAKAgeLLHGLgfsntqidyavsDFSGGWRMRLNLAQALIRDADLLLLDE 175
Cdd:cd03226 87 DSVREELLLGLKELDAGNEQAETVLKDLDLYALK--ERHPL------------SLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 800951443 176 PTNHLDLDAVYWLERFLRSYAG---TLVLISHDREFL 209
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAqgkAVIVITHDYEFL 189
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
17-213 |
4.26e-17 |
|
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: 80.27 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVP-----KEWS-IASVKQETPALA---ITALEYVLQG 87
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFgkpleKERKrIGYVPQRRSIDRdfpISVRDVVLMG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 88 NPDYYALRCQLKQAEQqgdgetqAQVHQQLELMkgysieakagellhGL-GFSNTQIdyavSDFSGGWRMRLNLAQALIR 166
Cdd:cd03235 95 LYGHKGLFRRLSKADK-------AKVDEALERV--------------GLsELADRQI----GELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 800951443 167 DADLLLLDEPTNHLDL---DAVYWLERFLRSYAGTLVLISHD----REFLDAVV 213
Cdd:cd03235 150 DPDLLLLDEPFAGVDPktqEDIYELLRELRREGMTILVVTHDlglvLEYFDRVL 203
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
11-205 |
4.38e-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: 81.40 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 11 RGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKE----WS-------IASVKQETP-ALAI 78
Cdd:TIGR03873 11 AGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVdlhgLSrrararrVALVEQDSDtAVPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 79 TALEYVLQGNPDYYALrcqlkqaeQQGDGETQAQVHQQLELMKGYSIEAkagellhglgfsntqiDYAVSDFSGGWRMRL 158
Cdd:TIGR03873 91 TVRDVVALGRIPHRSL--------WAGDSPHDAAVVDRALARTELSHLA----------------DRDMSTLSGGERQRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 800951443 159 NLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG---TLVLISHD 205
Cdd:TIGR03873 147 HVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHD 196
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-233 |
4.63e-17 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 85.27 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 16 LLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKV---------PKEW--SIASVKQETPALAITALEYV 84
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidlrqidPASLrrQIGVVLQDVFLFSGTIRENI 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 85 LQGNPD------YYALRcqlkqaeqqgdgetQAQVHQQLELM-KGYsieakagellhglgfsNTQIDYAVSDFSGGWRMR 157
Cdd:COG2274 570 TLGDPDatdeeiIEAAR--------------LAGLHDFIEALpMGY----------------DTVVGEGGSNLSGGQRQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 158 LNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG--TLVLISHDREFLDAvVGEIWHIDQQQInVYKGNYSQ 233
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL-ADRIIVLDKGRI-VEDGTHEE 695
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
313-505 |
5.18e-17 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 79.18 E-value: 5.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTT--ILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVffhqglkvgyfaqhQLEALDL 390
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV--------------RLDGADI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 391 QaspvthlqrlnpQASEQSLRDFLGGFA-----FIGDKAlDPVapFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEM 465
Cdd:cd03246 67 S------------QWDPNELGDHVGYLPqddelFSGSIA-ENI--LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 800951443 466 RHALVMALQSFDGAMVT---VSHDRHLLKnTADEFYLVDSGEV 505
Cdd:cd03246 132 ERALNQAIAALKAAGATrivIAHRPETLA-SADRILVLEDGRV 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
322-509 |
5.55e-17 |
|
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: 80.11 E-value: 5.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGD--VFFHQGLK--------VGYFAQHQ------- 384
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatVAGHDVVReprevrrrIGIVFQDLsvddelt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 385 -LEALDLQASpvthLQRLNPQASEQSLRDFLGGFAfIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDL 463
Cdd:cd03265 90 gWENLYIHAR----LYGVPGAERRERIDELLDFVG-LLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 800951443 464 EMRHAL---VMALQ-SFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:cd03265 165 QTRAHVweyIEKLKeEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
322-509 |
7.84e-17 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 79.49 E-value: 7.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF----------HQGlKVGYFAQH-----QLE 386
Cdd:cd03259 10 YGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdgrdvtgvppERR-NIGMVFQDyalfpHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 387 ALDLQASPVTHLQRLNPQASEQ--SLRDFLGgfafIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLD-- 462
Cdd:cd03259 89 VAENIAFGLKLRGVPKAEIRARvrELLELVG----LEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDak 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 800951443 463 --LEMRHALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:cd03259 165 lrEELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
338-575 |
7.99e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 83.79 E-value: 7.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 338 GSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGLKVGY-----FAQHQLEALDLQASPVTHLQRL---------NP 403
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKlrqdqFAFEEFTVLDTVIMGHTELWEVkqerdriyaLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 404 QASEQS---LRDFLGGFA-FIGDKA---------------------LDPVAPfsgGEKARLVLAMLVYQKPNLLLLDEPT 458
Cdd:PRK15064 107 EMSEEDgmkVADLEVKFAeMDGYTAearagelllgvgipeeqhyglMSEVAP---GWKLRVLLAQALFSNPDILLLDEPT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 459 NHLDLEMRHALVMALQSFDGAMVTVSHDRHLLK----NTADefylVDSGEVRQFGYDLDAYyqwLTKANQEQKQTQVEPD 534
Cdd:PRK15064 184 NNLDINTIRWLEDVLNERNSTMIIISHDRHFLNsvctHMAD----LDYGELRVYPGNYDEY---MTAATQARERLLADNA 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 800951443 535 KANS------------SANRkeQKRKEAEFRkhvqplKKAIDKLekQLDTLAP 575
Cdd:PRK15064 257 KKKAqiaelqsfvsrfSANA--SKAKQATSR------AKQIDKI--KLEEVKP 299
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
322-497 |
1.44e-16 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 77.47 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHqGLKVgyfaqhqlealdlqaspvthlQRL 401
Cdd:cd03216 10 FGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-GKEV---------------------SFA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 402 NPQASEQSlrdflgGFAFigdkaldpVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDL---EMRHALVMALQSFDG 478
Cdd:cd03216 68 SPRDARRA------GIAM--------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPaevERLFKVIRRLRAQGV 133
|
170
....*....|....*....
gi 800951443 479 AMVTVSHDRHLLKNTADEF 497
Cdd:cd03216 134 AVIFISHRLDEVFEIADRV 152
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
322-509 |
1.46e-16 |
|
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: 78.86 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVGYFAQHQL----EALDL------- 390
Cdd:cd03269 10 FGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-DGKPLDIAARNRIgylpEERGLypkmkvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 391 -QASPVTHLQRLNPQASEQSLRDFLGGFAfIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLD---LEMR 466
Cdd:cd03269 89 dQLVYLAQLKGLKKEEARRRIDEWLERLE-LSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDpvnVELL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 800951443 467 HALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:cd03269 168 KDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-203 |
1.65e-16 |
|
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: 78.41 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVpkeWSIASVKQETPALAITAL 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF---DGKSYQKNIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 82 -EYvlqgnPDYYALRCqlkqaeqqgdGETQAQVHQqLELMKGYSIeakAGELLHGLGFSNTQiDYAVSDFSGGWRMRLNL 160
Cdd:cd03268 78 iEA-----PGFYPNLT----------ARENLRLLA-RLLGIRKKR---IDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGI 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 800951443 161 AQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYA--GTLVLIS 203
Cdd:cd03268 138 ALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRdqGITVLIS 182
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-236 |
2.34e-16 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 82.99 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 12 GPkCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSIASVKQEtpalAITALEyvLQGNPDY 91
Cdd:PLN03073 521 GP-LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQH----HVDGLD--LSSNPLL 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 92 YALRCQLKQAEQQgdgetqaqvhqqlelmkgysIEAKAGELlhglGFSNTQIDYAVSDFSGGWRMRLNLAQALIRDADLL 171
Cdd:PLN03073 594 YMMRCFPGVPEQK--------------------LRAHLGSF----GVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIL 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 172 LLDEPTNHLDLDAVYWLERFLRSYAGTLVLISHDREFLDAVVGEIWHIDQQQINVYKGNYSQFER 236
Cdd:PLN03073 650 LLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKK 714
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
321-486 |
3.08e-16 |
|
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: 77.93 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 321 GYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF----------HQGLKVGYFAQHqlEALDL 390
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIngysirtdrkAARQSLGYCPQF--DALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 391 QASPVTHLQ---RL-------NPQASEQSLRDFLggfafIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNH 460
Cdd:cd03263 89 ELTVREHLRfyaRLkglpkseIKEEVELLLRVLG-----LTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180
....*....|....*....|....*...
gi 800951443 461 LDLEMRHALVMALQSFDG--AMVTVSHD 486
Cdd:cd03263 164 LDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
315-509 |
3.18e-16 |
|
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: 78.24 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 315 LDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVGYFAQHQLEALDLQASP 394
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF-DGRDITGLPPHERARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 395 VThlQRLNPQAS-EQSLRdfLGGFAFIGDKALDPVA------P------------FSGGEKARLVLAMLVYQKPNLLLLD 455
Cdd:cd03224 82 EG--RRIFPELTvEENLL--LGAYARRRAKRKARLErvyelfPrlkerrkqlagtLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 800951443 456 EPTnhLDL-----EMRHALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:cd03224 158 EPS--EGLapkivEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEG 214
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
326-505 |
4.90e-16 |
|
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: 78.69 E-value: 4.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 326 TILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVGYFAQHQLEAL--DLQ------------ 391
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSF-RGQDLYQLDRKQRRAFrrDVQlvfqdspsavnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 392 --------ASPVTHLQRLNPQASEQSLRDFLGGFAFIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDL 463
Cdd:TIGR02769 104 rmtvrqiiGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 800951443 464 EMRHALVMAL----QSFDGAMVTVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:TIGR02769 184 VLQAVILELLrklqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-237 |
5.34e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 81.43 E-value: 5.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 14 KCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDaGNAKV---------PKEW--SIASVKQETPALAITALE 82
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKIngielreldPESWrkHLSWVGQNPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 83 YVLQGNPDYyalrcqlkqaeqqgdgeTQAQVHQQLELmkgysieAKAGE----LLHGLgfsntqiDYAVSD----FSGGW 154
Cdd:PRK11174 442 NVLLGNPDA-----------------SDEQLQQALEN-------AWVSEflplLPQGL-------DTPIGDqaagLSVGQ 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 155 RMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG--TLVLISHDREFLDAvVGEIWHIDQQQInVYKGNYS 232
Cdd:PRK11174 491 AQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRrqTTLMVTHQLEDLAQ-WDQIWVMQDGQI-VQQGDYA 568
|
....*
gi 800951443 233 QFERQ 237
Cdd:PRK11174 569 ELSQA 573
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
322-509 |
5.66e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 77.83 E-value: 5.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVG---------------YFAQH--- 383
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIV-DGLKVNdpkvderlirqeagmVFQQFylf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 384 -QLEALDLQASPVTHLQRLNPQASEQSLRDFLG--GFAfigDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNH 460
Cdd:PRK09493 90 pHLTALENVMFGPLRVRGASKEEAEKQARELLAkvGLA---ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 800951443 461 LDLEMRHALVMALQSF--DG-AMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:PRK09493 167 LDPELRHEVLKVMQDLaeEGmTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
329-509 |
6.70e-16 |
|
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: 79.77 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 329 HSIKLNL-VPGS-RIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH--------QGL-------KVGYFAQhqlealdlQ 391
Cdd:TIGR02142 12 FSLDADFtLPGQgVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgrtlfdsrKGIflppekrRIGYVFQ--------E 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 392 ASPVTHL---QRLN----------PQASEQSLRDFLGgfafIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPT 458
Cdd:TIGR02142 84 ARLFPHLsvrGNLRygmkrarpseRRISFERVIELLG----IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 459 NHLDLEMRHALVMALQS----FDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:TIGR02142 160 AALDDPRKYEILPYLERlhaeFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAG 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
303-475 |
7.73e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.10 E-value: 7.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 303 AEPDALPNPLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVGYFAQ 382
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV-LGVPVPARAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 383 ---------HQLEALDLQASPVTHLQ------RLNPQASEQSLRDFLGgFAFIGDKALDPVAPFSGGEKARLVLAMLVYQ 447
Cdd:PRK13536 111 lararigvvPQFDNLDLEFTVRENLLvfgryfGMSTREIEAVIPSLLE-FARLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180
....*....|....*....|....*...
gi 800951443 448 KPNLLLLDEPTNHLDLEMRHALVMALQS 475
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRS 217
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
304-505 |
9.84e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.52 E-value: 9.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 304 EPDALPNPLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHqglkvgyfaQH 383
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLD---------AQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 384 QLEALDLQ--ASPVTHLQRLNPQASEQSLRDF-----------LGGF------------AFIGDKALDP--VAPFSGGEK 436
Cdd:PRK10575 74 PLESWSSKafARKVAYLPQQLPAAEGMTVRELvaigrypwhgaLGRFgaadrekveeaiSLVGLKPLAHrlVDSLSGGER 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 800951443 437 ARLVLAMLVYQKPNLLLLDEPTNHLDLEMR---HALVMALQSFDGAMV-TVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQvdvLALVHRLSQERGLTViAVLHDINMAARYCDYLVALRGGEM 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
311-509 |
1.27e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.12 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 311 PLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF-----------HQGLKVGY 379
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagddvealsarAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 380 FAQHQLEALDLQASPVT------HLQRLNP------QASEQSLRDflGGFAFIGDKaldPVAPFSGGEKARLVLAMLVYQ 447
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVemgrtpHRSRFDTwtetdrAAVERAMER--TGVAQFADR---PVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 448 KPNLLLLDEPTNHLDLEmrHA-----LVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:PRK09536 157 ATPVLLLDEPTASLDIN--HQvrtleLVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
306-503 |
1.51e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.92 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 306 DALPNPLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF----------HQGL 375
Cdd:PRK13537 1 GPMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgepvpsrarHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 376 KVGYFAQhqLEALDLQASPVTHLQRLN-----PQASEQSLRDFLGGFAFIGDKALDPVAPFSGGEKARLVLAMLVYQKPN 450
Cdd:PRK13537 81 RVGVVPQ--FDNLDPDFTVRENLLVFGryfglSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 800951443 451 LLLLDEPTNHLDLEMRHALVMALQSFDGAMVTVSHDRHLLKNT---ADEFYLVDSG 503
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAerlCDRLCVIEEG 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-207 |
2.34e-15 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 76.28 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGEL-QLDAGNAKV----PKEWSIASVKQE--- 72
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLfgerRGGEDVWELRKRigl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 73 -TPALA------ITALEYVLQGnpdYYA---LRCQLkqaeqqgdgeTQAQVHQQLELMKGYSIEAKAGELLHGLgfsntq 142
Cdd:COG1119 83 vSPALQlrfprdETVLDVVLSG---FFDsigLYREP----------TDEQRERARELLELLGLAHLADRPFGTL------ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 800951443 143 idyavsdfSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG----TLVLISHDRE 207
Cdd:COG1119 144 --------SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegapTLVLVTHHVE 204
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-207 |
2.70e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.58 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 16 LLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSIASVKQET---PALAITALEYVLQGnpdyy 92
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSevpDSLPLTVRDLVAMG----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 93 alRCQLKQAEQQGDGETQAQVHQQLELMkgysieakagellhGL-GFSNTQIDyavsDFSGGWRMRLNLAQALIRDADLL 171
Cdd:NF040873 82 --RWARRGLWRRLTRDDRAAVDDALERV--------------GLaDLAGRQLG----ELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190
....*....|....*....|....*....|....*....
gi 800951443 172 LLDEPTNHLDLDAVYWLERFLRSYAG---TLVLISHDRE 207
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLE 180
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-204 |
3.39e-15 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 73.57 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 12 GPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNakvpkewsiasvkqetpalaITALEYVLQgNPDY 91
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGE--------------------ILIDGVDLR-DLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 92 YALRCQLkqaeqqgdgetqAQVHQQLELMKGySIeakAGELLhglgfsntqidyavsdfSGGWRMRLNLAQALIRDADLL 171
Cdd:cd03228 72 ESLRKNI------------AYVPQDPFLFSG-TI---RENIL-----------------SGGQRQRIAIARALLRDPPIL 118
|
170 180 190
....*....|....*....|....*....|....*
gi 800951443 172 LLDEPTNHLDLDAVYWLERFLRSYAG--TLVLISH 204
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKgkTVIVIAH 153
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
311-512 |
3.58e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.87 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 311 PLiALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDvffhqgLKVGyfaqhqlealdl 390
Cdd:PRK11247 12 PL-LLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE------LLAG------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 391 qASPVTHLQ----------RLNP-----------------QASEQSLRDFlgGFAfigDKALDPVAPFSGGEKARLVLAM 443
Cdd:PRK11247 73 -TAPLAEARedtrlmfqdaRLLPwkkvidnvglglkgqwrDAALQALAAV--GLA---DRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 800951443 444 LVYQKPNLLLLDEPTNHLD----LEMRHALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVrqfGYDL 512
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI---GLDL 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-203 |
3.86e-15 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 74.71 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDI----ELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPkewSIASVKQetPAL 76
Cdd:cd03266 1 MITADALtkrfRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVD---GFDVVKE--PAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 77 AITALEYVlqgnPDYYALRCQLKQAEqqgdgetQAQVHQQLELMKGYSIEAKAGELLHGLGFSNTqIDYAVSDFSGGWRM 156
Cdd:cd03266 76 ARRRLGFV----SDSTGLYDRLTARE-------NLEYFAGLYGLKGDELTARLEELADRLGMEEL-LDRRVGGFSTGMRQ 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 800951443 157 RLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSY--AGTLVLIS 203
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLraLGKCILFS 192
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
313-523 |
5.32e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.12 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHqGlKVGYFaqhqleaLDLQA 392
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN-G-RVSAL-------LELGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 393 SpvthlqrLNPqasEQSLRD--FLGG-------------------FAFIGDkALD-PVAPFSGGEKARLVLAMLVYQKPN 450
Cdd:COG1134 98 G-------FHP---ELTGREniYLNGrllglsrkeidekfdeiveFAELGD-FIDqPVKTYSSGMRARLAFAVATAVDPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 451 LLLLDEPTNHLDLEMRHALVMALQSF---DGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFGyD----LDAYYQWLTKAN 523
Cdd:COG1134 167 ILLVDEVLAVGDAAFQKKCLARIRELresGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDG-DpeevIAAYEALLAGRE 245
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
322-471 |
5.43e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.12 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVGYFAQHQLeALDL----QASPVT- 396
Cdd:COG4604 11 YGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLV-DGLDVATTPSREL-AKRLailrQENHINs 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 397 --------------HLQ-RLNP---QASEQSLRDF-LGGFAfigDKALDPVapfSGGEKARLVLAMLVYQKPNLLLLDEP 457
Cdd:COG4604 89 rltvrelvafgrfpYSKgRLTAedrEIIDEAIAYLdLEDLA---DRYLDEL---SGGQRQRAFIAMVLAQDTDYVLLDEP 162
|
170
....*....|....
gi 800951443 458 TNHLDleMRHALVM 471
Cdd:COG4604 163 LNNLD--MKHSVQM 174
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
323-493 |
9.52e-15 |
|
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: 73.60 E-value: 9.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAG-------DVFFHQGLKVGYFAQH------------ 383
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGtirvngqDVSDLRGRAIPYLRRKigvvfqdfrllp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 384 QLEALDLQASP--VTHLQRLNPQASEQSLRDFLGgfafIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHL 461
Cdd:cd03292 92 DRNVYENVAFAleVTGVPPREIRKRVPAALELVG----LSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
170 180 190
....*....|....*....|....*....|....*
gi 800951443 462 DLEMRHALVMALQSFDGAMVTV---SHDRHLLKNT 493
Cdd:cd03292 168 DPDTTWEIMNLLKKINKAGTTVvvaTHAKELVDTT 202
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
300-509 |
9.72e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.56 E-value: 9.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 300 FSFAEPDALPNPLIALDGAQAGYGDTT--ILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKV 377
Cdd:PRK11160 326 FPTTSTAAADQVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL-NGQPI 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 378 GYFAQHQLEAldlQASPVThlQRL--------------NPQASEQSLRDFLG--GFAFI--GDKALDpvA-------PFS 432
Cdd:PRK11160 405 ADYSEAALRQ---AISVVS--QRVhlfsatlrdnlllaAPNASDEALIEVLQqvGLEKLleDDKGLN--AwlgeggrQLS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 433 GGEKARLVLA-MLVYQKPnLLLLDEPTNHLDLEM-RHALVMALQSFDG-AMVTVSHDRHLLKNTaDEFYLVDSGEVRQFG 509
Cdd:PRK11160 478 GGEQRRLGIArALLHDAP-LLLLDEPTEGLDAETeRQILELLAEHAQNkTVLMITHRLTGLEQF-DRICVMDNGQIIEQG 555
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
326-505 |
1.06e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.86 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 326 TILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELapqAGDVFFHQGLKVGYFAqhqLEALDLQASPVTHLQRLN--- 402
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL---TGGGAPRGARVTGDVT---LNGEPLAAIDAPRLARLRavl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 403 PQASEQ----SLRDF--LGGF---------------------AFIGDKALD--PVAPFSGGEKARL----VLAML----- 444
Cdd:PRK13547 89 PQAAQPafafSAREIvlLGRYpharragalthrdgeiawqalALAGATALVgrDVTTLSGGELARVqfarVLAQLwpphd 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 445 VYQKPNLLLLDEPTNHLDLEMRHAL---VMAL-QSFDGAMVTVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:PRK13547 169 AAQPPRYLLLDEPTAALDLAHQHRLldtVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
326-505 |
1.14e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 74.72 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 326 TILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHqGLKVGYFAQHQLEAL--DLQ------------ 391
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR-GEPLAKLNRAQRKAFrrDIQmvfqdsisavnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 392 --------ASPVTHLQRLNPQASEQSLRDFLGGFAfIGDKALDPVAP-FSGGEKARLVLAMLVYQKPNLLLLDEPTNHLD 462
Cdd:PRK10419 105 rktvreiiREPLRHLLSLDKAERLARASEMLRAVD-LDDSVLDKRPPqLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 800951443 463 LeMRHALVMAL-----QSFDGAMVTVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:PRK10419 184 L-VLQAGVIRLlkklqQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
329-509 |
1.36e-14 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 73.10 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 329 HSIKLNL-VPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH---------------QGLKVGY-FAQHQL-EALDL 390
Cdd:cd03297 13 FTLKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsrkkinlppQQRKIGLvFQQYALfPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 391 QASPVTHLQRLNPQASEQSLRDFLGGFAfIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALV 470
Cdd:cd03297 93 RENLAFGLKRKRNREDRISVDELLDLLG-LDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 800951443 471 MAL----QSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:cd03297 172 PELkqikKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
17-212 |
1.43e-14 |
|
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: 73.19 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSIASVKQETP----ALAITALEYV---LQGNP 89
Cdd:TIGR02324 24 LKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEGAWVDLAQASPrevlEVRRKTIGYVsqfLRVIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 90 DYYALRCQLKQAEQQGDGETQAQvhqqlelmkgysieAKAGELLHGLGFSNTQIDYAVSDFSGGWRMRLNLAQALIRDAD 169
Cdd:TIGR02324 104 RVSALEVVAEPLLERGVPREAAR--------------ARARELLARLNIPERLWHLPPATFSGGEQQRVNIARGFIADYP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 800951443 170 LLLLDEPTNHLDL---DAVYWLERFLRSYAGTLVLISHDREFLDAV 212
Cdd:TIGR02324 170 ILLLDEPTASLDAanrQVVVELIAEAKARGAALIGIFHDEEVRELV 215
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
322-505 |
1.45e-14 |
|
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: 73.92 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF--------------HQGL------------ 375
Cdd:COG0411 14 FGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFdgrditglpphriaRLGIartfqnprlfpe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 376 -------KVGYFAQHqlealdlQASPVTHLQRL-NPQASEQSLR-------DFLGgfafIGDKALDPVAPFSGGEKARLV 440
Cdd:COG0411 94 ltvlenvLVAAHARL-------GRGLLAALLRLpRARREEREAReraeellERVG----LADRADEPAGNLSYGQQRRLE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 800951443 441 LAMLVYQKPNLLLLDEPTNHLDLEMRHALV---MALQSFDG-AMVTVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:COG0411 163 IARALATEPKLLLLDEPAAGLNPEETEELAeliRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
313-462 |
1.71e-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: 73.37 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGD-TTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF---------HQGL-----KV 377
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIdgtdinklkGKALrqlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 378 GY-FAQHQL-EALD-LQASPVTHLQRLNPqaseqsLRDFLGGF-------AF-------IGDKALDPVAPFSGGEKARLV 440
Cdd:cd03256 81 GMiFQQFNLiERLSvLENVLSGRLGRRST------WRSLFGLFpkeekqrALaalervgLLDKAYQRADQLSGGQQQRVA 154
|
170 180
....*....|....*....|..
gi 800951443 441 LAMLVYQKPNLLLLDEPTNHLD 462
Cdd:cd03256 155 IARALMQQPKLILADEPVASLD 176
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-207 |
1.78e-14 |
|
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: 72.94 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGN--------AKVPKEW-SIASVKQE 72
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEilidgrdvTGVPPERrNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 73 tPAL--AITALEYVLqgnpdyYALRCQLKQAEQQgdgetQAQVHQQLELMKgysIEAKAGELLHGLgfsntqidyavsdf 150
Cdd:cd03259 81 -YALfpHLTVAENIA------FGLKLRGVPKAEI-----RARVRELLELVG---LEGLLNRYPHEL-------------- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 800951443 151 SGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSY---AG-TLVLISHDRE 207
Cdd:cd03259 132 SGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELqreLGiTTIYVTHDQE 192
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
309-487 |
1.82e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 75.13 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 309 PNPLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQ----GLK-----VGY 379
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvtGLPpekrnVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 380 FAQHqlEALdlqaSPvtHL------------QRLNPQASEQSLRDFL-----GGFAfigDK---ALdpvapfSGGEKARL 439
Cdd:COG3842 82 VFQD--YAL----FP--HLtvaenvafglrmRGVPKAEIRARVAELLelvglEGLA---DRyphQL------SGGQQQRV 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 800951443 440 VLA-MLVYqKPNLLLLDEPTNHLDL----EMRHALVMALQSFDGAMVTVSHDR 487
Cdd:COG3842 145 ALArALAP-EPRVLLLDEPLSALDAklreEMREELRRLQRELGITFIYVTHDQ 196
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
324-491 |
2.50e-14 |
|
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: 71.03 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 324 DTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAqELAP-QAGDVFFHQGLKVGYFAQHqlealdlqaspvthlqrln 402
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALA-GLWPwGSGRIGMPEGEDLLFLPQR------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 403 PQASEQSLRDFLggfAFIGDKALdpvapfSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSFDGAMVT 482
Cdd:cd03223 73 PYLPLGTLREQL---IYPWDDVL------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVIS 143
|
....*....
gi 800951443 483 VSHDRHLLK 491
Cdd:cd03223 144 VGHRPSLWK 152
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
313-515 |
2.76e-14 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 72.76 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH---------QGLKVGYFAQH 383
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedatdvpvQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 384 ----------QLEALDLQASPVThlQRLNPQASEQSLRDFLG--GFAFIGDKAldPvAPFSGGEKARLVLAMLVYQKPNL 451
Cdd:cd03296 83 yalfrhmtvfDNVAFGLRVKPRS--ERPPEAEIRAKVHELLKlvQLDWLADRY--P-AQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 452 LLLDEPTNHLDLEMRHALVMALQSFDGAM----VTVSHDRHLLKNTADEFYLVDSGEVRQFGYDLDAY 515
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELhvttVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
323-503 |
3.15e-14 |
|
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: 72.47 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 GDTTI--LHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF-HQGLKV------------------GYFA 381
Cdd:COG4778 20 GGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrHDGGWVdlaqaspreilalrrrtiGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 382 QH-----QLEALDLQASPVTHLQRLNPQASEQSlRDFLGGFAFigDKALDPVAP--FSGGEKARLVLAMLVYQKPNLLLL 454
Cdd:COG4778 100 QFlrvipRVSALDVVAEPLLERGVDREEARARA-RELLARLNL--PERLWDLPPatFSGGEQQRVNIARGFIADPPLLLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 800951443 455 DEPTNHLDLEMRHA---LVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSG 503
Cdd:COG4778 177 DEPTASLDAANRAVvveLIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
282-509 |
3.95e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 75.59 E-value: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 282 ALERMEKL--APAHVDSPFDfsfAEPDALPNPLIALDGAQAGY-GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLL 358
Cdd:COG1132 310 SAERIFELldEPPEIPDPPG---AVPLPPVRGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 359 AQELAPQAGDVFFHqGLKVgyfAQHQLEALDLQASPVthLQ-------------RL-NPQASEQSLR---------DFLG 415
Cdd:COG1132 387 LRFYDPTSGRILID-GVDI---RDLTLESLRRQIGVV--PQdtflfsgtireniRYgRPDATDEEVEeaakaaqahEFIE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 416 GF-----AFIGDKALDpvapFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSF--DGAMVTVSHDRH 488
Cdd:COG1132 461 ALpdgydTVVGERGVN----LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLmkGRTTIVIAHRLS 536
|
250 260
....*....|....*....|.
gi 800951443 489 LLKNtADEFYLVDSGEVRQFG 509
Cdd:COG1132 537 TIRN-ADRILVLDDGRIVEQG 556
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
310-505 |
4.20e-14 |
|
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: 75.32 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 310 NPLIALDGAQAGY--GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQA---GDVFFH-----------Q 373
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDgrdllelsealR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 374 GLKVGYFAQHQLEALDlqasPVT---------HLQRLNPQASEQSLRDFLGgFAFIGDKALDPVAPFSGGEKARLVLAML 444
Cdd:COG1123 82 GRRIGMVFQDPMTQLN----PVTvgdqiaealENLGLSRAEARARVLELLE-AVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 445 VYQKPNLLLLDEPTNHLDLEMRH---ALVMALQSFDG-AMVTVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAeilDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
313-505 |
5.53e-14 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 71.41 E-value: 5.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHqGL--------------KVG 378
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIID-GLkltddkkninelrqKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 379 YFAQH-----QLEALD-LQASPVThLQRLNPQASEQSLRDFLG--GFAfigDKALDPVAPFSGGEKARLVLAMLVYQKPN 450
Cdd:cd03262 80 MVFQQfnlfpHLTVLEnITLAPIK-VKGMSKAEAEERALELLEkvGLA---DKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 451 LLLLDEPTNHLDLEMRHAL--VMALQSFDG-AMVTVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVldVMKDLAEEGmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
321-509 |
8.30e-14 |
|
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: 70.27 E-value: 8.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 321 GYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQA--GDVFFH------QGLK--VGYFAQH-----QL 385
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINgrpldkRSFRkiIGYVPQDdilhpTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 386 ---EALDLQAspvtHLQRLnpqaseqslrdflggfafigdkaldpvapfSGGEKARLVLAMLVYQKPNLLLLDEPTNHLD 462
Cdd:cd03213 98 tvrETLMFAA----KLRGL------------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 800951443 463 LEMRHALVMALQ--SFDG--AMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:cd03213 144 SSSALQVMSLLRrlADTGrtIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
319-505 |
1.06e-13 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 70.60 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 319 QAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF---------HQGL------KVGY-FAQ 382
Cdd:cd03255 11 GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdgtdisklsEKELaafrrrHIGFvFQS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 383 HQL----EALDLQASPVTHLQRLNPQASEQSLR--DFLGgfafIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDE 456
Cdd:cd03255 91 FNLlpdlTALENVELPLLLAGVPKKERRERAEEllERVG----LGDRLNHYPSELSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 800951443 457 PTNHLDLEMRHAlVMAL-----QSFDGAMVTVSHDRhLLKNTADEFYLVDSGEV 505
Cdd:cd03255 167 PTGNLDSETGKE-VMELlrelnKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
313-515 |
1.20e-13 |
|
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: 70.73 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH----QGL-----KVGYFAQH 383
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgkdiTNLpphkrPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 384 -----QLEALDLQASPVThLQRLNPQASEQSLRDFLGGFAFIGDKALDPvAPFSGGEKARLVLAMLVYQKPNLLLLDEPT 458
Cdd:cd03300 81 yalfpHLTVFENIAFGLR-LKKLPKAEIKERVAEALDLVQLEGYANRKP-SQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 800951443 459 NHLDLEMRHAL---VMALQSFDG-AMVTVSHDRHLLKNTADEFYLVDSGEVRQFGYDLDAY 515
Cdd:cd03300 159 GALDLKLRKDMqleLKRLQKELGiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
311-486 |
1.25e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.11 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 311 PLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGLKV------------- 377
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQlrdlyalseaerr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 378 -------GYFAQHQLEALDLQASP------------VTHLQRLNPQASeqslrDFLGGFAFIGDKALDPVAPFSGGEKAR 438
Cdd:PRK11701 85 rllrtewGFVHQHPRDGLRMQVSAggnigerlmavgARHYGDIRATAG-----DWLERVEIDAARIDDLPTTFSGGMQQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 439 LVLAMLVYQKPNLLLLDEPTNHLD-------LEMRHALVMALQSfdgAMVTVSHD 486
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDvsvqarlLDLLRGLVRELGL---AVVIVTHD 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
323-492 |
1.26e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 70.47 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF---------HQGL-----KVGY-FAQHQL-- 385
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVngqdlsrlkRREIpylrrRIGVvFQDFRLlp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 386 -----E--ALDLQAspvthlQRLNPQASEQSLRDFLG--GfafIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDE 456
Cdd:COG2884 93 drtvyEnvALPLRV------TGKSRKEIRRRVREVLDlvG---LSDKAKALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 800951443 457 PTNHLDLEMRHALVMALQSFDGAMVTV---SHDRHLLKN 492
Cdd:COG2884 164 PTGNLDPETSWEIMELLEEINRRGTTVliaTHDLELVDR 202
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
312-505 |
1.33e-13 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 70.99 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 312 LIALDGAQAGYG----DTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF-----HQGLKVGYFAQ 382
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgrpvTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 383 HQLEALDLQASpvthlqrLNPQaseQSLRDFLG------GFAFIG---DKALDPVA---------P--FSGGEKARLVLA 442
Cdd:COG1124 81 VQMVFQDPYAS-------LHPR---HTVDRILAeplrihGLPDREeriAELLEQVGlppsfldryPhqLSGGQRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 443 MLVYQKPNLLLLDEPTNHLDLEMRhALVMAL-----QSFDGAMVTVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQ-AEILNLlkdlrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-204 |
1.87e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 73.32 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIEL--LRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALL-------KGELQLDAGNAKvpkEWSIASVKQe 72
Cdd:PRK11160 339 LTLNNVSFtyPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLtrawdpqQGEILLNGQPIA---DYSEAALRQ- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 73 tpalAITALE---YVLQGnpdyyALRCQLKQAEQQGDGETQAQVHQQLELmkGYSIEAKAGeLLHGLGFSNTQIdyavsd 149
Cdd:PRK11160 415 ----AISVVSqrvHLFSA-----TLRDNLLLAAPNASDEALIEVLQQVGL--EKLLEDDKG-LNAWLGEGGRQL------ 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 800951443 150 fSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAvywlER----FLRSYAG--TLVLISH 204
Cdd:PRK11160 477 -SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET----ERqileLLAEHAQnkTVLMITH 532
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
17-181 |
2.46e-13 |
|
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: 69.46 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEwSIASvkqeTPALAITALEYVLQGNPDYYALrc 96
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY-SIRT----DRKAARQSLGYCPQFDALFDEL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 97 qlkqaeqqgdgeTqaqVHQQLELM---KGYS---IEAKAGELLHGLGFSntqiDYA---VSDFSGGWRMRLNLAQALIRD 167
Cdd:cd03263 91 ------------T---VREHLRFYarlKGLPkseIKEEVELLLRVLGLT----DKAnkrARTLSGGMKRKLSLAIALIGG 151
|
170
....*....|....
gi 800951443 168 ADLLLLDEPTNHLD 181
Cdd:cd03263 152 PSVLLLDEPTSGLD 165
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-205 |
2.62e-13 |
|
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: 72.78 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEwSIASVKQETPALAI------------TALEYV 84
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV-PVSSLDQDEVRRRVsvcaqdahlfdtTVRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 85 LQGNPD------YYALRcqlkqaeqqgdgetQAQVHQQLElmkgysieakagELLHGLgfsNTQIDYAVSDFSGGWRMRL 158
Cdd:TIGR02868 430 RLARPDatdeelWAALE--------------RVGLADWLR------------ALPDGL---DTVLGEGGARLSGGERQRL 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 800951443 159 NLAQALIRDADLLLLDEPTNHLDLD-AVYWLERFLRSYAG-TLVLISHD 205
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAEtADELLEDLLAALSGrTVVLITHH 529
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-205 |
2.71e-13 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 69.42 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDI----ELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEwsiaSVKQETPALA 77
Cdd:cd03293 1 LEVRNVsktyGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE----PVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 78 I-----------TALEYVLqgnpdyYALRCQLKqaeqqGDGETQAQVHQQLELMkgysieakagellhGL-GFSNtqidY 145
Cdd:cd03293 77 YvfqqdallpwlTVLDNVA------LGLELQGV-----PKAEARERAEELLELV--------------GLsGFEN----A 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 800951443 146 AVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD----LDAVYWLERFLRSYAGTLVLISHD 205
Cdd:cd03293 128 YPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDaltrEQLQEELLDIWRETGKTVLLVTHD 191
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
303-492 |
3.05e-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: 72.70 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 303 AEPDALPNPLIALDGAQAGYGDTT-ILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF---------- 371
Cdd:TIGR02857 312 APVTAAPASSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpladada 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 372 -HQGLKVGYFAQHqleALDLQASPVTHLQRLNPQASEQSLRDFL-------------GGFAF-IGDKAldpvAPFSGGEK 436
Cdd:TIGR02857 392 dSWRDQIAWVPQH---PFLFAGTIAENIRLARPDASDAEIREALeragldefvaalpQGLDTpIGEGG----AGLSGGQA 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 437 ARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSF-DGAMV-TVSHDRHLLKN 492
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaQGRTVlLVTHRLALAAL 522
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
313-509 |
3.70e-13 |
|
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: 69.13 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLA-----QELAPQAGDVFFhqGLKVGYFAQHQLEA 387
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrlndlIPGAPDEGEVLL--DGKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 388 LDLQASPVthLQRLNP-------------------------QASEQSLRDflggfAFIGDKALDPVAPF--SGGEKARLV 440
Cdd:cd03260 79 LRRRVGMV--FQKPNPfpgsiydnvayglrlhgiklkeeldERVEEALRK-----AALWDEVKDRLHALglSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800951443 441 LAMLVYQKPNLLLLDEPTNHLDLEMRHA---LVMALQSfDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKieeLIAELKK-EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
337-490 |
4.06e-13 |
|
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: 67.01 E-value: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 337 PGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhqglkvgyfaqhqlealdlqaspvthlqrLNPQASEQSLRDFLGG 416
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------------------IDGEDILEEVLDQLLL 51
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 800951443 417 FAFIGDKaldpvAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSFDGAMVTVSHDRHLL 490
Cdd:smart00382 52 IIVGGKK-----ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
327-495 |
5.99e-13 |
|
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: 68.57 E-value: 5.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 327 ILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF-HQG------------------LKVGYFAQH---- 383
Cdd:TIGR02324 23 VLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVrHEGawvdlaqasprevlevrrKTIGYVSQFlrvi 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 384 -QLEALDLQASPVthLQR-LNPQASEQSLRDFLGGFAFigDKALDPVAP--FSGGEKARLVLAMLVYQKPNLLLLDEPTN 459
Cdd:TIGR02324 103 pRVSALEVVAEPL--LERgVPREAARARARELLARLNI--PERLWHLPPatFSGGEQQRVNIARGFIADYPILLLDEPTA 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 800951443 460 HLDLEMRHALVMALQSFDG---AMVTVSHDRHLLKNTAD 495
Cdd:TIGR02324 179 SLDAANRQVVVELIAEAKArgaALIGIFHDEEVRELVAD 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
313-532 |
6.59e-13 |
|
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: 71.37 E-value: 6.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLL--AQELAPQAGDVFFHQGL--KVGYF-------- 380
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHVALceKCGYVerpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 381 ------AQHQLEALDL--QASPVTH---------LQRLNPQASEQSLRD----FLGGFAFIGDKALDPVAPF-------- 431
Cdd:TIGR03269 81 pcpvcgGTLEPEEVDFwnLSDKLRRrirkriaimLQRTFALYGDDTVLDnvleALEEIGYEGKEAVGRAVDLiemvqlsh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 432 ---------SGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLE----MRHALVMALQSFDGAMVTVSHDRHLLKNTADEFY 498
Cdd:TIGR03269 161 rithiardlSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtaklVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270
....*....|....*....|....*....|....
gi 800951443 499 LVDSGEVRQFGYDLDAYYQWLTKANQEQKQTQVE 532
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVE 274
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
310-487 |
7.28e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.20 E-value: 7.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 310 NPLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQG------------LKV 377
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLF-EGedistlkpeiyrQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 378 GYFAqhQLEAL------DLQASPvthLQRLNPQASEQSLRDFLGGFAFIGDKALDPVAPFSGGEKARLVLAMLVYQKPNL 451
Cdd:PRK10247 84 SYCA--QTPTLfgdtvyDNLIFP---WQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 800951443 452 LLLDEPTNHLDL-------EMRHALVMALQSfdgAMVTVSHDR 487
Cdd:PRK10247 159 LLLDEITSALDEsnkhnvnEIIHRYVREQNI---AVLWVTHDK 198
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
321-463 |
7.30e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.24 E-value: 7.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 321 GYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF-----------HQGLKVGYFAQHQLEALD 389
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdgehiqhyaskEVARRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 390 LQASPV------------THLQRLNPQASEQSLRDflggfAFIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEP 457
Cdd:PRK10253 96 ITVQELvargryphqplfTRWRKEDEEAVTKAMQA-----TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
....*.
gi 800951443 458 TNHLDL 463
Cdd:PRK10253 171 TTWLDI 176
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
310-491 |
9.13e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 68.15 E-value: 9.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 310 NPLIALDGA----QAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH----QGL------ 375
Cdd:COG1136 2 SPLLELRNLtksyGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgqdiSSLserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 376 -----KVGY-FAQHQL-------E--ALDLQASPVTHLQRlNPQASEqsLRDFLGgfafIGDKALDPVAPFSGGEKARLV 440
Cdd:COG1136 82 rlrrrHIGFvFQFFNLlpeltalEnvALPLLLAGVSRKER-RERARE--LLERVG----LGDRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 800951443 441 LAMLVYQKPNLLLLDEPTNHLDLEMRHAlVMAL-----QSFDGAMVTVSHDRHLLK 491
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEE-VLELlrelnRELGTTIVMVTHDPELAA 209
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-181 |
1.18e-12 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 67.22 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATlFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGN-----AKVPKEWS-----IASVKQ 71
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLT-LGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTiridgQDVLKQPQklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 72 E-TPALAITALEYVlqgnpDYYALrcqLKqaeqqgdGETQAQVHQQLELMKgysieakagELLHGLGFSNTqidyAVSDF 150
Cdd:cd03264 80 EfGVYPNFTVREFL-----DYIAW---LK-------GIPSKEVKARVDEVL---------ELVNLGDRAKK----KIGSL 131
|
170 180 190
....*....|....*....|....*....|.
gi 800951443 151 SGGWRMRLNLAQALIRDADLLLLDEPTNHLD 181
Cdd:cd03264 132 SGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-224 |
1.51e-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: 67.53 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEwSIASVKQEtpalaital 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGE-DISGLSEA--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 82 eyvlqgnpDYYALRCQLKQAEQQG---DGETQAQ-----VHQQLELMKGySIEAKAGELLHGLGFSNTQiDYAVSDFSGG 153
Cdd:cd03261 71 --------ELYRLRRRMGMLFQSGalfDSLTVFEnvafpLREHTRLSEE-EIREIVLEKLEAVGLRGAE-DLYPAELSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 154 WRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAGTL----VLISHDREFLDAVVGEIWHIDQQQI 224
Cdd:cd03261 141 MKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELgltsIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
323-505 |
1.58e-12 |
|
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: 66.78 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLA--QELAPQAGDVFFhqglkvgyfaqhqlEALDLQASPVTHLQR 400
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILF--------------KGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 401 ----LNPQASEQ----SLRDFLggfAFIGDKaldpvapFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLD---LEMRHAL 469
Cdd:cd03217 77 lgifLAFQYPPEipgvKNADFL---RYVNEG-------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDidaLRLVAEV 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 800951443 470 VMALQSFDGAMVTVSHDRHLLK-NTADEFYLVDSGEV 505
Cdd:cd03217 147 INKLREEGKSVLIITHYQRLLDyIKPDRVHVLYDGRI 183
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
330-509 |
1.78e-12 |
|
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: 67.43 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 330 SIKLNLVPGS-----RIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVGYFAQhQLEAldlqaspvthlqrlnpq 404
Cdd:cd03237 12 EFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQ-YIKA----------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 405 ASEQSLRDFL-------GGFAFIGDKALDP----------VAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRH 467
Cdd:cd03237 73 DYEGTVRDLLssitkdfYTHPYFKTEIAKPlqieqildreVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 800951443 468 ALVMALQSF-----DGAMVtVSHDRHLLKNTADEFyLVDSGEVRQFG 509
Cdd:cd03237 153 MASKVIRRFaenneKTAFV-VEHDIIMIDYLADRL-IVFEGEPSVNG 197
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
313-509 |
1.84e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 67.09 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTTIlhSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVGYFAQHQlealdlqa 392
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW-NGQDLTALPPAE-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 393 SPVT----------HLQ-------------RLNPQASEQsLRDFLG--GFAFIGDK---ALdpvapfSGGEKARLVLA-M 443
Cdd:COG3840 71 RPVSmlfqennlfpHLTvaqniglglrpglKLTAEQRAQ-VEQALErvGLAGLLDRlpgQL------SGGQRQRVALArC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 800951443 444 LVYQKPnLLLLDEPTNHLDLEMRH---ALVMALQSFDGAMV-TVSHD----RHLlkntADEFYLVDSGEVRQFG 509
Cdd:COG3840 144 LVRKRP-ILLLDEPFSALDPALRQemlDLVDELCRERGLTVlMVTHDpedaARI----ADRVLLVADGRIAADG 212
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
311-458 |
1.97e-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: 67.31 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 311 PLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVGYFAQHQLEALDL 390
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRF-DGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 391 QASPvthlQ--RLNPQAS-EQSLRdfLGGFAFIGDKALDPVAPF-------------------SGGEKARLVLAM-LVyQ 447
Cdd:COG0410 81 GYVP----EgrRIFPSLTvEENLL--LGAYARRDRAEVRADLERvyelfprlkerrrqragtlSGGEQQMLAIGRaLM-S 153
|
170
....*....|.
gi 800951443 448 KPNLLLLDEPT 458
Cdd:COG0410 154 RPKLLLLDEPS 164
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
313-509 |
2.09e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.96 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH---------QGLKVGYFAQH 383
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgtdvsrlhaRDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 384 -----QLEALDLQASPVTHL---QRLNPQASEQSLRDFLG--GFAFIGDKAldPvAPFSGGEKARLVLAMLVYQKPNLLL 453
Cdd:PRK10851 83 yalfrHMTVFDNIAFGLTVLprrERPNAAAIKAKVTQLLEmvQLAHLADRY--P-AQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 454 LDEPTNHLDLEMRHALVMAL----QSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
337-505 |
2.32e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.17 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 337 PGSRIALLGRNGAGKSTLIKLLAQeLAPQAGDVFF-----------HQGLKVGYFAQHQLEALDLqasPV-----THLQR 400
Cdd:COG4138 21 AGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLngrplsdwsaaELARHRAYLSQQQSPPFAM---PVfqylaLHQPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 401 LNPQASEQSLRDFLGGFAFIGDKALDPVAPFSGGEKARLVLAMLVYQ-------KPNLLLLDEPTNHLDLEMRHALVMAL 473
Cdd:COG4138 97 GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRLL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 800951443 474 QSFDGAMVTV---SHD-----RHllkntADEFYLVDSGEV 505
Cdd:COG4138 177 RELCQQGITVvmsSHDlnhtlRH-----ADRVWLLKQGKL 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-205 |
2.55e-12 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 66.82 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALL------------KGELQLDAGNAKVPKEW----- 64
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndlipgapdEGEVLLDGKDIYDLDVDvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 65 -SIASVKQETPALAITALEYVLqgnpdyYALRCQLKQaeqqGDGETQAQVHQQLELMkgySIEAKAGELLHGLGFSntqi 143
Cdd:cd03260 81 rRVGMVFQKPNPFPGSIYDNVA------YGLRLHGIK----LKEELDERVEEALRKA---ALWDEVKDRLHALGLS---- 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 800951443 144 dyavsdfsGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG--TLVLISHD 205
Cdd:cd03260 144 --------GGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
11-205 |
3.09e-12 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 66.38 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 11 RGPKCLLKNANATLFPQHKVGLVGSNGCGKSSL-FALLK------GELQLDAGN-AKVPKEW------SIASVKQEtpal 76
Cdd:cd03257 15 GGSVKALDDVSFSIKKGETLGLVGESGSGKSTLaRAILGllkptsGSIIFDGKDlLKLSRRLrkirrkEIQMVFQD---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 77 AITALeyvlqgNPdYYALRCQLKQAeqqgdgetqAQVHQQLElmKGYSIEAKAGELLHGLGFSNTQIDYAVSDFSGGWRM 156
Cdd:cd03257 91 PMSSL------NP-RMTIGEQIAEP---------LRIHGKLS--KKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 800951443 157 RLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLR----SYAGTLVLISHD 205
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKklqeELGLTLLFITHD 205
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
321-519 |
3.76e-12 |
|
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: 66.49 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 321 GYGDTT--ILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVGYFAQHQLEALDLQASPVTHL 398
Cdd:cd03251 9 RYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILI-DGHDVRDYTLASLRRQIGLVSQDVFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 399 ----QRLN-----PQASEQSLR---------DFLGGF-----AFIGDKALDpvapFSGGEKARLVLAMLVYQKPNLLLLD 455
Cdd:cd03251 88 fndtVAENiaygrPGATREEVEeaaraanahEFIMELpegydTVIGERGVK----LSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 800951443 456 EPTNHLDLEMRHALVMALQSF--DGAMVTVSHDRHLLKNtADEFYLVDSGEVRQFG-----YDLDAYYQWL 519
Cdd:cd03251 164 EATSALDTESERLVQAALERLmkNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGtheelLAQGGVYAKL 233
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
307-509 |
3.77e-12 |
|
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: 69.01 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 307 ALPNP--LIALDGAQAGY--GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF-----HQ---- 373
Cdd:COG4618 323 PLPRPkgRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLdgadlSQwdre 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 374 --GLKVGYFAQH-QL---------------------EALdlQASPVTHL-QRLnPQASEQSLRDflGGfafigdkaldpv 428
Cdd:COG4618 403 elGRHIGYLPQDvELfdgtiaeniarfgdadpekvvAAA--KLAGVHEMiLRL-PDGYDTRIGE--GG------------ 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 429 APFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSF--DGA-MVTVSHDRHLLkNTADEFYLVDSGEV 505
Cdd:COG4618 466 ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkaRGAtVVVITHRPSLL-AAVDKLLVLRDGRV 544
|
....
gi 800951443 506 RQFG 509
Cdd:COG4618 545 QAFG 548
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
322-509 |
3.91e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.95 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVGYfAQHQLEALDLQASPVThlqrl 401
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLW-QGKPLDY-SKRGLLALRQQVATVF----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 402 npQASEQ-------------SLRDFLGGFAFIG---DKAL----------DPVAPFSGGEKARLVLAMLVYQKPNLLLLD 455
Cdd:PRK13638 84 --QDPEQqifytdidsdiafSLRNLGVPEAEITrrvDEALtlvdaqhfrhQPIQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 456 EPTNHLDLEMRHALVMALQSFDGA---MVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
313-509 |
3.98e-12 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 66.36 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYG--DTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVF---FHQGL--------KVGY 379
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLvdgHDLALadpawlrrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 380 FAQHQL-------EALDLqASPVTHLQRLNPQASEQSLRDF-----LGGFAFIGDKAldpvAPFSGGEKARLVLAMLVYQ 447
Cdd:cd03252 81 VLQENVlfnrsirDNIAL-ADPGMSMERVIEAAKLAGAHDFiselpEGYDTIVGEQG----AGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 800951443 448 KPNLLLLDEPTNHLDLEMRHALVMALQSF-DGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDIcAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQG 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
313-486 |
4.24e-12 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 65.96 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGD----TTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH------QGLKVGY-FA 381
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDgepvtgPGPDRGYvFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 382 QHQL---------EALDLQASPVTHLQRLnpQASEQSLRDF-LGGFAfigDK---ALdpvapfSGGEKARLVLAMLVYQK 448
Cdd:cd03293 81 QDALlpwltvldnVALGLELQGVPKAEAR--ERAEELLELVgLSGFE---NAyphQL------SGGMRQRVALARALAVD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 800951443 449 PNLLLLDEPTNHLD----LEMRHALVMALQSFDGAMVTVSHD 486
Cdd:cd03293 150 PDVLLLDEPFSALDaltrEQLQEELLDIWRETGKTVLLVTHD 191
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
17-204 |
4.35e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 69.04 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGN--------AKVPKEW---SIASVKQETPALAITALEYVL 85
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRilidgvdiRDLTLESlrrQIGVVPQDTFLFSGTIRENIR 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 86 QGNPDYyalrcqlkqaeqqgdgeTQAQVHQQLELmkgysieAKAGELLHGL--GFsNTQIDYAVSDFSGGWRMRLNLAQA 163
Cdd:COG1132 436 YGRPDA-----------------TDEEVEEAAKA-------AQAHEFIEALpdGY-DTVVGERGVNLSGGQRQRIAIARA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 800951443 164 LIRDADLLLLDEPTNHLD-------LDAvywLERFLRSYagTLVLISH 204
Cdd:COG1132 491 LLKDPPILILDEATSALDtetealiQEA---LERLMKGR--TTIVIAH 533
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-207 |
6.80e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 67.09 E-value: 6.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAG----NAKV------PKEWSIASVKQ 71
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGrivlNGRDlftnlpPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 72 EtPAL--AITALEYVLQGnpdyyaLRCQlkqaeQQGDGETQAQVHQQLELMKgysieakagelLHGLGfsntqiDYAVSD 149
Cdd:COG1118 83 H-YALfpHMTVAENIAFG------LRVR-----PPSKAEIRARVEELLELVQ-----------LEGLA------DRYPSQ 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 150 FSGGWRMRLNLAQALIRDADLLLLDEPTNHLDldaVY-------WLERFLRSYAGTLVLISHDRE 207
Cdd:COG1118 134 LSGGQRQRVALARALAVEPEVLLLDEPFGALD---AKvrkelrrWLRRLHDELGGTTVFVTHDQE 195
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-204 |
1.01e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.78 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGN-----AKVPKEWSIASVK-QETPA 75
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKitvlgVPVPARARLARARiGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 76 LAITALEYVLQGNPDYYALRCQLKQAeqqgdgETQAQVHQQLELMKgysIEAKAgellhglgfsntqiDYAVSDFSGGWR 155
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGMSTR------EIEAVIPSLLEFAR---LESKA--------------DARVSDLSGGMK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 800951443 156 MRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSY---AGTLVLISH 204
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLlarGKTILLTTH 230
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-212 |
1.03e-11 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 64.92 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKewsiASVKQETPALAITALEYVLQGNPDYYA-LR 95
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG----TDIRQLDPADLRRNIGYVPQDVTLFYGtLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 96 CQLKQAEQQGDGEtqaqvhqqlELMKGYSIeAKAGELL--HGLGFsNTQIDYAVSDFSGGWRMRLNLAQALIRDADLLLL 173
Cdd:cd03245 96 DNITLGAPLADDE---------RILRAAEL-AGVTDFVnkHPNGL-DLQIGERGRGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 800951443 174 DEPTNHLDLDAVYWLERFLRSYAG--TLVLISHDREFLDAV 212
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLDLV 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-212 |
1.09e-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: 63.75 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNakvpkewsiasvkqetpalaital 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGS------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 82 eyVLQGNPDYYALRCQLKQAEQQgdgetQAQVHQQLELMKGYSIEAKAGELLhglgfsntqidyavsdfSGGWRMRLNLA 161
Cdd:cd03229 57 --ILIDGEDLTDLEDELPPLRRR-----IGMVFQDFALFPHLTVLENIALGL-----------------SGGQQQRVALA 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 162 QALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG----TLVLISHDREFLDAV 212
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqlgiTVVLVTHDLDEAARL 167
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
318-490 |
1.10e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.90 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 318 AQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF--HQ--GLK----------VGYFAQH 383
Cdd:PRK10908 8 SKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsgHDitRLKnrevpflrrqIGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 384 QLEALDLQASPVTHLQRLNPQASEQSLR-------DFLGgfafIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDE 456
Cdd:PRK10908 88 HHLLMDRTVYDNVAIPLIIAGASGDDIRrrvsaalDKVG----LLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 800951443 457 PTNHLDLEMRHALVMALQSFDGAMVTV---SHDRHLL 490
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNRVGVTVlmaTHDIGLI 200
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
10-212 |
2.02e-11 |
|
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: 63.99 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 10 LRGPKCL--LKNANATLFPQHKVGLVGSNGCGKSSLfalLK----------GELQLDAGNAKV------PKEwsIASVKQ 71
Cdd:COG4778 18 LQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTL---LKciygnylpdsGSILVRHDGGWVdlaqasPRE--ILALRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 72 ET-----------PAlaITALEYVLQgnpdyyALRcqlkqaeQQGDGETQAqvhqqlelmkgysiEAKAGELLHGLGFSN 140
Cdd:COG4778 93 RTigyvsqflrviPR--VSALDVVAE------PLL-------ERGVDREEA--------------RARARELLARLNLPE 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 800951443 141 TQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDL---DAVYWLERFLRSyAGT-LVLISHDREFLDAV 212
Cdd:COG4778 144 RLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAanrAVVVELIEEAKA-RGTaIIGIFHDEEVREAV 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-509 |
2.06e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 64.68 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 324 DTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELapQAGDVFFHQGLKVGYFAQH--QLEALDL---------QA 392
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLI--EIYDSKIKVDGKVLYFGKDifQIDAIKLrkevgmvfqQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 393 SPVTHL-----------------QRLNPQASEQSLRDfLGGFAFIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLD 455
Cdd:PRK14246 100 NPFPHLsiydniayplkshgikeKREIKKIVEECLRK-VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 456 EPTNHLDLEMRHA---LVMALQSfDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:PRK14246 179 EPTSMIDIVNSQAiekLITELKN-EIAIVIVSHNPQQVARVADYVAFLYNGELVEWG 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-509 |
2.07e-11 |
|
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: 66.75 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKG--ELQLDAGN-----AKVPK-EWSIASVKQET 73
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRiiyhvALCEKcGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 74 P------ALAITALEYVLQGNPDYYALRCQLKQAEQQ-----GDGETQAQVHQQLELMkGYSIEA---KAGELLHGLGFS 139
Cdd:TIGR03269 81 PcpvcggTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRtfalyGDDTVLDNVLEALEEI-GYEGKEavgRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 140 NtQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD---LDAVY-WLERFLRSYAGTLVLISHDREFLDAVVGE 215
Cdd:TIGR03269 160 H-RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKLVHnALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 216 -IWhIDQQQInvykgnysqferqkaerlaqqqaqfdkqqEQIAHLEKFITRFKAKaskakqaqsrVKALERMEKLApahv 294
Cdd:TIGR03269 239 aIW-LENGEI-----------------------------KEEGTPDEVVAVFMEG----------VSEVEKECEVE---- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 295 dspfdfsfaepdaLPNPLIALDGAQAGY-----GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDV 369
Cdd:TIGR03269 275 -------------VGEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 370 FFHQG------LKVGYF----AQHQLEALDLQASPVTH---LQRLNPQASEQSLRDF--------LGGFAFIGDKALD-- 426
Cdd:TIGR03269 342 NVRVGdewvdmTKPGPDgrgrAKRYIGILHQEYDLYPHrtvLDNLTEAIGLELPDELarmkavitLKMVGFDEEKAEEil 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 427 PVAP--FSGGEKARLVLAMLVYQKPNLLLLDEPTNHLD----LEMRHALVMALQSFDGAMVTVSHDRHLLKNTADEFYLV 500
Cdd:TIGR03269 422 DKYPdeLSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM 501
|
....*....
gi 800951443 501 DSGEVRQFG 509
Cdd:TIGR03269 502 RDGKIVKIG 510
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
323-462 |
2.19e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.74 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGlkvgyfAQHqLEALDLQASPVTHLQRLN 402
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG------DID-DPDVAEACHYLGHRNAMK 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 403 PQAS-EQSL---RDFLGGF-----AFIGDKALDPVA--PF---SGGEKARLVLA-MLVYQKPnLLLLDEPTNHLD 462
Cdd:PRK13539 86 PALTvAENLefwAAFLGGEeldiaAALEAVGLAPLAhlPFgylSAGQKRRVALArLLVSNRP-IWILDEPTAALD 159
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-181 |
2.85e-11 |
|
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: 63.71 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALL-------KGELQLDAGNAK--VPKEW--SIASVKQEtPAL-AITALEYV 84
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEILLDGVDIRdlNLRWLrsQIGLVSQE-PVLfDGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 85 LQGNPDyyalrcqlKQAEQQGDGETQAQVHQQLE-LMKGYSIEakagellhgLGFSNTQIdyavsdfSGGWRMRLNLAQA 163
Cdd:cd03249 98 RYGKPD--------ATDEEVEEAAKKANIHDFIMsLPDGYDTL---------VGERGSQL-------SGGQKQRIAIARA 153
|
170
....*....|....*...
gi 800951443 164 LIRDADLLLLDEPTNHLD 181
Cdd:cd03249 154 LLRNPKILLLDEATSALD 171
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-205 |
3.23e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.88 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLfPQHKV-GLVGSNGCGKSSL---FA-LLK---GELQLD--AGNAKVPKEWS--IAS 68
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSL-PTGKItALIGPNGCGKSTLlkcFArLLTpqsGTVFLGdkPISMLSSRQLArrLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 69 VKQE--TPAlAITALEYVLQGNPDYYALRCQLKQAEQQgdgetqaQVHQQLELMKgysIEAKAgellhglgfsntqiDYA 146
Cdd:PRK11231 81 LPQHhlTPE-GITVRELVAYGRSPWLSLWGRLSAEDNA-------RVNQAMEQTR---INHLA--------------DRR 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800951443 147 VSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLR--SYAG-TLVLISHD 205
Cdd:PRK11231 136 LTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRelNTQGkTVVTVLHD 197
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
30-205 |
3.24e-11 |
|
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: 63.51 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 30 VGLVGSNGCGKSSLFALLKGELQLDAGNAKV----PKEWSIASVKQETPALAI-TALEYVLqgnP--DYYALrcqLKQAE 102
Cdd:cd03267 50 VGFIGPNGAGKTTTLKILSGLLQPTSGEVRVaglvPWKRRKKFLRRIGVVFGQkTQLWWDL---PviDSFYL---LAAIY 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 103 QQGDGETQAQVHQQLELMKgysieakAGELLhglgfsntqiDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDL 182
Cdd:cd03267 124 DLPPARFKKRLDELSELLD-------LEELL----------DTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180
....*....|....*....|....*..
gi 800951443 183 DAVYWLERFLRSY----AGTLVLISHD 205
Cdd:cd03267 187 VAQENIRNFLKEYnrerGTTVLLTSHY 213
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
289-505 |
3.52e-11 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 63.26 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 289 LAPAHVDSPFDF---SFAEPDalpNPlialdgaqagygDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQ 365
Cdd:cd03248 3 LAPDHLKGIVKFqnvTFAYPT---RP------------DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 366 AGDVFF---------HQGL--KVGYFAQH-QLEALDLQAS-----PVTHLQRLNPQASEQSLRDFLGGFAF-----IGDK 423
Cdd:cd03248 68 GGQVLLdgkpisqyeHKYLhsKVSLVGQEpVLFARSLQDNiayglQSCSFECVKEAAQKAHAHSFISELASgydteVGEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 424 AldpvAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSfDGAMVTVSHDRHLLKNT--ADEFYLVD 501
Cdd:cd03248 148 G----SQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVerADQILVLD 222
|
....
gi 800951443 502 SGEV 505
Cdd:cd03248 223 GGRI 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
324-517 |
3.63e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 66.28 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 324 DTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDV-------------FFHQglKVGYFAQHQLE---- 386
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlldgvplvqydhhYLHR--QVALVGQEPVLfsgs 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 387 -----ALDLQASPVTHLQRLnpqASEQSLRDFLGGFAFIGDKALDPVAPF-SGGEKARLVLAMLVYQKPNLLLLDEPTNH 460
Cdd:TIGR00958 571 vreniAYGLTDTPDEEIMAA---AKAANAHDFIMEFPNGYDTEVGEKGSQlSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 800951443 461 LDLEMRHALVMALQSFDGAMVTVSHDRHLLKNtADEFYLVDSGEVRQFGY------DLDAYYQ 517
Cdd:TIGR00958 648 LDAECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGThkqlmeDQGCYKH 709
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
322-505 |
3.74e-11 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 63.47 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH-------------QGLKVGYFAQH----- 383
Cdd:COG1126 11 FGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDgedltdskkdinkLRRKVGMVFQQfnlfp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 384 QLEALD-LQASPVTHLQRLNPQASEQSLR--DFLGgfafIGDKA------LdpvapfSGGEK-----ARlVLAMlvyqKP 449
Cdd:COG1126 91 HLTVLEnVTLAPIKVKKMSKAEAEERAMEllERVG----LADKAdaypaqL------SGGQQqrvaiAR-ALAM----EP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 800951443 450 NLLLLDEPTNHLDLEMRHAL--VMALQSFDG-AMVTVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVldVMRDLAKEGmTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
319-491 |
3.99e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.30 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 319 QAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH-QGL--------------KVGYFAQ- 382
Cdd:PRK11629 16 QEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgQPMsklssaakaelrnqKLGFIYQf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 383 HQL----EALDLQASPVThLQRLNPQASEQSLRDFLGGFAfIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPT 458
Cdd:PRK11629 96 HHLlpdfTALENVAMPLL-IGKKKPAEINSRALEMLAAVG-LEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 800951443 459 NHLDLEMRHALVMALQSFD----GAMVTVSHDRHLLK 491
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNrlqgTAFLVVTHDLQLAK 210
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-181 |
4.21e-11 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 63.40 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALL-------KGELQLDAGNAK-VPKEW---SIASVKQETPALAITALEYVL 85
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLmrfydpqKGQILIDGIDIRdISRKSlrsMIGVVLQDTFLFSGTIMENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 86 QGNPDyyalrcqlKQAEQQGDGETQAQVHQQLE-LMKGYsieakagellhglgfsNTQIDYAVSDFSGGWRMRLNLAQAL 164
Cdd:cd03254 99 LGRPN--------ATDEEVIEAAKEAGAHDFIMkLPNGY----------------DTVLGENGGNLSQGERQLLAIARAM 154
|
170
....*....|....*..
gi 800951443 165 IRDADLLLLDEPTNHLD 181
Cdd:cd03254 155 LRDPKILILDEATSNID 171
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-203 |
5.08e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.58 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEwsiasvKQETPALAiTA 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG------DIDDPDVA-EA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 81 LEYVlqGNPDyyALRCQLKQAE-----QQGDGETQAQVHQQLELMKGYSIE-AKAGELlhglgfsntqidyavsdfSGGW 154
Cdd:PRK13539 75 CHYL--GHRN--AMKPALTVAEnlefwAAFLGGEELDIAAALEAVGLAPLAhLPFGYL------------------SAGQ 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 800951443 155 RMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSY--AGTLVLIS 203
Cdd:PRK13539 133 KRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHlaQGGIVIAA 183
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
17-208 |
5.47e-11 |
|
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: 62.51 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKV---------PKEWS------IASVKQET---PALai 78
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdgtdisklsEKELAafrrrhIGFVFQSFnllPDL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 79 TALEYVlqgnpdyyALRCQLKQaeqqgdgetqaqvhqqlelMKGYSIEAKAGELLHGLGFSNtQIDYAVSDFSGGWRMRL 158
Cdd:cd03255 98 TALENV--------ELPLLLAG-------------------VPKKERRERAEELLERVGLGD-RLNHYPSELSGGQQQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 800951443 159 NLAQALIRDADLLLLDEPTNHLDLD---AVYWLERFLRSYAG-TLVLISHDREF 208
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSEtgkEVMELLRELNKEAGtTIVVVTHDPEL 203
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-204 |
8.11e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 65.13 E-value: 8.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLK-------GELQLDAgnakVP-KEWS-------IASVKQETPALAITAL 81
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQnlyqptgGQVLLDG----VPlVQYDhhylhrqVALVGQEPVLFSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 82 EYVLQGnpdyyalrCQLKQAEQQGDGETQAQVHQQL-ELMKGYsieakagellhglgfsNTQIDYAVSDFSGGWRMRLNL 160
Cdd:TIGR00958 573 ENIAYG--------LTDTPDEEIMAAAKAANAHDFImEFPNGY----------------DTEVGEKGSQLSGGQKQRIAI 628
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 800951443 161 AQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAGTLVLISH 204
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
324-489 |
8.66e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 64.83 E-value: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 324 DTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQeLAPQA-GDVFFHQGLKV------GYFAQHQL-EALDLQASPv 395
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYGsGRIARPAGARVlflpqrPYLPLGTLrEALLYPATA- 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 396 thlQRLNPQASEQSLRDF-LGGFAfigdKALDPVAP----FSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALV 470
Cdd:COG4178 453 ---EAFSDAELREALEAVgLGHLA----ERLDEEADwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY 525
|
170 180
....*....|....*....|....*....
gi 800951443 471 MALQS--FDGAMVTVSH--------DRHL 489
Cdd:COG4178 526 QLLREelPGTTVISVGHrstlaafhDRVL 554
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-204 |
9.12e-11 |
|
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: 62.25 E-value: 9.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 16 LLKNANATLFPQHKVGLVGSNGCGKSSLFALL-------KGELQLDAGNAKVPKEWS----IASVKQETPALAITALEYV 84
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvsSGSILIDGQDIREVTLDSlrraIGVVPQDTVLFNDTIGYNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 85 LQGNPDyyalrcqlKQAEQQGDGETQAQVHQQLELM-KGYsiEAKAGEllHGLgfsntqidyavsDFSGGWRMRLNLAQA 163
Cdd:cd03253 96 RYGRPD--------ATDEEVIEAAKAAQIHDKIMRFpDGY--DTIVGE--RGL------------KLSGGEKQRVAIARA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 800951443 164 LIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG--TLVLISH 204
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAH 194
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
313-509 |
9.67e-11 |
|
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: 61.89 E-value: 9.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVGY-----------FA 381
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYI-GGRDVTDlppkdrdiamvFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 382 QHQL----EALDLQASPVThLQRLNPQASEQSLRD---FLGgfafIgDKALD-PVAPFSGGEKARLVLAMLVYQKPNLLL 453
Cdd:cd03301 80 NYALyphmTVYDNIAFGLK-LRKVPKDEIDERVREvaeLLQ----I-EHLLDrKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 454 LDEPTNHLD----LEMRHALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:cd03301 154 MDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
337-505 |
9.89e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.64 E-value: 9.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 337 PGSRIALLGRNGAGKSTLIKLLAQeLAPQAGDVFF-----------HQGLKVGYFAQHQLEALdlqASPV-----THLQR 400
Cdd:PRK03695 21 AGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFagqpleawsaaELARHRAYLSQQQTPPF---AMPVfqyltLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 401 LNPQASEQSLRDFLGGFAFIGDKALDPVAPFSGGEKARLVLAMLVYQ-----KPN--LLLLDEPTNHLDLEMRHAL---V 470
Cdd:PRK03695 97 KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSLDVAQQAALdrlL 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 800951443 471 MALQSFDGAMVTVSHD-RHLLKNtADEFYLVDSGEV 505
Cdd:PRK03695 177 SELCQQGIAVVMSSHDlNHTLRH-ADRVWLLKQGKL 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
338-505 |
9.95e-11 |
|
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: 61.74 E-value: 9.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 338 GSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHqGLKVGY-----------FAQHQLEA-------LDLQASPVTHLQ 399
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN-GVDVTAappadrpvsmlFQENNLFAhltveqnVGLGLSPGLKLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 400 RLNPQASEQSLRDfLGgfafIGDKALDPVAPFSGGEKARLVLA-MLVYQKPnLLLLDEPTNHLDLEMRH---ALVMALQS 475
Cdd:cd03298 103 AEDRQAIEVALAR-VG----LAGLEKRLPGELSGGERQRVALArVLVRDKP-VLLLDEPFAALDPALRAemlDLVLDLHA 176
|
170 180 190
....*....|....*....|....*....|.
gi 800951443 476 FDGAMV-TVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:cd03298 177 ETKMTVlMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-205 |
1.21e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 63.71 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKV---------PKEWS--IASV 69
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagddvealsARAASrrVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 70 KQETP-ALAITALEYVLQGNPDYyalRCQLKQAEQQGDgetqAQVHQQLElmkgySIEAKAgellhglgFSntqiDYAVS 148
Cdd:PRK09536 83 PQDTSlSFEFDVRQVVEMGRTPH---RSRFDTWTETDR----AAVERAME-----RTGVAQ--------FA----DRPVT 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 149 DFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLD-AVYWLE--RFLRSYAGTLVLISHD 205
Cdd:PRK09536 139 SLSGGERQRVLLARALAQATPVLLLDEPTASLDINhQVRTLElvRRLVDDGKTAVAAIHD 198
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
322-505 |
1.24e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.56 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGD-TTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH--------QGL-----KVGYFAQ---HQ 384
Cdd:PRK13636 15 YSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkpidysrKGLmklreSVGMVFQdpdNQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 385 L-----------EALDLQAsPVTHLQRLNPQASEQSlrdflgGFAFIGDKaldPVAPFSGGEKARLVLAMLVYQKPNLLL 453
Cdd:PRK13636 95 LfsasvyqdvsfGAVNLKL-PEDEVRKRVDNALKRT------GIEHLKDK---PTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 800951443 454 LDEPTNHLD----LEMRHALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:PRK13636 165 LDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
17-204 |
1.39e-10 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 60.40 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNakvpkewsiasvkqetpalaitaleyVLQGNPDYYALRC 96
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGE--------------------------ITLDGVPVSDLEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 97 QLKQAeqqgdgetQAQVHQQLELMkgysieakAGELLHGLGfsntqidyavSDFSGGWRMRLNLAQALIRDADLLLLDEP 176
Cdd:cd03247 72 ALSSL--------ISVLNQRPYLF--------DTTLRNNLG----------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190
....*....|....*....|....*....|
gi 800951443 177 TNHLDLDAVYWLERFLRSYA--GTLVLISH 204
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLkdKTLIWITH 155
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
322-462 |
1.42e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 62.82 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQ------------------GL----KVG- 378
Cdd:COG4152 11 FGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGepldpedrrrigylpeerGLypkmKVGe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 379 ---YFAQhqlealdlqaspvthLQRLNPQASEQSLRDFLGGFAfIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLD 455
Cdd:COG4152 91 qlvYLAR---------------LKGLSKAEAKRRADEWLERLG-LGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
....*..
gi 800951443 456 EPTNHLD 462
Cdd:COG4152 155 EPFSGLD 161
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-212 |
1.73e-10 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 60.31 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 16 LLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGnakvpkewsiasvkqetpalaitalEYVLQGNPdyyalr 95
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSG-------------------------RVRLDGAD------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 96 cqLKQAEQQGDGETQAQVHQQLELMKGySIeakagellhglgfsntqidyAVSDFSGGWRMRLNLAQALIRDADLLLLDE 175
Cdd:cd03246 66 --ISQWDPNELGDHVGYLPQDDELFSG-SI--------------------AENILSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 800951443 176 PTNHLDLD---AVYWLERFLRSYAGTLVLISHDREFLDAV 212
Cdd:cd03246 123 PNSHLDVEgerALNQAIAALKAAGATRIVIAHRPETLASA 162
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
31-224 |
1.96e-10 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 61.23 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 31 GLVGSNGCGKSSLFALLKGELQLDAGNAKV--------PKE--WSIASVKQEtPAL--AITALEYVLqgnpdyyalrcql 98
Cdd:cd03265 30 GLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvrePREvrRRIGIVFQD-LSVddELTGWENLY------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 99 kqaeqqgdgetqaqVHQQLELMKGYSIEAKAGELLHGLGFSNTQiDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTN 178
Cdd:cd03265 96 --------------IHARLYGVPGAERRERIDELLDFVGLLEAA-DRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 800951443 179 HLDLDAV--YW--LERFLRSYAGTLVLISHDREFLDAVVGEIWHIDQQQI 224
Cdd:cd03265 161 GLDPQTRahVWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-203 |
2.01e-10 |
|
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: 61.13 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 16 LLKNANATlFPQHKV-GLVGSNGCGKSSLFALLKGELQLDA---------GNAKVPKEW--SIASVKQ-ETPALAITALE 82
Cdd:cd03234 22 ILNDVSLH-VESGQVmAILGSSGSGKTTLLDAISGRVEGGGttsgqilfnGQPRKPDQFqkCVAYVRQdDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 83 YVlqgnpdYYALRCQLKqaEQQGDGETQAQVHQqlELMKGYSIEAKAGELLHGLgfsntqidyavsdfSGGWRMRLNLAQ 162
Cdd:cd03234 101 TL------TYTAILRLP--RKSSDAIRKKRVED--VLLRDLALTRIGGNLVKGI--------------SGGERRRVSIAV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 800951443 163 ALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYA--GTLVLIS 203
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLArrNRIVILT 199
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
322-499 |
2.37e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHqglkvGYFAQHQLEALDLQASPVTHLQRL 401
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFE-----RQSIKKDLCTYQKQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 402 NPQAS--EQSLRDFLGGFAFIG----------DKALD-PVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLD---LEM 465
Cdd:PRK13540 86 NPYLTlrENCLYDIHFSPGAVGitelcrlfslEHLIDyPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDelsLLT 165
|
170 180 190
....*....|....*....|....*....|....*
gi 800951443 466 RHALVMALQSFDGAMVTVSH-DRHLLKNTADEFYL 499
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSHqDLPLNKADYEEYHL 200
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-212 |
2.79e-10 |
|
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: 60.97 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPK----CLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEwsiaSVKQETPAL 76
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR----PVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 77 AITALEYVLQgnpDYYA-------LRCQLKQAeqqgdgetqaqvhqqLELMKGYSIEAKAGELLHGLGFSNTQIDYAVSD 149
Cdd:COG1124 77 FRRRVQMVFQ---DPYAslhprhtVDRILAEP---------------LRIHGLPDREERIAELLEQVGLPPSFLDRYPHQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 150 FSGGWRMRLNLAQALIRDADLLLLDEPTNHLD-------LDAvywLERFLRSYAGTLVLISHDREFLDAV 212
Cdd:COG1124 139 LSGGQRQRVAIARALILEPELLLLDEPTSALDvsvqaeiLNL---LKDLREERGLTYLFVSHDLAVVAHL 205
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
328-509 |
2.91e-10 |
|
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: 60.46 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 328 LHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGD---------------------VFFHQGL--------KVG 378
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFatvdgfdvvkepaearrrlgfVSDSTGLydrltareNLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 379 YFAQ-HQLEALDLQAspvthlqRLNPQASEQSLRDFLggfafigDKaldPVAPFSGGEKARLVLAMLVYQKPNLLLLDEP 457
Cdd:cd03266 101 YFAGlYGLKGDELTA-------RLEELADRLGMEELL-------DR---RVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 458 TNHLDLEMRHAL---VMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:cd03266 164 TTGLDVMATRALrefIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-205 |
3.18e-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: 60.88 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 30 VGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEwSIASVKQETPALAITALEYVLQG-NPDYYalrcqlkqaeqqgdge 108
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQYIKADYEGTVRDLLSSiTKDFY---------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 109 TQAQVhqQLELMKGYSIEAkagellhglgfsntQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD----LDA 184
Cdd:cd03237 91 THPYF--KTEIAKPLQIEQ--------------ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrLMA 154
|
170 180
....*....|....*....|.
gi 800951443 185 VYWLERFLRSYAGTLVLISHD 205
Cdd:cd03237 155 SKVIRRFAENNEKTAFVVEHD 175
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
322-517 |
4.11e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 61.66 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF--------------------------HQGL 375
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdgedvthrsiqqrdicmvfqsyalfpHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 376 --KVGYfaqhqleALDLQASPVTHLQRLNPQASEqsLRDfLGGFafiGDKALDPVapfSGGEKARLVLAMLVYQKPNLLL 453
Cdd:PRK11432 96 geNVGY-------GLKMLGVPKEERKQRVKEALE--LVD-LAGF---EDRYVDQI---SGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 454 LDEPTNHLDLEMRHAL---VMALQ-SFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFGYDLDAYYQ 517
Cdd:PRK11432 160 FDEPLSNLDANLRRSMrekIRELQqQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-204 |
4.20e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.36 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGnakvpkewSIASVKQETPALAITAL 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAG--------SISLCGEPVPSRARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 82 EYVlqG--------NPDYYALRCQLKQAEQQG--DGETQAQVHQQLELMKgysIEAKAgellhglgfsntqiDYAVSDFS 151
Cdd:PRK13537 80 QRV--GvvpqfdnlDPDFTVRENLLVFGRYFGlsAAAARALVPPLLEFAK---LENKA--------------DAKVGELS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 800951443 152 GGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG---TLVLISH 204
Cdd:PRK13537 141 GGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLArgkTILLTTH 196
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
333-467 |
5.73e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 59.98 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 333 LNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVF--------------------------------------FHQG 374
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTlngqdhtttppsrrpvsmlfqennlfshltvaqniglgLNPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 375 LKVGYFAQHQLEALDLQASPVTHLQRLNPQaseqslrdflggfafigdkaldpvapFSGGEKARLVLAM-LVYQKPnLLL 453
Cdd:PRK10771 100 LKLNAAQREKLHAIARQMGIEDLLARLPGQ--------------------------LSGGQRQRVALARcLVREQP-ILL 152
|
170
....*....|....
gi 800951443 454 LDEPTNHLDLEMRH 467
Cdd:PRK10771 153 LDEPFSALDPALRQ 166
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-207 |
6.40e-10 |
|
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: 59.62 E-value: 6.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 25 FPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKE-WSIASVKQETP----ALAITALEYVLQGNPDYYA-LRCQL 98
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvLFDSRKKINLPpqqrKIGLVFQQYALFPHLNVREnLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 99 KQAEQqgdGETQAQVHQQLELMKgysieakagelLHGLGFSNtqidyaVSDFSGGWRMRLNLAQALIRDADLLLLDEPTN 178
Cdd:cd03297 101 KRKRN---REDRISVDELLDLLG-----------LDHLLNRY------PAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190
....*....|....*....|....*....|...
gi 800951443 179 HLDLDAVYWLERFLR----SYAGTLVLISHDRE 207
Cdd:cd03297 161 ALDRALRLQLLPELKqikkNLNIPVIFVTHDLS 193
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
327-457 |
6.69e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 59.02 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 327 ILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHqgLKVGYFAQhqlEALDLQAS---PVTHLQRLNP 403
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP--GSIAYVSQ---EPWIQNGTireNILFGKPFDE 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 800951443 404 QASEQSLR------DF----LGGFAFIGDK--ALdpvapfSGGEKARLVLAMLVYQKPNLLLLDEP 457
Cdd:cd03250 95 ERYEKVIKacalepDLeilpDGDLTEIGEKgiNL------SGGQKQRISLARAVYSDADIYLLDDP 154
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
323-491 |
9.08e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 59.70 E-value: 9.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLA--QELAPQAGDVFFH---------------------Q------ 373
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDgedilelspderaragiflafQypveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 374 GLKVGYFAQHQLEALDLQASPVTH-LQRLNPQASEQSL-RDFLggfafigDKALDpvAPFSGGEKARL-VLAMLVyQKPN 450
Cdd:COG0396 91 GVSVSNFLRTALNARRGEELSAREfLKLLKEKMKELGLdEDFL-------DRYVN--EGFSGGEKKRNeILQMLL-LEPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 800951443 451 LLLLDEPTNHLDLEmrhAL------VMALQSFDGAMVTVSHDRHLLK 491
Cdd:COG0396 161 LAILDETDSGLDID---ALrivaegVNKLRSPDRGILIITHYQRILD 204
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
326-475 |
1.08e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.22 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 326 TILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAP---QAGDVFFHqGLKV---------GYFAQHQL-------- 385
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLN-GMPIdakemraisAYVQQDDLfiptltvr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 386 EALDLQA--------SPVTHLQRLNPQASEQSLRDflGGFAFIGDKalDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEP 457
Cdd:TIGR00955 118 EHLMFQAhlrmprrvTKKEKRERVDEVLQALGLRK--CANTRIGVP--GRVKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170
....*....|....*...
gi 800951443 458 TNHLDLEMRHALVMALQS 475
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-213 |
1.50e-09 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 57.05 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVP-KEWSIASVKQetpalaitaleyvlqgnpdyyalr 95
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDgKEVSFASPRD------------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 96 cqlkqAEQQGdgetQAQVHQqlelmkgysieakagellhglgfsntqidyavsdFSGGWRMRLNLAQALIRDADLLLLDE 175
Cdd:cd03216 72 -----ARRAG----IAMVYQ----------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 800951443 176 PTNHLDLDAVYWLERFLRSYAG---TLVLISH----DREFLDAVV 213
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAqgvAVIFISHrldeVFEIADRVT 153
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
322-505 |
1.67e-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: 58.50 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDV-------------FFHQ-GLkvgYFAQHQLEA 387
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvaglvpwkrrkkFLRRiGV---VFGQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 388 LDLQA----SPVTHLQRLNPQASEQSLrDFLGGFAFIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDL 463
Cdd:cd03267 108 WDLPVidsfYLLAAIYDLPPARFKKRL-DELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 800951443 464 EMRHAL---VMALQSFDGAMVTV-SHDRHLLKNTADEFYLVDSGEV 505
Cdd:cd03267 187 VAQENIrnfLKEYNRERGTTVLLtSHYMKDIEALARRVLVIDKGRL 232
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
309-489 |
1.91e-09 |
|
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: 58.21 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 309 PNPLIALDGA----QAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVffhqglkvgYFAQHQ 384
Cdd:COG4181 5 SAPIIELRGLtktvGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTV---------RLAGQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 385 LEALD---------------LQASP-VTHLQRL-----------NPQASEQSLRdflggfafigdkALDPV--------- 428
Cdd:COG4181 76 LFALDedararlrarhvgfvFQSFQlLPTLTALenvmlplelagRRDARARARA------------LLERVglghrldhy 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 800951443 429 -APFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHA---LVMALQSFDGA-MVTVSHDRHL 489
Cdd:COG4181 144 pAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQiidLLFELNRERGTtLVLVTHDPAL 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
313-522 |
2.04e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 58.49 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDV------F-FHQGL---------- 375
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLniaghqFdFSQKPsekairllrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 376 KVGY-FAQHQL----EALD-LQASPVTHLQRLNPQASEQS--------LRDFLGGFafigdkaldPVApFSGGEKARLVL 441
Cdd:COG4161 83 KVGMvFQQYNLwphlTVMEnLIEAPCKVLGLSKEQAREKAmkllarlrLTDKADRF---------PLH-LSGGQQQRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 442 AMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSFDGAMVT---VSHDRHLLKNTADEFYLVDSGEVRQFGyDLDAYYQW 518
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITqviVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQP 231
|
....
gi 800951443 519 LTKA 522
Cdd:COG4161 232 QTEA 235
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
323-509 |
2.59e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 58.66 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVF----------FHQGLK-VGYFAQHQLEAL--- 388
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLirgepitkenIREVRKfVGLVFQNPDDQIfsp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 389 ----DLQASPVThlQRLNPQASEQSLRDFLggfAFIGDKALDPVAP--FSGGEKARLVLAMLVYQKPNLLLLDEPTNHLD 462
Cdd:PRK13652 95 tveqDIAFGPIN--LGLDEETVAHRVSSAL---HMLGLEELRDRVPhhLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 800951443 463 LEMRHALVMALQSFD---GAMVTVS-HDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:PRK13652 170 PQGVKELIDFLNDLPetyGMTVIFStHQLDLVPEMADYIYVMDKGRIVAYG 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
313-509 |
2.69e-09 |
|
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: 58.01 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDT-TILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH-QGLKvgyfaQHQLEALDL 390
Cdd:cd03253 1 IEFENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgQDIR-----EVTLDSLRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 391 QASPVTHLQRL------------NPQASEQSLR---------DFLGGFAF-----IGDKALDpvapFSGGEKARLVLAML 444
Cdd:cd03253 76 AIGVVPQDTVLfndtigynirygRPDATDEEVIeaakaaqihDKIMRFPDgydtiVGERGLK----LSGGEKQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 445 VYQKPNLLLLDEPTNHLDLEMRHALVMALQS-FDG-AMVTVSHDRHLLKNtADEFYLVDSGEVRQFG 509
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDvSKGrTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
323-481 |
2.97e-09 |
|
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: 57.12 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQG---LKVGYFAQ------HQlEALDLQAS 393
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldFQRDSIARgllylgHA-PGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 394 PVTHLQRLNPQAS----EQSLRDF-LGGFAFIgdkaldPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDL--EMR 466
Cdd:cd03231 90 VLENLRFWHADHSdeqvEEALARVgLNGFEDR------PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKagVAR 163
|
170
....*....|....*
gi 800951443 467 HALVMALQSFDGAMV 481
Cdd:cd03231 164 FAEAMAGHCARGGMV 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
319-505 |
3.23e-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: 57.59 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 319 QAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH----QGL----------KVGYFAQH- 383
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtdlTLLsgkelrkarrRIGMIFQHf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 384 ----QLEALDLQASP--VTHLQRLNPQASEQSLRDFLGgfafIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEP 457
Cdd:cd03258 92 nllsSRTVFENVALPleIAGVPKAEIEERVLELLELVG----LEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 800951443 458 TNHLDLEMRHALVMAL----QSFDGAMVTVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:cd03258 168 TSALDPETTQSILALLrdinRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
311-482 |
3.34e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.17 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 311 PLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH-QGLKVGYFAQH-----Q 384
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDgKTATRGDRSRFmaylgH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 385 LEALDLQASPVTHLQRLNPQASEQSLRDFLGGFAFIG--DKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLD 462
Cdd:PRK13543 90 LPGLKADLSTLENLHFLCGLHGRRAKQMPGSALAIVGlaGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180
....*....|....*....|....
gi 800951443 463 LE----MRHALVMALQSFDGAMVT 482
Cdd:PRK13543 170 LEgitlVNRMISAHLRGGGAALVT 193
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
30-205 |
3.35e-09 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 58.18 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 30 VGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEwsiaSVKQETPALAI-----------TALEYVLqgnpdyYALRCQL 98
Cdd:COG1116 40 VALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK----PVTGPGPDRGVvfqepallpwlTVLDNVA------LGLELRG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 99 KQAEqqgdgETQAQVHQQLELMkgysieakagellhGL-GFSN---TQIdyavsdfSGGWRMRLNLAQALIRDADLLLLD 174
Cdd:COG1116 110 VPKA-----ERRERARELLELV--------------GLaGFEDaypHQL-------SGGMRQRVAIARALANDPEVLLMD 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 800951443 175 EPTNHLD------LDAvyWLERFLRSYAGTLVLISHD 205
Cdd:COG1116 164 EPFGALDaltrerLQD--ELLRLWQETGKTVLFVTHD 198
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-176 |
3.42e-09 |
|
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: 57.09 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 16 LLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKewSIASVKQETPALAITALEYVLQGNP---DYY 92
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEPWIQNGTIRENILFGKPfdeERY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 93 --ALR-CQLKQaeqqgDgetqaqvhqqLELMKgysieakagellHGLgfsNTQI-DYAVSdFSGGWRMRLNLAQALIRDA 168
Cdd:cd03250 98 ekVIKaCALEP-----D----------LEILP------------DGD---LTEIgEKGIN-LSGGQKQRISLARAVYSDA 146
|
....*...
gi 800951443 169 DLLLLDEP 176
Cdd:cd03250 147 DIYLLDDP 154
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-210 |
3.79e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 57.76 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 30 VGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSiasvkqetpalaiTALEYV----LQgnpDYYalrcqlkqaEQQG 105
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWD-------------EILDEFrgseLQ---NYF---------TKLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 106 DGETQAQVHQQLELMKGYSIEAKAGELL---HGLGFSNTQI---------DYAVSDFSGGWRMRLNLAQALIRDADLLLL 173
Cdd:cd03236 84 EGDVKVIVKPQYVDLIPKAVKGKVGELLkkkDERGKLDELVdqlelrhvlDRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 800951443 174 DEPTNHLDLDAVYWLERFLRSYA---GTLVLISHDREFLD 210
Cdd:cd03236 164 DEPSSYLDIKQRLNAARLIRELAeddNYVLVVEHDLAVLD 203
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
30-207 |
5.45e-09 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 56.96 E-value: 5.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 30 VGLVGSNGCGKSSLFALLKGELQLDAGN---------AKVPKEWSIASVKQETpAL--AITALEYVLQGnpdyyaLRCQl 98
Cdd:cd03296 31 VALLGPSGSGKTTLLRLIAGLERPDSGTilfggedatDVPVQERNVGFVFQHY-ALfrHMTVFDNVAFG------LRVK- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 99 KQAEQQGDGETQAQVHQQLELMKgysieakagelLHGLGfsntqiDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTN 178
Cdd:cd03296 103 PRSERPPEAEIRAKVHELLKLVQ-----------LDWLA------DRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFG 165
|
170 180 190
....*....|....*....|....*....|...
gi 800951443 179 HLDLDAVYWLERFLRSYAG----TLVLISHDRE 207
Cdd:cd03296 166 ALDAKVRKELRRWLRRLHDelhvTTVFVTHDQE 198
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
310-505 |
6.00e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 57.72 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 310 NPLIALDGAQAGYGDTT--ILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDV-FFHQGL----------K 376
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItVGGMVLseetvwdvrrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 377 VGYFAQ---HQLE----------ALDLQASPVTHLQRLNPQASEQ-SLRDFLggfafigdkaLDPVAPFSGGEKARLVLA 442
Cdd:PRK13635 83 VGMVFQnpdNQFVgatvqddvafGLENIGVPREEMVERVDQALRQvGMEDFL----------NREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 800951443 443 MLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSF-DGAMVTVSHDRHLLKNTA--DEFYLVDSGEV 505
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAAqaDRVIVMNKGEI 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
330-509 |
6.21e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.49 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 330 SIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF--HQgLKVGYFAQHQLEALDLQASPVTHL---QR---- 400
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIddHP-LHFGDYSYRSQRIRMIFQDPSTSLnprQRisqi 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 401 ----------LNPQASEQSLRDFLGGFAFIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALV 470
Cdd:PRK15112 110 ldfplrlntdLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLI 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 800951443 471 ---MALQSFDG-AMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:PRK15112 190 nlmLELQEKQGiSYIYVTQHLGMMKHISDQVLVMHQGEVVERG 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
313-494 |
7.20e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.95 E-value: 7.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQ------AGDVF-FHQGL---------- 375
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRsgtlniAGNHFdFSKTPsdkairelrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 376 KVGY-FAQHQL-----------EAldlqasPVTHLQRLNPQASEQS--------LRDFLGGFafigdkaldPVApFSGGE 435
Cdd:PRK11124 83 NVGMvFQQYNLwphltvqqnliEA------PCRVLGLSKDQALARAekllerlrLKPYADRF---------PLH-LSGGQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800951443 436 KARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSFDGAMVT---VSHDRHLLKNTA 494
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITqviVTHEVEVARKTA 208
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
160-358 |
7.30e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 160 LAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG---TLVLISHDREFLDAVVGEIWHIDQQQINvykgnySQFER 236
Cdd:PRK10938 146 LCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLVLNRFDEIPDFVQFAGVLADCTLA------ETGER 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 237 QKAERLAQQQaqfdkqqeQIAHlekfitrfkakaskakqaqsrvkalerMEKLAPAHVDSPFDFSfAEPdALP--NPLIA 314
Cdd:PRK10938 220 EEILQQALVA--------QLAH---------------------------SEQLEGVQLPEPDEPS-ARH-ALPanEPRIV 262
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 800951443 315 LDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLL 358
Cdd:PRK10938 263 LNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI 306
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
311-490 |
8.29e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.96 E-value: 8.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 311 PLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQ--AGDVFF--------------HQG 374
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFkgesildlepeeraHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 375 LKVGYfaQHQLEaldlqASPVTHLQRL----NPQASEQSLRDF--LGGFAFIGDK----ALDPV-------APFSGGEKA 437
Cdd:CHL00131 86 IFLAF--QYPIE-----IPGVSNADFLrlayNSKRKFQGLPELdpLEFLEIINEKlklvGMDPSflsrnvnEGFSGGEKK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 800951443 438 R---LVLAMLvyqKPNLLLLDEPTNHLDLEMRHALVMALQSF---DGAMVTVSHDRHLL 490
Cdd:CHL00131 159 RneiLQMALL---DSELAILDETDSGLDIDALKIIAEGINKLmtsENSIILITHYQRLL 214
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
325-462 |
8.61e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.12 E-value: 8.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 325 TTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHqgLKVGYFAQHQ--LEALDLQASPVTHLQRLN 402
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD--VPDNQFGREAslIDAIGRKGDFKDAVELLN 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800951443 403 PqaseqslrdflggfAFIGDKAL--DPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLD 462
Cdd:COG2401 121 A--------------VGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
30-208 |
8.83e-09 |
|
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: 56.59 E-value: 8.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 30 VGLVGSNGCGKSSLFALLKGELQLDAG---------------------------NAKVPKEwsiasvkqetpalaITALE 82
Cdd:COG0411 33 VGLIGPNGAGKTTLFNLITGFYRPTSGrilfdgrditglpphriarlgiartfqNPRLFPE--------------LTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 83 YVL-----QGNPDYYALRCQLKQAEQQgDGETQAQVHQQLELMKgysIEAKAGELlhglgfsntqidyaVSDFSGGWRMR 157
Cdd:COG0411 99 NVLvaahaRLGRGLLAALLRLPRARRE-EREARERAEELLERVG---LADRADEP--------------AGNLSYGQQRR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 158 LNLAQALIRDADLLLLDEPT---NHLDLDAVYWLERFLRSYAG-TLVLISHDREF 208
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDL 215
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
324-505 |
9.08e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 57.01 E-value: 9.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 324 DTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF--------HQGL-----KVGYFAQH---QLEA 387
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkgepikydKKSLlevrkTVGIVFQNpddQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 388 ----LDLQASPVThlQRLNPQASEQSLRDFLggfAFIGDKALDPVAP--FSGGEKARLVLAMLVYQKPNLLLLDEPTNHL 461
Cdd:PRK13639 94 ptveEDVAFGPLN--LGLSKEEVEKRVKEAL---KAVGMEGFENKPPhhLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 800951443 462 DLEMRHALVMALQSFDGAMVTV---SHDRHLLKNTADEFYLVDSGEV 505
Cdd:PRK13639 169 DPMGASQIMKLLYDLNKEGITIiisTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
327-509 |
9.16e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 55.88 E-value: 9.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 327 ILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVffhqglkvgyfaqhQLEALDLQASPVTHLQR------ 400
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI--------------EIDGIDISTIPLEDLRSsltiip 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 401 LNPQASEQSLRDFLGGFAFIGDKALDPV-------APFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMAL 473
Cdd:cd03369 89 QDPTLFSGTIRSNLDPFDEYSDEEIYGAlrvseggLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTI 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 800951443 474 -QSFDGA-MVTVSHDRHLLKNtADEFYLVDSGEVRQFG 509
Cdd:cd03369 169 rEEFTNStILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
112-505 |
9.24e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.18 E-value: 9.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 112 QVHQQLELMKGYSIEAKAGELLHGLgfSNTQIDYA---VSDF----SGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDA 184
Cdd:PRK15134 114 QLYEVLSLHRGMRREAARGEILNCL--DRVGIRQAakrLTDYphqlSGGERQRVMIAMALLTRPELLIADEPTTALDVSV 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 185 ---VYWLERFLRSYAG-TLVLISHDrefLDAVvgeiwhidqqqinvykgnysqfeRQKAERLAQQQAQFDKqqEQIAHLE 260
Cdd:PRK15134 192 qaqILQLLRELQQELNmGLLFITHN---LSIV-----------------------RKLADRVAVMQNGRCV--EQNRAAT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 261 KFItrfkakaskakqaqsrvkalermeklAPAHvdsPFDFSF--AEPDALP-------NPLIALDGAQAGY--------- 322
Cdd:PRK15134 244 LFS--------------------------APTH---PYTQKLlnSEPSGDPvplpepaSPLLDVEQLQVAFpirkgilkr 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 --GDTTILHSIKLNLVPGSRIALLGRNGAGKST----LIKLLAQElapqaGDVFFhQGLKVGYFAQHQLEALDLQASPV- 395
Cdd:PRK15134 295 tvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWF-DGQPLHNLNRRQLLPVRHRIQVVf 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 396 ----------------------THLQRLNPQASEQSLRdflggfAFIGDKALDPV------APFSGGEKARLVLAMLVYQ 447
Cdd:PRK15134 369 qdpnsslnprlnvlqiieeglrVHQPTLSAAQREQQVI------AVMEEVGLDPEtrhrypAEFSGGQRQRIAIARALIL 442
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800951443 448 KPNLLLLDEPTNHLDLEMRH---ALVMALQSFDG-AMVTVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:PRK15134 443 KPSLIILDEPTSSLDKTVQAqilALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
328-517 |
9.82e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.05 E-value: 9.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 328 LHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGLKVGYFAQHQLEALDLQASPVthLQRLNPQASE 407
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVV--FQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 408 QS-LRDFLGG---FAF-------IGDKALDPV---------APF--SGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEM 465
Cdd:PRK13643 100 ETvLKDVAFGpqnFGIpkekaekIAAEKLEMVgladefwekSPFelSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 466 RHALVMALQSFDGAMVTVSHDRHLLKNT---ADEFYLVDSGEVRQFGYDLDAYYQ 517
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMDDVadyADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-204 |
1.04e-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: 55.94 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 16 LLKNANATLFPQHKVGLVGSNGCGKSSLFALL-------KGELQLDAGNAKVPK----EWSIASVKQEtPALAITALE-- 82
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLenfyqpqGGQVLLDGKPISQYEhkylHSKVSLVGQE-PVLFARSLQdn 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 83 --YVLQGNPDYyalrcQLKQAEQQGDGETQAQvhqqlELMKGYSIEA-KAGELLhglgfsntqidyavsdfSGGWRMRLN 159
Cdd:cd03248 108 iaYGLQSCSFE-----CVKEAAQKAHAHSFIS-----ELASGYDTEVgEKGSQL-----------------SGGQKQRVA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 800951443 160 LAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSY--AGTLVLISH 204
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH 207
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
151-226 |
1.14e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 55.69 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 151 SGGWRM------RLNLAQALIRDADLLLLDEPTNHLDLDAVYW-LERFLRSYAGT----LVLISHDREFLDAvVGEIWHI 219
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQknfqLIVITHDEELVDA-ADHIYRV 195
|
....*..
gi 800951443 220 DQQQINV 226
Cdd:cd03240 196 EKDGRQK 202
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
322-505 |
1.31e-08 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 56.01 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF----------HQ--GLKVGYFAQH-----Q 384
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLdgqditklpmHKraRLGIGYLPQEasifrK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 385 LEALD-LQAspVTHLQRLNPQASEQSLRDFLGGFAfIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLD- 462
Cdd:cd03218 90 LTVEEnILA--VLEIRGLSKKEREEKLEELLEEFH-ITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDp 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 800951443 463 ---LEMRHaLVMALQSFD-GAMVTVSHDRHLLKnTADEFYLVDSGEV 505
Cdd:cd03218 167 iavQDIQK-IIKILKDRGiGVLITDHNVRETLS-ITDRAYIIYEGKV 211
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
319-509 |
1.31e-08 |
|
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: 57.83 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 319 QAGYGDTtILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHqGLKVGYFAQHQL------------- 385
Cdd:TIGR01193 482 SYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN-GFSLKDIDRHTLrqfinylpqepyi 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 386 ------EALDLQASPVTHLQRLNPQASEQSLRDFLGGFAFIGDKALDPVA-PFSGGEKARLVLAMLVYQKPNLLLLDEPT 458
Cdd:TIGR01193 560 fsgsilENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGsSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 800951443 459 NHLDLEMRHALVMALQSF-DGAMVTVSHDRHLLKNTaDEFYLVDSGEVRQFG 509
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLqDKTIIFVAHRLSVAKQS-DKIIVLDHGKIIEQG 690
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
308-477 |
1.67e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.66 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 308 LPNPLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH-QGLKVGYFAQHQLE 386
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgKDITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 387 ALDLQASPVTHLQRL-------------NPQASEQSLRDFLGGFAFIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLL 453
Cdd:PRK11614 81 AVAIVPEGRRVFSRMtveenlamggffaERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180
....*....|....*....|....
gi 800951443 454 LDEPTNHLdlemrhALVMALQSFD 477
Cdd:PRK11614 161 LDEPSLGL------APIIIQQIFD 178
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
328-509 |
1.85e-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: 55.42 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 328 LHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH----QGLK-----VGYFAQH-----QLEALDLQAS 393
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkdiTNLPpekrdISYVPQNyalfpHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 394 PVTHLQRLNPQASEQSLR--DFLGgfafIgDKALD-PVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALV 470
Cdd:cd03299 95 GLKKRKVDKKEIERKVLEiaEMLG----I-DHLLNrKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 800951443 471 MAL----QSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:cd03299 170 EELkkirKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
425-500 |
2.06e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 54.92 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 425 LDPVAPFSGGEKA------RLVLAMLVYQKPNLLLLDEPTNHLDLE-MRHALVMALQSFDGA----MVTVSHDRHlLKNT 493
Cdd:cd03240 110 LDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEESLAEIIEERKSQknfqLIVITHDEE-LVDA 188
|
....*..
gi 800951443 494 ADEFYLV 500
Cdd:cd03240 189 ADHIYRV 195
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-205 |
2.08e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 55.15 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPkcLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGN---------AKVPKEWSIASVKQ 71
Cdd:COG3840 1 MLRLDDLTYRYGD--FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRilwngqdltALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 72 ET---PALaiTALEYVlqgnpdYYALRCQLKQAEQQgdgetQAQVHQQLELMKgysieakagelLHGLGfsntqiDYAVS 148
Cdd:COG3840 79 ENnlfPHL--TVAQNI------GLGLRPGLKLTAEQ-----RAQVEQALERVG-----------LAGLL------DRLPG 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 800951443 149 DFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD-------LDavyWLERFLRSYAGTLVLISHD 205
Cdd:COG3840 129 QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrqemLD---LVDELCRERGLTVLMVTHD 189
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
337-495 |
2.67e-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: 55.45 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 337 PGSRIALLGRNGAGKSTLIKLLAQELAPQAG---------DVF-FHQGLKV-GYFAQhqleALDLQASPVTHLQRLN--P 403
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILdEFRGSELqNYFTK----LLEGDVKVIVKPQYVDliP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 404 QASEQSLRDFL------GGFAFIGDK-ALDPV-----APFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMR---HA 468
Cdd:cd03236 101 KAVKGKVGELLkkkderGKLDELVDQlELRHVldrniDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRlnaAR 180
|
170 180
....*....|....*....|....*..
gi 800951443 469 LVMALQSFDGAMVTVSHDRHLLKNTAD 495
Cdd:cd03236 181 LIRELAEDDNYVLVVEHDLAVLDYLSD 207
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
328-469 |
2.80e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 55.86 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 328 LHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVffhqglKV-GY--------FAQH---------QL---- 385
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV------RVlGYvpfkrrkeFARRigvvfgqrsQLwwdl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 386 ---EALDLQA-----SPVTHLQRLNpqaseqSLRDFLGgfafIGDKALDPVAPFSGGE--KARLVLAMLvyQKPNLLLLD 455
Cdd:COG4586 112 paiDSFRLLKaiyriPDAEYKKRLD------ELVELLD----LGELLDTPVRQLSLGQrmRCELAAALL--HRPKILFLD 179
|
170
....*....|....
gi 800951443 456 EPTNHLDLEMRHAL 469
Cdd:COG4586 180 EPTIGLDVVSKEAI 193
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-181 |
2.86e-08 |
|
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: 54.93 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVP----KEWSIAS-------VKQETPALAITALEYVL 85
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghdvRDYTLASlrrqiglVSQDVFLFNDTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 86 QGNPDyyALRCQLKQAEQQgdgetqAQVHQQLELM-KGYsieakagellhglgfsNTQIDYAVSDFSGGWRMRLNLAQAL 164
Cdd:cd03251 98 YGRPG--ATREEVEEAARA------ANAHEFIMELpEGY----------------DTVIGERGVKLSGGQRQRIAIARAL 153
|
170
....*....|....*..
gi 800951443 165 IRDADLLLLDEPTNHLD 181
Cdd:cd03251 154 LKDPPILILDEATSALD 170
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
11-224 |
2.94e-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: 55.20 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 11 RGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEwSIASVKQETPALAITALEYVLQGNPD 90
Cdd:TIGR02769 21 KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQ-DLYQLDRKQRRAFRRDVQLVFQDSPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 91 YYALRCQLkqaeqqgdGETQAQVHQQLELMKGYSIEAKAGELLHGLGFSNTQIDYAVSDFSGGWRMRLNLAQALIRDADL 170
Cdd:TIGR02769 100 AVNPRMTV--------RQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 171 LLLDEPTNHLDL---DAVYWLERFLRSYAGT-LVLISHDREFLDAVVGEIWHIDQQQI 224
Cdd:TIGR02769 172 IVLDEAVSNLDMvlqAVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
312-462 |
3.42e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.09 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 312 LIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGD-----------------VFFHQG 374
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSitldgkpvegpgaergvVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 375 LKVGYFAQHQLeALDLQASPVTHLQRlnpqasEQSLRDFLGGFAFIGDKAlDPVAPFSGGEKARLVLAMLVYQKPNLLLL 454
Cdd:PRK11248 81 LLPWRNVQDNV-AFGLQLAGVEKMQR------LEIAHQMLKKVGLEGAEK-RYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
....*...
gi 800951443 455 DEPTNHLD 462
Cdd:PRK11248 153 DEPFGALD 160
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
327-509 |
3.70e-08 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 54.54 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 327 ILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF---------HQGL--KVGY-------FAQHQLEAL 388
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdgidirdisRKSLrsMIGVvlqdtflFSGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 389 DLqASPVTHLQRLNPQASEQSLRDFL-----GGFAFIGDKALDpvapFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDL 463
Cdd:cd03254 98 RL-GRPNATDEEVIEAAKEAGAHDFImklpnGYDTVLGENGGN----LSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 800951443 464 EMRHALVMALQS-FDGAMVTV-SHDRHLLKNtADEFYLVDSGEVRQFG 509
Cdd:cd03254 173 ETEKLIQEALEKlMKGRTSIIiAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
331-509 |
4.25e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 55.61 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 331 IKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFfhqglkvgyfaqhqLEALDLqaSPVTHLQR---------- 400
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM--------------LDGVDL--SHVPPYQRpinmmfqsya 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 401 LNPQAS-EQSLrdflgGFAFIGDK--------------ALDPVAPF--------SGGEKARLVLAMLVYQKPNLLLLDEP 457
Cdd:PRK11607 102 LFPHMTvEQNI-----AFGLKQDKlpkaeiasrvnemlGLVHMQEFakrkphqlSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 800951443 458 TNHLDLE----MRHALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:PRK11607 177 MGALDKKlrdrMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
323-519 |
4.36e-08 |
|
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: 54.57 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLA----------------QELAPQAGDVFFHQGLKVGYfaQHQLE 386
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghpsyevtsgtilfkgQDLLELEPDERARAGLFLAF--QYPEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 387 -----ALDLQASPVTHLQRLNPQAsEQSLRDFlggFAFIGDK--ALDPVAP---------FSGGEKAR---LVLAMLvyq 447
Cdd:TIGR01978 89 ipgvsNLEFLRSALNARRSARGEE-PLDLLDF---EKLLKEKlaLLDMDEEflnrsvnegFSGGEKKRneiLQMALL--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 448 KPNLLLLDEPTNHLD---LEMRHALVMALQSFDGAMVTVSHDRHLLKN-TADEFYLVDSGEVRQFG-----YDLDAY-YQ 517
Cdd:TIGR01978 162 EPKLAILDEIDSGLDidaLKIVAEGINRLREPDRSFLIITHYQRLLNYiKPDYVHVLLDGRIVKSGdvelaKELEAKgYD 241
|
..
gi 800951443 518 WL 519
Cdd:TIGR01978 242 WV 243
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
337-485 |
4.46e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.56 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 337 PGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF------------HQGLkvGYFAQhqLEALD--------------L 390
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVagksiltnisdvHQNM--GYCPQ--FDAIDdlltgrehlylyarL 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 391 QASPVTHLQRLnPQASEQSLrdflgGFAFIGDKAldpVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHAL- 469
Cdd:TIGR01257 2040 RGVPAEEIEKV-ANWSIQSL-----GLSLYADRL---AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLw 2110
|
170
....*....|....*...
gi 800951443 470 --VMALQSFDGAMVTVSH 485
Cdd:TIGR01257 2111 ntIVSIIREGRAVVLTSH 2128
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-219 |
4.61e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 53.68 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFallkgelqldagnakvpkewsiasvkqetpalaital 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLA------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 82 eYVLQGNPDYYalrcqlkqaeqqgdgETQAQVhqqleLMKGYSI-------EAKAGEllhGLGFSN-------TQIDY-- 145
Cdd:cd03217 44 -KTIMGHPKYE---------------VTEGEI-----LFKGEDItdlppeeRARLGI---FLAFQYppeipgvKNADFlr 99
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 146 AVSD-FSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG---TLVLISHDREFLDAVVGEIWHI 219
Cdd:cd03217 100 YVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITHYQRLLDYIKPDRVHV 177
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
322-458 |
4.66e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.80 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHqG-------------LKVGYFAQH----- 383
Cdd:COG3845 15 FGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID-GkpvrirsprdaiaLGIGMVHQHfmlvp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 384 ---QLEALDLQASPvTHLQRLNPQASEQSLRDFLGGFAFigdkALDPVAP---FSGGEKARL-VLAMLvYQKPNLLLLDE 456
Cdd:COG3845 94 nltVAENIVLGLEP-TKGGRLDRKAARARIRELSERYGL----DVDPDAKvedLSVGEQQRVeILKAL-YRGARILILDE 167
|
..
gi 800951443 457 PT 458
Cdd:COG3845 168 PT 169
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-209 |
4.68e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 54.32 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKewSIASVkqetpaLAITAleyvlqG-NPDY---- 91
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--RVSAL------LELGA------GfHPELtgre 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 92 --YaLRCQLKqaeqqgdGETQAQVHQQLElmkgySIEAKAgellhGLG-FsntqIDYAVSDFSGGWRMRLNLAQALIRDA 168
Cdd:COG1134 108 niY-LNGRLL-------GLSRKEIDEKFD-----EIVEFA-----ELGdF----IDQPVKTYSSGMRARLAFAVATAVDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 169 DLLLLDEptnhldldavyWL----ERF----------LRSYAGTLVLISHDREFL 209
Cdd:COG1134 166 DILLVDE-----------VLavgdAAFqkkclarireLRESGRTVIFVSHSMGAV 209
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-224 |
5.15e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 54.63 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGnakvpkewsiasvkqetpalaita 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKG------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 81 lEYVLQGNPDYYALRCQLKQAEQqgdgetQAQVHQQLELMKGYS-IEAKAGELLHGLGFSNTQIDYAVSD---------- 149
Cdd:PRK13638 57 -AVLWQGKPLDYSKRGLLALRQQ------VATVFQDPEQQIFYTdIDSDIAFSLRNLGVPEAEITRRVDEaltlvdaqhf 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 150 -------FSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAGT---LVLISHDREFLDAVVGEIWHI 219
Cdd:PRK13638 130 rhqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYVL 209
|
....*
gi 800951443 220 DQQQI 224
Cdd:PRK13638 210 RQGQI 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-182 |
6.78e-08 |
|
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: 54.48 E-value: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 16 LLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGnaKVPKEWSIASVKQETPALAITALEYVLQG-NPDYYAL 94
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG--KIKHSGRISFSSQFSWIMPGTIKENIIFGvSYDEYRY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 95 RCQLKQAEQQGDGETQAQvhqqlelmKGYSIEAKAGELLhglgfsntqidyavsdfSGGWRMRLNLAQALIRDADLLLLD 174
Cdd:cd03291 130 KSVVKACQLEEDITKFPE--------KDNTVLGEGGITL-----------------SGGQRARISLARAVYKDADLYLLD 184
|
....*...
gi 800951443 175 EPTNHLDL 182
Cdd:cd03291 185 SPFGYLDV 192
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
309-371 |
7.61e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 55.41 E-value: 7.61e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 800951443 309 PNPLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF 371
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL 63
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
17-242 |
7.84e-08 |
|
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: 53.73 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVP-------KEWSIASVKQET------PALA--ITAL 81
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdinklKGKALRQLRRQIgmifqqFNLIerLSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 82 EYVLQG----NPDYYALRCQLKQAEQQgdgetqaqvhqqlelmkgysieaKAGELLHGLGFSntqiDYA---VSDFSGGW 154
Cdd:cd03256 97 ENVLSGrlgrRSTWRSLFGLFPKEEKQ-----------------------RALAALERVGLL----DKAyqrADQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 155 RMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYA---GTLVLIS-HD----REFLDAVVGeiwhIDQQQInV 226
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreeGITVIVSlHQvdlaREYADRIVG----LKDGRI-V 224
|
250
....*....|....*.
gi 800951443 227 YKGNYSQFERQKAERL 242
Cdd:cd03256 225 FDGPPAELTDEVLDEI 240
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
313-485 |
7.86e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 53.76 E-value: 7.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQ--ELAPQA---GDVFfhqglkvgyfaqhqLEA 387
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVY--------------LDG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 388 LDLQASPVTHLQRL--------NP-----------------------QASEQSLRDFLGGFAF---IGDKALDPVAPFSG 433
Cdd:PRK14247 70 QDIFKMDVIELRRRvqmvfqipNPipnlsifenvalglklnrlvkskKELQERVRWALEKAQLwdeVKDRLDAPAGKLSG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 434 GEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMR---HALVMALQSfDGAMVTVSH 485
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDPENTakiESLFLELKK-DMTIVLVTH 203
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-212 |
8.92e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.72 E-value: 8.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 30 VGLVGSNGCGKSSLFALLKGELqlDAGNAKVPKEWSIASVKQETPALAITALEYVLQGnpdyyalrCQLKQAEQQGDGET 109
Cdd:TIGR00957 667 VAVVGQVGCGKSSLLSALLAEM--DKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFG--------KALNEKYYQQVLEA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 110 QAQVhQQLELMKGysieakaGEllhglgfsNTQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD-------L 182
Cdd:TIGR00957 737 CALL-PDLEILPS-------GD--------RTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkhiF 800
|
170 180 190
....*....|....*....|....*....|
gi 800951443 183 DAVYWLERFLRSyaGTLVLISHDREFLDAV 212
Cdd:TIGR00957 801 EHVIGPEGVLKN--KTRILVTHGISYLPQV 828
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
324-505 |
1.00e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.59 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 324 DTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVF-----FHQGL------KVGYFAQ---HQLEAL- 388
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvmgreVNAENekwvrsKVGLVFQdpdDQVFSSt 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 389 ---DLQASPVThlQRLNPQASEQSLRDFLggfAFIGDKALDPVAPF--SGGEKARLVLAMLVYQKPNLLLLDEPTNHLDL 463
Cdd:PRK13647 97 vwdDVAFGPVN--MGLDKDEVERRVEEAL---KAVRMWDFRDKPPYhlSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 800951443 464 EMRHALVMALQSFDGAMVTV---SHDRHLLKNTADEFYLVDSGEV 505
Cdd:PRK13647 172 RGQETLMEILDRLHNQGKTVivaTHDVDLAAEWADQVIVLKEGRV 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
324-509 |
1.15e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 55.02 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 324 DTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVgyfAQHQLEALDLQASPVT---HL-- 398
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL-DGHDL---RDYTLASLRNQVALVSqnvHLfn 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 399 ---------QRLNPQASEQSLRDFLGGFA--FIG--DKALDPV-----APFSGGEKARLVLAMLVYQKPNLLLLDEPTNH 460
Cdd:PRK11176 431 dtianniayARTEQYSREQIEEAARMAYAmdFINkmDNGLDTVigengVLLSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 800951443 461 LDLEMRHALVMALQSF--DGAMVTVSHDRHLLKNtADEFYLVDSGEVRQFG 509
Cdd:PRK11176 511 LDTESERAIQAALDELqkNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-181 |
1.16e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 54.64 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALL-------KGELQLDAGNAKvpkewsiasvkqetpalaitalEYVLQgnp 89
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLtrfydidEGEILLDGHDLR----------------------DYTLA--- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 90 dyyALRCQLkqaeqqgdgetqAQVHQQLELM-------------KGYSIE--AKAGELLHGLGFSN-------TQIDYAV 147
Cdd:PRK11176 414 ---SLRNQV------------ALVSQNVHLFndtianniayartEQYSREqiEEAARMAYAMDFINkmdngldTVIGENG 478
|
170 180 190
....*....|....*....|....*....|....
gi 800951443 148 SDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD 181
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
32-209 |
1.23e-07 |
|
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: 52.72 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 32 LVGSNGCGKSSLFALLKGELQLDAGNAkvpkEWSIASVKQETPALAITALEYVLQgnpdYYALRCQLKQAEQQGDGETQA 111
Cdd:cd03290 32 IVGQVGCGKSSLLLAILGEMQTLEGKV----HWSNKNESEPSFEATRSRNRYSVA----YAAQKPWLLNATVEENITFGS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 112 QVHQQL--ELMKGYSIEAKAGELLHGlgfSNTQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLE 189
Cdd:cd03290 104 PFNKQRykAVTDACSLQPDIDLLPFG---DQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLM 180
|
170 180
....*....|....*....|....*
gi 800951443 190 -----RFLRSYAGTLVLISHDREFL 209
Cdd:cd03290 181 qegilKFLQDDKRTLVLVTHKLQYL 205
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
327-505 |
1.26e-07 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 52.66 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 327 ILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQA---GDVFF-------HQGLK-VGYFAQHQ--LEALD---- 389
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFngqprkpDQFQKcVAYVRQDDilLPGLTvret 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 390 LQASPVTHLQRLNPQASEQSLRDFLGgfafIGDKALDPVA-----PFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLE 464
Cdd:cd03234 102 LTYTAILRLPRKSSDAIRKKRVEDVL----LRDLALTRIGgnlvkGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 800951443 465 MRHALVMALQSF----DGAMVTVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:cd03234 178 TALNLVSTLSQLarrnRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
32-224 |
1.30e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 52.75 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 32 LVGSNGCGKSSLFALLKGELQLDAGNAKVpKEWSIASVKQEtpalAITALE----YVLQgnpDY-------------YAL 94
Cdd:COG2884 33 LTGPSGAGKSTLLKLLYGEERPTSGQVLV-NGQDLSRLKRR----EIPYLRrrigVVFQ---DFrllpdrtvyenvaLPL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 95 RCQlkqaeqqgdGETQAQVHQQL-ELMKGYSIEAKAGELLHGLgfsntqidyavsdfSGGWRMRLNLAQALIRDADLLLL 173
Cdd:COG2884 105 RVT---------GKSRKEIRRRVrEVLDLVGLSDKAKALPHEL--------------SGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 800951443 174 DEPTNHLDLDAVYW----LERFLRsyAGTLVLI-SHDREFLDAVVGEIWHIDQQQI 224
Cdd:COG2884 162 DEPTGNLDPETSWEimelLEEINR--RGTTVLIaTHDLELVDRMPKRVLELEDGRL 215
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
12-205 |
1.34e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.45 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 12 GPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLK-------GELQLDA------GNAKVPKEWSIASVKQETPAlAI 78
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSrlmtpahGHVWLDGehiqhyASKEVARRIGLLAQNATTPG-DI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 79 TALEYVLQGNPDYYALRCQLKQAEQqgDGETQAqvhqqlelMKGYSIEAKAGEllhglgfsntqidyAVSDFSGGWRMRL 158
Cdd:PRK10253 97 TVQELVARGRYPHQPLFTRWRKEDE--EAVTKA--------MQATGITHLADQ--------------SVDTLSGGQRQRA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 800951443 159 NLAQALIRDADLLLLDEPTNHLD----LDAVYWLERFLRSYAGTLVLISHD 205
Cdd:PRK10253 153 WIAMVLAQETAIMLLDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHD 203
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
311-487 |
1.41e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 54.18 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 311 PLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVF-------------------F 371
Cdd:PRK09452 13 PLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMldgqdithvpaenrhvntvF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 372 HQ---------------GLKVGYFAQHQLEALDLQASPVTHLQRLNPQASEQslrdflggfafigdkaldpvapFSGGEK 436
Cdd:PRK09452 93 QSyalfphmtvfenvafGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQ----------------------LSGGQQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 437 ARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVM---ALQSFDG-AMVTVSHDR 487
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNelkALQRKLGiTFVFVTHDQ 205
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-205 |
1.56e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 52.78 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATlFPQHKV-GLVGSNGCGKSSLFALLKGELQLDAGNAKVpKEWSIASVKQETPA--LA 77
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLT-IPKGGItALIGPNGAGKSTLLSMISRLLPPDSGEVLV-DGLDVATTPSRELAkrLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 78 ItaleyvlqgnpdyyalrcqLKQAEQ-------------------QG--DGETQAQVHQQLELMkgySIEAKAGELLHGL 136
Cdd:COG4604 79 I-------------------LRQENHinsrltvrelvafgrfpysKGrlTAEDREIIDEAIAYL---DLEDLADRYLDEL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 800951443 137 gfsntqidyavsdfSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG----TLVLISHD 205
Cdd:COG4604 137 --------------SGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADelgkTVVIVLHD 195
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
326-501 |
1.67e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.47 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 326 TILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVF-----FHQ----------GLKVGYFAQ-------- 382
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlvgqpLHQmdeearaklrAKHVGFVFQsfmliptl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 383 HQLEALDLQASpvthLQRLNPQASEQSLRDFLGGFAfIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLD 462
Cdd:PRK10584 104 NALENVELPAL----LRGESSRQSRNGAKALLEQLG-LGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 800951443 463 LEMRHALVMALQS----FDGAMVTVSHDRHLLKNTADEFYLVD 501
Cdd:PRK10584 179 RQTGDKIADLLFSlnreHGTTLILVTHDLQLAARCDRRLRLVN 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
323-549 |
1.69e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.57 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVffHQGLKVGYFAQHQLEALDLQASPVTHLQRLN 402
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV--HMKGSVAYVPQQAWIQNDSLRENILFGKALN 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 403 PQASEQSLR--------DFL--GGFAFIGDKALDpvapFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMA 472
Cdd:TIGR00957 727 EKYYQQVLEacallpdlEILpsGDRTEIGEKGVN----LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEH 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 473 LQSFDGAM-----VTVSHDRHLLKNTaDEFYLVDSGEVRQFG-----YDLD-AYYQWL-TKANQEQKQTQVEPDKANSSA 540
Cdd:TIGR00957 803 VIGPEGVLknktrILVTHGISYLPQV-DVIIVMSGGKISEMGsyqelLQRDgAFAEFLrTYAPDEQQGHLEDSWTALVSG 881
|
....*....
gi 800951443 541 NRKEQKRKE 549
Cdd:TIGR00957 882 EGKEAKLIE 890
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-224 |
1.93e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 52.40 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLF----ALLK---GELQLDAGNAKVPKEwSIASVKQET 73
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrcinKLEEitsGDLIVDGLKVNDPKV-DERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 74 ----------PALaiTALEYVLQGnpdyyalrcqlkqaEQQGDGETQAQVHQQlelmkgysieakAGELLHGLGFSNTQI 143
Cdd:PRK09493 80 gmvfqqfylfPHL--TALENVMFG--------------PLRVRGASKEEAEKQ------------ARELLAKVGLAERAH 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 144 DYAvSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG---TLVLISHDREFLDAVVGEIWHID 220
Cdd:PRK09493 132 HYP-SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFID 210
|
....
gi 800951443 221 QQQI 224
Cdd:PRK09493 211 KGRI 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
310-509 |
1.98e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 52.83 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 310 NPLIALDGAQAGY-GDTTI-LHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF---------------H 372
Cdd:PRK13648 5 NSIIVFKNVSFQYqSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYnnqaitddnfeklrkH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 373 QGLK--------VGYFAQHQLE-ALDLQASPVTHLQRLNPQASEQSlrDFLggfafigDKALDPVAPFSGGEKARLVLAM 443
Cdd:PRK13648 85 IGIVfqnpdnqfVGSIVKYDVAfGLENHAVPYDEMHRRVSEALKQV--DML-------ERADYEPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800951443 444 LVYQKPNLLLLDEPTNHLDLEMRHALVMALQSF----DGAMVTVSHDrhlLKNTADEFYLV--DSGEVRQFG 509
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITHD---LSEAMEADHVIvmNKGTVYKEG 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
326-509 |
1.99e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.44 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 326 TILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF-------------HQGL------KVGYFAQ---- 382
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsqQKGLirqlrqHVGFVFQnfnl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 383 --HQLEALDLQASPVThLQRLNPQASEQSLRDFLGGFAFIGDKALDPvAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNH 460
Cdd:PRK11264 97 fpHRTVLENIIEGPVI-VKGEPKEEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 800951443 461 LDLEMRH---ALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:PRK11264 175 LDPELVGevlNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
30-211 |
2.04e-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: 52.02 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 30 VGLVGSNGCGKSSLFALLKGELQLDAG-------------NAKVPK-EWSIASVKQETPALA-ITALEYVLqgnpdyYAL 94
Cdd:cd03292 30 VFLVGPSGAGKSTLLKLIYKEELPTSGtirvngqdvsdlrGRAIPYlRRKIGVVFQDFRLLPdRNVYENVA------FAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 95 RCQlkqaeQQGDGETQAQVHQQLELmkgysieakagellhgLGFSNTQIDYAvSDFSGGWRMRLNLAQALIRDADLLLLD 174
Cdd:cd03292 104 EVT-----GVPPREIRKRVPAALEL----------------VGLSHKHRALP-AELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 800951443 175 EPTNHLDLDAVYWLERFLRSY--AGTLVLIS-HDREFLDA 211
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKInkAGTTVVVAtHAKELVDT 201
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
328-515 |
2.43e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.82 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 328 LHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF-------------------HQGLkVGYFAQHQL--E 386
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVddtlitstsknkdikqirkKVGL-VFQFPESQLfeE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 387 AL--DLQASPVTHlqRLNPQASEQSLRDFLggfAFIG-DKALDPVAPF--SGGEKARLVLAMLVYQKPNLLLLDEPTNHL 461
Cdd:PRK13649 102 TVlkDVAFGPQNF--GVSQEEAEALAREKL---ALVGiSESLFEKNPFelSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 462 DLEMRHALVMALQSFDGAMVTVSHDRHLL---KNTADEFYLVDSGEVRQFGYDLDAY 515
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLVTHLMddvANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-205 |
2.48e-07 |
|
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: 51.87 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKV---------PKEWSIASVKQE 72
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIggrdvtdlpPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 73 tpalaitaleYVLQGNPDYYA-LRCQLKQAEQQGDgETQAQVHQQLELMKgysIEakagELLhglgfsntqiDYAVSDFS 151
Cdd:cd03301 81 ----------YALYPHMTVYDnIAFGLKLRKVPKD-EIDERVREVAELLQ---IE----HLL----------DRKPKQLS 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 152 GGWRMRLNLAQALIRDADLLLLDEPTNHLD----LDAVYWLERFLRSYAGTLVLISHD 205
Cdd:cd03301 133 GGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
337-487 |
2.57e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 53.81 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 337 PGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH---------QGLK--VGYFAQhqlEALDLQASPVTHLQRLNPQA 405
Cdd:PRK13657 360 PGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDgtdirtvtrASLRrnIAVVFQ---DAGLFNRSIEDNIRVGRPDA 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 406 SEQSLRDFLGGFA---FIGDKA--LDPVA-----PFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQs 475
Cdd:PRK13657 437 TDEEMRAAAERAQahdFIERKPdgYDTVVgergrQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALD- 515
|
170
....*....|..
gi 800951443 476 fdgamvTVSHDR 487
Cdd:PRK13657 516 ------ELMKGR 521
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
30-212 |
2.78e-07 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 52.05 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 30 VGLVGSNGCGKSSLFALLKGELQLDAGnakvpkewSI----ASVKQETPALAI-----------------TALEYVLqgn 88
Cdd:cd03219 29 HGLIGPNGAGKTTLFNLISGFLRPTSG--------SVlfdgEDITGLPPHEIArlgigrtfqiprlfpelTVLENVM--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 89 pdyyaLRCQLKQAEQQGDGETQAQVHQqlelmkgysIEAKAGELLHGLGFSNtQIDYAVSDFSGGWRMRLNLAQALIRDA 168
Cdd:cd03219 98 -----VAAQARTGSGLLLARARREERE---------ARERAEELLERVGLAD-LADRPAGELSYGQQRRLEIARALATDP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 800951443 169 DLLLLDEPT---NHLDLDAVYWLERFLRSYAGTLVLISHDrefLDAV 212
Cdd:cd03219 163 KLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHD---MDVV 206
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
17-207 |
2.85e-07 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 52.05 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGN----------------AKVPKEwSIASVKQE---TPALa 77
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTvrlagqdlfaldedarARLRAR-HVGFVFQSfqlLPTL- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 78 iTALEYVLQgnPdyyalrcqlkqAEQQGDGETQAQVHQQLELMkgysieakagellhGLGfsnTQIDYAVSDFSGGWRMR 157
Cdd:COG4181 106 -TALENVML--P-----------LELAGRRDARARARALLERV--------------GLG---HRLDHYPAQLSGGEQQR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 158 LNLAQALIRDADLLLLDEPTNHLD-------LDAvywLERFLRSYAGTLVLISHDRE 207
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDaatgeqiIDL---LFELNRERGTTLVLVTHDPA 208
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
12-206 |
2.95e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 52.55 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 12 GPKCLLKNANATLFPQHKVGLVGSNGCGKSSLF-ALLK-----GELQLDAGNakvpkeWSIASVKQETPALA-ITALEYV 84
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsAFLRllnteGDIQIDGVS------WNSVPLQKWRKAFGvIPQKVFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 85 LQGnpdyyALRCQLKQAEQQGDGETQaQVHQQLELMKgySIEAKAGELlhglgfsNTQIDYAVSDFSGGWRMRLNLAQAL 164
Cdd:cd03289 89 FSG-----TFRKNLDPYGKWSDEEIW-KVAEEVGLKS--VIEQFPGQL-------DFVLVDGGCVLSHGHKQLMCLARSV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 800951443 165 IRDADLLLLDEPTNHLDLDAVYWLERFLR-SYAGTLVLISHDR 206
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKqAFADCTVILSEHR 196
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
324-509 |
3.15e-07 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 51.77 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 324 DTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF-HQGLK----------VGY-------FAQHQL 385
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIRdlnlrwlrsqIGLvsqepvlFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 386 EALDLQASPVTHLQRLnpQASEQS-LRDFLGGFA-----FIGDKAldpvAPFSGGEKARLVLAMLVYQKPNLLLLDEPTN 459
Cdd:cd03249 95 ENIRYGKPDATDEEVE--EAAKKAnIHDFIMSLPdgydtLVGERG----SQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 460 HLDLEMRHALVMALqsfDGAM-----VTVSHDRHLLKNtADEFYLVDSGEVRQFG 509
Cdd:cd03249 169 ALDAESEKLVQEAL---DRAMkgrttIVIAHRLSTIRN-ADLIAVLQNGQVVEQG 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
322-509 |
3.69e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.89 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQ-----------GLKVgyFAQHQLEAL-- 388
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgQLKV--ADKNQLRLLrt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 389 -------------------DLQASPVTHLQRLNPQASEQSLRdFLGGFAFIGDKALDPVAPFSGGEKARLVLAMLVYQKP 449
Cdd:PRK10619 93 rltmvfqhfnlwshmtvleNVMEAPIQVLGLSKQEARERAVK-YLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 800951443 450 NLLLLDEPTNHLDLEMRHALVMALQSF--DG-AMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLaeEGkTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
312-506 |
3.91e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 51.91 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 312 LIALDGAQAGYGD-TTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVGYFAQHQ----LE 386
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV-SGIDTGDFSKLQgirkLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 387 ALDLQASPVTHLQR--------------LNP----QASEQSLRDF-LGGFAFIGDKALdpvapfSGGEKARLVLAMLVYQ 447
Cdd:PRK13644 80 GIVFQNPETQFVGRtveedlafgpenlcLPPieirKRVDRALAEIgLEKYRHRSPKTL------SGGQGQCVALAGILTM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 800951443 448 KPNLLLLDEPTNHLDLEMRHALVMALQSFDGAMVTVSHDRHLLK--NTADEFYLVDSGEVR 506
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEelHDADRIIVMDRGKIV 214
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
331-509 |
3.93e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 53.31 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 331 IKLNLVPGSRIALLGRNGAGKSTLIKLLAQELApqagdvffHQG-LKVGyfaQHQLEALDLQaspvTHLQRL-----NPQ 404
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP--------YQGsLKIN---GIELRELDPE----SWRKHLswvgqNPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 405 ASEQSLRD-FLGGFAFIGDKALDPV-------------------------APFSGGEKARLVLAMLVYQKPNLLLLDEPT 458
Cdd:PRK11174 434 LPHGTLRDnVLLGNPDASDEQLQQAlenawvseflpllpqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 459 NHLDLEMRHALVMALQSFDGA----MVTvshdrHLLKNTA--DEFYLVDSGEVRQFG 509
Cdd:PRK11174 514 ASLDAHSEQLVMQALNAASRRqttlMVT-----HQLEDLAqwDQIWVMQDGQIVQQG 565
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-181 |
4.30e-07 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 52.80 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAkvpkewsiasvkqetpalaitaleyVLQGNP--DYY-- 92
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI-------------------------LLDGHDlaDYTla 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 93 ALRCQLKQAEQQ--------------GDGET--QAQVHQQLElmkgysiEAKAGELLHGL--GFsNTQIDYAVSDFSGGW 154
Cdd:TIGR02203 403 SLRRQVALVSQDvvlfndtianniayGRTEQadRAEIERALA-------AAYAQDFVDKLplGL-DTPIGENGVLLSGGQ 474
|
170 180
....*....|....*....|....*..
gi 800951443 155 RMRLNLAQALIRDADLLLLDEPTNHLD 181
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALD 501
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
19-216 |
4.31e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 52.53 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 19 NANATLFPQHKVGLVGSNGCGKSSLFALL-------KGELQLDAGN-AKVPKEWSIASVKQETPAL--AITALEYVLQGn 88
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLagfeqptAGQIMLDGVDlSHVPPYQRPINMMFQSYALfpHMTVEQNIAFG- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 89 pdyyalrcqLKQaEQQGDGETQAQVHQQLELMKgysIEAKAGELLHGLgfsntqidyavsdfSGGWRMRLNLAQALIRDA 168
Cdd:PRK11607 116 ---------LKQ-DKLPKAEIASRVNEMLGLVH---MQEFAKRKPHQL--------------SGGQRQRVALARSLAKRP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 800951443 169 DLLLLDEPTNHLD--------LDAVYWLERFlrsyAGTLVLISHDREFLDAVVGEI 216
Cdd:PRK11607 169 KLLLLDEPMGALDkklrdrmqLEVVDILERV----GVTCVMVTHDQEEAMTMAGRI 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
323-462 |
4.52e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.96 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVF------------FHQGLkvgYFAQHQLeALDL 390
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgepirrqrdeYHQDL---LYLGHQP-GIKT 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 391 QASPVTHL---QRLNPQASEQSLRDFLGGFAFIGDKALdPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLD 462
Cdd:PRK13538 88 ELTALENLrfyQRLHGPGDDEALWEALAQVGLAGFEDV-PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
312-504 |
4.64e-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: 52.90 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 312 LIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLA----------------QELAPQ-------AGD 368
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSgvyphgtwdgeiywsgSPLKASnirdterAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 369 VFFHQGLKVgyfaQHQLEALD--LQASPVTHL-QRLNPQASEQSLRDFLGGFAFIGDKALDPVAPFSGGEKARLVLAMLV 445
Cdd:TIGR02633 81 VIIHQELTL----VPELSVAEniFLGNEITLPgGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800951443 446 YQKPNLLLLDEPTNHL---DLEMRHALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGE 504
Cdd:TIGR02633 157 NKQARLLILDEPSSSLtekETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
322-457 |
5.06e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 51.18 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF----------HQ----GLkvGYFAQH---- 383
Cdd:COG1137 13 YGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLdgedithlpmHKrarlGI--GYLPQEasif 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 384 -QLEALD-----LQASPVTHLQRLnpQASEQSLRDFlgGFAFIGDK---ALdpvapfSGGEKARL----VLAMlvyqKPN 450
Cdd:COG1137 91 rKLTVEDnilavLELRKLSKKERE--ERLEELLEEF--GITHLRKSkaySL------SGGERRRVeiarALAT----NPK 156
|
....*..
gi 800951443 451 LLLLDEP 457
Cdd:COG1137 157 FILLDEP 163
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
323-548 |
5.19e-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: 52.99 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQeLAPQAGDVFFHQGLKVGYFAQHQLEALDLQASPV-----TH 397
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLR-LLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVfifsgTF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 398 LQRLNPQ-----------ASEQSLRDFLGGFAFIGDKAL-DPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEM 465
Cdd:TIGR01271 1309 RKNLDPYeqwsdeeiwkvAEEVGLKSVIEQFPDKLDFVLvDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVT 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 466 RHALVMAL-QSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFgydlDAYYQWLTKANQ-EQKQTQVEPDKANSSANRK 543
Cdd:TIGR01271 1389 LQIIRKTLkQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQY----DSIQKLLNETSLfKQAMSAADRLKLFPLHRRN 1464
|
....*
gi 800951443 544 EQKRK 548
Cdd:TIGR01271 1465 SSKRK 1469
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-182 |
5.23e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 51.31 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAG----NAKVPKEWS-------IASV 69
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGevrlNGRPLADWSpaelarrRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 70 KQETP-ALAITALEYVLQGNPDYyalrcqlkqaeQQGDGETQAQVHQQLELMkgySIEAKAGELLHGLgfsntqidyavs 148
Cdd:PRK13548 82 PQHSSlSFPFTVEEVVAMGRAPH-----------GLSRAEDDALVAAALAQV---DLAHLAGRDYPQL------------ 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 800951443 149 dfSGGWRMRLNLAQAL--IRDAD----LLLLDEPTNHLDL 182
Cdd:PRK13548 136 --SGGEQQRVQLARVLaqLWEPDgpprWLLLDEPTSALDL 173
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
323-517 |
5.83e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.03 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 GDTTILHSIKLNLVPGSRIALLGRNGAGKS----TLIKLLAQElAPQAGDVFFhQGLKVGYFAQHQLEALDLQ------A 392
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAAN-GRIGGSATF-NGREILNLPEKELNKLRAEqismifQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 393 SPVThlqRLNP---------------------QASEQSLRdflggfafigdkALDPVA-------------PFSGGEKAR 438
Cdd:PRK09473 105 DPMT---SLNPymrvgeqlmevlmlhkgmskaEAFEESVR------------MLDAVKmpearkrmkmyphEFSGGMRQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 439 LVLAMLVYQKPNLLLLDEPTNHLDLEMRhALVMAL-----QSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFGYDLD 513
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQ-AQIMTLlnelkREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
....
gi 800951443 514 AYYQ 517
Cdd:PRK09473 249 VFYQ 252
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
328-536 |
6.09e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.36 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 328 LHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGLKV-----GYFAQH------QLEALDLQASPvT 396
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSViaisaGLSGQLtgieniEFKMLCMGFKR-K 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 397 HLQRLNPQASEqslrdflggFAFIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSF 476
Cdd:PRK13546 119 EIKAMTPKIIE---------FSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 800951443 477 DGAMVT---VSHDRHLLKNTADEFYLVDSGEVRQFGyDLD----AYYQWLT----KANQEQKQTQVEPDKA 536
Cdd:PRK13546 190 KEQNKTiffVSHNLGQVRQFCTKIAWIEGGKLKDYG-ELDdvlpKYEAFLNdfkkKSKAEQKEFRNKLDES 259
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-182 |
7.17e-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: 52.61 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 5 TDIELLRGPkcLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGnaKVPKEWSIASVKQETPALAITALEYV 84
Cdd:TIGR01271 432 SNFSLYVTP--VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG--KIKHSGRISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 85 LQG-NPDYYALRCQLKQAEQQGDGETQAQvHQQLELMKGysieakagellhglGFSntqidyavsdFSGGWRMRLNLAQA 163
Cdd:TIGR01271 508 IFGlSYDEYRYTSVIKACQLEEDIALFPE-KDKTVLGEG--------------GIT----------LSGGQRARISLARA 562
|
170
....*....|....*....
gi 800951443 164 LIRDADLLLLDEPTNHLDL 182
Cdd:TIGR01271 563 VYKDADLYLLDSPFTHLDV 581
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
335-486 |
7.32e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 335 LVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDvffHQG-------LKvgYFAQHQLEaldlqaspvTHLQRL------ 401
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD---YEEepswdevLK--RFRGTELQ---------NYFKKLyngeik 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 402 ---NPQASEQ-------SLRDFLGGFAFIG-----------DKALD-PVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTN 459
Cdd:PRK13409 162 vvhKPQYVDLipkvfkgKVRELLKKVDERGkldevverlglENILDrDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180
....*....|....*....|....*....
gi 800951443 460 HLDLEMRHALVMALQSF--DGAMVTVSHD 486
Cdd:PRK13409 242 YLDIRQRLNVARLIRELaeGKYVLVVEHD 270
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
306-369 |
7.89e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.98 E-value: 7.89e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 800951443 306 DALPNPLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDV 369
Cdd:PRK15439 5 DTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL 68
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
338-491 |
8.04e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.06 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 338 GSRIALLGRNGAGKSTLIKLLAqELAP-QAGDVFFHQGLKVGYFAQHQLEAL----DLQASPVTHLQRLNPQASEQSLRD 412
Cdd:TIGR00954 478 GNNLLICGPNGCGKSSLFRILG-ELWPvYGGRLTKPAKGKLFYVPQRPYMTLgtlrDQIIYPDSSEDMKRRGLSDKDLEQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 413 FL------------GGFAFIGD-KALdpvapFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSFDGA 479
Cdd:TIGR00954 557 ILdnvqlthilereGGWSAVQDwMDV-----LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGIT 631
|
170
....*....|..
gi 800951443 480 MVTVSHDRHLLK 491
Cdd:TIGR00954 632 LFSVSHRKSLWK 643
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
323-508 |
8.29e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 51.01 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQaGDVFFHQGLKVGYFAQHQLEALDLQASPV-----TH 397
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVfifsgTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 398 LQRLNPQ-----------ASEQSLRDFLGGFAFIGDKAL-DPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEM 465
Cdd:cd03289 94 RKNLDPYgkwsdeeiwkvAEEVGLKSVIEQFPGQLDFVLvDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 800951443 466 RHALVMAL-QSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQF 508
Cdd:cd03289 174 YQVIRKTLkQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQY 217
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
337-486 |
8.34e-07 |
|
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: 52.09 E-value: 8.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 337 PGSRIALLGRNGAGKSTLIKLLAQELAPQAGDvFFHQG-----LKvgYFAQHQLEaldlqaspvTHLQRL---------N 402
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGD-YDEEPswdevLK--RFRGTELQ---------DYFKKLangeikvahK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 403 PQASEQ-------SLRDFL------GGFAFIGDK-ALDP-----VAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDL 463
Cdd:COG1245 166 PQYVDLipkvfkgTVRELLekvderGKLDELAEKlGLENildrdISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180
....*....|....*....|....*.
gi 800951443 464 EMRHALVMALQSF---DGAMVTVSHD 486
Cdd:COG1245 246 YQRLNVARLIRELaeeGKYVLVVEHD 271
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-221 |
8.58e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.50 E-value: 8.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSIASVKQET---PALA 77
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLyldTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 78 ITALEYVlqgnpdyyalrcQLKQAEQQGDgetqaqvhqQLELMKgysiEAKAGELLhglgfsntqiDYAVSDFSGGWRMR 157
Cdd:PRK09544 84 LTVNRFL------------RLRPGTKKED---------ILPALK----RVQAGHLI----------DAPMQKLSGGETQR 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 158 LNLAQALIRDADLLLLDEPTNHLDLD---AVYWLERFLRSYAGTLVL-ISHDREFLDAVVGEIWHIDQ 221
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVDVNgqvALYDLIDQLRRELDCAVLmVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
311-506 |
8.72e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 50.81 E-value: 8.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 311 PLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQ--ELAPQA---GDV-FFHQGLkvgYFAQHQ 384
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRmnELESEVrveGRVeFFNQNI---YERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 385 LEALDLQASPVTHLQRLNPQaseqSLRDFLG-GFAFIG-------------------------DKALDPVAPFSGGEKAR 438
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFPM----SVYDNVAyGVKIVGwrpkleiddivesalkdadlwdeikHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800951443 439 LVLAMLVYQKPNLLLLDEPTNHLD----LEMRHALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVR 506
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
311-369 |
9.43e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.71 E-value: 9.43e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 800951443 311 PLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDV 369
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI 62
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
325-509 |
1.11e-06 |
|
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: 50.63 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 325 TTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFfHQGlKVGYFAQHQL-------EALDLQASPVTH 397
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-HSG-RISFSSQFSWimpgtikENIIFGVSYDEY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 398 LQRLNPQASEqsLRDFLGGFAfigDKALDPVAP----FSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDL----EMRHAL 469
Cdd:cd03291 128 RYKSVVKACQ--LEEDITKFP---EKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVftekEIFESC 202
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 800951443 470 VMALQSFDGAMVTVSHDRHLLKntADEFYLVDSGEVRQFG 509
Cdd:cd03291 203 VCKLMANKTRILVTSKMEHLKK--ADKILILHEGSSYFYG 240
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-211 |
1.15e-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: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 16 LLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGEL--QLDAGNAKVPK-EWSiasvkQETPAL-AITALEYVLQgnpdy 91
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDnQFG-----REASLIdAIGRKGDFKD----- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 92 yalrcqlkqaeqqgdgetqaqvhqqlelmkgysieakAGELLHGLGFSNTQIDYA-VSDFSGGWRMRLNLAQALIRDADL 170
Cdd:COG2401 115 -------------------------------------AVELLNAVGLSDAVLWLRrFKELSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 800951443 171 LLLDEPTNHLDLD----AVYWLERFLRSYAGTLVLISHDREFLDA 211
Cdd:COG2401 158 LVIDEFCSHLDRQtakrVARNLQKLARRAGITLVVATHHYDVIDD 202
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-206 |
1.16e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.83 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLF-ALLK-----GELQLDAgnakvpKEWSIASVKQETP 74
Cdd:TIGR01271 1219 DVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLsALLRllsteGEIQIDG------VSWNSVTLQTWRK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 75 ALAITALE-YVLQGNpdyyaLRCQLKQAEQQGDGETQaQVHQQLELMKgySIEAKAGELlhglgfsntqiDYAVSD---- 149
Cdd:TIGR01271 1293 AFGVIPQKvFIFSGT-----FRKNLDPYEQWSDEEIW-KVAEEVGLKS--VIEQFPDKL-----------DFVLVDggyv 1353
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 150 FSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLR-SYAGTLVLISHDR 206
Cdd:TIGR01271 1354 LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKqSFSNCTVILSEHR 1411
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
336-509 |
1.16e-06 |
|
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: 50.87 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 336 VPGSRI-ALLGRNGAGKSTLIKLLAQELAPQAG------DVFFHQGLK---------VGY-FAQHQLEAldlqaspvtHL 398
Cdd:COG4148 22 LPGRGVtALFGPSGSGKTTLLRAIAGLERPDSGrirlggEVLQDSARGiflpphrrrIGYvFQEARLFP---------HL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 399 ---------QRLNPQASEQSLRD----FLGgfafIGDKaLD-PVAPFSGGEKARLVL--AMLVyqKPNLLLLDEPTNHLD 462
Cdd:COG4148 93 svrgnllygRKRAPRAERRISFDevveLLG----IGHL-LDrRPATLSGGERQRVAIgrALLS--SPRLLLMDEPLAALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 463 LEMRHALVMAL----QSFDGAMVTVSHD----RHLlkntADEFYLVDSGEVRQFG 509
Cdd:COG4148 166 LARKAEILPYLerlrDELDIPILYVSHSldevARL----ADHVVLLEQGRVVASG 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-212 |
1.23e-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: 51.94 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 26 PQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSIASVKQETPALA----ITALEYVLQGNPDYYaLRCQLKQA 101
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGycpqFDAIDDLLTGREHLY-LYARLRGV 2042
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 102 EQQgdgetqaqvhqQLELMKGYSIEAkagellhgLGFSnTQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD 181
Cdd:TIGR01257 2043 PAE-----------EIEKVANWSIQS--------LGLS-LYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
170 180 190
....*....|....*....|....*....|....
gi 800951443 182 LDAVYWLERFLRSY---AGTLVLISHDREFLDAV 212
Cdd:TIGR01257 2103 PQARRMLWNTIVSIireGRAVVLTSHSMEECEAL 2136
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
312-500 |
1.31e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.15 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 312 LIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVGYFAQHQLEAL--- 388
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILF-DGENIPAMSRSRLYTVrkr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 389 ------------DLQ-----ASPVTHLQRLNPQASEQSLRDFLGGFAFIGDKALDPvAPFSGGEKARLVLAMLVYQKPNL 451
Cdd:PRK11831 86 msmlfqsgalftDMNvfdnvAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMP-SELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 800951443 452 LLLDEPTNHLDLEMRHALVMALQSFDGAM----VTVSHDRHLLKNTADEFYLV 500
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALgvtcVVVSHDVPEVLSIADHAYIV 217
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
25-205 |
1.37e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 50.17 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 25 FPQHKV-GLVGSNGCGKSSLFALL-------KGELQLdagNAKVPKEWS-------IASVKQETPAL-AITALEYVLQGN 88
Cdd:PRK10575 34 FPAGKVtGLIGHNGSGKSTLLKMLgrhqppsEGEILL---DAQPLESWSskafarkVAYLPQQLPAAeGMTVRELVAIGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 89 -PDYYALrcqlkqaeqqgdGETQAQVHQQLElmkgysiEAKAgelLHGLG-FSNTQIDyavsDFSGGWRMRLNLAQALIR 166
Cdd:PRK10575 111 yPWHGAL------------GRFGAADREKVE-------EAIS---LVGLKpLAHRLVD----SLSGGERQRAWIAMLVAQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 800951443 167 DADLLLLDEPTNHLDL----DAVYWLERFLRSYAGTLVLISHD 205
Cdd:PRK10575 165 DSRCLLLDEPTSALDIahqvDVLALVHRLSQERGLTVIAVLHD 207
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-204 |
1.42e-06 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 49.79 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 16 LLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGN--------AKVPKEW---SIASVKQETPALAITALEYV 84
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRvlvdghdlALADPAWlrrQVGVVLQENVLFNRSIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 85 LQGNPDyyalrcqlKQAEQQGDGETQAQVHQ-QLELMKGYsiEAKAGELLHGLgfsntqidyavsdfSGGWRMRLNLAQA 163
Cdd:cd03252 97 ALADPG--------MSMERVIEAAKLAGAHDfISELPEGY--DTIVGEQGAGL--------------SGGQRQRIAIARA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 800951443 164 LIRDADLLLLDEPTNHLDLDAVYWLERFLRSY-AG-TLVLISH 204
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDIcAGrTVIIIAH 195
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-237 |
1.49e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 51.25 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAG-----NAKVPK----EW-SIASVKQETPAL-AITALEYVL 85
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGdirfhDIPLTKlqldSWrSRLAVVSQTPFLfSDTVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 86 QGNPDyyALRCQLKQAEQQgdgetqAQVHQQ-LELMKGYSIE-AKAGELLhglgfsntqidyavsdfSGGWRMRLNLAQA 163
Cdd:PRK10789 411 LGRPD--ATQQEIEHVARL------ASVHDDiLRLPQGYDTEvGERGVML-----------------SGGQKQRISIARA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 164 LIRDADLLLLDEPTNHLDLDAVYWLERFLRSY-AGTLVLISHDRefLDAVVG--EIWHIDQQQInVYKGNYSQFERQ 237
Cdd:PRK10789 466 LLLNAEILILDDALSAVDGRTEHQILHNLRQWgEGRTVIISAHR--LSALTEasEILVMQHGHI-AQRGNHDQLAQQ 539
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
325-509 |
1.57e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.45 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 325 TTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFfHQGlKVGYFAQHQ--------------LEALDL 390
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-HSG-RISFSPQTSwimpgtikdniifgLSYDEY 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 391 QASPVTHLQRLNPQASEQSLRDFLggfaFIGDKALDpvapFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDL----EMR 466
Cdd:TIGR01271 517 RYTSVIKACQLEEDIALFPEKDKT----VLGEGGIT----LSGGQRARISLARAVYKDADLYLLDSPFTHLDVvtekEIF 588
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 800951443 467 HALVMALQSFDGAMVTVSHDRHLLKntADEFYLVDSGEVRQFG 509
Cdd:TIGR01271 589 ESCLCKLMSNKTRILVTSKLEHLKK--ADKILLLHEGVCYFYG 629
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-219 |
1.60e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.17 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGnakvpkewsiasvkqetpalaitalEYVLQGNPdyyalrC 96
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSG-------------------------EILLDGEP------V 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 97 QL---KQAEQQGdgetQAQVHQQL----------------ELMKGYSI-----EAKAGELLHGLGFSntqIDYA--VSDF 150
Cdd:COG1129 69 RFrspRDAQAAG----IAIIHQELnlvpnlsvaeniflgrEPRRGGLIdwramRRRARELLARLGLD---IDPDtpVGDL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800951443 151 SGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG---TLVLISHdreFLDavvgEIWHI 219
Cdd:COG1129 142 SVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAqgvAIIYISH---RLD----EVFEI 206
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-205 |
1.67e-06 |
|
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: 50.50 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 20 ANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKE-WSIASVKQETPALAiTALEYVLQGN---PdYYALR 95
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtLFDSRKGIFLPPEK-RRIGYVFQEArlfP-HLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 96 CQLKQAEQQGDGEtQAQVHqqlelmkgysiEAKAGELLhGLGfsnTQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDE 175
Cdd:TIGR02142 94 GNLRYGMKRARPS-ERRIS-----------FERVIELL-GIG---HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190
....*....|....*....|....*....|....
gi 800951443 176 PTNHLDLDAVY----WLERFLRSYAGTLVLISHD 205
Cdd:TIGR02142 158 PLAALDDPRKYeilpYLERLHAEFGIPILYVSHS 191
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
322-457 |
1.82e-06 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 49.58 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF----------HQ--GLKVGYFAQH-----Q 384
Cdd:TIGR04406 11 YKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIdgqdithlpmHEraRLGIGYLPQEasifrK 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 385 LEALDLQASPVTHLQRLNPQASEQSLRDFLGGF--AFIGDKaldPVAPFSGGEKARLVLAMLVYQKPNLLLLDEP 457
Cdd:TIGR04406 91 LTVEENIMAVLEIRKDLDRAEREERLEALLEEFqiSHLRDN---KAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
329-509 |
2.01e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 50.26 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 329 HSIKLNL-VPGSRI-ALLGRNGAGKSTLIKLLAQELAPQAG------DVFF--HQGL-------KVGYFAQhqlEAldlq 391
Cdd:PRK11144 13 LCLTVNLtLPAQGItAIFGRSGAGKTSLINAISGLTRPQKGrivlngRVLFdaEKGIclppekrRIGYVFQ---DA---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 392 aspvthlqRLNPQAS----------EQSLRDFLGGFAFIGDKALDPVAPF--SGGEKARLVLAMLVYQKPNLLLLDEPTN 459
Cdd:PRK11144 86 --------RLFPHYKvrgnlrygmaKSMVAQFDKIVALLGIEPLLDRYPGslSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 800951443 460 HLDLEMRHALVMALQ----SFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:PRK11144 158 SLDLPRKRELLPYLErlarEINIPILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-216 |
2.18e-06 |
|
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: 49.07 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLfPQH-KVGLVGSNGCGKSSLFALLKGELQLDAGNAKVpkewsiasVKQETPALAITA-LEYVLQGNpDYYAL 94
Cdd:cd03220 38 LKDVSFEV-PRGeRIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV--------RGRVSSLLGLGGgFNPELTGR-ENIYL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 95 RCQLKqaeqqgdGETQAQVHQQLELMKGYSieakagellhGLG-FsntqIDYAVSDFSGGWRMRLNLAQALIRDADLLLL 173
Cdd:cd03220 108 NGRLL-------GLSRKEIDEKIDEIIEFS----------ELGdF----IDLPVKTYSSGMKARLAFAIATALEPDILLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 174 DEptnhldldavyWL------------ERF--LRSYAGTLVLISHD----REFLDAVV----GEI 216
Cdd:cd03220 167 DE-----------VLavgdaafqekcqRRLreLLKQGKTVILVSHDpssiKRLCDRALvlekGKI 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-205 |
2.19e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.54 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNA------KVPKEWSIASvKQETP 74
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdGQLRDLYALS-EAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 75 ALAITALEYVLQGNPDyyALRCQLKQAEQQGDgetqaqvhqqlELM----KGY-SIEAKAGELLHGLGFSNTQIDYAVSD 149
Cdd:PRK11701 85 RLLRTEWGFVHQHPRD--GLRMQVSAGGNIGE-----------RLMavgaRHYgDIRATAGDWLERVEIDAARIDDLPTT 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 150 FSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAGTL----VLISHD 205
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglavVIVTHD 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-224 |
2.22e-06 |
|
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: 49.07 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSL---FALL----KGELQLDAGNAKVPKEwSIASVKQET- 73
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrcINLLeepdSGTIIIDGLKLTDDKK-NINELRQKVg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 74 ---------PALaiTALEYVLqgnpdyYALRCQLKQAEQQGdgetqaqvhqqlelmkgysiEAKAGELLHGLGFSNtQID 144
Cdd:cd03262 80 mvfqqfnlfPHL--TVLENIT------LAPIKVKGMSKAEA--------------------EERALELLEKVGLAD-KAD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 145 YAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG---TLVLISHDREFLDAVVGEIWHIDQ 221
Cdd:cd03262 131 AYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEegmTMVVVTHEMGFAREVADRVIFMDD 210
|
...
gi 800951443 222 QQI 224
Cdd:cd03262 211 GRI 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-181 |
2.58e-06 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 49.48 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIEL----LRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGnakvpkewsiasvkqetpal 76
Cdd:COG4525 3 MLTVRHVSVrypgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSG-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 77 aitalEYVLQGNPdyyalrcqlkqaeQQGDGETQAQVHQQLELM---------------KGYS---IEAKAGELLHGLGF 138
Cdd:COG4525 63 -----EITLDGVP-------------VTGPGADRGVVFQKDALLpwlnvldnvafglrlRGVPkaeRRARAEELLALVGL 124
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 800951443 139 SNtQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD 181
Cdd:COG4525 125 AD-FARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-207 |
2.82e-06 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 48.63 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALL----------KGELQLDagnakvpkEWSIASVK 70
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtlspafsaSGEVLLN--------GRRLTALP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 71 QETPALAI---TALEY----VLQGNPdyYALRCQLKQAEQQgdgetqAQVHQQLElmkgysieaKAGelLHGLGfsntqi 143
Cdd:COG4136 73 AEQRRIGIlfqDDLLFphlsVGENLA--FALPPTIGRAQRR------ARVEQALE---------EAG--LAGFA------ 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 144 DYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERF----LRSYAGTLVLISHDRE 207
Cdd:COG4136 128 DRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDEE 195
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
324-462 |
2.86e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 49.28 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 324 DTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGL--------------KVGYFAQ---HQL- 385
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIII-DGVditdkkvklsdirkKVGLVFQypeYQLf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 386 -EAL--DLQASPvthlQRLNPQASEQSLR-----DFLG-GFAFIGDKAldpvaPF--SGGEKARLVLAMLVYQKPNLLLL 454
Cdd:PRK13637 98 eETIekDIAFGP----INLGLSEEEIENRvkramNIVGlDYEDYKDKS-----PFelSGGQKRRVAIAGVVAMEPKILIL 168
|
....*...
gi 800951443 455 DEPTNHLD 462
Cdd:PRK13637 169 DEPTAGLD 176
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-224 |
3.26e-06 |
|
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: 50.21 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKG--------------ELQLDAGNAKVPKEWSIASVKQE-TPALAITAL 81
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywsGSPLKASNIRDTERAGIVIIHQElTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 82 EYVLQGNpdyyalrcqlkqaeqqgdgetqaQVHQQLELMKGYSIEAKAGELLHGLGFSNTQIDYAVSDFSGGWRMRLNLA 161
Cdd:TIGR02633 97 ENIFLGN-----------------------EITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 162 QALIRDADLLLLDEPTNHL---DLDAVYWLERFLRSYAGTLVLISHDREFLDAVVGEIWHI-DQQQI 224
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLtekETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIrDGQHV 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
328-484 |
3.27e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 49.24 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 328 LHSIKLNLVPGSRIALLGRNGAGKSTLIKLLA--------------------QELAPQAGDVFFHQGlKVGYFAQ----- 382
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSglitgdksagshiellgrtvQREGRLARDIRKSRA-NTGYIFQqfnlv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 383 HQLEALD------LQASPV--THLQRLNPQASEQSLRDF--LGGFAFigdkALDPVAPFSGGEKARLVLAMLVYQKPNLL 452
Cdd:PRK09984 99 NRLSVLEnvligaLGSTPFwrTCFSWFTREQKQRALQALtrVGMVHF----AHQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190
....*....|....*....|....*....|....*
gi 800951443 453 LLDEPTNHLDLEMRHALVMALQSF---DGAMVTVS 484
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDInqnDGITVVVT 209
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
11-224 |
3.83e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.03 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 11 RGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKE-WSIASVKQETPALAItaleyVLQgNP 89
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpITKENIREVRKFVGL-----VFQ-NP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 90 DYYALRCQLKQAEQQG------DGETqaqvhqqlelmkgysIEAKAGELLHGLGFSNTQiDYAVSDFSGGWRMRLNLAQA 163
Cdd:PRK13652 88 DDQIFSPTVEQDIAFGpinlglDEET---------------VAHRVSSALHMLGLEELR-DRVPHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 164 LIRDADLLLLDEPTNHLDLDAVYWLERFLR----SYAGTLVLISHDREFLDAVVGEIWHIDQQQI 224
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNdlpeTYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-205 |
4.25e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 48.27 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 16 LLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGeLQLDAGNAKVPKEWSIASVKQETPA-LAITALEYVLQGN---PDY 91
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGG-LDTPTSGDVIFNGQPMSKLSSAAKAeLRNQKLGFIYQFHhllPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 92 YALRCQLKQAEQQGDGETQAQvhqqlelmkgysieAKAGELLHGLGFSNtQIDYAVSDFSGGWRMRLNLAQALIRDADLL 171
Cdd:PRK11629 103 TALENVAMPLLIGKKKPAEIN--------------SRALEMLAAVGLEH-RANHRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 800951443 172 LLDEPTNHLDL---DAVYWLERFLRSYAGTLVL-ISHD 205
Cdd:PRK11629 168 LADEPTGNLDArnaDSIFQLLGELNRLQGTAFLvVTHD 205
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
322-516 |
4.85e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 49.26 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLA-----------------QELAPQ---AGDVF----------- 370
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAgleditsgdlfigekrmNDVPPAergVGMVFqsyalyphlsv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 371 -----FhqGLKVGYFAQHQLEaldlqaspvthlQRLNpQASE--QslrdfLGGFAFIGDKALdpvapfSGGEKARLVLAM 443
Cdd:PRK11000 93 aenmsF--GLKLAGAKKEEIN------------QRVN-QVAEvlQ-----LAHLLDRKPKAL------SGGQRQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 444 LVYQKPNLLLLDEPTNHLD----LEMRHALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFGYDLDAYY 516
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYH 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
30-205 |
4.99e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 48.52 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 30 VGLVGSNGCGKSSLFALLKG-----ELQLDAGNAkvpkewSIASVKQETPALAITALEYVLQGNPDYYALrcQLKqaeqq 104
Cdd:PRK11247 41 VAVVGRSGCGKSTLLRLLAGletpsAGELLAGTA------PLAEAREDTRLMFQDARLLPWKKVIDNVGL--GLK----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 105 gdGETQAQVHQQLELMkgySIEAKAGELLHGLgfsntqidyavsdfSGGWRMRLNLAQALIRDADLLLLDEPTNHLD--- 181
Cdd:PRK11247 108 --GQWRDAALQALAAV---GLADRANEWPAAL--------------SGGQKQRVALARALIHRPGLLLLDEPLGALDalt 168
|
170 180
....*....|....*....|....*
gi 800951443 182 -LDAVYWLERFLRSYAGTLVLISHD 205
Cdd:PRK11247 169 rIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-205 |
5.33e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.39 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 32 LVGSNGCGKSSLFALL------KGELQLdagNAKVPKEWSIAS--------VKQETPALAITALEYVlqgnpdyyalrcQ 97
Cdd:PRK03695 27 LVGPNGAGKSTLLARMagllpgSGSIQF---AGQPLEAWSAAElarhraylSQQQTPPFAMPVFQYL------------T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 98 LKQAEQQGDGETQAQVHQQLELMKgysieakageLLHGLGFSNTQIdyavsdfSGGWRMRLNLAQALIR-------DADL 170
Cdd:PRK03695 92 LHQPDKTRTEAVASALNEVAEALG----------LDDKLGRSVNQL-------SGGEWQRVRLAAVVLQvwpdinpAGQL 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 800951443 171 LLLDEPTNHLDLDAVYWLERFLRSYA---GTLVLISHD 205
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
31-204 |
5.63e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.25 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 31 GLVGSNGCGKSSLFALLKGELQLDAGNAKVP-KEWSIASvkqetPALAI-----------------TALEYVLQGNPDYY 92
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPDSGEILIDgKPVRIRS-----PRDAIalgigmvhqhfmlvpnlTVAENIVLGLEPTK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 93 ALRCQLKQAEqqgdgetqAQVHqqlELMKGYsieakagellhGLgfsntQID-YA-VSDFSGGWRMRLNLAQALIRDADL 170
Cdd:COG3845 110 GGRLDRKAAR--------ARIR---ELSERY-----------GL-----DVDpDAkVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 800951443 171 LLLDEPTNHLDLDAVYWLERFLRSYAG---TLVLISH 204
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRRLAAegkSIIFITH 199
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
326-473 |
5.63e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 48.16 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 326 TILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVGYFAQHQ--------------------- 384
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILI-DGKDVTKLPEYKrakyigrvfqdpmmgtapsmt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 385 -LEALDLqASPVTHLQRLNPqASEQSLRDF---------LGgfafIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLL 454
Cdd:COG1101 99 iEENLAL-AYRRGKRRGLRR-GLTKKRRELfrellatlgLG----LENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLL 172
|
170
....*....|....*....
gi 800951443 455 DEPTNHLDLEmRHALVMAL 473
Cdd:COG1101 173 DEHTAALDPK-TAALVLEL 190
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
338-501 |
5.97e-06 |
|
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: 47.18 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 338 GSRIALLGRNGAGKSTLIKLLAQELAPQAGDvffhqglkvgyfaqhqlealdlqaspvTHLQRLNPQASEQSLRdflggf 417
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDN---------------------------DEWDGITPVYKPQYID------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 418 afigdkaldpvapFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSF----DGAMVTVSHDRHLLKNT 493
Cdd:cd03222 72 -------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYL 138
|
....*...
gi 800951443 494 ADEFYLVD 501
Cdd:cd03222 139 SDRIHVFE 146
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
338-486 |
6.05e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 48.19 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 338 GSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGL-----------KVGYFAQH--------QLE---ALDLQASPV 395
Cdd:PRK13650 33 GEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdirhKIGMVFQNpdnqfvgaTVEddvAFGLENKGI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 396 THLQRLNpqASEQSLrDFLGGFAFigdKALDPvAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQS 475
Cdd:PRK13650 113 PHEEMKE--RVNEAL-ELVGMQDF---KEREP-ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKG 185
|
170
....*....|....*
gi 800951443 476 ----FDGAMVTVSHD 486
Cdd:PRK13650 186 irddYQMTVISITHD 200
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-182 |
6.44e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.28 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGEL--QLDAGNAKVPKEWSIASvkqeTPALAI 78
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgGGAPRGARVTGDVTLNG----EPLAAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 79 TAleyvlqgnPDYYALRCQLKQAEQQGdgetQAQVHQQLELMKGYSIEAKAGELLH----------GLGFSNTQIDYAVS 148
Cdd:PRK13547 77 DA--------PRLARLRAVLPQAAQPA----FAFSAREIVLLGRYPHARRAGALTHrdgeiawqalALAGATALVGRDVT 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 800951443 149 DFSGGWRMRLNLAQAL---------IRDADLLLLDEPTNHLDL 182
Cdd:PRK13547 145 TLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-205 |
7.30e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.14 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 11 RGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEwSIASVKQETPALAITALEYVLQGNPD 90
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGE-PLAKLNRAQRKAFRRDIQMVFQDSIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 91 YYALRCQLkqaeqqgdGETQAQVHQQLELMKGYSIEAKAGELLHGLGFSNTQIDYAVSDFSGGWRMRLNLAQALIRDADL 170
Cdd:PRK10419 101 AVNPRKTV--------REIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 800951443 171 LLLDEPTNHLDL----DAVYWLERfLRSYAGT-LVLISHD 205
Cdd:PRK10419 173 LILDEAVSNLDLvlqaGVIRLLKK-LQQQFGTaCLFITHD 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
126-207 |
7.42e-06 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 47.35 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 126 EAKAGELLHGLGFSNtQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD-------LDAvywLERFLRSYAGT 198
Cdd:COG1136 122 RERARELLERVGLGD-RLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDsktgeevLEL---LRELNRELGTT 197
|
....*....
gi 800951443 199 LVLISHDRE 207
Cdd:COG1136 198 IVMVTHDPE 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
142-242 |
7.56e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.04 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 142 QIDYAVsDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYA---GTLVLISHDREFLDAVVGEIWH 218
Cdd:PRK10619 146 QGKYPV-HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIF 224
|
90 100
....*....|....*....|....
gi 800951443 219 IDQQQINVYKGNYSQFERQKAERL 242
Cdd:PRK10619 225 LHQGKIEEEGAPEQLFGNPQSPRL 248
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-207 |
7.91e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.47 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 26 PQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEWSIASVKQETPALAITALEYVLQGN---PDYYALR-CQLKQA 101
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFmliPTLNALEnVELPAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 102 EQqgdGETQAQVHQQlelmkgysieakAGELLHGLGFSNtQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD 181
Cdd:PRK10584 115 LR---GESSRQSRNG------------AKALLEQLGLGK-RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190
....*....|....*....|....*....|...
gi 800951443 182 -------LDAVYWLErflRSYAGTLVLISHDRE 207
Cdd:PRK10584 179 rqtgdkiADLLFSLN---REHGTTLILVTHDLQ 208
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
328-504 |
9.74e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 328 LHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVGYfaQHQLEALDLQASPVtHlQRLNpQASE 407
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF-QGKEIDF--KSSKEALENGISMV-H-QELN-LVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 408 QSLRD--FLGGFAFIG-------------------DKALDP---VAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHL-D 462
Cdd:PRK10982 88 RSVMDnmWLGRYPTKGmfvdqdkmyrdtkaifdelDIDIDPrakVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 800951443 463 LEMRH--ALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGE 504
Cdd:PRK10982 168 KEVNHlfTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
313-535 |
9.82e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.70 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDTT-----ILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAG-----DVFFHQGLK------ 376
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgDYAIPANLKkikevk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 377 --------VGYFAQHQL--EAL--DLQASPVtHLQRlNPQASEQSLRDFLGGFAFIGDKALDPVAPFSGGEKARLVLAML 444
Cdd:PRK13645 87 rlrkeiglVFQFPEYQLfqETIekDIAFGPV-NLGE-NKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 445 VYQKPNLLLLDEPTNHLDLEMRHALVMAL----QSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFGYDLDAYyqwlt 520
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFerlnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF----- 239
|
250
....*....|....*.
gi 800951443 521 kANQE-QKQTQVEPDK 535
Cdd:PRK13645 240 -SNQElLTKIEIDPPK 254
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
125-216 |
1.02e-05 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 47.19 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 125 IEAKAGELLHGLGFSNTQIDYAvSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD-------LDAVYWLERFLRSyag 197
Cdd:cd03258 117 IEERVLELLELVGLEDKADAYP-AQLSGGQKQRVGIARALANNPKVLLCDEATSALDpettqsiLALLRDINRELGL--- 192
|
90
....*....|....*....
gi 800951443 198 TLVLISHDREfldaVVGEI 216
Cdd:cd03258 193 TIVLITHEME----VVKRI 207
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-205 |
1.03e-05 |
|
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: 47.28 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGnakvpkewsiaSVK---QETPALA 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSG-----------EILvdgQDITGLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 78 ITALE-------YVLQGNpdyyAL----------------RCQLKQAEqqgdgetqaqvhqqlelmkgysIEAKAGELLH 134
Cdd:COG1127 74 EKELYelrrrigMLFQGG----ALfdsltvfenvafplreHTDLSEAE----------------------IRELVLEKLE 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 135 GLGFSNTqIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD---LDAVYWLERFLR-SYAGTLVLISHD 205
Cdd:COG1127 128 LVGLPGA-ADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDpitSAVIDELIRELRdELGLTSVVVTHD 201
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
313-509 |
1.08e-05 |
|
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: 47.10 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGYGDT--TILHSIKLNLVPGSRIALLGRNGAGKSTLI--------------------------KLLAQELA- 363
Cdd:cd03244 3 IEFKNVSLRYRPNlpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLlalfrlvelssgsilidgvdiskiglHDLRSRISi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 364 -PQagDVFFHQG---LKVGYFAQHQLEALDlqaspvthlqrlnpQASEQ-SLRDFLGGFAFIGD-KALDPVAPFSGGEKA 437
Cdd:cd03244 83 iPQ--DPVLFSGtirSNLDPFGEYSDEELW--------------QALERvGLKEFVESLPGGLDtVVEEGGENLSVGQRQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 800951443 438 RLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQS-FDGAMV-TVSHDRHLLKNtADEFYLVDSGEVRQFG 509
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDPETDALIQKTIREaFKDCTVlTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-204 |
1.09e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.24 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAG------------NAKVPKEWSIAS 68
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGtitinninynklDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 69 VKQETPAL-AITALEYVLQGnpdyyalRCQLKQAeqqgdgetqaqvhQQLELMKGYSIEAKAGELLHGLGFsNTQIDYAV 147
Cdd:PRK09700 85 IYQELSVIdELTVLENLYIG-------RHLTKKV-------------CGVNIIDWREMRVRAAMMLLRVGL-KVDLDEKV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 148 SDFSGGWRMRLNLAQALIRDADLLLLDEPTNHL---DLDAVYWLERFLRSYAGTLVLISH 204
Cdd:PRK09700 144 ANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
11-204 |
1.24e-05 |
|
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: 46.72 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 11 RGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKvpkeWSIASVKQETPALAiTALEYVLQGNpd 90
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVL----LNGGPLDFQRDSIA-RGLLYLGHAP-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 91 yyALRCQLKQAEQ----QGDGETqAQVHQQLelmkgysieAKAGelLHGLGfsntqiDYAVSDFSGGWRMRLNLAQALIR 166
Cdd:cd03231 83 --GIKTTLSVLENlrfwHADHSD-EQVEEAL---------ARVG--LNGFE------DRPVAQLSAGQQRRVALARLLLS 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 800951443 167 DADLLLLDEPTNHLDLDAVYWLERFLRSYA---GTLVLISH 204
Cdd:cd03231 143 GRPLWILDEPTTALDKAGVARFAEAMAGHCargGMVVLTTH 183
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-216 |
1.24e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.31 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGEL-----QLDAGNAKVPKEWS-IASVKQETPALAItaleyVLQgNPD 90
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIisetgQTIVGDYAIPANLKkIKEVKRLRKEIGL-----VFQ-FPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 91 YyalrcQLKQAEQQGD--------GETQAQVHQqlelmkgysieaKAGELLHGLGFSNTQIDYAVSDFSGGWRMRLNLAQ 162
Cdd:PRK13645 101 Y-----QLFQETIEKDiafgpvnlGENKQEAYK------------KVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 163 ALIRDADLLLLDEPTNHLD----LDAVYWLERFLRSYAGTLVLISHDREFLDAVVGEI 216
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDpkgeEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEV 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-205 |
1.27e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 48.18 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPKEwSIASVkqETPALAITALEY---VLQgnpdYYA 93
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQ-DVATL--DADALAQLRREHfgfIFQ----RYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 94 LRCQLkQAEQqgDGETQAqVHQQLELMKGysiEAKAGELLHGLGFSNtQIDYAVSDFSGGWRMRLNLAQALIRDADLLLL 173
Cdd:PRK10535 97 LLSHL-TAAQ--NVEVPA-VYAGLERKQR---LLRAQELLQRLGLED-RVEYQPSQLSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190
....*....|....*....|....*....|....*
gi 800951443 174 DEPTNHLDL---DAVYWLERFLRSYAGTLVLISHD 205
Cdd:PRK10535 169 DEPTGALDShsgEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-181 |
1.35e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.16 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 12 GPKCLLKNANATLFPQHKVGLVGSNGCGKSSL-FALLK-----GELQLDAG-------NAKVPKEWSIASVKQEtPALAI 78
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTgLALLRlinsqGEIWFDGQplhnlnrRQLLPVRHRIQVVFQD-PNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 79 taleyvlqgNPdyyalRCQLKQAEQQGdgetqAQVHQQLelMKGYSIEAKAGELLHGLGFSNTQIDYAVSDFSGGWRMRL 158
Cdd:PRK15134 376 ---------NP-----RLNVLQIIEEG-----LRVHQPT--LSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRI 434
|
170 180
....*....|....*....|...
gi 800951443 159 NLAQALIRDADLLLLDEPTNHLD 181
Cdd:PRK15134 435 AIARALILKPSLIILDEPTSSLD 457
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
326-476 |
1.41e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.34 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 326 TILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQ--AGDVFFHQG-------LKVGYFAQHQL--EALDLQASP 394
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRkptkqilKRTGFVTQDDIlyPHLTVRETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 395 V-THLQRLNPQASEQ-------SLRDFLG----GFAFIGDKALDPVapfSGGEKARLVLAMLVYQKPNLLLLDEPTNHLD 462
Cdd:PLN03211 162 VfCSLLRLPKSLTKQekilvaeSVISELGltkcENTIIGNSFIRGI---SGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170
....*....|....
gi 800951443 463 LEMRHALVMALQSF 476
Cdd:PLN03211 239 ATAAYRLVLTLGSL 252
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-203 |
1.45e-05 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 46.00 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 14 KCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGelQLDAGNAKvpkewsiASVKqetpalaitaleyvLQGNPDY-Y 92
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG--RRTGLGVS-------GEVL--------------INGRPLDkR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 93 ALRCQLKQAEQQgDgetqaQVHQQLELMKGYSIEAKagelLHGLgfsntqidyavsdfSGGWRMRLNLAQALIRDADLLL 172
Cdd:cd03213 79 SFRKIIGYVPQD-D-----ILHPTLTVRETLMFAAK----LRGL--------------SGGERKRVSIALELVSNPSLLF 134
|
170 180 190
....*....|....*....|....*....|...
gi 800951443 173 LDEPTNHLDLDAVYWLERFLRSYA--GTLVLIS 203
Cdd:cd03213 135 LDEPTSGLDSSSALQVMSLLRRLAdtGRTIICS 167
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
31-204 |
1.51e-05 |
|
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: 46.50 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 31 GLVGSNGCGKSSLFALLKGELQLDAGNAKVPKewsiasvKQETPAlAITALEYVlqgnPDYYALRCQLKQAEQqgdgetq 110
Cdd:cd03269 30 GLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-------KPLDIA-ARNRIGYL----PEERGLYPKMKVIDQ------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 111 AQVHQQLELMKGYSIEAKAGELLHGLGFSNTQiDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLER 190
Cdd:cd03269 91 LVYLAQLKGLKKEEARRRIDEWLERLELSEYA-NKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKD 169
|
170
....*....|....*..
gi 800951443 191 FLRSYAG---TLVLISH 204
Cdd:cd03269 170 VIRELARagkTVILSTH 186
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
327-551 |
1.62e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 327 ILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQglKVGYFAQH----------------QLEALDL 390
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER--SIAYVPQQawimnatvrgnilffdEEDAARL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 391 Q-ASPVTHLqrlnpqasEQSLRDFLGGFAF-IGDKALDpvapFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHA 468
Cdd:PTZ00243 753 AdAVRVSQL--------EADLAQLGGGLETeIGEKGVN----LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGER 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 469 LVMALqsFDGAM-----VTVSHDRHLLKNtADEFYLVDSGEVRQFGYDLD----AYYQWLTKANQEQKqtqvepDKANSS 539
Cdd:PTZ00243 821 VVEEC--FLGALagktrVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADfmrtSLYATLAAELKENK------DSKEGD 891
|
250
....*....|..
gi 800951443 540 ANRKEQKRKEAE 551
Cdd:PTZ00243 892 ADAEVAEVDAAP 903
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-204 |
1.67e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKC--LLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVpKEWSIASvkqetpaLAI 78
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLppVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMI-DDCDVAK-------FGL 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 79 TALEYVLQGNPDYYAL-----RCQLKQAEQQGDGETQAQVHQqlelmkgysieAKAGELLHGLGFS-NTQIDYAVSDFSG 152
Cdd:PLN03232 1306 TDLRRVLSIIPQSPVLfsgtvRFNIDPFSEHNDADLWEALER-----------AHIKDVIDRNPFGlDAEVSEGGENFSV 1374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 800951443 153 GWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRS--YAGTLVLISH 204
Cdd:PLN03232 1375 GQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREefKSCTMLVIAH 1428
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
322-462 |
1.73e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 46.76 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQ--ELAPQA---GDV-FFHQGL------------KVGYFAQH 383
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEArveGEVrLFGRNIyspdvdpievrrEVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 384 qlealdlqASPVTHLQ---------RLNPQASEQSLRDFLGGFAF--------IGDKALDPVAPFSGGEKARLVLAMLVY 446
Cdd:PRK14267 94 --------PNPFPHLTiydnvaigvKLNGLVKSKKELDERVEWALkkaalwdeVKDRLNDYPSNLSGGQRQRLVIARALA 165
|
170
....*....|....*.
gi 800951443 447 QKPNLLLLDEPTNHLD 462
Cdd:PRK14267 166 MKPKILLMDEPTANID 181
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
33-205 |
2.00e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 46.88 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 33 VGSNGCGKSSLFALL-------KGELQLDAGNAKVPKEwsiasvkqETPALAITALEYVLQgNPdYYALRCQLKqaeqqg 105
Cdd:PRK11308 47 VGESGCGKSTLARLLtmietptGGELYYQGQDLLKADP--------EAQKLLRQKIQIVFQ-NP-YGSLNPRKK------ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 106 dgetqaqVHQQLE--LMKGYSIEA-----KAGELLHGLGFSNTQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTN 178
Cdd:PRK11308 111 -------VGQILEepLLINTSLSAaerreKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190
....*....|....*....|....*....|....*
gi 800951443 179 HLDLDA---VYWL-----ERFLRSYagtlVLISHD 205
Cdd:PRK11308 184 ALDVSVqaqVLNLmmdlqQELGLSY----VFISHD 214
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-207 |
2.14e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 46.62 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGnakvpkewsiasvkqetpalAITa 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHG--------------------SIT- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 81 leyvLQGNPdyyalrCQLKQAEQ----QGDG-----ETQAQVHQQLEL--MKGYSIEAKAGELLHGLGFSNTQIDYaVSD 149
Cdd:PRK11248 60 ----LDGKP------VEGPGAERgvvfQNEGllpwrNVQDNVAFGLQLagVEKMQRLEIAHQMLKKVGLEGAEKRY-IWQ 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800951443 150 FSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWL-ERFLRSYAGT---LVLISHDRE 207
Cdd:PRK11248 129 LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMqTLLLKLWQETgkqVLLITHDIE 190
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-182 |
2.46e-05 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 47.43 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRG-PKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAG----NAKVPKEWS-------IASV 69
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGeillNGFSLKDIDrhtlrqfINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 70 KQETPALAITALEYVLQGNPDyyalrcqlkqaeqqgdGETQAQVHQQLELMKgysIEAKAGELLHGLGfsnTQIDYAVSD 149
Cdd:TIGR01193 554 PQEPYIFSGSILENLLLGAKE----------------NVSQDEIWAACEIAE---IKDDIENMPLGYQ---TELSEEGSS 611
|
170 180 190
....*....|....*....|....*....|...
gi 800951443 150 FSGGWRMRLNLAQALIRDADLLLLDEPTNHLDL 182
Cdd:TIGR01193 612 ISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
149-227 |
2.52e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.26 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 149 DFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD----LDAVYWLERFLRSYAGTLVLISHDREFLDaVVGEIWHIDQQQI 224
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNAARAIRRLSEEGKKTALVVEHDLAVLD-YLSDRIHVFEGEP 149
|
...
gi 800951443 225 NVY 227
Cdd:cd03222 150 GVY 152
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
30-181 |
2.61e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 47.26 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 30 VGLVGSNGCGKSSLFALLK-------GELQLDAGN-AKVPKE---WSIASVKQETPALAITALEYVLQGNPDyyalrcql 98
Cdd:PRK13657 364 VAIVGPTGAGKSTLINLLQrvfdpqsGRILIDGTDiRTVTRAslrRNIAVVFQDAGLFNRSIEDNIRVGRPD-------- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 99 kqaeqqgdgETQAQVHQQLELMKGYS-IEAKAGellhglGFsNTQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPT 177
Cdd:PRK13657 436 ---------ATDEEMRAAAERAQAHDfIERKPD------GY-DTVVGERGRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
....
gi 800951443 178 NHLD 181
Cdd:PRK13657 500 SALD 503
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-204 |
2.75e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 16 LLKNANATLFPQHKVGLVGSNGCGKSSLFALLK-------GELQL-DAGNAK-VPKEW---SIASVKQEtPAL------- 76
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIErlydpteGDIIInDSHNLKdINLKWwrsKIGVVSQD-PLLfsnsikn 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 77 -------AITALEYVLQ-----GNPDYYAL----RCQLKQAEQQGDGETQAQVHQQLELMKGYS-------IEAKAGELL 133
Cdd:PTZ00265 479 nikyslySLKDLEALSNyynedGNDSQENKnkrnSCRAKCAGDLNDMSNTTDSNELIEMRKNYQtikdsevVDVSKKVLI 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 134 HGLGFS-----NTQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAGT----LVLISH 204
Cdd:PTZ00265 559 HDFVSAlpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNenriTIIIAH 638
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
319-508 |
2.86e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 46.99 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 319 QAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKS----TLIKLLAQELAPQAGDVFFhqglkvgyfaqhqlEALDLQASP 394
Cdd:COG4172 17 GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILF--------------DGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 395 VTHLQR----------------LNP------QASE-----QSLRdflggfafiGDKAL-------------DPVAP---- 430
Cdd:COG4172 83 ERELRRirgnriamifqepmtsLNPlhtigkQIAEvlrlhRGLS---------GAAARaralellervgipDPERRlday 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 431 ---FSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRhALVMAL-----QSFDGAMVTVSHDRHLLKNTADEFY---- 498
Cdd:COG4172 154 phqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQ-AQILDLlkdlqRELGMALLLITHDLGVVRRFADRVAvmrq 232
|
250
....*....|..
gi 800951443 499 --LVDSGEVRQF 508
Cdd:COG4172 233 geIVEQGPTAEL 244
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
282-507 |
2.90e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.89 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 282 ALERMEKLAPAhvdsPFDFSFAEPDALPN-PLIALDGAQAGYGDTTI-LHSIKLNLVPGSRIALLGRNGAGKSTLIKLLA 359
Cdd:PRK10522 295 AFNKLNKLALA----PYKAEFPRPQAFPDwQTLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLT 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 360 QELAPQAGDVFFhQGLKVgyfAQHQLEALDLQASPV---THL--QRLNPQASE------QSLRDFLG---GFAFIGDKAL 425
Cdd:PRK10522 371 GLYQPQSGEILL-DGKPV---TAEQPEDYRKLFSAVftdFHLfdQLLGPEGKPanpalvEKWLERLKmahKLELEDGRIS 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 426 DPvaPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMR----HALVMALQSFDGAMVTVSHDRHLLKNtADEFYLVD 501
Cdd:PRK10522 447 NL--KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRrefyQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMR 523
|
....*.
gi 800951443 502 SGEVRQ 507
Cdd:PRK10522 524 NGQLSE 529
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
126-224 |
3.23e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 45.90 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 126 EAKAGELLHGLGFSNTQIDYAvSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG---TLVLI 202
Cdd:PRK11264 122 TARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQekrTMVIV 200
|
90 100
....*....|....*....|..
gi 800951443 203 SHDREFLDAVVGEIWHIDQQQI 224
Cdd:PRK11264 201 THEMSFARDVADRAIFMDQGRI 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-181 |
3.26e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 47.32 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 21 NATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNAKVPK---EWSIASVKQE---TPALAI-----TALEYVLqgnp 89
Cdd:TIGR01257 950 NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdiETNLDAVRQSlgmCPQHNIlfhhlTVAEHIL---- 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 90 dYYAlrcQLKqaeqqgdGETQAQVHQQLELMkgysieakagelLHGLGFSNTQIDYAvSDFSGGWRMRLNLAQALIRDAD 169
Cdd:TIGR01257 1026 -FYA---QLK-------GRSWEEAQLEMEAM------------LEDTGLHHKRNEEA-QDLSGGMQRKLSVAIAFVGDAK 1081
|
170
....*....|..
gi 800951443 170 LLLLDEPTNHLD 181
Cdd:TIGR01257 1082 VVVLDEPTSGVD 1093
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
32-207 |
3.48e-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: 45.69 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 32 LVGSNGCGKSSLFALLKGELQLDAGNAKV---------PKEWSIASVKQET---PALAITaleyvlqgnpDYYALRCQLK 99
Cdd:cd03300 31 LLGPSGCGKTTLLRLIAGFETPTSGEILLdgkditnlpPHKRPVNTVFQNYalfPHLTVF----------ENIAFGLRLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 100 QAEQQgdgETQAQVHQQLELMKgysieakagelLHGLGfsntqiDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNH 179
Cdd:cd03300 101 KLPKA---EIKERVAEALDLVQ-----------LEGYA------NRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190
....*....|....*....|....*....|..
gi 800951443 180 LDL----DAVYWLERFLRSYAGTLVLISHDRE 207
Cdd:cd03300 161 LDLklrkDMQLELKRLQKELGITFVFVTHDQE 192
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
30-181 |
3.61e-05 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 46.22 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 30 VGLVGSNGCGKSSLFALLKGELQLDAG---------NAKVPKEWSIASVKQEtpalaitaleYVLqgnpdY--------- 91
Cdd:COG3839 32 LVLLGPSGCGKSTLLRMIAGLEDPTSGeiliggrdvTDLPPKDRNIAMVFQS----------YAL-----Yphmtvyeni 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 92 -YALRCQ-LKQAEQQgdgetqAQVHQQLELMKgysIEA----KAGELlhglgfsntqidyavsdfSGGWRMRLNLAQALI 165
Cdd:COG3839 97 aFPLKLRkVPKAEID------RRVREAAELLG---LEDlldrKPKQL------------------SGGQRQRVALGRALV 149
|
170
....*....|....*.
gi 800951443 166 RDADLLLLDEPTNHLD 181
Cdd:COG3839 150 REPKVFLLDEPLSNLD 165
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-181 |
3.86e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 45.85 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGP-----KCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGN--------AKVPkEWS-- 65
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSilidgkdvTKLP-EYKra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 66 --IASVKQET-----PALAIT---ALEYvLQGNPdyYALRCQLKQAEqqgdgetQAQVHQQLELMkgysieakagellhG 135
Cdd:COG1101 80 kyIGRVFQDPmmgtaPSMTIEenlALAY-RRGKR--RGLRRGLTKKR-------RELFRELLATL--------------G 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 800951443 136 LGFSNtQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD 181
Cdd:COG1101 136 LGLEN-RLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
328-554 |
4.81e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.42 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 328 LHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQG---LKVGYFAQHQLEALD-------LQASPVTH 397
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaalIAISSGLNGQLTGIEnielkglMMGLTKEK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 398 LQRLNPQASEqslrdflggFAFIGDKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSFD 477
Cdd:PRK13545 120 IKEIIPEIIE---------FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 478 GAMVT---VSHDRHLLKNTADEFYLVDSGEVRQFGyDL----DAYYQWLTKANQ----EQKQTQVEP-----------DK 535
Cdd:PRK13545 191 EQGKTiffISHSLSQVKSFCTKALWLHYGQVKEYG-DIkevvDHYDEFLKKYNQmsveERKDFREEQisqfqhgllqeDQ 269
|
250
....*....|....*....
gi 800951443 536 ANSSANRKEQKRKEAEFRK 554
Cdd:PRK13545 270 TGRERKRKKGKKTSRKFKK 288
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
323-474 |
5.10e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 44.54 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 323 GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQE-----------LAPQAGDVFFHQGlkVGYFAQHQL------ 385
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRktagvitgeilINGRPLDKNFQRS--TGYVEQQDVhspnlt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 386 --EALDLQAspvthlqrlnpqaseqSLRDflggfafigdkaldpvapFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDL 463
Cdd:cd03232 96 vrEALRFSA----------------LLRG------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170
....*....|.
gi 800951443 464 EMRHALVMALQ 474
Cdd:cd03232 142 QAAYNIVRFLK 152
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
328-496 |
5.24e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.73 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 328 LHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVgyfaqhqlealdLQASPVTHLQR------- 400
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYY-QGQDL------------LKADPEAQKLLrqkiqiv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 401 -LNPQAS---EQSLRDFLGGFAFIG---------DKALDPVA------------P--FSGGEKARLVLA---MLvyqKPN 450
Cdd:PRK11308 98 fQNPYGSlnpRKKVGQILEEPLLINtslsaaerrEKALAMMAkvglrpehydryPhmFSGGQRQRIAIAralML---DPD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 800951443 451 LLLLDEPTNHLDLEMRHA---LVMALQ-SFDGAMVTVSHDRHLLKNTADE 496
Cdd:PRK11308 175 VVVADEPVSALDVSVQAQvlnLMMDLQqELGLSYVFISHDLSVVEHIADE 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
333-509 |
5.34e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 45.79 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 333 LNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFhQGLKVGYFAQHQLE-------ALDLQA-SPVTHLQRLNPQ 404
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI-DGVDIAKISDAELRevrrkkiAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 405 ASEQSLRDFLGgfAFIGDKALDPVA-------------PFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLD----LEMRH 467
Cdd:PRK10070 128 AFGMELAGINA--EERREKALDALRqvglenyahsypdELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEMQD 205
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 800951443 468 ALVMALQSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVRQFG 509
Cdd:PRK10070 206 ELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
151-243 |
5.41e-05 |
|
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: 45.02 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 151 SGGWRMRLNLAQALIRDADLLLLDEPTNHLDL----DAVYWLERFLRSYAGTLVLISHDreFLDAVV----------GEI 216
Cdd:cd03299 131 SGGEQQRVAIARALVVNPKILLLDEPFSALDVrtkeKLREELKKIRKEFGVTVLHVTHD--FEEAWAladkvaimlnGKL 208
|
90 100
....*....|....*....|....*..
gi 800951443 217 WHIDQQQinvykgnySQFERQKAERLA 243
Cdd:cd03299 209 IQVGKPE--------EVFKKPKNEFVA 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
150-218 |
7.08e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 45.83 E-value: 7.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 150 FSGGWRMRLNLAQALIRDADLLLLDEPTNHLD-------LDavywLERFL-RSYAGTLVLISHDrefLdAVVGEIWH 218
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDvsvqaqiLD----LLRDLqREHGLAYLFISHD---L-AVVRALAH 494
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
324-485 |
8.97e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 44.24 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 324 DTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQGLK---------------VGYFAQH----- 383
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNEsepsfeatrsrnrysVAYAAQKpwlln 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 384 -QLEALDLQASPVTHlQRLNPQASEQSLR---DFL--GGFAFIGDKALDpvapFSGGEKARLVLAMLVYQKPNLLLLDEP 457
Cdd:cd03290 93 aTVEENITFGSPFNK-QRYKAVTDACSLQpdiDLLpfGDQTEIGERGIN----LSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190
....*....|....*....|....*....|...
gi 800951443 458 TNHLDLE-----MRHALVMALQSFDGAMVTVSH 485
Cdd:cd03290 168 FSALDIHlsdhlMQEGILKFLQDDKRTLVLVTH 200
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
322-510 |
9.51e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.12 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 322 YGDTTILHsiklnLVPGSRIALLGRNGAGKSTLIKllaqelapqagdvffhqglkvgyfaqhQLEALDLQASPVTHLQRL 401
Cdd:cd03227 10 YFVPNDVT-----FGEGSLTIITGPNGSGKSTILD---------------------------AIGLALGGAQSATRRRSG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 402 NPQASEQSLRDFlgGFAFIGDKAldpvapfSGGEKARLVLAMLV----YQKPNLLLLDEPTNHLDLEMRHAL--VMALQS 475
Cdd:cd03227 58 VKAGCIVAAVSA--ELIFTRLQL-------SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALaeAILEHL 128
|
170 180 190
....*....|....*....|....*....|....*.
gi 800951443 476 FDGAMV-TVSHDrHLLKNTADEFYlvDSGEVRQFGY 510
Cdd:cd03227 129 VKGAQViVITHL-PELAELADKLI--HIKKVITGVY 161
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
303-462 |
9.65e-05 |
|
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: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 303 AEPDALPNPLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQ--ELAPQA---GDVFFHqGLKV 377
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLIPGArveGEILLD-GEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 378 gyfaqhqleaLDLQASPVTH-------LQRLNP-------------------------QASEQSLRDflggfAFI----G 421
Cdd:COG1117 81 ----------YDPDVDVVELrrrvgmvFQKPNPfpksiydnvayglrlhgikskseldEIVEESLRK-----AALwdevK 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 800951443 422 DKALDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLD 462
Cdd:COG1117 146 DRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
153-205 |
1.01e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 44.69 E-value: 1.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 153 GWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYA----GTLVLISHD 205
Cdd:COG4586 158 GQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNrergTTILLTSHD 214
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
313-474 |
1.02e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 45.48 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 313 IALDGAQAGY-GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFF---------HQGLKVGyFAQ 382
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLdgrplsslsHSVLRQG-VAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 383 HQLEALDLQAS---PVTHLQRLNPQASEQSL---------RDFLGG-FAFIGDKAldpvAPFSGGEKARLVLAMLVYQKP 449
Cdd:PRK10790 420 VQQDPVVLADTflaNVTLGRDISEEQVWQALetvqlaelaRSLPDGlYTPLGEQG----NNLSVGQKQLLALARVLVQTP 495
|
170 180
....*....|....*....|....*
gi 800951443 450 NLLLLDEPTNHLDLEMRHALVMALQ 474
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALA 520
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
150-486 |
1.05e-04 |
|
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: 45.06 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 150 FSGGWRMRLNLAQALIRDADLLLLDEPTNHLD-------LDAvywLERFLRSYAGTLVLISHD----REFLDAVV----G 214
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqaqiLDL---LKDLQRELGMALLLITHDlgvvRRFADRVAvmrqG 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 215 EIwhidqqqinVykgnysqfERQKAERLaqqqaqfdkqqeqiahlekfitrFKakaskakqaqsrvkalermeklAPAHv 294
Cdd:COG4172 234 EI---------V--------EQGPTAEL-----------------------FA----------------------APQH- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 295 dsP-----FDfsfAEPDALPNP-------LIALDGAQAGY-----------GDTTILHSIKLNLVPGSRIALLGRNGAGK 351
Cdd:COG4172 251 --PytrklLA---AEPRGDPRPvppdappLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 352 STLIKLLAQeLAPQAGDVFFH----QGLKvgyfaQHQLEAL--DLQA---------SP------------VTHLQRLNPQ 404
Cdd:COG4172 326 STLGLALLR-LIPSEGEIRFDgqdlDGLS-----RRALRPLrrRMQVvfqdpfgslSPrmtvgqiiaeglRVHGPGLSAA 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 405 ASEQSLRDFLggfafiGDKALDPVA----P--FSGGEKARLVLA--MLVyqKPNLLLLDEPTNHLDLEMRH---ALVMAL 473
Cdd:COG4172 400 ERRARVAEAL------EEVGLDPAArhryPheFSGGQRQRIAIAraLIL--EPKLLVLDEPTSALDVSVQAqilDLLRDL 471
|
410
....*....|....
gi 800951443 474 QS-FDGAMVTVSHD 486
Cdd:COG4172 472 QReHGLAYLFISHD 485
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
324-552 |
1.08e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 324 DTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFHQG------------LKVGYFAQ--------- 382
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrSKIGVVSQdpllfsnsi 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 383 -----------HQLEALD-------------------------------LQASPVTHL--QRLNPQASEQS--------- 409
Cdd:PTZ00265 477 knnikyslyslKDLEALSnyynedgndsqenknkrnscrakcagdlndmSNTTDSNELieMRKNYQTIKDSevvdvskkv 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 410 -LRDFLGGF-----AFIGDKAldpvAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSFDG----A 479
Cdd:PTZ00265 557 lIHDFVSALpdkyeTLVGSNA----SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnenrI 632
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 800951443 480 MVTVSHDRHLLKNTADEFYLvdSGEVRQFGYDLDAYYQWLTKANQEQKQTQVEPDKANSSANRKEQKRKEAEF 552
Cdd:PTZ00265 633 TIIIAHRLSTIRYANTIFVL--SNRERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNAGSY 703
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
322-369 |
1.15e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 1.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDV 369
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV 58
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
30-216 |
1.19e-04 |
|
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: 44.66 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 30 VGLVGSNGCGKSSL-FALLkgelQLDAGNAKV---------------PKEWS------IASVKQEtpalAITALeyvlqg 87
Cdd:COG0444 34 LGLVGESGSGKSTLaRAIL----GLLPPPGITsgeilfdgedllklsEKELRkirgreIQMIFQD----PMTSL------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 88 NPdYYALRCQLKQAeqqgdgetqAQVHQqleLMKGYSIEAKAGELLHGLGfsntqIDYAVSD-------FSGGWRMRLNL 160
Cdd:COG0444 100 NP-VMTVGDQIAEP---------LRIHG---GLSKAEARERAIELLERVG-----LPDPERRldrypheLSGGMRQRVMI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 800951443 161 AQALIRDADLLLLDEPTNHLD-------LDAvywLERFLRSYAGTLVLISHDrefLdAVVGEI 216
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDvtiqaqiLNL---LKDLQRELGLAILFITHD---L-GVVAEI 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-207 |
1.25e-04 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 44.70 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGnakvpkewSIAsVKQETpalaITA 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSG--------RIL-LDGRD----VTG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 81 LE-------YVLQgnpDY-------------YALRCQ-LKQAEQQgdgetqAQVHQQLEL--MKGYSiEAKAGELlhglg 137
Cdd:COG3842 72 LPpekrnvgMVFQ---DYalfphltvaenvaFGLRMRgVPKAEIR------ARVAELLELvgLEGLA-DRYPHQL----- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 800951443 138 fsntqidyavsdfSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDA----VYWLERFLRSYAGTLVLISHDRE 207
Cdd:COG3842 137 -------------SGGQQQRVALARALAPEPRVLLLDEPLSALDAKLreemREELRRLQRELGITFIYVTHDQE 197
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
34-200 |
1.35e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 43.68 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 34 GSNGCGKSSLFALLKGELQLDAGNAKVPKEwsiaSVKQETPALAITALEYVLQGNPDYYALRcqlkqaeqqgdgetqaQV 113
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGK----TATRGDRSRFMAYLGHLPGLKADLSTLE----------------NL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 114 HQqLELMKGYSIEAKAGELLHGLGFSNTQiDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERF-- 191
Cdd:PRK13543 104 HF-LCGLHGRRAKQMPGSALAIVGLAGYE-DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMis 181
|
170
....*....|.
gi 800951443 192 --LRSYAGTLV 200
Cdd:PRK13543 182 ahLRGGGAALV 192
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
327-370 |
1.63e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 43.83 E-value: 1.63e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 800951443 327 ILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVF 370
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIK 67
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
32-213 |
1.66e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 43.72 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 32 LVGSNGCGKSSLFALLKGELQLDAGNA--------KVPKEWSIASVKQETP---ALAITALEYVLQGNPDYYALRCQLKQ 100
Cdd:PRK15056 38 LVGVNGSGKSTLFKALMGFVRLASGKIsilgqptrQALQKNLVAYVPQSEEvdwSFPVLVEDVVMMGRYGHMGWLRRAKK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 101 AEQQGDGETQAQVHQqlelmkgysieakagellhgLGFSNTQIdyavSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHL 180
Cdd:PRK15056 118 RDRQIVTAALARVDM--------------------VEFRHRQI----GELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 800951443 181 DLDA---VYWLERFLRSYAGTLVLISHD----REFLDAVV 213
Cdd:PRK15056 174 DVKTearIISLLRELRDEGKTMLVSTHNlgsvTEFCDYTV 213
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
311-369 |
1.71e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 1.71e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 800951443 311 PLIALDGAQAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDV 369
Cdd:PRK11288 3 PYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI 61
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
305-358 |
1.73e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 44.81 E-value: 1.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 800951443 305 PDALP----NPLIALDGAQAGY-GDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLL 358
Cdd:COG5265 346 PDAPPlvvgGGEVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLL 404
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
314-358 |
1.80e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.61 E-value: 1.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 800951443 314 ALDGAQagygdttilhsikLNLVPGSRIALLGRNGAGKSTLIKLL 358
Cdd:PRK10762 19 ALSGAA-------------LNVYPGRVMALVGENGAGKSTMMKVL 50
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-204 |
1.81e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.61 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 17 LKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGNakvpkewsiasvkqetpalaitaLEYvlQGNPDYYAlrc 96
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGS-----------------------ILY--LGKEVTFN--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 97 QLKQAEQQGDGetqaQVHQQLELMKGYSIE----------------------AKAGELLHGLGFSNTQiDYAVSDFSGGW 154
Cdd:PRK10762 72 GPKSSQEAGIG----IIHQELNLIPQLTIAeniflgrefvnrfgridwkkmyAEADKLLARLNLRFSS-DKLVGELSIGE 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 800951443 155 RMRLNLAQALIRDADLLLLDEPTNHL---DLDAVYWLERFLRSYAGTLVLISH 204
Cdd:PRK10762 147 QQMVEIAKVLSFESKVIIMDEPTDALtdtETESLFRVIRELKSQGRGIVYISH 199
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
126-205 |
1.84e-04 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 43.79 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 126 EAKAGELLHGLGFSNtQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD-------LDAVYWLERFLRSyagT 198
Cdd:cd03294 138 EERAAEALELVGLEG-WEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirremQDELLRLQAELQK---T 213
|
....*..
gi 800951443 199 LVLISHD 205
Cdd:cd03294 214 IVFITHD 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
122-207 |
1.93e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 43.92 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 122 GYSIEAKAGELLHGLGFSNTQIDYAvSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRS----YAG 197
Cdd:PRK10851 110 AAAIKAKVTQLLEMVQLAHLADRYP-AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQlheeLKF 188
|
90
....*....|
gi 800951443 198 TLVLISHDRE 207
Cdd:PRK10851 189 TSVFVTHDQE 198
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
427-503 |
2.38e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 427 PVAPFSGGEKARLVLA---MLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSF---DGAMVTVSHDRHLLKnTADefYLV 500
Cdd:PRK00635 806 PLSSLSGGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLthqGHTVVIIEHNMHVVK-VAD--YVL 882
|
...
gi 800951443 501 DSG 503
Cdd:PRK00635 883 ELG 885
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
150-213 |
2.50e-04 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 43.13 E-value: 2.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 150 FSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG---TLVLISHDREFLDAVV 213
Cdd:COG0396 141 FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpdrGILIITHYQRILDYIK 207
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
140-212 |
2.60e-04 |
|
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: 43.97 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 140 NTQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD-------LDAVywleRFLRSYAGTLVLISHDREFLDAV 212
Cdd:COG4618 458 DTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalAAAI----RALKARGATVVVITHRPSLLAAV 533
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
431-508 |
2.82e-04 |
|
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: 43.50 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 431 FSGGEKARLVLAM-LVYqKPNLLLLDEPTNHLDLEMRhALVMAL-----QSFDGAMVTVSHDRHLLKNTADE---FYL-- 499
Cdd:COG0444 151 LSGGMRQRVMIARaLAL-EPKLLIADEPTTALDVTIQ-AQILNLlkdlqRELGLAILFITHDLGVVAEIADRvavMYAgr 228
|
90
....*....|
gi 800951443 500 -VDSGEVRQF 508
Cdd:COG0444 229 iVEEGPVEEL 238
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
150-205 |
3.06e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 43.16 E-value: 3.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 150 FSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG--TLVLISHD 205
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
328-505 |
3.25e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 43.23 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 328 LHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFfHQGLKVgyfaQHQLEalDLQASPVTHLQRLNPQASE 407
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVT-VDDITI----THKTK--DKYIRPVRKRIGMVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 408 QSL------RDFLGG---FAF----IGDKALD------------PVAPF--SGGEKARLVLAMLVYQKPNLLLLDEPTNH 460
Cdd:PRK13646 96 SQLfedtveREIIFGpknFKMnldeVKNYAHRllmdlgfsrdvmSQSPFqmSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 800951443 461 LDLEMRHALVMALQSF----DGAMVTVSHDRHLLKNTADEFYLVDSGEV 505
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLqtdeNKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-229 |
3.34e-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: 42.48 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 30 VGLVGSNGCGKSSLFALLKGELQLDAGN---------AKVPKEWSIASVKQETPALA-ITALEYVLQG-NPdyyalRCQL 98
Cdd:cd03298 27 TAIVGPSGSGKSTLLNLIAGFETPQSGRvlingvdvtAAPPADRPVSMLFQENNLFAhLTVEQNVGLGlSP-----GLKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 99 KQAEQQGDGETQAQVHQQlELMKgysieAKAGELlhglgfsntqidyavsdfSGGWRMRLNLAQALIRDADLLLLDEPTN 178
Cdd:cd03298 102 TAEDRQAIEVALARVGLA-GLEK-----RLPGEL------------------SGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 179 HLD-------LDAVYWLErflRSYAGTLVLISHDREFLDAVVGEIWHIDQQQInVYKG 229
Cdd:cd03298 158 ALDpalraemLDLVLDLH---AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI-AAQG 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-181 |
4.22e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 30 VGLVGSNGCGKSSLFALLKGELQlDAGNAKVPKEWSIASVKQETPALAITALEYVLQGNpDYyalrcqlkQAEQQGDGET 109
Cdd:PLN03232 646 VAIVGGTGEGKTSLISAMLGELS-HAETSSVVIRGSVAYVPQVSWIFNATVRENILFGS-DF--------ESERYWRAID 715
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800951443 110 QAQVHQQLELMKGYSIeakagellhglgfsnTQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD 181
Cdd:PLN03232 716 VTALQHDLDLLPGRDL---------------TEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-205 |
4.38e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 42.38 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLR--GPKCLLKNANATLFPQHKVGLVGSNGCGKS-SLFALL----------KGELQLDaGNAKVPkewsiA 67
Cdd:PRK10418 1 MPQQIELRNIAlqAAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpagvrqtAGRVLLD-GKPVAP-----C 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 68 SVKQETPALaitaleyVLQgNPD--YYALRCQLKQAEqqgdgETQAQVHQQlelmkgySIEAKAGELLHGLGFSNTQIDY 145
Cdd:PRK10418 75 ALRGRKIAT-------IMQ-NPRsaFNPLHTMHTHAR-----ETCLALGKP-------ADDATLTAALEAVGLENAARVL 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 800951443 146 AVSDF--SGGWRMRLNLAQALIRDADLLLLDEPTNhlDLDAVY------WLERFLRSYAGTLVLISHD 205
Cdd:PRK10418 135 KLYPFemSGGMLQRMMIALALLCEAPFIIADEPTT--DLDVVAqarildLLESIVQKRALGMLLVTHD 200
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
12-176 |
5.22e-04 |
|
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: 42.14 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 12 GPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLDAGnaKV-----------------------PKEWSI-- 66
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSG--KIlldgqditklpmhkrarlgigylPQEASIfr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 67 -ASVKQEtpalaitaleyvlqgnpdyyaLRCQLkqaEQQGDGETQaqvhqqlelmkgysIEAKAGELLHGLGFSNTQIDY 145
Cdd:cd03218 89 kLTVEEN---------------------ILAVL---EIRGLSKKE--------------REEKLEELLEEFHITHLRKSK 130
|
170 180 190
....*....|....*....|....*....|.
gi 800951443 146 AVSdFSGGWRMRLNLAQALIRDADLLLLDEP 176
Cdd:cd03218 131 ASS-LSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-211 |
5.58e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 42.87 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 16 LLKNANATLFPQHKVGLVGSNGCGKSSLFALL-------KGELQLdagnakvPKEWSIASVKQEtPalaitaleYVLQGN 88
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygSGRIAR-------PAGARVLFLPQR-P--------YLPLGT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 89 pdyyaLRCQL---KQAEQQGDgetqAQVHQQLELMkgysieakagellhGLGFSNTQIDyAVSD----FSGGWRMRLNLA 161
Cdd:COG4178 442 -----LREALlypATAEAFSD----AELREALEAV--------------GLGHLAERLD-EEADwdqvLSLGEQQRLAFA 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 800951443 162 QALIRDADLLLLDEPTNHLDLDAVYWLERFLRS--YAGTLVLISHdREFLDA 211
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAA 548
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
144-204 |
5.66e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.14 E-value: 5.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 800951443 144 DYAvSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG--TLVLISH 204
Cdd:PRK14267 145 DYP-SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
326-484 |
6.25e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.40 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 326 TILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH-------QGLKVGYFAqHQL---------EALD 389
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKncninniAKPYCTYIG-HNLglklemtvfENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 390 LQASPVTHLQRLNPQASEQSLRDFLGgfafigdkalDPVAPFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHAL 469
Cdd:PRK13541 93 FWSEIYNSAETLYAAIHYFKLHDLLD----------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
170
....*....|....*..
gi 800951443 470 --VMALQSFDGAMVTVS 484
Cdd:PRK13541 163 nnLIVMKANSGGIVLLS 179
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
324-372 |
6.83e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.78 E-value: 6.83e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 800951443 324 DTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELAPQAGDVFFH 372
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFH 375
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
125-205 |
6.95e-04 |
|
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: 41.90 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 125 IEAKAGELLHGLGFSNTQI-DYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD-------LDAVYWLERFLRSya 196
Cdd:cd03295 110 IRERADELLALVGLDPAEFaDRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDpitrdqlQEEFKRLQQELGK-- 187
|
....*....
gi 800951443 197 gTLVLISHD 205
Cdd:cd03295 188 -TIVFVTHD 195
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
432-509 |
6.98e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.04 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 432 SGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHA---LVMALQSFDG-AMVTVSHDRHLLKNTADEFYLVDSGEVRQ 507
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQiieLLLELQQKENmALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
..
gi 800951443 508 FG 509
Cdd:PRK11022 235 TG 236
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
432-495 |
1.01e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 800951443 432 SGGEKA------RLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSF---DGAMVTVSHDRHlLKNTAD 495
Cdd:PRK03918 790 SGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYlrkIPQVIIVSHDEE-LKDAAD 861
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
111-210 |
1.06e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.05 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 111 AQVHQQLELMKGYSIEAKAGELLHGLGFSNTQIDYAVSDFSGGWRMRLNLAQALIR--DADLLLLDEPTNHLD------- 181
Cdd:smart00382 20 RALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARklKPDVLILDEITSLLDaeqeall 99
|
90 100 110
....*....|....*....|....*....|.
gi 800951443 182 --LDAVYWLERFLRSYAGTLVLISHDREFLD 210
Cdd:smart00382 100 llLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
149-230 |
1.18e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 41.62 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 149 DFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLD----AVYWLERFLRSYAGTLVLISHDRefldAVVGeiwHIDQQQI 224
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSiqaqVVNLLQQLQREMGLSLIFIAHDL----AVVK---HISDRVL 233
|
....*.
gi 800951443 225 NVYKGN 230
Cdd:PRK15079 234 VMYLGH 239
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-204 |
1.23e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 41.05 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLF------------ALLKGELQLDAGNA-KVP------K 62
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrlielypeARVSGEVYLDGQDIfKMDvielrrR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 63 EWSIASVKQETPALAItaLEYVlqgnpdyyALRCQLKQAEQQgDGETQAQVHQQLELMKGYSiEAKagellhglgfsnTQ 142
Cdd:PRK14247 84 VQMVFQIPNPIPNLSI--FENV--------ALGLKLNRLVKS-KKELQERVRWALEKAQLWD-EVK------------DR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 800951443 143 IDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG--TLVLISH 204
Cdd:PRK14247 140 LDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-205 |
1.35e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 40.80 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 1 MIQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLKGELQLdaGNAKVPKEWSIASVKQETPALaita 80
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEI--YDSKIKVDGKVLYFGKDIFQI---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 81 leyvlqgnpDYYALRCQLKQAEQQGDGETQAQVHQQLEL-MKGYSIEAK------AGELLHGLGF---SNTQIDYAVSDF 150
Cdd:PRK14246 84 ---------DAIKLRKEVGMVFQQPNPFPHLSIYDNIAYpLKSHGIKEKreikkiVEECLRKVGLwkeVYDRLNSPASQL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 151 SGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG--TLVLISHD 205
Cdd:PRK14246 155 SGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
149-205 |
1.47e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 41.25 E-value: 1.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 800951443 149 DFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDA----VYWLERFLRSYAGTLVLISHD 205
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqiMTLLNELKREFNTAIIMITHD 221
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
159-363 |
1.57e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 41.71 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 159 NLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAGTLVLISHDREFLDAVVGEIWHIDQQQINVYKGNYSQFERQK 238
Cdd:COG5635 1 LLLLLALILALLALVLLLDLLVTRLAIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 239 AERLAQQQAQFDKQQEQIAHLEKFITRFKAKASKAKQAQSRVKALERMEKLAPAHVDSPFDFSFAEPDALPNPLIALDGA 318
Cdd:COG5635 81 LLVLLLLESLLLLLLLLLLLAEALLALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 800951443 319 QAGYGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLLAQELA 363
Cdd:COG5635 161 LNLLERIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELA 205
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
322-358 |
1.62e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.45 E-value: 1.62e-03
10 20 30
....*....|....*....|....*....|....*..
gi 800951443 322 YGDTTILHSIKLNLVPGSRIALLGRNGAGKSTLIKLL 358
Cdd:PRK13549 15 FGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL 51
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
420-505 |
1.77e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 40.99 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 420 IGDKALDpVAPF--SGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSFDGAMVTVSHDRHLLKNT---A 494
Cdd:PRK13631 165 LDDSYLE-RSPFglSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVlevA 243
|
90
....*....|.
gi 800951443 495 DEFYLVDSGEV 505
Cdd:PRK13631 244 DEVIVMDKGKI 254
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
429-505 |
2.07e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.87 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 429 APFSGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRHALVMALQSF--DGAMVTVSHD-RHLLKNTADEFYLVDSGEV 505
Cdd:NF000106 143 AKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvrDGATVLLTTQyMEEAEQLAHELTVIDRGRV 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
151-177 |
2.10e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 2.10e-03
10 20
....*....|....*....|....*..
gi 800951443 151 SGGWRMRLNLAQALIRDADLLLLDEPT 177
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
127-224 |
2.10e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.87 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 127 AKAGELLHGLGFSNTQiDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD---LDAVYWLERFLRSYAGTLVLIS 203
Cdd:NF000106 123 ARADELLERFSLTEAA-GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDprtRNEVWDEVRSMVRDGATVLLTT 201
|
90 100
....*....|....*....|.
gi 800951443 204 HDREFLDAVVGEIWHIDQQQI 224
Cdd:NF000106 202 QYMEEAEQLAHELTVIDRGRV 222
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
150-219 |
2.38e-03 |
|
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: 39.94 E-value: 2.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 800951443 150 FSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG---TLVLISHDREFLDAVVGEIWHI 219
Cdd:TIGR01978 145 FSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREpdrSFLIITHYQRLLNYIKPDYVHV 217
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
150-205 |
2.50e-03 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 40.49 E-value: 2.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 800951443 150 FSGGWRMRLNLAQALIRDADLLLLDEPTNHLD---------LdavywLERFLRSYAGTLVLISHD 205
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqaqvlnL-----LEDLQDELGLTYLFISHD 217
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
147-211 |
2.52e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 2.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 800951443 147 VSDFSGGWRM------RLNLAQALIRDADLLLLDEPTNHLDLDAVYWL----ERFLRSYAG--TLVLISHDREFLDA 211
Cdd:PRK01156 799 IDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLkdiiEYSLKDSSDipQVIMISHHRELLSV 875
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
151-243 |
3.09e-03 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 39.61 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 151 SGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG---TLVLISHDREFLDAVVGEIWHIDQQQInVY 227
Cdd:COG4161 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIVTHEVEFARKVASQVVYMEKGRI-IE 221
|
90
....*....|....*.
gi 800951443 228 KGNYSQFERQKAERLA 243
Cdd:COG4161 222 QGDASHFTQPQTEAFA 237
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
380-490 |
3.11e-03 |
|
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: 40.07 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 380 FAQHQLEALDLQASPVTHLQRLNPQASEQSLRDFLGGFAFIGDKALDPVAPF--SGGEK--ARLVLAMLVYQKPN-LLLL 454
Cdd:pfam13304 184 LLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFelSDGTKrlLALLAALLSALPKGgLLLI 263
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 800951443 455 DEPTNHLDLEMRHALV--MALQSFDGA--MVTvSHDRHLL 490
Cdd:pfam13304 264 DEPESGLHPKLLRRLLelLKELSRNGAqlILT-THSPLLL 302
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
6-196 |
3.26e-03 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 39.15 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 6 DIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALL---------KGELQLDAgnakvpkewsiasvKQETPAL 76
Cdd:cd03232 12 TVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktagviTGEILING--------------RPLDKNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 77 AITAlEYVlqgnpdyyalrcqlkqaEQQGDGETQAQVHQQLElmkgYSieakagELLHGLGFSNtqidyavsdfsggwRM 156
Cdd:cd03232 78 QRST-GYV-----------------EQQDVHSPNLTVREALR----FS------ALLRGLSVEQ--------------RK 115
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 800951443 157 RLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYA 196
Cdd:cd03232 116 RLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA 155
|
|
| PRK08154 |
PRK08154 |
anaerobic benzoate catabolism transcriptional regulator; Reviewed |
339-363 |
3.41e-03 |
|
anaerobic benzoate catabolism transcriptional regulator; Reviewed
Pssm-ID: 236167 [Multi-domain] Cd Length: 309 Bit Score: 39.94 E-value: 3.41e-03
10 20
....*....|....*....|....*
gi 800951443 339 SRIALLGRNGAGKSTLIKLLAQELA 363
Cdd:PRK08154 134 RRIALIGLRGAGKSTLGRMLAARLG 158
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
142-211 |
3.42e-03 |
|
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: 38.67 E-value: 3.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 800951443 142 QIDYAVSD-FSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAGTLVLISHdREFLDA 211
Cdd:cd03223 83 QLIYPWDDvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWK 152
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
282-371 |
3.46e-03 |
|
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: 40.55 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 282 ALERMEKLAPAhVDSPFDFSFAEPDALPNPL---IALDGAQAGYGDTT-----ILHSIKLNLVPGSRIALLGRNGAGKST 353
Cdd:COG4615 295 ALRKIEELELA-LAAAEPAAADAAAPPAPADfqtLELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKST 373
|
90
....*....|....*...
gi 800951443 354 LIKLLAQELAPQAGDVFF 371
Cdd:COG4615 374 LAKLLTGLYRPESGEILL 391
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
149-205 |
3.56e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 39.63 E-value: 3.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 800951443 149 DFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYA----GTLVLISHD 205
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHN 210
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
125-205 |
5.13e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 39.38 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 125 IEAKAGELLHGLGFSNTQIDYAVSDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYA----GTLV 200
Cdd:PRK13646 121 VKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTII 200
|
....*
gi 800951443 201 LISHD 205
Cdd:PRK13646 201 LVSHD 205
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
151-196 |
5.32e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 39.86 E-value: 5.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 800951443 151 SGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYA 196
Cdd:PLN03211 208 SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLA 253
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
148-181 |
5.41e-03 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 38.79 E-value: 5.41e-03
10 20 30
....*....|....*....|....*....|....
gi 800951443 148 SDFSGGWRMRLNLAQALIRDADLLLLDEPTNHLD 181
Cdd:PRK10771 128 GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-243 |
6.06e-03 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 38.84 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 2 IQITDIELLRGPKCLLKNANATLFPQHKVGLVGSNGCGKSSLFALLK-------GELQLdAGN----AKVPKEWSIASVK 70
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNllemprsGTLNI-AGNhfdfSKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 71 QET----------PALAitaleyVLQgnpdyyalrcQLKQAEQQGDGETQAQVHQQ-LELMKGYSIEAKAGEL-LHglgf 138
Cdd:PRK11124 82 RNVgmvfqqynlwPHLT------VQQ----------NLIEAPCRVLGLSKDQALARaEKLLERLRLKPYADRFpLH---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 139 sntqidyavsdFSGGWRMRLNLAQALIRDADLLLLDEPTNHLDLDAVYWLERFLRSYAG---TLVLISHDREFLDAVVGE 215
Cdd:PRK11124 142 -----------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtgiTQVIVTHEVEVARKTASR 210
|
250 260
....*....|....*....|....*...
gi 800951443 216 IWHIDQQQInVYKGNYSQFERQKAERLA 243
Cdd:PRK11124 211 VVYMENGHI-VEQGDASCFTQPQTEAFK 237
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
151-177 |
6.21e-03 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 38.57 E-value: 6.21e-03
10 20
....*....|....*....|....*..
gi 800951443 151 SGGWRMRLNLAQALIRDADLLLLDEPT 177
Cdd:cd03224 134 SGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
432-509 |
6.77e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 39.45 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800951443 432 SGGEKARLVLAMLVYQKPNLLLLDEPTNHLDLEMRhALVMAL-----QSFDGAMVTVSHDRHLLKNTADEFYLVDSGEVR 506
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQ-AQILQLikvlqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
...
gi 800951443 507 QFG 509
Cdd:PRK10261 249 ETG 251
|
|
| |
