|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-552 |
0e+00 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 1173.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 1 MAQYVYSMNRVSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALPMPGLTIGYLEQEPKL 80
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 81 NPEHTVRESVEESMGAVNAAKKRLEEVYELYAAEDADFDALAAEQAELEAIIATA-GTDSEHQLEIAADALRLPAWDAKI 159
Cdd:PRK11819 82 DPEKTVRENVEEGVAEVKAALDRFNEIYAAYAEPDADFDALAAEQGELQEIIDAAdAWDLDSQLEIAMDALRCPPWDAKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 160 GVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEWILELDRGRGIPW 239
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 240 KGNYSTWLEQKGERLAQEQKSEEAHAKALKKELEWSRQNPKARQAKSKSRLARFEELSDVEYQKRNETQEIFIPVAERLG 319
Cdd:PRK11819 242 EGNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWVRQSPKARQAKSKARLARYEELLSEEYQKRNETNEIFIPPGPRLG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 320 SQVFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQARDALAD 399
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 400 QKTVWEDISGGLDIINVGKFQMASRAYAGRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETL 479
Cdd:PRK11819 402 NKTVWEEISGGLDIIKVGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETL 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 480 RALEDALLEFAGTVMVISHDRWFLDRIATHILAAEGDSQWTFFDGNYQEYEADKKKRLGEEGAKPKRMRYKAL 552
Cdd:PRK11819 482 RALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDSQVEWFEGNFQEYEEDKKRRLGADAARPHRIKYKKL 554
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-552 |
0e+00 |
|
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: 1077.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 2 AQYVYSMNRVSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALPMPGLTIGYLEQEPKLN 81
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 82 PEHTVRESVEESMGAVNAAKKRLEEVYELYAAEDADFDALAAEQAELEAIIATAGT-DSEHQLEIAADALRLPAWDAKIG 160
Cdd:TIGR03719 81 PTKTVRENVEEGVAEIKDALDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAwDLDSQLEIAMDALRCPPWDADVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 161 VLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEWILELDRGRGIPWK 240
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 241 GNYSTWLEQKGERLAQEQKSEEAHAKALKKELEWSRQNPKARQAKSKSRLARFEELSDVEYQKRNETQEIFIPVAERLGS 320
Cdd:TIGR03719 241 GNYSSWLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLARYEELLSQEFQKRNETAEIYIPPGPRLGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 321 QVFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQARDALADQ 400
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 401 KTVWEDISGGLDIINVGKFQMASRAYAGRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLR 480
Cdd:TIGR03719 401 KTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLR 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 481 ALEDALLEFAGTVMVISHDRWFLDRIATHILAAEGDSQWTFFDGNYQEYEADKKKRLGEEGAKPKRMRYKAL 552
Cdd:TIGR03719 481 ALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEWFEGNFSEYEEDKKRRLGEDADQPHRIKYKKL 552
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-532 |
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: 705.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 8 MNRVSKTVPpKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALPMPGLTIGYLEQEPKLNPEHTVR 87
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 88 ESVEESMGAVNAAKKRLEEVYELYAAEDADFDALAAEQAELEAIiatAGTDSEHQLEIAADALRLPA--WDAKIGVLSGG 165
Cdd:COG0488 80 DTVLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEAL---GGWEAEARAEEILSGLGFPEedLDRPVSELSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 166 EKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEWILELDRGRGIPWKGNYST 245
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 246 WLEQKGERLAQEQKSEEAHAKALKKELEWSRQN-PKARQAK-SKSRLARFEELSDVEYQKRNETQEIFIPVAERLGSQVF 323
Cdd:COG0488 237 YLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFrAKARKAKqAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLGKKVL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQARDALADQKTV 403
Cdd:COG0488 317 ELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 404 WEDISGGLDiinvGKFQMASRAYAGRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALE 483
Cdd:COG0488 397 LDELRDGAP----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 518484691 484 DALLEFAGTVMVISHDRWFLDRIATHILAAEgDSQWTFFDGNYQEYEAD 532
Cdd:COG0488 473 EALDDFPGTVLLVSHDRYFLDRVATRILEFE-DGGVREYPGGYDDYLEK 520
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-528 |
1.65e-108 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 337.69 E-value: 1.65e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 31 PGAKIGVLGLNGSGKSTLLKIMAGvdkEI---EGEALPMPGLTIGYLEQEPKLNPEHTVRESVEESMGAVNAAKKRLEEV 107
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKILNG---EVlldDGRIIYEQDLIVARLQQDPPRNVEGTVYDFVAEGIEEQAEYLKRYHDI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 108 YELYAAEDADfdALAAEQAELEAIIatagtdsEH----QLE--IAA--DALRLPAwDAKIGVLSGGEKRRVALCRLLLSK 179
Cdd:PRK11147 105 SHLVETDPSE--KNLNELAKLQEQL-------DHhnlwQLEnrINEvlAQLGLDP-DAALSSLSGGWLRKAALGRALVSN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 180 PDMLLLDEPTNHLDAESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEWILELDRGRGIPWKGNYSTWLEQKGERLAQEQK 259
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALRVEEL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 260 SEEAHAKALKKELEWSRQNPKARQAKSKSRLARFEELSdVEYQKRNETQ---EIFIPVAERLGSQVFEFKNVSKSFGDRL 336
Cdd:PRK11147 255 QNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALR-RERSERREVMgtaKMQVEEASRSGKIVFEMENVNYQIDGKQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 337 LIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQARDALADQKTVWEDISGGLDIINV 416
Cdd:PRK11147 334 LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTVMDNLAEGKQEVMV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 417 GKFQMASRAYAGRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAGTVMVI 496
Cdd:PRK11147 414 NGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLV 493
|
490 500 510
....*....|....*....|....*....|..
gi 518484691 497 SHDRWFLDRIATHILAAEGDSQWTFFDGNYQE 528
Cdd:PRK11147 494 SHDRQFVDNTVTECWIFEGNGKIGRYVGGYHD 525
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
25-533 |
2.81e-79 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 258.28 E-value: 2.81e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 25 ISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALPMPGLTIGYLEQEPKLNPEHTVRESVeeSMGAVN--AAKK 102
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTV--IMGHTElwEVKQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 103 RLEEVYELyaAEDADFDALAAeqAELEAIIA-----TA-----------GTDSE-HQLEIAADAlrlPAWdakigvlsgg 165
Cdd:PRK15064 98 ERDRIYAL--PEMSEEDGMKV--ADLEVKFAemdgyTAearagelllgvGIPEEqHYGLMSEVA---PGW---------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 166 eKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEWILELDRGRGIPWKGNYST 245
Cdd:PRK15064 161 -KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 246 WLEQKGerLAQEQK-SEEAHAKALKKELE-----WSRQNPKARQAKSKSRLARFEELSDVEYQKRnetQEIFIPVAE--R 317
Cdd:PRK15064 240 YMTAAT--QARERLlADNAKKKAQIAELQsfvsrFSANASKAKQATSRAKQIDKIKLEEVKPSSR---QNPFIRFEQdkK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 318 LGSQVFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFV--DQARD 395
Cdd:PRK15064 315 LHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYaqDHAYD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 396 aLADQKTVWEDIS----GGLDIINVgkfqmasRAYAGRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPS 471
Cdd:PRK15064 395 -FENDLTLFDWMSqwrqEGDDEQAV-------RGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 472 NDLDVETLRALEDALLEFAGTVMVISHDRWFLDRIATHILAAEGDsQWTFFDGNYQEYEADK 533
Cdd:PRK15064 467 NHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPD-GVVDFSGTYEEYLRSQ 527
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-545 |
1.27e-68 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 233.14 E-value: 1.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGvDKEIEGEALPMPG-LTIGYLEQE-PKLnpEHTVRESVEESMGA 96
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKN-EISADGGSYTFPGnWQLAWVNQEtPAL--PQPALEYVIDGDRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 97 VNAAKKRLEEvyelyAAEDADFDALAAEQAELEAI----IATAGTDSEHQLEIAADALRLPAWDakigvLSGGEKRRVAL 172
Cdd:PRK10636 91 YRQLEAQLHD-----ANERNDGHAIATIHGKLDAIdawtIRSRAASLLHGLGFSNEQLERPVSD-----FSGGWRMRLNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 173 CRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEWILELDRGRGIPWKGNYSTWLEQKGE 252
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 253 RLAQEQ---KSEEAHAKALKKELEWSR-QNPKARQAKSKSR-LARFEELSDVEYQkrNETQEIFiPVAERLGSQVFEFKN 327
Cdd:PRK10636 241 RLAQQQamyESQQERVAHLQSYIDRFRaKATKAKQAQSRIKmLERMELIAPAHVD--NPFHFSF-RAPESLPNPLLKMEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 328 VSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQARDAL--ADQKTVWE 405
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFlrADESPLQH 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 406 disggLDIINVGKFQMASRAYAGRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDA 485
Cdd:PRK10636 398 -----LARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 486 LLEFAGTVMVISHDRWFLdRIATHILAAEGDSQWTFFDG---NYQEYEADKKKRLGEEGAKPK 545
Cdd:PRK10636 473 LIDFEGALVVVSHDRHLL-RSTTDDLYLVHDGKVEPFDGdleDYQQWLSDVQKQENQTDEAPK 534
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
325-537 |
8.24e-64 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 217.24 E-value: 8.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 325 FKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQArDALADQKTVW 404
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQE-PPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 405 EDISGGL----------------------DIINVGKFQMA----------SRA--YAGRFNFNGADQQKKVGTLSGGERG 450
Cdd:COG0488 80 DTVLDGDaelraleaeleeleaklaepdeDLERLAELQEEfealggweaeARAeeILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 451 RLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAGTVMVISHDRWFLDRIATHILAAEgDSQWTFFDGNYQEYE 530
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELD-RGKLTLYPGNYSAYL 238
|
....*..
gi 518484691 531 ADKKKRL 537
Cdd:COG0488 239 EQRAERL 245
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-530 |
7.47e-61 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 213.57 E-value: 7.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMA--------------GVDKEIEG--------------EALPMPGLT 70
Cdd:PLN03073 190 RDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipkncqilHVEQEVVGddttalqcvlntdiERTQLLEEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 71 IGYLEQEPKLNPEHTVRESVEESMGAVN--AAKKRLEEVYELYAAEDADfdalaAEQAELEAIIATAGTDSEHQLEiaad 148
Cdd:PLN03073 270 AQLVAQQRELEFETETGKGKGANKDGVDkdAVSQRLEEIYKRLELIDAY-----TAEARAASILAGLSFTPEMQVK---- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 149 alrlpawdaKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEWI 228
Cdd:PLN03073 341 ---------ATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDI 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 229 LELDRGRGIPWKGNYSTWLEQKGERLAQEQKSEEAHAKA---LKKELEWSRQNPKaRQAKSKSRLARFEELSDVEYQKRN 305
Cdd:PLN03073 412 LHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSrshMQAFIDKFRYNAK-RASLVQSRIKALDRLGHVDAVVND 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 306 ETQEIFIPVAE-RLGSQVFEFKNVSKSF-GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQ 383
Cdd:PLN03073 491 PDYKFEFPTPDdRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 384 TVKMAFVDQARdaladqktvwediSGGLDIINVGKFQMAS----------RAYAGRFNFNGADQQKKVGTLSGGERGRLH 453
Cdd:PLN03073 571 KVRMAVFSQHH-------------VDGLDLSSNPLLYMMRcfpgvpeqklRAHLGSFGVTGNLALQPMYTLSGGQKSRVA 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 454 LAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAGTVMVISHDRwfldriatHILAAEGDSQW-------TFFDGNY 526
Cdd:PLN03073 638 FAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDE--------HLISGSVDELWvvsegkvTPFHGTF 709
|
....
gi 518484691 527 QEYE 530
Cdd:PLN03073 710 HDYK 713
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
324-516 |
1.49e-56 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 186.12 E-value: 1.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQardaladqktv 403
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 404 wedisggldiinvgkfqmasrayagrfnfngadqqkkvgtLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALE 483
Cdd:cd03221 71 ----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE 110
|
170 180 190
....*....|....*....|....*....|...
gi 518484691 484 DALLEFAGTVMVISHDRWFLDRIATHILAAEGD 516
Cdd:cd03221 111 EALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-235 |
8.96e-53 |
|
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: 176.10 E-value: 8.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 7 SMNRVSKTVPpKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALPMPGLTIGYLEQepklnpehtv 86
Cdd:cd03221 2 ELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 87 resveesmgavnaakkrleevyelyaaedadfdalaaeqaeleaiiatagtdsehqleiaadalrlpawdakigvLSGGE 166
Cdd:cd03221 71 ---------------------------------------------------------------------------LSGGE 75
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518484691 167 KRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:cd03221 76 KMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-511 |
1.74e-42 |
|
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: 159.30 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV---DKEIEGEAL-----------PMPGLTIGYLEQEPK--LNP 82
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLldgrdllelseALRGRRIGMVFQDPMtqLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 83 eHTVRESVEESMGAVNAAKK-RLEEVYELyaaedadfdalaAEQAELEAIiatagtdsehqleiaadalrlpaWDAKIGV 161
Cdd:COG1123 99 -VTVGDQIAEALENLGLSRAeARARVLEL------------LEAVGLERR-----------------------LDRYPHQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 162 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEWILELDRGRGI 237
Cdd:COG1123 143 LSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 238 pwkgnystwleqkgerlaqeqksEEAHAKALkkelewsrqnpkarqaksksrLARFEELSDVEyqkRNETQEIFIPVAER 317
Cdd:COG1123 223 -----------------------EDGPPEEI---------------------LAAPQALAAVP---RLGAARGRAAPAAA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 318 LGSQVFEFKNVSKSF-----GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV------ 385
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdGKDLtklsrr 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 386 -------KMAFVDQ-ARDALADQKTVWEDISGGLDIINVGKF-QMASRAYA--GRFNFNGADQQKKVGTLSGGERGRLHL 454
Cdd:COG1123 336 slrelrrRVQMVFQdPYSSLNPRMTVGDIIAEPLRLHGLLSRaERRERVAEllERVGLPPDLADRYPHELSGGQRQRVAI 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518484691 455 AKTLIAGGNVLLLDEPSNDLDVET----LRALEDALLEFAGTVMVISHDRWFLDRIATHIL 511
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVqaqiLNLLRDLQRELGLTYLFISHDLAVVRYIADRVA 476
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
324-511 |
5.05e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 137.12 E-value: 5.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV---------KMAFVDQa 393
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlGEDVardpaevrrRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 394 RDALADQKTVWE--DISGGLDIINVGKFQMASRAYAGRFNFNGAdQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPS 471
Cdd:COG1131 81 EPALYPDLTVREnlRFFARLYGLPRKEARERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 518484691 472 NDLDVETLRALEDALLEFAG---TVMVISHDRWFLDRIATHIL 511
Cdd:COG1131 160 SGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCDRVA 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
322-511 |
1.18e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 136.37 E-value: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV-----KMAFVDQARD 395
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPrrarrRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 396 ALADQK-TVWEDISGGLDiINVGKFQMASRAYAGRfnfngADQ-----------QKKVGTLSGGERGRLHLAKTLIAGGN 463
Cdd:COG1121 86 VDWDFPiTVRDVVLMGRY-GRRGLFRRPSRADREA-----VDEalervgledlaDRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518484691 464 VLLLDEPSNDLDVETLRALEDALLEFAG---TVMVISHDRWFLDRIATHIL 511
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVL 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
324-511 |
4.41e-35 |
|
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: 131.12 E-value: 4.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEV-VIGQTVKM-----AFVDQARDAL 397
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrVFGKPLEKerkriGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 398 ADQK-TVWEDISGGLDiINVGKFQMASRAYA----------GRFNFngADQQkkVGTLSGGERGRLHLAKTLIAGGNVLL 466
Cdd:cd03235 81 RDFPiSVRDVVLMGLY-GHKGLFRRLSKADKakvdealervGLSEL--ADRQ--IGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518484691 467 LDEPSNDLDVETLRALEDALLEFAG---TVMVISHDRWFLDRIATHIL 511
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVL 203
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
324-511 |
4.83e-35 |
|
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: 131.90 E-value: 4.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV---------KMAFVDQA 393
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdGEDVrkeprearrQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 394 RdALADQKTVWEDI------SGGLDIINVGKFQMasraYAGRFNFnGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLL 467
Cdd:COG4555 83 R-GLYDRLTVRENIryfaelYGLFDEELKKRIEE----LIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518484691 468 DEPSNDLDVETLRALEDALLEFAG---TVMVISHDRWFLDRIATHIL 511
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRVV 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
324-511 |
8.64e-35 |
|
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: 129.05 E-value: 8.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARD--ALADQ 400
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDIKKEPEEVKRRigYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 401 KTVWEDISggldiinvgkfqmasrayaGRFNFNgadqqkkvgtLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLR 480
Cdd:cd03230 82 PSLYENLT-------------------VRENLK----------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180 190
....*....|....*....|....*....|....
gi 518484691 481 ALEDALLEFA---GTVMVISHDRWFLDRIATHIL 511
Cdd:cd03230 133 EFWELLRELKkegKTILLSSHILEEAERLCDRVA 166
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
323-511 |
2.08e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.17 E-value: 2.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 323 FEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV----------KMAFVD 391
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdGKPLsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 392 QARDALADqkTVWEDISGGLDIINVGKFQMASRAYAGRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPS 471
Cdd:COG4619 81 QEPALWGG--TVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518484691 472 NDLDVETLRALEDALLEFA----GTVMVISHDRWFLDRIATHIL 511
Cdd:COG4619 159 SALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVL 202
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
324-507 |
4.55e-34 |
|
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: 128.41 E-value: 4.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVK----------MAFVDq 392
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDVTgvpperrnigMVFQD- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 393 arDALADQKTVWEDISGGLDIINVGKFQMASRAYAGRFNFNGADQ-QKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPS 471
Cdd:cd03259 81 --YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLlNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518484691 472 NDLDVET---LRALEDALLEFAG-TVMVISHDR----WFLDRIA 507
Cdd:cd03259 159 SALDAKLreeLREELKELQRELGiTTIYVTHDQeealALADRIA 202
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
324-511 |
6.31e-34 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 125.82 E-value: 6.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDALAdqkt 402
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIdGKDIAKLPLEELRRRIG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 403 vwedisggldIInvgkFQmasrayagrfnfngadqqkkvgtLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRAL 482
Cdd:cd00267 77 ----------YV----PQ-----------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|..
gi 518484691 483 EDALLEFAG---TVMVISHDRWFLDRIATHIL 511
Cdd:cd00267 120 LELLRELAEegrTVIIVTHDPELAELAADRVI 151
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
19-235 |
1.28e-33 |
|
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: 126.82 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEALPMPGLT----IGYLEQEPKLNPEHTVRE 88
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPpsagevLWNGEPIRDAREDyrrrLAYLGHADGLKPELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 89 SVeesmgavnaakkrleevyELYAAedadFDALAAEQAELEAiiatagtdsehqleiAADALRL-PAWDAKIGVLSGGEK 167
Cdd:COG4133 95 NL------------------RFWAA----LYGLRADREAIDE---------------ALEAVGLaGLADLPVRQLSAGQK 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518484691 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFP---GTVVAITHDRYFLDNAAEwiLELDRGR 235
Cdd:COG4133 138 RRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAARV--LDLGDFK 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
324-511 |
1.75e-33 |
|
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: 126.43 E-value: 1.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGD--RLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDALA-- 398
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLTKLSLKELRRKVGlv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 399 -----DQ---KTVWEDISGGLDIINVGKFQMASRA--YAGRFNFNGAdQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLD 468
Cdd:cd03225 81 fqnpdDQffgPTVEEEVAFGLENLGLPEEEIEERVeeALELVGLEGL-RDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518484691 469 EPSNDLDVETLRALEDALLEFAG---TVMVISHDRWFLDRIATHIL 511
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVI 205
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
322-512 |
2.31e-33 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 127.47 E-value: 2.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV----------KMAFV 390
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLaslsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 391 DQARDALADQkTVwedisggLDIINVGKFqmasrAYAGRF-NFNGADQQ----------------KKVGTLSGGERGRLH 453
Cdd:COG1120 81 PQEPPAPFGL-TV-------RELVALGRY-----PHLGLFgRPSAEDREaveealertglehladRPVDELSGGERQRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 454 LAKTLIAGGNVLLLDEPSNDLD----VETLRALEDaLLEFAG-TVMVISHDrwfLD---RIATHILA 512
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDlahqLEVLELLRR-LARERGrTVVMVLHD---LNlaaRYADRLVL 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-190 |
3.27e-33 |
|
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: 123.91 E-value: 3.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL-----------PMPGLTIGYLEQEPKLNPEHTVRESV 90
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 91 EESMgavnaakkrleEVYELYAAEDadfdalaaeQAELEAIIATAGtdsehQLEIAADALRLPAwdakiGVLSGGEKRRV 170
Cdd:pfam00005 81 RLGL-----------LLKGLSKREK---------DARAEEALEKLG-----LGDLADRPVGERP-----GTLSGGQRQRV 130
|
170 180
....*....|....*....|
gi 518484691 171 ALCRLLLSKPDMLLLDEPTN 190
Cdd:pfam00005 131 AIARALLTKPKLLLLDEPTA 150
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
17-237 |
4.20e-33 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 126.70 E-value: 4.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 17 PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLT-------IGYLEQEPKLNPEHT 85
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgrDLASLSrrelarrIAYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 86 VRESVeeSMGavnaakkRLeevyelyaaedADFDALAAEQAELEAIIATAgtdsEHQLEIAADALRLpawdakIGVLSGG 165
Cdd:COG1120 92 VRELV--ALG-------RY-----------PHLGLFGRPSAEDREAVEEA----LERTGLEHLADRP------VDELSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518484691 166 EKRRVALCRLLLSKPDMLLLDEPTNHLD-AESVEWLEVF--LQRFPG-TVVAITHDryfLDNAAEW---ILELDRGRGI 237
Cdd:COG1120 142 ERQRVLIARALAQEPPLLLLDEPTSHLDlAHQLEVLELLrrLARERGrTVVMVLHD---LNLAARYadrLVLLKDGRIV 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-235 |
7.97e-33 |
|
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: 124.89 E-value: 7.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 7 SMNRVSKTVPPK-RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE-----------ALPMPGLTIGYL 74
Cdd:cd03225 1 ELKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEvlvdgkdltklSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 75 EQepklNPEH-----TVREsvEESMGAVNaakkrleevyelyaaedadfdaLAAEQAELEAIIATAgtdsehqleiaADA 149
Cdd:cd03225 81 FQ----NPDDqffgpTVEE--EVAFGLEN----------------------LGLPEEEIEERVEEA-----------LEL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 150 LRLPAW-DAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG---TVVAITHDRYFLDNAA 225
Cdd:cd03225 122 VGLEGLrDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELA 201
|
250
....*....|
gi 518484691 226 EWILELDRGR 235
Cdd:cd03225 202 DRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-235 |
8.83e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.59 E-value: 8.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEALPMPGLTIGYLEQEPKLNPEH--TVRES 89
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPptsgtvRLFGKPPRRARRRIGYVPQRAEVDWDFpiTVRDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 90 VeeSMGAVnaAKKRLeevYELYAAEDADfdalAAEQAeLEaiiatagtdsehQLEIAADAlrlpawDAKIGVLSGGEKRR 169
Cdd:COG1121 98 V--LMGRY--GRRGL---FRRPSRADRE----AVDEA-LE------------RVGLEDLA------DRPIGELSGGQQQR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518484691 170 VALCRLLLSKPDMLLLDEPTNHLDAESVEWL-EVF--LQRFPGTVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALyELLreLRREGKTILVVTHDLGAVREYFDRVLLLNRGL 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
19-235 |
1.30e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 124.16 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL-------PMPGLT----IGYLEQEPKLnPEHTVR 87
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkplsAMPPPEwrrqVAYVPQEPAL-WGGTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 88 EsveesmgavNaakkrLEEVYELyaaEDADFDALAAEQAeLEaiiatagtdsehQLEIAADALrlpawDAKIGVLSGGEK 167
Cdd:COG4619 92 D---------N-----LPFPFQL---RERKFDRERALEL-LE------------RLGLPPDIL-----DKPVERLSGGER 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFP----GTVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:COG4619 137 QRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
322-499 |
2.86e-32 |
|
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: 122.97 E-value: 2.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQAR------ 394
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWnGEPIRDAREDYRRrlaylg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 395 --DALADQKTVWEdisggldiiNVgkfQMASRAYAGRFNFNGADQ-----------QKKVGTLSGGERGRLHLAKTLIAG 461
Cdd:COG4133 82 haDGLKPELTVRE---------NL---RFWAALYGLRADREAIDEaleavglaglaDLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518484691 462 GNVLLLDEPSNDLDVETLRALEDALLEFA---GTVMVISHD 499
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQ 190
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
324-512 |
4.34e-32 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 121.77 E-value: 4.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV----------KMAFVDQ 392
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLdGKDLaslspkelarKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 393 ArdaladqktvwedisggLDIINVGKFqmasrayAGRFnfngadqqkkVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSN 472
Cdd:cd03214 81 A-----------------LELLGLAHL-------ADRP----------FNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518484691 473 DLDV-------ETLRALEDallEFAGTVMVISHDRWFLDRIATHILA 512
Cdd:cd03214 127 HLDIahqiellELLRRLAR---ERGKTVVMVLHDLNLAARYADRVIL 170
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
338-472 |
4.69e-32 |
|
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: 120.45 E-value: 4.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 338 IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV----------KMAFVDQArDALADQKTVWED 406
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdGQDLtdderkslrkEIGYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518484691 407 ISGGLDIINVGKFQMASRAYAGRFNFNGADQQKKV-----GTLSGGERGRLHLAKTLIAGGNVLLLDEPSN 472
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
323-511 |
2.45e-31 |
|
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: 121.29 E-value: 2.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 323 FEFKNVSKSF-GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDALA-- 398
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdGKDITKKNLRELRRKVGlv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 399 -----DQ---KTVWEDISGGLDIINVGKFQMASRA--YAGRFNFNG-ADqqKKVGTLSGGERGRLHLAKTLIAGGNVLLL 467
Cdd:COG1122 81 fqnpdDQlfaPTVEEDVAFGPENLGLPREEIRERVeeALELVGLEHlAD--RPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518484691 468 DEPSNDLDVETLRALEDALLEFAG---TVMVISHDRWFLDRIATHIL 511
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVI 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-235 |
3.11e-31 |
|
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: 120.90 E-value: 3.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 11 VSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV-----------DKEIEGEALPMPGLTIGYLEQepk 79
Cdd:COG1122 6 LSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLlkptsgevlvdGKDITKKNLRELRRKVGLVFQ--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 80 lNPEH-----TVRESVeeSMGAVNaakkrleevyelyaaedadfdaLAAEQAELEAIIATAgtdsehqleiaADALRLPA 154
Cdd:COG1122 83 -NPDDqlfapTVEEDV--AFGPEN----------------------LGLPREEIRERVEEA-----------LELVGLEH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 155 W-DAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG---TVVAITHDRYFLDNAAEWILE 230
Cdd:COG1122 127 LaDRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIV 206
|
....*
gi 518484691 231 LDRGR 235
Cdd:COG1122 207 LDDGR 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
324-510 |
6.38e-31 |
|
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: 119.92 E-value: 6.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGD--RLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQAR------- 394
Cdd:cd03263 2 QIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARqslgycp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 395 --DALADQKTVWE--DISGGLDIINVGKFQMASRAYAGRFNFnGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEP 470
Cdd:cd03263 82 qfDALFDELTVREhlRFYARLKGLPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518484691 471 SNDLDVETLRALEDALLEFAG--TVMVISHDRWFLDRIATHI 510
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRI 202
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
324-499 |
6.66e-31 |
|
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: 119.88 E-value: 6.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDR----LLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEV------VIGQTVKMAFVDQa 393
Cdd:cd03293 2 EVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepVTGPGPDRGYVFQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 394 RDALADQKTVWEDISGGLDIINVGKFQMASRAyagrfnfngADQQKKVG----------TLSGGERGRLHLAKTLIAGGN 463
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARERA---------EELLELVGlsgfenayphQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518484691 464 VLLLDEPSNDLDVETLRALEDALL----EFAGTVMVISHD 499
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLdiwrETGKTVLLVTHD 191
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-507 |
1.85e-30 |
|
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: 124.91 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVD--KEIEGEALPMPGL--TIGYLEQEPKLNPEHTVRESV--EES 93
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHVALceKCGYVERPSKVGEPCPVCGGTlePEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 94 MGAVNAAKKRLEEVYELYAAEDADFDALAAEQAELEAIIAT---AGTDSEHQLEIAADALRLPAWDAKIG----VLSGGE 166
Cdd:TIGR03269 94 VDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEAleeIGYEGKEAVGRAVDLIEMVQLSHRIThiarDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 167 KRRVALCRLLLSKPDMLLLDEPTNHLDAESVEW----LEVFLQRFPGTVVAITHDRYFLDNAAEwileldrgrgipwkgn 242
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDLSD---------------- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 243 YSTWLEqKGErLAQEQKSEEAHAKALkkelewsrqnpkarqaksksrlarfEELSDVEYQKRNEtqeifipvaerLGSQV 322
Cdd:TIGR03269 238 KAIWLE-NGE-IKEEGTPDEVVAVFM-------------------------EGVSEVEKECEVE-----------VGEPI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 323 FEFKNVSKSFG--DRLLI---DNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGE--VVIGQ----TVKMAFVD 391
Cdd:TIGR03269 280 IKVRNVSKRYIsvDRGVVkavDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDewvdMTKPGPDG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 392 QARD-----------ALADQKTVWEDISG--GLDIinvgKFQMASRAYAGRFNFNGADQQKKVG-------TLSGGERGR 451
Cdd:TIGR03269 360 RGRAkryigilhqeyDLYPHRTVLDNLTEaiGLEL----PDELARMKAVITLKMVGFDEEKAEEildkypdELSEGERHR 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518484691 452 LHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALL----EFAGTVMVISHDRWFL----DRIA 507
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILkareEMEQTFIIVSHDMDFVldvcDRAA 499
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
324-498 |
1.92e-30 |
|
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: 116.71 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRL--LIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDALA-- 398
Cdd:cd03228 2 EFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIdGVDLRDLDLESLRKNIAyv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 399 DQK------TVWEDIsggldiinvgkfqmasrayagrfnfngadqqkkvgtLSGGERGRLHLAKTLIAGGNVLLLDEPSN 472
Cdd:cd03228 82 PQDpflfsgTIRENI------------------------------------LSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180
....*....|....*....|....*...
gi 518484691 473 DLDVETLRALEDALLEFAG--TVMVISH 498
Cdd:cd03228 126 ALDPETEALILEALRALAKgkTVIVIAH 153
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-251 |
3.54e-30 |
|
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: 124.49 E-value: 3.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 7 SMNRVSKTVPP-KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGL-------TIGYL 74
Cdd:COG4987 335 ELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvDLRDLdeddlrrRIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 75 EQEPklnpeH----TVRESVeesmgavnaakkrleevyeLYAAEDADFDAL--AAEQAELEAIIAtagtdsehqleiaad 148
Cdd:COG4987 415 PQRP-----HlfdtTLRENL-------------------RLARPDATDEELwaALERVGLGDWLA--------------- 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 149 alRLPA-WDAKIGV----LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESV-EWLEVFLQRFPG-TVVAITHDRYFL 221
Cdd:COG4987 456 --ALPDgLDTWLGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEqALLADLLEALAGrTVLLITHRLAGL 533
|
250 260 270
....*....|....*....|....*....|
gi 518484691 222 DNAAEwILELDRGRGIPwKGNYSTWLEQKG 251
Cdd:COG4987 534 ERMDR-ILVLEDGRIVE-QGTHEELLAQNG 561
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-258 |
4.09e-30 |
|
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: 125.33 E-value: 4.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 6 YSMNRVSKTVPPKRQ-ILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE---------ALPMPGLT--IGY 73
Cdd:COG2274 474 IELENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRilidgidlrQIDPASLRrqIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 74 LEQEPKLNPEhTVRESVeeSMGAVNAAKKRLEEvyelyaaedadfdalAAEQAELEAIIAtagtdsehqleiaadalRLP 153
Cdd:COG2274 554 VLQDVFLFSG-TIRENI--TLGDPDATDEEIIE---------------AARLAGLHDFIE-----------------ALP 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 154 A-WDAKIG----VLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG--TVVAITHDRYFLDNaAE 226
Cdd:COG2274 599 MgYDTVVGeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL-AD 677
|
250 260 270
....*....|....*....|....*....|....
gi 518484691 227 WILELDRGRgIPWKGNYSTWLEQKGE--RLAQEQ 258
Cdd:COG2274 678 RIIVLDKGR-IVEDGTHEELLARKGLyaELVQQQ 710
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
324-499 |
5.74e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 118.27 E-value: 5.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSF----GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVK-----MAFVDQa 393
Cdd:COG1116 9 ELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdGKPVTgpgpdRGVVFQ- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 394 RDALADQKTVWEDISGGLDIINVGKFQMASRA--YAGRFNFNGAdQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPS 471
Cdd:COG1116 88 EPALLPWLTVLDNVALGLELRGVPKAERRERAreLLELVGLAGF-EDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPF 166
|
170 180 190
....*....|....*....|....*....|..
gi 518484691 472 NDLDVETLRALEDALLEFAG----TVMVISHD 499
Cdd:COG1116 167 GALDALTRERLQDELLRLWQetgkTVLFVTHD 198
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-234 |
1.47e-29 |
|
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: 115.71 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEA------LPMPGLTIGYLEQEPKLNPEH--TVRESV 90
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrvfgkpLEKERKRIGYVPQRRSIDRDFpiSVRDVV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 91 eeSMGAVnaAKKRLeevYELYAAEDADfdalAAEQAeLEAIIATAgtdsehqleiaadalrlpAWDAKIGVLSGGEKRRV 170
Cdd:cd03235 92 --LMGLY--GHKGL---FRRLSKADKA----KVDEA-LERVGLSE------------------LADRQIGELSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 171 ALCRLLLSKPDMLLLDEPTNHLDAESVE-WLEVF--LQRFPGTVVAITHDRYFLDNAAEWILELDRG 234
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEdIYELLreLRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
11-251 |
2.09e-29 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 122.17 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 11 VSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLT-------IGYLEQEPK 79
Cdd:COG4988 342 VSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvDLSDLDpaswrrqIAWVPQNPY 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 80 LnPEHTVRESVeeSMGAVNAAKKRLEEvyelyaaedadfdalAAEQAELEAIIAtagtdsehqleiaadalRLPA-WDAK 158
Cdd:COG4988 422 L-FAGTIRENL--RLGRPDASDEELEA---------------ALEAAGLDEFVA-----------------ALPDgLDTP 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 159 IGV----LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESvEW--LEVFLQRFPG-TVVAITHDRYFLDNaAEWILEL 231
Cdd:COG4988 467 LGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAET-EAeiLQALRRLAKGrTVILITHRLALLAQ-ADRILVL 544
|
250 260
....*....|....*....|
gi 518484691 232 DRGRGIPwKGNYSTWLEQKG 251
Cdd:COG4988 545 DDGRIVE-QGTHEELLAKNG 563
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
323-512 |
2.21e-29 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 114.21 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 323 FEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV------------KMAF 389
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdGEDLtdledelpplrrRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 390 VDQaRDALADQKTVWEDIsggldiinvgkfqmasrAYAgrfnfngadqqkkvgtLSGGERGRLHLAKTLIAGGNVLLLDE 469
Cdd:cd03229 81 VFQ-DFALFPHLTVLENI-----------------ALG----------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518484691 470 PSNDLDVETLRALEDALL----EFAGTVMVISHDRWFLDRIATHILA 512
Cdd:cd03229 127 PTSALDPITRREVRALLKslqaQLGITVVLVTHDLDEAARLADRVVV 173
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
326-511 |
9.55e-29 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 113.12 E-value: 9.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKSFGD-RLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG--------QTVKMAFVDQARDa 396
Cdd:cd03226 3 ENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNgkpikakeRRKSIGYVMQDVD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 397 laDQ---KTVWEDISGGLDiiNVGKFQMASRAYAGRFNFNGADQQKKVgTLSGGERGRLHLAKTLIAGGNVLLLDEPSND 473
Cdd:cd03226 82 --YQlftDSVREELLLGLK--ELDAGNEQAETVLKDLDLYALKERHPL-SLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518484691 474 LDVETLRALEDALLEFAG---TVMVISHDRWFLDRIATHIL 511
Cdd:cd03226 157 LDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVL 197
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-515 |
1.14e-28 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 120.30 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 31 PGAKIGVLGLNGSGKSTLLKIMAG----------------------------------VDKEIEgealpmPGLTIGYLEQ 76
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGelipnlgdyeeepswdevlkrfrgtelqnyfkklYNGEIK------VVHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 77 EPKLnpehtVRESVEESMGAVNAAKKrLEEVyelyaaedadfdalaAEQAELEAIiatagtdsehqleiaadalrlpaWD 156
Cdd:PRK13409 172 IPKV-----FKGKVRELLKKVDERGK-LDEV---------------VERLGLENI-----------------------LD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 157 AKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAEsvewlevflQRF----------PG-TVVAITHDRYFLDNAA 225
Cdd:PRK13409 208 RDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR---------QRLnvarlirelaEGkYVLVVEHDLAVLDYLA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 226 EWILELdrgRGIPwkGNYSTWLEQKGERLAQEQkseeahakALKKELEwsRQNPKARQaksksrlarfeelSDVEYQKRN 305
Cdd:PRK13409 279 DNVHIA---YGEP--GAYGVVSKPKGVRVGINE--------YLKGYLP--EENMRIRP-------------EPIEFEERP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 306 ETQEIFIPVaerlgsqVFEFKNVSKSFGDrllidnLSFNVPAGAI-----VGIIGPNGAGKSTLFKLLAGKEKPDSGEVV 380
Cdd:PRK13409 331 PRDESERET-------LVEYPDLTKKLGD------FSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 381 IG-------QTVKMAFVDQARDALADQKT------VWEDISGGLDIINVgkfqmasrayagrfnfngadQQKKVGTLSGG 447
Cdd:PRK13409 398 PElkisykpQYIKPDYDGTVEDLLRSITDdlgssyYKSEIIKPLQLERL--------------------LDKNVKDLSGG 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 448 ERGRLHLAKTLIAGGNVLLLDEPSNDLDVE----TLRALEDALLEFAGTVMVISHDRWFLDRIATHILAAEG 515
Cdd:PRK13409 458 ELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
327-553 |
3.34e-28 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 118.90 E-value: 3.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 327 NVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQ--ARDAladQKTVW 404
Cdd:PRK11147 8 GAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQdpPRNV---EGTVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 405 EDISGGL----------------------------------DIINVGKFQMASrayagRFNFN----GADQQKKVGTLSG 446
Cdd:PRK11147 85 DFVAEGIeeqaeylkryhdishlvetdpseknlnelaklqeQLDHHNLWQLEN-----RINEVlaqlGLDPDAALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 447 GERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAGTVMVISHDRWFLDRIATHILAAEgDSQWTFFDGNY 526
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLD-RGKLVSYPGNY 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 518484691 527 QEY----------EADKK----KRLGEE------GAKPKRM----RYKALK 553
Cdd:PRK11147 239 DQYllekeealrvEELQNaefdRKLAQEevwirqGIKARRTrnegRVRALK 289
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-470 |
3.50e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.81 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 2 AQYVYSMNRVSKTVPPkRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV---DK---EIEGEALPMPG------L 69
Cdd:COG1129 1 AEPLLEMRGISKSFGG-VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVyqpDSgeiLLDGEPVRFRSprdaqaA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 70 TIGYLEQEPKLNPEHTVRESVeeSMGAVNAAKKRLeevyelyaaedaDFDALAAEQAELEAiiatagtdsehQLEIAADA 149
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENI--FLGREPRRGGLI------------DWRAMRRRARELLA-----------RLGLDIDP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 150 lrlpawDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG---TVVAITHdryFLDnaaE 226
Cdd:COG1129 135 ------DTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAqgvAIIYISH---RLD---E 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 227 wILEL-DR------GRGIpwkgnystwleqkGERLAQEQkseeahakalkkelewsrqnpkarqakSKSRLARF---EEL 296
Cdd:COG1129 203 -VFEIaDRvtvlrdGRLV-------------GTGPVAEL---------------------------TEDELVRLmvgREL 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 297 SDVEYQKRNETQEIfipvaerlgsqVFEFKNVSksfgDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDS 376
Cdd:COG1129 242 EDLFPKRAAAPGEV-----------VLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADS 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 377 GEVVI-GQTVK-----------MAFV--DQARDALADQKTVWEDIS---------GGLdiINVGKFQMASRAYAGRFNFN 433
Cdd:COG1129 307 GEIRLdGKPVRirsprdairagIAYVpeDRKGEGLVLDLSIRENITlasldrlsrGGL--LDRRRERALAEEYIKRLRIK 384
|
490 500 510
....*....|....*....|....*....|....*..
gi 518484691 434 GADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEP 470
Cdd:COG1129 385 TPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-235 |
4.47e-28 |
|
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: 109.64 E-value: 4.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 7 SMNRVSKTVPpKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpmpgltigYLEQEPKLNPEHTV 86
Cdd:cd00267 1 EIENLSFRYG-GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL--------IDGKDIAKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 87 RESVeesmGAVnaakkrleevyelyaaedadfdalaaeqaeleaiiatagtdseHQLeiaadalrlpawdakigvlSGGE 166
Cdd:cd00267 72 RRRI----GYV-------------------------------------------PQL-------------------SGGQ 85
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 167 KRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG---TVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:cd00267 86 RQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
326-510 |
6.52e-28 |
|
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: 111.15 E-value: 6.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQAR-DALADQKTV 403
Cdd:cd03268 4 NDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdGKSYQKNIEALRRiGALIEAPGF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 404 WEDISGGLDIINVGKFQMASRAYA----GRFNFnGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD---V 476
Cdd:cd03268 84 YPNLTARENLRLLARLLGIRKKRIdevlDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDpdgI 162
|
170 180 190
....*....|....*....|....*....|....
gi 518484691 477 ETLRALEDALLEFAGTVMVISHDRWFLDRIATHI 510
Cdd:cd03268 163 KELRELILSLRDQGITVLISSHLLSEIQKVADRI 196
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
324-511 |
1.02e-27 |
|
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: 110.66 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGD----RLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV------------- 385
Cdd:cd03255 2 ELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTDIsklsekelaafrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 386 -KMAFVDQARDALADQkTVWEDISGGLDIINVGKFQMASRAYA--GRFNFnGADQQKKVGTLSGGERGRLHLAKTLIAGG 462
Cdd:cd03255 82 rHIGFVFQSFNLLPDL-TALENVELPLLLAGVPKKERRERAEEllERVGL-GDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518484691 463 NVLLLDEPSNDLDVETLRALEDALLEFAG----TVMVISHDRwFLDRIATHIL 511
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKeagtTIVVVTHDP-ELAEYADRII 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
9-252 |
1.25e-27 |
|
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: 111.10 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 9 NRVSKTvPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEALPMPGLT----IGYLEQEP 78
Cdd:COG4555 5 ENLSKK-YGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKpdsgsiLIDGEDVRKEPREarrqIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 79 KLNPEHTVRESVE---ESMG-AVNAAKKRLEEVyelyaaedadfdalaAEQAELEAIIatagtdsehqleiaadalrlpa 154
Cdd:COG4555 84 GLYDRLTVRENIRyfaELYGlFDEELKKRIEEL---------------IELLGLEEFL---------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 155 wDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRF---PGTVVAITHDRYFLDNAAEWILEL 231
Cdd:COG4555 127 -DRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVIL 205
|
250 260
....*....|....*....|.
gi 518484691 232 DRGRgIPWKGNYSTWLEQKGE 252
Cdd:COG4555 206 HKGK-VVAQGSLDELREEIGE 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
11-235 |
1.80e-27 |
|
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: 109.89 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 11 VSKTVPP---KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGE---ALPMPGLT------IG 72
Cdd:cd03255 6 LSKTYGGggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRptsgevRVDGTdisKLSEKELAafrrrhIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 73 YLEQEPKLNPEHTVRESVEesMGAVNAAKKRLEevyelyaaedadfdalAAEQAE--LEaiiatagtdsehQLEIAADAL 150
Cdd:cd03255 86 FVFQSFNLLPDLTALENVE--LPLLLAGVPKKE----------------RRERAEelLE------------RVGLGDRLN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 151 RLPAWdakigvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAE-SVEWLEVF--LQRFPG-TVVAITHDRyFLDNAAE 226
Cdd:cd03255 136 HYPSE------LSGGQQQRVAIARALANDPKIILADEPTGNLDSEtGKEVMELLreLNKEAGtTIVVVTHDP-ELAEYAD 208
|
....*....
gi 518484691 227 WILELDRGR 235
Cdd:cd03255 209 RIIELRDGK 217
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
333-542 |
2.03e-27 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 116.81 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 333 GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQARDAL--------------- 397
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALpqpaleyvidgdrey 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 398 ---------ADQKTVWEDIS---GGLDIINVGKFQMASRAYAGRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVL 465
Cdd:PRK10636 92 rqleaqlhdANERNDGHAIAtihGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518484691 466 LLDEPSNDLDVETLRALEDALLEFAGTVMVISHDRWFLDRIATHILAAEgdsQWTFFD--GNYQEYEADKKKRLGEEGA 542
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIE---QQSLFEytGNYSSFEVQRATRLAQQQA 247
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
324-510 |
1.29e-26 |
|
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: 108.14 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV-------------KMAF 389
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVdGQDItglsekelyelrrRIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 390 VDQArDALADQKTVWEdisggldiiNVGkFQMasrayagRFNFNGADQQKK---------VG----------TLSGGERG 450
Cdd:COG1127 87 LFQG-GALFDSLTVFE---------NVA-FPL-------REHTDLSEAEIRelvleklelVGlpgaadkmpsELSGGMRK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518484691 451 RLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLE----FAGTVMVISHDRWFLDRIATHI 510
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHDLDSAFAIADRV 212
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
326-516 |
1.44e-26 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 107.91 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV-KMAFVDQARDALA----- 398
Cdd:cd03219 4 RGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFdGEDItGLPPHEIARLGIGrtfqi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 399 ----DQKTVWEDI--------SGGLDIINVGKFQMASRAYAGRF-NFNG----ADQQkkVGTLSGGERGRLHLAKTLIAG 461
Cdd:cd03219 84 prlfPELTVLENVmvaaqartGSGLLLARARREEREARERAEELlERVGladlADRP--AGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 462 GNVLLLDEPS---NDLDVETLRALEDALLEFAGTVMVISHDRWFLDRIATHILA-------AEGD 516
Cdd:cd03219 162 PKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVldqgrviAEGT 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
324-511 |
1.53e-26 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 108.35 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFG----DRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVK------------ 386
Cdd:COG1124 3 EVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdGRPVTrrrrkafrrrvq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 387 MAFVDqARDALADQKTVWEDISGGLDIInvGKFQMASR------------AYAGRFnfngadqqkkVGTLSGGERGRLHL 454
Cdd:COG1124 83 MVFQD-PYASLHPRHTVDRILAEPLRIH--GLPDREERiaelleqvglppSFLDRY----------PHQLSGGQRQRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518484691 455 AKTLIAGGNVLLLDEPSNDLDV----ETLRALEDALLEFAGTVMVISHDRWFLDRIATHIL 511
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVA 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
323-499 |
1.73e-26 |
|
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: 107.65 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 323 FEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAG-----KEKPDSGEVVI-GQTV----------- 385
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLdGKDIydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 386 -KMAFVDQARDALAdqKTVWEDISGGLDIINV-GKFQMASRAY-----AGRFNfNGADQQKKVGtLSGGERGRLHLAKTL 458
Cdd:cd03260 81 rRVGMVFQKPNPFP--GSIYDNVAYGLRLHGIkLKEELDERVEealrkAALWD-EVKDRLHALG-LSGGQQQRLCLARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 518484691 459 IAGGNVLLLDEPSNDLDVETLRALEDALLEFAG--TVMVISHD 499
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
324-507 |
2.36e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 110.19 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV--------KMAFVDQaR 394
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLdGRDVtglppekrNVGMVFQ-D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 395 DALADQKTVWEDISGGLDIINVGKFQMASRA-----------YAGRfnfngadqqkKVGTLSGGERGRLHLAKTLIAGGN 463
Cdd:COG3842 86 YALFPHLTVAENVAFGLRMRGVPKAEIRARVaellelvglegLADR----------YPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518484691 464 VLLLDEP-SNdLDV---ETLRA-LEDALLEFAGTVMVISHDR----WFLDRIA 507
Cdd:COG3842 156 VLLLDEPlSA-LDAklrEEMREeLRRLQRELGITFIYVTHDQeealALADRIA 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
293-499 |
2.71e-26 |
|
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: 113.39 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 293 FEELSDV-EYQKRNETQEIFIPVAERLGSqvFEFKNVSKSFGDR--LLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLA 369
Cdd:COG2274 445 LERLDDIlDLPPEREEGRSKLSLPRLKGD--IELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 370 GKEKPDSGEVVI-GQTVK----------MAFVDQARDALADqkTVWEDISGGLDIINVGKFQMASRAyAGRFNF-----N 433
Cdd:COG2274 523 GLYEPTSGRILIdGIDLRqidpaslrrqIGVVLQDVFLFSG--TIRENITLGDPDATDEEIIEAARL-AGLHDFiealpM 599
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 434 GADQQkkVG----TLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAG--TVMVISHD 499
Cdd:COG2274 600 GYDTV--VGeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHR 669
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
18-235 |
2.79e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 107.07 E-value: 2.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLT------IGYLEQEPKLNPEHTVR 87
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgeDVARDPaevrrrIGYVPQEPALYPDLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 88 ESveesmgavnaakkrLEEVYELYAAEDADFDALAAEQAELeaiiatagtdsehqLEIAADAlrlpawDAKIGVLSGGEK 167
Cdd:COG1131 92 EN--------------LRFFARLYGLPRKEARERIDELLEL--------------FGLTDAA------DRKVGTLSGGMK 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518484691 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG---TVVAITHDryfLDNA---AEWILELDRGR 235
Cdd:COG1131 138 QRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAegkTVLLSTHY---LEEAerlCDRVAIIDKGR 208
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
331-499 |
4.67e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.39 E-value: 4.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 331 SFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQaRDALADQ--KTVWEDIS 408
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ-RSEVPDSlpLTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 409 GGL--DIINVGKFQMASRAYAG----RFNFNG-ADQQkkVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRA 481
Cdd:NF040873 80 MGRwaRRGLWRRLTRDDRAAVDdaleRVGLADlAGRQ--LGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180
....*....|....*....|.
gi 518484691 482 LEDALLEFAG---TVMVISHD 499
Cdd:NF040873 158 IIALLAEEHArgaTVVVVTHD 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
324-511 |
4.76e-26 |
|
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: 106.51 E-value: 4.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDR----LLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDA-- 396
Cdd:cd03258 3 ELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdGTDLTLLSGKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 397 ----------LADQKTVWEDISGGLDIINVGKFQMASRAYAgRFNFNGADQQKKV--GTLSGGERGRLHLAKTLIAGGNV 464
Cdd:cd03258 83 rigmifqhfnLLSSRTVFENVALPLEIAGVPKAEIEERVLE-LLELVGLEDKADAypAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518484691 465 LLLDEPSNDLDVETLRALEDALL----EFAGTVMVISHDRWFLDRIATHIL 511
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRdinrELGLTIVLITHEMEVVKRICDRVA 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
324-500 |
1.57e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 107.88 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVdQARD------- 395
Cdd:PRK11432 8 VLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdGEDVTHRSI-QQRDicmvfqs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 396 -ALADQKTVWEDISGGLDIINVGKFQMASR-----------AYAGRFnfngADQqkkvgtLSGGERGRLHLAKTLIAGGN 463
Cdd:PRK11432 87 yALFPHMSLGENVGYGLKMLGVPKEERKQRvkealelvdlaGFEDRY----VDQ------ISGGQQQRVALARALILKPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518484691 464 VLLLDEPSNDLDVETLRALEDALLE----FAGTVMVISHDR 500
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRElqqqFNITSLYVTHDQ 197
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-235 |
1.57e-25 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 103.25 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 9 NRVSKTVPpKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLT------IGYLEQEP 78
Cdd:cd03230 4 RNLSKRYG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvlgkDIKKEPeevkrrIGYLPEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 79 KLNPEHTVRESVEesmgavnaakkrleevyelyaaedadfdalaaeqaeleaiiatagtdsehqleiaadalrlpawdak 158
Cdd:cd03230 83 SLYENLTVRENLK------------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 159 igvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRF---PGTVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:cd03230 96 ---LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
7-217 |
1.71e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 105.56 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 7 SMNRVSKTVPPK---RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEALPMPGLTIGYLEQE 77
Cdd:COG1116 9 ELRGVSKRFPTGgggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKptsgevLVDGKPVTGPGPDRGVVFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 78 PKLNPEHTVRESVeesmgavnaakkrleevyelyaaedadfdALAAEQAeleaiiataGTDSEHQLEIAADALRL----P 153
Cdd:COG1116 89 PALLPWLTVLDNV-----------------------------ALGLELR---------GVPKAERRERARELLELvglaG 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 154 AWDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDA---ESV-EWLEVFLQRFPGTVVAITHD 217
Cdd:COG1116 131 FEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltrERLqDELLRLWQETGKTVLFVTHD 198
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
324-511 |
1.89e-25 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 104.89 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV-------------KMAF 389
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdGEDIsglseaelyrlrrRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 390 VDQArDALADQKTVWEdisggldiiNVG-----KFQMASRAYAGRFNFN------GADQQKKVGTLSGGERGRLHLAKTL 458
Cdd:cd03261 82 LFQS-GALFDSLTVFE---------NVAfplreHTRLSEEEIREIVLEKleavglRGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 459 IAGGNVLLLDEPSNDLDVETLRALEDALL----EFAGTVMVISHDRWFLDRIATHIL 511
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRslkkELGLTSIMVTHDLDTAFAIADRIA 208
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-515 |
1.96e-25 |
|
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: 110.26 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 31 PGAKIGVLGLNGSGKSTLLKIMAGVDKeiegealpmPGLtiGYLEQEPklnpehTVRESVEESMGavNAAKKRLEEVY-- 108
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELK---------PNL--GDYDEEP------SWDEVLKRFRG--TELQDYFKKLAng 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 109 ELYAAEDADFDALAAEQAELEAIIATAGTDSEHQLEIAADALRL-PAWDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDE 187
Cdd:COG1245 159 EIKVAHKPQYVDLIPKVFKGTVRELLEKVDERGKLDELAEKLGLeNILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 188 PTNHLDAEsvEWLEVF-----LQRFPGTVVAITHDRYFLDNAAEWILELdrgRGIPwkGNYSTWLEQKGERLAQEQ---- 258
Cdd:COG1245 239 PSSYLDIY--QRLNVArlireLAEEGKYVLVVEHDLAILDYLADYVHIL---YGEP--GVYGVVSKPKSVRVGINQyldg 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 259 --KSEeahakalkkelewsrqNPKARQAKsksrlarfeelsdVEYQKRNETQEIFIPVaerlgsqVFEFKNVSKSFGDrl 336
Cdd:COG1245 312 ylPEE----------------NVRIRDEP-------------IEFEVHAPRREKEEET-------LVEYPDLTKSYGG-- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 337 lidnLSFNVPAGAI-----VGIIGPNGAGKSTLFKLLAGKEKPDSGEVviGQTVKMAF------------VDQA-RDALA 398
Cdd:COG1245 354 ----FSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYkpqyispdydgtVEEFlRSANT 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 399 DQ---KTVWEDISGGLDIinvgkfqmaSRAYagrfnfngadqQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD 475
Cdd:COG1245 428 DDfgsSYYKTEIIKPLGL---------EKLL-----------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 518484691 476 VE----TLRALEDALLEFAGTVMVISHDRWFLDRIATHILAAEG 515
Cdd:COG1245 488 VEqrlaVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
324-512 |
2.07e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 104.36 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSF-GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV-------------KMA 388
Cdd:COG2884 3 RFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVnGQDLsrlkrreipylrrRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 389 FVDQarDA-LADQKTVWEDISGGLDIINVGKFQMASRAYA--------GRFNfngadqqKKVGTLSGGERGRLHLAKTLI 459
Cdd:COG2884 83 VVFQ--DFrLLPDRTVYENVALPLRVTGKSRKEIRRRVREvldlvglsDKAK-------ALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 460 AGGNVLLLDEPSNDLDVETLRALEDALLEF--AG-TVMVISHDRWFLDRIATHILA 512
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEInrRGtTVLIATHDLELVDRMPKRVLE 209
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
326-499 |
2.21e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.20 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTvkmAFVDQARDALADQK---- 401
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR---PLAAWSPWELARRRavlp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 402 ---------TVWEDISGGL-----------DIIN-----VGKFQMASRAYAgrfnfngadqqkkvgTLSGGERGRLHLAK 456
Cdd:COG4559 82 qhsslafpfTVEEVVALGRaphgssaaqdrQIVRealalVGLAHLAGRSYQ---------------TLSGGEQQRVQLAR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 457 TLI-------AGGNVLLLDEPSNDLDV----ETLRALEDalleFA---GTVMVISHD 499
Cdd:COG4559 147 VLAqlwepvdGGPRWLFLDEPTSALDLahqhAVLRLARQ----LArrgGGVVAVLHD 199
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-235 |
2.50e-25 |
|
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: 104.21 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 6 YSMNRVSKTVPP-KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL---------PMPGL--TIGY 73
Cdd:cd03245 3 IEFRNVSFSYPNqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLldgtdirqlDPADLrrNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 74 LEQEPKLNpEHTVRESVEesMGAVNAAKKRLEEvyelyAAEDADFDALAAEQAE-LEAIIATAGTDsehqleiaadalrl 152
Cdd:cd03245 83 VPQDVTLF-YGTLRDNIT--LGAPLADDERILR-----AAELAGVTDFVNKHPNgLDLQIGERGRG-------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 153 pawdakigvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG--TVVAITHdRYFLDNAAEWILE 230
Cdd:cd03245 141 ---------LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIV 210
|
....*
gi 518484691 231 LDRGR 235
Cdd:cd03245 211 MDSGR 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
326-507 |
3.32e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.85 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEV--------------------VIGQTV 385
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrlngrpladwspaelarrraVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 386 KMAF-----------------VDQARDALADQKtvwedisggLDIINVGKFqmASRAYAgrfnfngadqqkkvgTLSGGE 448
Cdd:PRK13548 86 SLSFpftveevvamgraphglSRAEDDALVAAA---------LAQVDLAHL--AGRDYP---------------QLSGGE 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518484691 449 RGRLHLAKTLI------AGGNVLLLDEPSNDLDV----ETLRALEDALLEFAGTVMVISHD-----RWfLDRIA 507
Cdd:PRK13548 140 QQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHDlnlaaRY-ADRIV 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-251 |
5.38e-25 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 108.83 E-value: 5.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALPMPGLTIGYLEQEpklnpeHTvrESVEESMgav 97
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQD------HA--YDFENDL--- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 98 naakkRLEEVYELYAAEDADfdalaaEQAeleaIIATAGtdsehQLEIAADALRlpawdAKIGVLSGGEKRRVALCRLLL 177
Cdd:PRK15064 400 -----TLFDWMSQWRQEGDD------EQA----VRGTLG-----RLLFSQDDIK-----KSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518484691 178 SKPDMLLLDEPTNHLDAESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEWILELDRGRGIPWKGNYSTWLEQKG 251
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQG 528
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
323-498 |
6.73e-25 |
|
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: 100.97 E-value: 6.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 323 FEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDAladqk 401
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVdGKEVSFASPRDARRA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 402 tvwedisgGLDIInvgkFQmasrayagrfnfngadqqkkvgtLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRA 481
Cdd:cd03216 76 --------GIAMV----YQ-----------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180
....*....|....*....|
gi 518484691 482 LEDALLEFAG---TVMVISH 498
Cdd:cd03216 121 LFKVIRRLRAqgvAVIFISH 140
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-280 |
7.70e-25 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 108.88 E-value: 7.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 5 VYSMNRVSKTVPPKrQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALPMPGLTIGYLEQ-EPKLNPE 83
Cdd:PRK11147 319 VFEMENVNYQIDGK-QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQhRAELDPE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 84 HTVRESVEEsmgavnaAKKrleEVyelyaaedadfdalaaeqaeleaiiaTAGTDSEHQLEIAADALRLPAwDAKIGV-- 161
Cdd:PRK11147 398 KTVMDNLAE-------GKQ---EV--------------------------MVNGRPRHVLGYLQDFLFHPK-RAMTPVka 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 162 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPGTVVAITHDRYFLDNAAE--WILELDrGRGIPW 239
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTecWIFEGN-GKIGRY 519
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 518484691 240 KGNYSTWLEQKGERLAQEQKSEEAHAKALKKELEWSRQNPK 280
Cdd:PRK11147 520 VGGYHDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSK 560
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
324-500 |
9.46e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 105.61 E-value: 9.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV---------KMAFVDQa 393
Cdd:COG1118 4 EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLnGRDLftnlpprerRVGFVFQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 394 rD-ALADQKTVWEDISGGLDIINVGKFQMASRA-----------YAGRFnfngadqqkkVGTLSGGERGRLHLAKTLIAG 461
Cdd:COG1118 83 -HyALFPHMTVAENIAFGLRVRPPSKAEIRARVeellelvqlegLADRY----------PSQLSGGQRQRVALARALAVE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 518484691 462 GNVLLLDEPSNDLDVETLRALEDALL----EFAGTVMVISHDR 500
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRRWLRrlhdELGGTTVFVTHDQ 194
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-236 |
1.07e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.97 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 16 PPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE-ALPmPGLTIGYLEQEPKLnPEHTVRESVeesm 94
Cdd:COG4178 373 PDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRiARP-AGARVLFLPQRPYL-PLGTLREAL---- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 95 gavnaakkrleevyeLYAAEDADFDalaaeQAELEAIIATAG-TDSEHQLEIAADalrlpaWDAkigVLSGGEKRRVALC 173
Cdd:COG4178 447 ---------------LYPATAEAFS-----DAELREALEAVGlGHLAERLDEEAD------WDQ---VLSLGEQQRLAFA 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 174 RLLLSKPDMLLLDEPTNHLDAESVEWL-EVFLQRFPG-TVVAITHdRYFLDNAAEWILELDRGRG 236
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALyQLLREELPGtTVISVGH-RSTLAAFHDRVLELTGDGS 561
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-235 |
1.20e-24 |
|
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: 102.96 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 11 VSKTVPPK---RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEALPMPGL-----TIGYLEQ 76
Cdd:COG1124 7 LSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERpwsgevTFDGRPVTRRRRkafrrRVQMVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 77 EPK--LNPEHTVRESVEESMGA--VNAAKKRLEEvyelyaaedadfdalAAEQAELEAIIATagtdsehqleiaadalRL 152
Cdd:COG1124 87 DPYasLHPRHTVDRILAEPLRIhgLPDREERIAE---------------LLEQVGLPPSFLD----------------RY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 153 PAwdakigVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEWI 228
Cdd:COG1124 136 PH------QLSGGQRQRVAIARALILEPELLLLDEPTSALDvsvqAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRV 209
|
....*..
gi 518484691 229 LELDRGR 235
Cdd:COG1124 210 AVMQNGR 216
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-235 |
1.27e-24 |
|
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: 100.54 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 7 SMNRVSKTVPPK-RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEALPMPGLT-----IGYL 74
Cdd:cd03228 2 EFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDptsgeiLIDGVDLRDLDLEslrknIAYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 75 EQEPKLNPEhTVREsveesmgavNaakkrleevyelyaaedadfdalaaeqaeleaiiatagtdsehqleiaadalrlpa 154
Cdd:cd03228 82 PQDPFLFSG-TIRE---------N-------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 155 wdakigVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES-VEWLEVFLQRFPG-TVVAITHdRYFLDNAAEWILELD 232
Cdd:cd03228 96 ------ILSGGQRQRIAIARALLRDPPILILDEATSALDPETeALILEALRALAKGkTVIVIAH-RLSTIRDADRIIVLD 168
|
...
gi 518484691 233 RGR 235
Cdd:cd03228 169 DGR 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
324-511 |
1.54e-24 |
|
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: 107.54 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGD-RLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDALA--D 399
Cdd:COG4988 338 ELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILInGVDLSDLDPASWRRQIAwvP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 400 QKTVWedISGGL-DIINVGKFQmAS---------RAYAGRF---NFNGADQQkkVG----TLSGGERGRLHLAKTLIAGG 462
Cdd:COG4988 418 QNPYL--FAGTIrENLRLGRPD-ASdeeleaaleAAGLDEFvaaLPDGLDTP--LGeggrGLSGGQAQRLALARALLRDA 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518484691 463 NVLLLDEPSNDLDVETLRALEDALLEFAG--TVMVISHdRWFLDRIATHIL 511
Cdd:COG4988 493 PLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITH-RLALLAQADRIL 542
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
11-217 |
2.13e-24 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 101.43 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 11 VSKTVPPKR---QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALPMP--------------GLTIGY 73
Cdd:cd03257 7 LSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirRKEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 74 LEQEP--KLNPEHTVRESVEESMGAVNAAKKrleevyelyaaedadfdalaaEQAELEAIIAtagtdSEHQLEIAADAL- 150
Cdd:cd03257 87 VFQDPmsSLNPRMTIGEQIAEPLRIHGKLSK---------------------KEARKEAVLL-----LLVGVGLPEEVLn 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 151 RLPAWdakigvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAeSVEW--LEVFL---QRFPGTVVAITHD 217
Cdd:cd03257 141 RYPHE------LSGGQRQRVAIARALALNPKLLIADEPTSALDV-SVQAqiLDLLKklqEELGLTLLFITHD 205
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
322-516 |
2.14e-24 |
|
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: 102.42 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV-KMAFVDQARDALA- 398
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFdGRDItGLPPHRIARLGIAr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 399 --------DQKTVWEdisggldiiNV---GKFQMASRAYAGRFNFNGADQQ----------------------KKVGTLS 445
Cdd:COG0411 84 tfqnprlfPELTVLE---------NVlvaAHARLGRGLLAALLRLPRARREereareraeellervgladradEPAGNLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 446 GGERGRLHLAKTLIAGGNVLLLDEP--------SNDLdVETLRALEDallEFAGTVMVISHDRWFLDRIATHILA----- 512
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPaaglnpeeTEEL-AELIRRLRD---ERGITILLIEHDMDLVMGLADRIVVldfgr 230
|
....*.
gi 518484691 513 --AEGD 516
Cdd:COG0411 231 viAEGT 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-235 |
2.34e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 101.28 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 8 MNRVSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEA---------LP---MPGL--TIGY 73
Cdd:COG2884 4 FENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlvngqdlsrLKrreIPYLrrRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 74 LEQEPKLNPEHTVRESVeesmgavnaakkrleevyelyaaedadfdALAaeqaeLEAIiataGTDSEhqlEIAAdalRLP 153
Cdd:COG2884 84 VFQDFRLLPDRTVYENV-----------------------------ALP-----LRVT----GKSRK---EIRR---RVR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 154 AW----------DAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAE-SVEWLEVF--LQRFPGTVVAITHDRYF 220
Cdd:COG2884 120 EVldlvglsdkaKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPEtSWEIMELLeeINRRGTTVLIATHDLEL 199
|
250
....*....|....*
gi 518484691 221 LDNAAEWILELDRGR 235
Cdd:COG2884 200 VDRMPKRVLELEDGR 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-217 |
2.52e-24 |
|
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: 101.01 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 7 SMNRVSKTVPPKR---QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEALPMPGLTIGYLEQE 77
Cdd:cd03293 2 EVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERptsgevLVDGEPVTGPGPDRGYVFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 78 PKLNPEHTVRESVEESMGAVNAAKKRLEEvyelyaaedadfdalaaeqaELEAIIATAG-TDSEHqleiaadalRLPAwd 156
Cdd:cd03293 82 DALLPWLTVLDNVALGLELQGVPKAEARE--------------------RAEELLELVGlSGFEN---------AYPH-- 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 157 akigVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDA---ESV-EWLEVFLQRFPGTVVAITHD 217
Cdd:cd03293 131 ----QLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltrEQLqEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
17-225 |
2.61e-24 |
|
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: 99.82 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 17 PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEalpmpgltIgYLEQEPklnpehtvresvEESMGA 96
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGE--------I-LLDGKD------------LASLSP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 97 VNAAKKRleevyelyaaedadfdalaaeqaeleAIIATAgtdsEHQLEIAADALRLpawdakIGVLSGGEKRRVALCRLL 176
Cdd:cd03214 69 KELARKI--------------------------AYVPQA----LELLGLAHLADRP------FNELSGGERQRVLLARAL 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518484691 177 LSKPDMLLLDEPTNHLD-AESVEWLEVF--LQRFPG-TVVAITHDryfLDNAA 225
Cdd:cd03214 113 AQEPPILLLDEPTSHLDiAHQIELLELLrrLARERGkTVVMVLHD---LNLAA 162
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-507 |
2.84e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.26 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 1 MAQYVYSMNRVSKTVPPKRQiLKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEALPMPG------ 68
Cdd:COG3845 1 MMPPALELRGITKRFGGVVA-NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQpdsgeiLIDGKPVRIRSprdaia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 69 LTIGYLEQEPKLNPEHTVRESVeeSMGAVNAAKKRLeevyelyaaedadfdALAAEQAELEAIIATAGtdsehqleiaad 148
Cdd:COG3845 80 LGIGMVHQHFMLVPNLTVAENI--VLGLEPTKGGRL---------------DRKAARARIRELSERYG------------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 149 aLRLPaWDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG---TVVAITHDryfLDnaa 225
Cdd:COG3845 131 -LDVD-PDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAegkSIIFITHK---LR--- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 226 EwILEL-DR------GRGIpwkgnystwleqkGERLAQEQkseeahakalkkelewsrqnpkarqakSKSRLARfeeL-- 296
Cdd:COG3845 203 E-VMAIaDRvtvlrrGKVV-------------GTVDTAET---------------------------SEEELAE---Lmv 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 297 -SDVEYQKRNETQEifipvaerLGSQVFEFKNVS-KSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKP 374
Cdd:COG3845 239 gREVLLRVEKAPAE--------PGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPP 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 375 DSGEVVI-GQTV-----------KMAFV--DQARDALADQKTVWEDI-----------SGGldIINVGKFQMASRAYAGR 429
Cdd:COG3845 311 ASGSIRLdGEDItglsprerrrlGVAYIpeDRLGRGLVPDMSVAENLilgryrrppfsRGG--FLDRKAIRAFAEELIEE 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 430 FNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEF--AGT-VMVISHDrwfL--- 503
Cdd:COG3845 389 FDVRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELrdAGAaVLLISED---Ldei 465
|
....*...
gi 518484691 504 ----DRIA 507
Cdd:COG3845 466 lalsDRIA 473
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-234 |
5.39e-24 |
|
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: 99.64 E-value: 5.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 10 RVSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE--------ALPMPGLTIGYLEQEPKln 81
Cdd:cd03226 4 NISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSillngkpiKAKERRKSIGYVMQDVD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 82 pEHTVRESVEEsmgavnaakkrleevyELYAAEDAdfdaLAAEQAELEAIIATagtdsehqLEIAADALRLPaWDakigv 161
Cdd:cd03226 82 -YQLFTDSVRE----------------ELLLGLKE----LDAGNEQAETVLKD--------LDLYALKERHP-LS----- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 162 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWL-EVF--LQRFPGTVVAITHDRYFLDNAAEWILELDRG 234
Cdd:cd03226 127 LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVgELIreLAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
290-508 |
5.44e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 106.02 E-value: 5.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 290 LARFEELSDVEyqkrNETQEIFIPVAERLGSQVFEFKNVSksF---GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFK 366
Cdd:COG1132 311 AERIFELLDEP----PEIPDPPGAVPLPPVRGEIEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVN 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 367 LLAGKEKPDSGEVVI-GQTVK----------MAFVDQarDA--LADqkTVWEDISGGL------DIINVgkfqmASRAYA 427
Cdd:COG1132 385 LLLRFYDPTSGRILIdGVDIRdltleslrrqIGVVPQ--DTflFSG--TIRENIRYGRpdatdeEVEEA-----AKAAQA 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 428 GRF--NF-NGADQQkkVG----TLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAG--TVMVISH 498
Cdd:COG1132 456 HEFieALpDGYDTV--VGergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKgrTTIVIAH 533
|
250
....*....|
gi 518484691 499 drwfldRIAT 508
Cdd:COG1132 534 ------RLST 537
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
324-500 |
7.60e-24 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 105.06 E-value: 7.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDR-LLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDALA--- 398
Cdd:TIGR02857 323 EFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVnGVPLADADADSWRDQIAwvp 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 399 -----DQKTVWEDI------SGGLDIINVgkfqmASRAYAGRF-NFNGADQQKKVGT----LSGGERGRLHLAKTLIAGG 462
Cdd:TIGR02857 403 qhpflFAGTIAENIrlarpdASDAEIREA-----LERAGLDEFvAALPQGLDTPIGEggagLSGGQAQRLALARAFLRDA 477
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518484691 463 NVLLLDEPSNDLDVETLRALEDALLEFAG--TVMVISHDR 500
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRL 517
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
323-524 |
9.16e-24 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 99.53 E-value: 9.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 323 FEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV------------KMAF 389
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdGLKLtddkkninelrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 390 VDQARDaLADQKTVWEDISGGLdiINVGKfqmASRAYAGRfnfNGADQQKKVG----------TLSGGERGRLHLAKTLI 459
Cdd:cd03262 81 VFQQFN-LFPHLTVLENITLAP--IKVKG---MSKAEAEE---RALELLEKVGladkadaypaQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 460 AGGNVLLLDEPSNDLDVETLRALEDALLEFA--GTVMVI-SHDRWFLDRIATHILaaegdsqwtFFDG 524
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAeeGMTMVVvTHEMGFAREVADRVI---------FMDD 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
327-470 |
1.35e-23 |
|
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: 99.54 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 327 NVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQT--VKMAFVDQARDALA------ 398
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQdiTKLPMHKRARLGIGylpqea 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 399 ---DQKTVWEDISGGLDIINVGKFQMASRAYAGRFNFNGADQQKKVG-TLSGGERGRLHLAKTLIAGGNVLLLDEP 470
Cdd:cd03218 85 sifRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKAsSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
324-507 |
2.76e-23 |
|
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: 98.21 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGE-VVIGQTV---------KMAFVDQA 393
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHDVvreprevrrRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 394 RdALADQKTVWEDISGGLDIINVGKFQMASRA-----YAGRFNFngADqqKKVGTLSGGERGRLHLAKTLIAGGNVLLLD 468
Cdd:cd03265 82 L-SVDDELTGWENLYIHARLYGVPGAERRERIdelldFVGLLEA--AD--RLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518484691 469 EPSNDLDVET----LRALEDALLEFAGTVMVISHD----RWFLDRIA 507
Cdd:cd03265 157 EPTIGLDPQTrahvWEYIEKLKEEFGMTILLTTHYmeeaEQLCDRVA 203
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
324-515 |
2.85e-23 |
|
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: 103.69 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSF--GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG---------QTV--KMAFV 390
Cdd:COG4987 335 ELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGgvdlrdldeDDLrrRIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 391 DQA--------RDAL------ADQKTVW------------EDISGGLDIInVGKfqmasrayAGRfnfngadqqkkvgTL 444
Cdd:COG4987 415 PQRphlfdttlRENLrlarpdATDEELWaalervglgdwlAALPDGLDTW-LGE--------GGR-------------RL 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 445 SGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAG--TVMVISHDRWFLDRIATHILAAEG 515
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAgrTVLLITHRLAGLERMDRILVLEDG 545
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
11-235 |
2.99e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 98.19 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 11 VSKTVP---PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGE---ALPMPGLT------IG 72
Cdd:COG1136 10 LTKSYGtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRptsgevLIDGQdisSLSERELArlrrrhIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 73 YLEQEPKLNPEHTVRESVEesMGAVNAAKKRLEevyelyAAEDADfDALAaeqaeleaiiatagtdsehQLEIAAdalRL 152
Cdd:COG1136 90 FVFQFFNLLPELTALENVA--LPLLLAGVSRKE------RRERAR-ELLE-------------------RVGLGD---RL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 153 pawDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEwlEVF--LQRF---PG-TVVAITHDRyFLDNAAE 226
Cdd:COG1136 139 ---DHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGE--EVLelLRELnreLGtTIVMVTHDP-ELAARAD 212
|
....*....
gi 518484691 227 WILELDRGR 235
Cdd:COG1136 213 RVIRLRDGR 221
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
324-512 |
3.06e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 99.00 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV----------KMAFVDQ 392
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVdGLDVattpsrelakRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 393 A---------RDALA--------------DQKTVWEDISggldiinvgkfQMASRAYAGRFnfngadqqkkVGTLSGGER 449
Cdd:COG4604 83 EnhinsrltvRELVAfgrfpyskgrltaeDREIIDEAIA-----------YLDLEDLADRY----------LDELSGGQR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 450 GRLHLAKTLIAGGNVLLLDEPSNDLD----VETLRALEDALLEFAGTVMVISHDRWFLDRIATHILA 512
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVA 208
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
19-235 |
4.22e-23 |
|
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: 98.73 E-value: 4.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALP-------MP----GLTIGYLEQEPKLNPEHTVR 87
Cdd:TIGR03873 14 RLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLagvdlhgLSrrarARRVALVEQDSDTAVPLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 88 ESVeesmgAVNAAKKRleevyELYAAEDADFDALAAEqaeleAIIATagtdsehqlEIAADALRlpAWDAkigvLSGGEK 167
Cdd:TIGR03873 94 DVV-----ALGRIPHR-----SLWAGDSPHDAAVVDR-----ALART---------ELSHLADR--DMST----LSGGER 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518484691 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG---TVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:TIGR03873 144 QRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHDLNLAASYCDHVVVLDGGR 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
324-499 |
6.97e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 100.15 E-value: 6.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTV---------KMAFVDQaR 394
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdlppkdrNIAMVFQ-S 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 395 DALADQKTVWEDISGGLDIINVGKFQMASR-----------AYAGRfnfngadqqkKVGTLSGGERGRLHLAKTLIAGGN 463
Cdd:COG3839 84 YALYPHMTVYENIAFPLKLRKVPKAEIDRRvreaaellgleDLLDR----------KPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518484691 464 VLLLDEP-SNdLD----VET---LRALEDALlefaGTVMVI-SHD 499
Cdd:COG3839 154 VFLLDEPlSN-LDaklrVEMraeIKRLHRRL----GTTTIYvTHD 193
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
324-525 |
6.98e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 97.52 E-value: 6.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLidNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQT----------VKMAFVDQ 392
Cdd:COG3840 3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWnGQDltalppaerpVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 393 ardALADQKTVWEDISGGLDIinvgkfqmasrayAGRFNfngADQQKKV-----------------GTLSGGERGRLHLA 455
Cdd:COG3840 81 ---NLFPHLTVAQNIGLGLRP-------------GLKLT---AEQRAQVeqalervglaglldrlpGQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 456 KTLIAGGNVLLLDEPSNDLD----VETLRALEDALLEFAGTVMVISHDrwfLD---RIATH-ILAAEGDSQW-----TFF 522
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD---PEdaaRIADRvLLVADGRIAAdgptaALL 218
|
...
gi 518484691 523 DGN 525
Cdd:COG3840 219 DGE 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
324-499 |
8.66e-23 |
|
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: 96.92 E-value: 8.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG-----------QTVKMAFVDQ 392
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgkditnlpphkRPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 393 ardALADQKTVWEDISGGLDIINVGKFQMASR-AYAGRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPS 471
Cdd:cd03300 82 ---ALFPHLTVFENIAFGLRLKKLPKAEIKERvAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190
....*....|....*....|....*....|....*
gi 518484691 472 NDLDVEtLRalEDALLEFAG-------TVMVISHD 499
Cdd:cd03300 159 GALDLK-LR--KDMQLELKRlqkelgiTFVFVTHD 190
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
324-499 |
8.69e-23 |
|
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: 96.55 E-value: 8.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG-----------QTVKMAFVDQ 392
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvtdlppkdRDIAMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 393 ardALADQKTVWEDISGGLDIINVGKFQMASRAY-AGRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPS 471
Cdd:cd03301 82 ---ALYPHMTVYDNIAFGLKLRKVPKDEIDERVReVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190
....*....|....*....|....*....|..
gi 518484691 472 NDLD----VETLRALEDALLEFAGTVMVISHD 499
Cdd:cd03301 159 SNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
324-499 |
8.78e-23 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 97.41 E-value: 8.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG---------QTVKMAFVDQAR 394
Cdd:cd03296 4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedatdvpvQERNVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 395 dALADQKTVWEDISGGLDIINVG----KFQMASRA-----------YAGRFNfngadqqkkvGTLSGGERGRLHLAKTLI 459
Cdd:cd03296 84 -ALFRHMTVFDNVAFGLRVKPRSerppEAEIRAKVhellklvqldwLADRYP----------AQLSGGQRQRVALARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518484691 460 AGGNVLLLDEPSNDLDVET-------LRALEDallEFAGTVMVISHD 499
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVrkelrrwLRRLHD---ELHVTTVFVTHD 196
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
322-524 |
1.02e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 96.65 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLL----IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV-KMAfvDQARD 395
Cdd:COG1136 4 LLELRNLTKSYGTGEGevtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIdGQDIsSLS--ERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 396 ALADQK--------------TVWEDISGGLDIINVGKFQMASRAYA--GRFNFnGADQQKKVGTLSGGERGRLHLAKTLI 459
Cdd:COG1136 82 RLRRRHigfvfqffnllpelTALENVALPLLLAGVSRKERRERAREllERVGL-GDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518484691 460 AGGNVLLLDEPSNDLDVETLRALEDALLEFAG----TVMVISHDrwfldriatHILAAEGDSQWTFFDG 524
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRelgtTIVMVTHD---------PELAARADRVIRLRDG 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-235 |
2.02e-22 |
|
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: 100.75 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 16 PPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLT----------IGYLEQEPK-- 79
Cdd:COG1123 275 KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgkDLTKLSrrslrelrrrVQMVFQDPYss 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 80 LNPEHTVRESVEESM---GAVNAAKKRlEEVYELyaaedadfdalaAEQAELEaiiatagtdsehqleiAADALRLPawd 156
Cdd:COG1123 355 LNPRMTVGDIIAEPLrlhGLLSRAERR-ERVAEL------------LERVGLP----------------PDLADRYP--- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 157 akiGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAeSVEW--LEVF--LQRFPG-TVVAITHD----RYFldnaAEW 227
Cdd:COG1123 403 ---HELSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVQAqiLNLLrdLQRELGlTYLFISHDlavvRYI----ADR 474
|
....*...
gi 518484691 228 ILELDRGR 235
Cdd:COG1123 475 VAVMYDGR 482
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
324-514 |
2.95e-22 |
|
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: 95.17 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSF-GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV-------------KMA 388
Cdd:cd03292 2 EFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVsdlrgraipylrrKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 389 FVDQARDALADqKTVWEDISGGLDIINVGKFQMASRAYAGRFNFNGADQQKKVGT-LSGGERGRLHLAKTLIAGGNVLLL 467
Cdd:cd03292 82 VVFQDFRLLPD-RNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAeLSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518484691 468 DEPSNDLDVETLRALEDALLEF--AG-TVMVISHDRWFLDRIATHILAAE 514
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKInkAGtTVVVATHAKELVDTTRHRVIALE 210
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-217 |
3.39e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.22 E-value: 3.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 17 PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALPMPGLTIGYLEQEPKLNPEH--TVRESVeeSM 94
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLplTVRDLV--AM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 95 G--AVNAAKKRLeevyelyaaeDADfDALAAEQAeLEAiiatagtdsehqLEIAADALRlpawdaKIGVLSGGEKRRVAL 172
Cdd:NF040873 81 GrwARRGLWRRL----------TRD-DRAAVDDA-LER------------VGLADLAGR------QLGELSGGQRQRALL 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518484691 173 CRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG---TVVAITHD 217
Cdd:NF040873 131 AQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
324-499 |
3.73e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 96.72 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV----------------- 385
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGEPLdpedrrrigylpeergl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 386 --KMAFVDQ-----------ARDALADQKTvWedisggLDiinvgKFQMASRAYagrfnfngadqqKKVGTLSGGERGRL 452
Cdd:COG4152 83 ypKMKVGEQlvylarlkglsKAEAKRRADE-W------LE-----RLGLGDRAN------------KKVEELSKGNQQKV 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518484691 453 HLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFA--G-TVMVISHD 499
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAakGtTVIFSSHQ 188
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
324-511 |
4.29e-22 |
|
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: 94.65 E-value: 4.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIgQTVKMAFVDQARDA------- 396
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-DGKPLDIAARNRIGylpeerg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 397 LADQKTVWEDISGGLDIINVGKFQMASRA--YAGRFNFnGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDL 474
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLKGLKKEEARRRIdeWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518484691 475 DVETLRALEDALLEFAG---TVMVISHDRWFLDRIATHIL 511
Cdd:cd03269 160 DPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVL 199
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
323-498 |
4.77e-22 |
|
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: 93.43 E-value: 4.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 323 FEFKNVSKSFGD--RLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDALAd 399
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISQWDPNELGDHVG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 400 qkTVWEDI---SGGL-DIInvgkfqmasrayagrfnfngadqqkkvgtLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD 475
Cdd:cd03246 80 --YLPQDDelfSGSIaENI-----------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180
....*....|....*....|....*.
gi 518484691 476 VETLRALEDAL--LEFAG-TVMVISH 498
Cdd:cd03246 129 VEGERALNQAIaaLKAAGaTRIVIAH 154
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
323-506 |
5.14e-22 |
|
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: 94.94 E-value: 5.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 323 FEFKNVSKSFGD-RLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG----QTVKMAFVDQARDAL 397
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdiNKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 398 AdqkTVWED--ISGGLDII-NV--GKF-QMAS-RAYAGRfnFNGADQQ----------------KKVGTLSGGERGRLHL 454
Cdd:cd03256 81 G---MIFQQfnLIERLSVLeNVlsGRLgRRSTwRSLFGL--FPKEEKQralaalervglldkayQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 455 AKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAG----TVMVISHD----RWFLDRI 506
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReegiTVIVSLHQvdlaREYADRI 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
11-252 |
6.94e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 97.14 E-value: 6.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 11 VSKTVPpKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGE----ALPMPGLTIGYLEQEPKL 80
Cdd:COG1118 8 ISKRFG-SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETpdsgriVLNGRdlftNLPPRERRVGFVFQHYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 81 NPEHTVRESVEESMGAVNAAKKRLEE-VYELyaaedadfdalaaeqaeLEAIiatagtdsehQLEIAADalRLPAWdaki 159
Cdd:COG1118 87 FPHMTVAENIAFGLRVRPPSKAEIRArVEEL-----------------LELV----------QLEGLAD--RYPSQ---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 160 gvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAeSV-----EWLEVFLQRFPGTVVAITHDRyflDNAAEW---ILEL 231
Cdd:COG1118 134 --LSGGQRQRVALARALAVEPEVLLLDEPFGALDA-KVrkelrRWLRRLHDELGGTTVFVTHDQ---EEALELadrVVVM 207
|
250 260
....*....|....*....|.
gi 518484691 232 DRGRgipwkgnystwLEQKGE 252
Cdd:COG1118 208 NQGR-----------IEQVGT 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
328-514 |
9.88e-22 |
|
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: 93.51 E-value: 9.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 328 VSKSFGDRLLidNLSFNVPAGaIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTV---------------KMAFVDQ 392
Cdd:cd03297 6 IEKRLPDFTL--KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 393 aRDALADQKTVWEDISGGLDIINVGKFQMASRAYAGRFNFNGAdQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSN 472
Cdd:cd03297 83 -QYALFPHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518484691 473 DLDVET----LRALEDALLEFAGTVMVISHDRWFLDRIATHILAAE 514
Cdd:cd03297 161 ALDRALrlqlLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVME 206
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-218 |
1.13e-21 |
|
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: 93.35 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 9 NRVSKTVPPKRqILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLT-----IGYLEQEPK 79
Cdd:cd03259 4 KGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILidgrDVTGVPperrnIGMVFQDYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 80 LNPEHTVRESVeesmgavnaakkrleeVYELYAAEDADfdalAAEQAELEAIIAtagtdsehQLEIAADALRLPAwdaki 159
Cdd:cd03259 83 LFPHLTVAENI----------------AFGLKLRGVPK----AEIRARVRELLE--------LVGLEGLLNRYPH----- 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 160 gVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQR----FPGTVVAITHDR 218
Cdd:cd03259 130 -ELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKElqreLGITTIYVTHDQ 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
326-511 |
1.40e-21 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 93.03 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKSFGDRLLIDNLSFNVPAGaIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKmAFVDQARDALA------ 398
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVL-KQPQKLRRRIGylpqef 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 399 ---DQKTVWE--DISGGLDIINVGKFQMASRAYAGRFNFNGAdQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSND 473
Cdd:cd03264 82 gvyPNFTVREflDYIAWLKGIPSKEVKARVDEVLELVNLGDR-AKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 518484691 474 LDVETLRALEDALLEFAGTVMVIshdrwfldrIATHIL 511
Cdd:cd03264 161 LDPEERIRFRNLLSELGEDRIVI---------LSTHIV 189
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
329-515 |
1.48e-21 |
|
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: 94.01 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 329 SKSFGD-RLLIDNLSFNvpAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG--------QTVKMAFVDQARDALAD 399
Cdd:cd03237 7 KKTLGEfTLEVEGGSIS--ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEldtvsykpQYIKADYEGTVRDLLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 400 Q-KTVWEDISGGLDIINvgKFQMASRAyagrfnfngaDQQkkVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVET 478
Cdd:cd03237 85 ItKDFYTHPYFKTEIAK--PLQIEQIL----------DRE--VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518484691 479 LRALEDALLEFA----GTVMVISHDRWFLDRIATHILAAEG 515
Cdd:cd03237 151 RLMASKVIRRFAenneKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-217 |
1.71e-21 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 92.74 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSF-FPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEA---------------LPMPGLTIGYLEQEPKLN 81
Cdd:cd03297 8 KRLPDFTLKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsrkkinLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 82 PEHTVRESVEESMGAVNAAKKRLEEvyelyaaedadfdalaaeqaelEAIIATAGTDsehQLEiaadalrlpawDAKIGV 161
Cdd:cd03297 88 PHLNVRENLAFGLKRKRNREDRISV----------------------DELLDLLGLD---HLL-----------NRYPAQ 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 162 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQR----FPGTVVAITHD 217
Cdd:cd03297 132 LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQikknLNIPVIFVTHD 191
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
338-499 |
1.75e-21 |
|
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: 93.55 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 338 IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTV----KMAFVDQARDALADQKTVWEDISGgldi 413
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrRKKFLRRIGVVFGQKTQLWWDLPV---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 414 inVGKFQMASRAY---AGRFNFN----------GADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV---E 477
Cdd:cd03267 113 --IDSFYLLAAIYdlpPARFKKRldelselldlEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVvaqE 190
|
170 180
....*....|....*....|...
gi 518484691 478 TLRA-LEDALLEFAGTVMVISHD 499
Cdd:cd03267 191 NIRNfLKEYNRERGTTVLLTSHY 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
324-511 |
2.15e-21 |
|
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: 92.95 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLL----IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV------------- 385
Cdd:cd03257 3 EVKNLSVSFPTGGGsvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdGKDLlklsrrlrkirrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 386 KMAFVDQ-ARDALADQKTVWEDISGGLDI--INVGKFQMASRAYAGRFNFNGADQ--QKKVGTLSGGERGRLHLAKTLIA 460
Cdd:cd03257 83 EIQMVFQdPMSSLNPRMTIGEQIAEPLRIhgKLSKKEARKEAVLLLLVGVGLPEEvlNRYPHELSGGQRQRVAIARALAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 461 GGNVLLLDEPSNDLDV----ETLRALEDALLEFAGTVMVISHDRWFLDRIATHIL 511
Cdd:cd03257 163 NPKLLIADEPTSALDVsvqaQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVA 217
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-235 |
2.15e-21 |
|
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: 97.90 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 15 VPP--KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEG--------------EALpmpGLTIGYLEQEP 78
Cdd:COG4618 339 VPPgsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGsvrldgadlsqwdrEEL---GRHIGYLPQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 79 KLNPEhTVREsveesmgavNAAkkRLEEVyelyaaedadfDAlaaeqaelEAIIATAgtdsehqleIAADA----LRLP- 153
Cdd:COG4618 416 ELFDG-TIAE---------NIA--RFGDA-----------DP--------EKVVAAA---------KLAGVhemiLRLPd 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 154 AWDAKIG----VLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRF---PGTVVAITHDRYFLdNAAE 226
Cdd:COG4618 456 GYDTRIGeggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHRPSLL-AAVD 534
|
....*....
gi 518484691 227 WILELDRGR 235
Cdd:COG4618 535 KLLVLRDGR 543
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
322-470 |
2.15e-21 |
|
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: 93.11 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV-KMAFVDQAR----- 394
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIdGQDItHLPMHERARlgigy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 395 ---DALADQK-TVWEDISGGLDII-NVGKFQMASRAYAGRFNFNGAD-QQKKVGTLSGGERGRLHLAKTLIAGGNVLLLD 468
Cdd:TIGR04406 81 lpqEASIFRKlTVEENIMAVLEIRkDLDRAEREERLEALLEEFQISHlRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
..
gi 518484691 469 EP 470
Cdd:TIGR04406 161 EP 162
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
324-498 |
2.41e-21 |
|
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: 93.06 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGD-RLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDALA--D 399
Cdd:cd03253 2 EFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdGQDIREVTLDSLRRAIGvvP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 400 QKTV------WEDIS-GGLDIINVGKFQMASRAYAGRFNFNGADQ-QKKVG----TLSGGERGRLHLAKTLIAGGNVLLL 467
Cdd:cd03253 82 QDTVlfndtiGYNIRyGRPDATDEEVIEAAKAAQIHDKIMRFPDGyDTIVGerglKLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190
....*....|....*....|....*....|...
gi 518484691 468 DEPSNDLDVETLRALEDALLEFAG--TVMVISH 498
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSKgrTTIVIAH 194
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
323-506 |
2.48e-21 |
|
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: 92.65 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 323 FEFKNVSKSFGD--RLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGqTVKMAFVDQArDALADQ 400
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLD-GTDIRQLDPA-DLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 401 KTVWEDI---SGGL-DIINVGKFQ------MASRAYAGRFNF-----NGADQQkkVG----TLSGGERGRLHLAKTLIAG 461
Cdd:cd03245 81 GYVPQDVtlfYGTLrDNITLGAPLadderiLRAAELAGVTDFvnkhpNGLDLQ--IGergrGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518484691 462 GNVLLLDEPSNDLDVETLRALEDALLEFAG--TVMVISHDRWFL---DRI 506
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLdlvDRI 208
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-262 |
2.80e-21 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 97.54 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 16 PPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMA-------------GVD-KEIEGEALPMpglTIGYLEQEPKLN 81
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLrfydptsgrilidGVDiRDLTLESLRR---QIGVVPQDTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 82 PEhTVRESVeesmgavnaakkrleevyeLYAAEDADFDAL--AAEQAELEAIIAtagtdsehqleiaadalRLPA-WDAK 158
Cdd:COG1132 427 SG-TIRENI-------------------RYGRPDATDEEVeeAAKAAQAHEFIE-----------------ALPDgYDTV 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 159 IG----VLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESvewlEVFLQR-----FPG-TVVAITH--------DRyf 220
Cdd:COG1132 470 VGergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTET----EALIQEalerlMKGrTTIVIAHrlstirnaDR-- 543
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 518484691 221 ldnaaewILELDRGRgIPWKGNYSTWLEQKGE--RLAQEQKSEE 262
Cdd:COG1132 544 -------ILVLDDGR-IVEQGTHEELLARGGLyaRLYRLQFGEE 579
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
288-498 |
3.19e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 94.90 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 288 SRLARFEELSDVEYQKrnetQEIFIPVAERLGSQ---VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTL 364
Cdd:PRK13536 8 EEAPRRLELSPIERKH----QGISEAKASIPGSMstvAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 365 FKLLAGKEKPDSGEV-VIGQTVKmafvDQAR------------DALADQKTVWEDIsggldIINVGKFQMASR----AYA 427
Cdd:PRK13536 84 ARMILGMTSPDAGKItVLGVPVP----ARARlararigvvpqfDNLDLEFTVRENL-----LVFGRYFGMSTReieaVIP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 428 GRFNF----NGADqqKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV-------ETLRaledALLEFAGTVMVI 496
Cdd:PRK13536 155 SLLEFarleSKAD--ARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPharhliwERLR----SLLARGKTILLT 228
|
..
gi 518484691 497 SH 498
Cdd:PRK13536 229 TH 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
322-510 |
3.44e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.63 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDA---- 396
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPVRFRSPRDAQAAgiai 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 397 ------LADQKTVWEDI-------SGGLdiINVGKFQMASRAYAGRFNFNgADQQKKVGTLSGGERGRLHLAKTLIAGGN 463
Cdd:COG1129 84 ihqelnLVPNLSVAENIflgreprRGGL--IDWRAMRRRARELLARLGLD-IDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518484691 464 VLLLDEPS---NDLDVETLRALEDALLEfAGTVMV-ISHdrwFLD---RIATHI 510
Cdd:COG1129 161 VLILDEPTaslTEREVERLFRIIRRLKA-QGVAIIyISH---RLDevfEIADRV 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
326-499 |
5.91e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 92.43 E-value: 5.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQT--------VKMAFVDqARdaL 397
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAplaearedTRLMFQD-AR--L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 398 ADQKTVWEDISGGLDiinvGKFQMASR------AYAGRFNFNGAdqqkkvgTLSGGERGRLHLAKTLIAGGNVLLLDEPS 471
Cdd:PRK11247 93 LPWKKVIDNVGLGLK----GQWRDAALqalaavGLADRANEWPA-------ALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190
....*....|....*....|....*....|..
gi 518484691 472 NDLD----VETLRALEDALLEFAGTVMVISHD 499
Cdd:PRK11247 162 GALDaltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-288 |
8.49e-21 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 96.39 E-value: 8.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALPMPGLTIGYLEQEpklnpehtvresveesmgavn 98
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQH--------------------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 99 aakkRLEevyelyaaedadfdALAAEQAELEAIIATAGTDSEHQLE--IAADALRLPAWDAKIGVLSGGEKRRVALCRLL 176
Cdd:PRK10636 384 ----QLE--------------FLRADESPLQHLARLAPQELEQKLRdyLGGFGFQGDKVTEETRRFSGGEKARLVLALIV 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 177 LSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEWILELDRGRGIPWKG---NYSTWL-EQKGE 252
Cdd:PRK10636 446 WQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGdleDYQQWLsDVQKQ 525
|
250 260 270
....*....|....*....|....*....|....*.
gi 518484691 253 RLAQEQKSEEAHAKALKkelewSRQNPKARQAKSKS 288
Cdd:PRK10636 526 ENQTDEAPKENNANSAQ-----ARKDQKRREAELRT 556
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
326-470 |
8.76e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 91.63 E-value: 8.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV-KMAFVDQARDALA--DQK 401
Cdd:COG1137 7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLdGEDItHLPMHKRARLGIGylPQE 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518484691 402 -------TVWEDISGGLDIINVGKFQMASRAYA--GRFNFNG-ADQqkKVGTLSGGERGRLHLAKTLIAGGNVLLLDEP 470
Cdd:COG1137 87 asifrklTVEDNILAVLELRKLSKKEREERLEEllEEFGITHlRKS--KAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
327-497 |
1.18e-20 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 90.50 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 327 NVSKSFGDR----LLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG--QTVKMAFVDQAR------ 394
Cdd:cd03266 6 ALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfDVVKEPAEARRRlgfvsd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 395 -DALADQKTVWEDIS--GGLDIINVGKFQMASRAYAGRFNFNgADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPS 471
Cdd:cd03266 86 sTGLYDRLTARENLEyfAGLYGLKGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
|
170 180
....*....|....*....|....*...
gi 518484691 472 NDLDVETLRALEDALLEF--AGTVMVIS 497
Cdd:cd03266 165 TGLDVMATRALREFIRQLraLGKCILFS 192
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
324-498 |
1.38e-20 |
|
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: 90.75 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSF-GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVK----------MAFVD 391
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdGIDIRdisrkslrsmIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 392 QarDALADQKTVWEDISGGLDIINVGKFQMASRAyAGRFNF-----NGADQQ--KKVGTLSGGERGRLHLAKTLIAGGNV 464
Cdd:cd03254 84 Q--DTFLFSGTIMENIRLGRPNATDEEVIEAAKE-AGAHDFimklpNGYDTVlgENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 518484691 465 LLLDEPSNDLDVETLRALEDALLE-FAG-TVMVISH 498
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKlMKGrTSIIIAH 196
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
327-529 |
1.39e-20 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 94.96 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 327 NVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQARDALADQkTVwed 406
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEF-TV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 407 isggLDIINVGKFQMAS------RAYA----------------GRF-NFNGADQQKKVGTL------------------S 445
Cdd:PRK15064 82 ----LDTVIMGHTELWEvkqerdRIYAlpemseedgmkvadleVKFaEMDGYTAEARAGELllgvgipeeqhyglmsevA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 446 GGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAGTVMVISHDRWFLDRIATHIlaAEGD-SQWTFFDG 524
Cdd:PRK15064 158 PGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHM--ADLDyGELRVYPG 235
|
....*
gi 518484691 525 NYQEY 529
Cdd:PRK15064 236 NYDEY 240
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
323-498 |
1.84e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 88.91 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 323 FEFKNVSKSFG--DRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQARDALA-- 398
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISvl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 399 DQK------TVWEdisggldiiNVGKfqmasrayagRFnfngadqqkkvgtlSGGERGRLHLAKTLIAGGNVLLLDEPSN 472
Cdd:cd03247 81 NQRpylfdtTLRN---------NLGR----------RF--------------SGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180
....*....|....*....|....*...
gi 518484691 473 DLDVETLRALEDALLEFA--GTVMVISH 498
Cdd:cd03247 128 GLDPITERQLLSLIFEVLkdKTLIWITH 155
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
324-498 |
2.11e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.79 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAfVDQAR-------- 394
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVPSR-ARHARqrvgvvpq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 395 -DALADQKTVWEDIsggldIINVGKFQMASRAYAGR----FNF----NGADqqKKVGTLSGGERGRLHLAKTLIAGGNVL 465
Cdd:PRK13537 88 fDNLDPDFTVRENL-----LVFGRYFGLSAAAARALvpplLEFakleNKAD--AKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518484691 466 LLDEPSNDLDV-------ETLRaledALLEFAGTVMVISH 498
Cdd:PRK13537 161 VLDEPTTGLDPqarhlmwERLR----SLLARGKTILLTTH 196
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-210 |
2.25e-20 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 89.58 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 9 NRVSKTVPpKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL--------PMPGLT-IGYLEQEPK 79
Cdd:cd03268 4 NDLTKTYG-KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdgksyqkNIEALRrIGALIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 80 LNPEHTVRESVEesmgaVNAAKKRLEEvyelyaaedadfdalaaeqAELEAIIATAG-TDSEHQleiaadalrlpawdaK 158
Cdd:cd03268 83 FYPNLTARENLR-----LLARLLGIRK-------------------KRIDEVLDVVGlKDSAKK---------------K 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518484691 159 IGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPGT 210
Cdd:cd03268 124 VKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ 175
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
322-506 |
3.00e-20 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 89.33 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLL----IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV----------- 385
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLdtrvLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFnGQSLsklssnerakl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 386 ---KMAFVDQARDALADqKTVWEDISGGLDIINVGKFQMASRAYAGRFNFNGADQ-QKKVGTLSGGERGRLHLAKTLIAG 461
Cdd:TIGR02211 81 rnkKLGFIYQFHHLLPD-FTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRiNHRPSELSGGERQRVAIARALVNQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518484691 462 GNVLLLDEPSNDLDVETLRALEDALLEF---AGTVMVI-SHDRWFLDRI 506
Cdd:TIGR02211 160 PSLVLADEPTGNLDNNNAKIIFDLMLELnreLNTSFLVvTHDLELAKKL 208
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-235 |
3.10e-20 |
|
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: 89.39 E-value: 3.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 8 MNRVSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE--------------ALPMPGLTIGY 73
Cdd:cd03292 3 FINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTirvngqdvsdlrgrAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 74 LEQEPKLNPEHTVRESVEESMGAVNA----AKKRLEEVYELYAAEDADfDALAAEqaeleaiiatagtdsehqleiaada 149
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVppreIRKRVPAALELVGLSHKH-RALPAE------------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 150 lrlpawdakigvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAE-SVEWLEVF--LQRFPGTVVAITHDRYFLDNAAE 226
Cdd:cd03292 137 ------------LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDtTWEIMNLLkkINKAGTTVVVATHAKELVDTTRH 204
|
....*....
gi 518484691 227 WILELDRGR 235
Cdd:cd03292 205 RVIALERGK 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
326-499 |
3.74e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.07 E-value: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQ--ARDA--LADQK 401
Cdd:PRK11231 6 ENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRqlARRLalLPQHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 402 TVWEDISgGLDIINVGKFQMASraYAGRfnFNGADQQ----------------KKVGTLSGGERGRLHLAKTLIAGGNVL 465
Cdd:PRK11231 86 LTPEGIT-VRELVAYGRSPWLS--LWGR--LSAEDNArvnqameqtrinhladRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 518484691 466 LLDEPSNDLD----VETLRALEDalLEFAG-TVMVISHD 499
Cdd:PRK11231 161 LLDEPTTYLDinhqVELMRLMRE--LNTQGkTVVTVLHD 197
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
324-499 |
3.77e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.60 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAfvdQARDALADQKT 402
Cdd:PRK09536 5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVaGDDVEAL---SARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 403 VWEDISGGLDIINVGKFQMASRAYAGRF---------------NFNGADQ--QKKVGTLSGGERGRLHLAKTLIAGGNVL 465
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGRTPHRSRFdtwtetdraaveramERTGVAQfaDRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 518484691 466 LLDEPSNDLDV-ETLRALEDA--LLEFAGTVMVISHD 499
Cdd:PRK09536 162 LLDEPTASLDInHQVRTLELVrrLVDDGKTAVAAIHD 198
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-233 |
3.83e-20 |
|
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: 93.89 E-value: 3.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 7 SMNRVSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLT-------IGYLE 75
Cdd:TIGR02857 323 EFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvPLADADadswrdqIAWVP 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 76 QEPKLnPEHTVRESVeesmgavnaakkrleevyeLYAAEDADFDAL--AAEQAELEAIIATagtdsehqleiaadalrLP 153
Cdd:TIGR02857 403 QHPFL-FAGTIAENI-------------------RLARPDASDAEIreALERAGLDEFVAA-----------------LP 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 154 A-WDAKIGV----LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES-VEWLEVFLQRFPG-TVVAITHDRyfldnaaE 226
Cdd:TIGR02857 446 QgLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETeAEVLEALRALAQGrTVLLVTHRL-------A 518
|
....*..
gi 518484691 227 WILELDR 233
Cdd:TIGR02857 519 LAALADR 525
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
324-507 |
5.07e-20 |
|
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: 89.32 E-value: 5.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLiDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV--------KMAFVDQAR 394
Cdd:cd03299 2 KVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDItnlppekrDISYVPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 395 dALADQKTVWEDISGGLDIINVGKFQMASRAY--AGrfnFNGADQ--QKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEP 470
Cdd:cd03299 81 -ALFPHMTVYKNIAYGLKKRKVDKKEIERKVLeiAE---MLGIDHllNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518484691 471 SNDLDVET----LRALEDALLEFAGTVMVISHD----RWFLDRIA 507
Cdd:cd03299 157 FSALDVRTkeklREELKKIRKEFGVTVLHVTHDfeeaWALADKVA 201
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
322-511 |
5.67e-20 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 93.04 E-value: 5.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSF--GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFK----------------LLAGKEKPDSGEVVIGQ 383
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALalmgllphggrisgevLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 384 TVKMAFVDqARDALaDQKTVWEDISGGLDIINVGKFQMASRAYAgRFNFNGADQ--QKKVGTLSGGERGRLHLAKTLIAG 461
Cdd:COG1123 84 RIGMVFQD-PMTQL-NPVTVGDQIAEALENLGLSRAEARARVLE-LLEAVGLERrlDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518484691 462 GNVLLLDEPSNDLDV----ETLRALEDALLEFAGTVMVISHDRWFLDRIATHIL 511
Cdd:COG1123 161 PDLLIADEPTTALDVttqaEILDLLRELQRERGTTVLLITHDLGVVAEIADRVV 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-216 |
5.99e-20 |
|
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: 87.99 E-value: 5.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 12 SKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG--VDKEIEGEAL----PMPGLT----IGYLEQEPKLN 81
Cdd:cd03213 15 SSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLingrPLDKRSfrkiIGYVPQDDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 82 PEHTVRESVEesmgavnaakkrleevyelYAAEdadfdalaaeqaeleaiiatagtdsehqleiaadaLRlpawdakigV 161
Cdd:cd03213 95 PTLTVRETLM-------------------FAAK-----------------------------------LR---------G 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 162 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG---TVVAITH 216
Cdd:cd03213 112 LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtgrTIICSIH 169
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
324-511 |
7.29e-20 |
|
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: 88.65 E-value: 7.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSF-----GDRLL--IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI---GQTVKMAfvdQA 393
Cdd:COG4778 6 EVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWVDLA---QA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 394 --RDALADQKTVwedIS------------GGLDI-----INVGKFQMASRAYAG----RFNFNGADQQKKVGTLSGGERG 450
Cdd:COG4778 83 spREILALRRRT---IGyvsqflrviprvSALDVvaeplLERGVDREEARARARellaRLNLPERLWDLPPATFSGGEQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518484691 451 RLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEF--AGTVMV-ISHDRWFLDRIATHIL 511
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkaRGTAIIgIFHDEEVREAVADRVV 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
324-499 |
8.75e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 90.52 E-value: 8.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSF----GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVD----QAR- 394
Cdd:COG1135 3 ELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelrAARr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 395 --------DALADQKTVWEDISGGLDIINVGKfqmasrayagrfnfngADQQKKVG-----------------TLSGGER 449
Cdd:COG1135 83 kigmifqhFNLLSSRTVAENVALPLEIAGVPK----------------AEIRKRVAellelvglsdkadaypsQLSGGQK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 450 GRLHLAKTLIAGGNVLLLDEPSNDLDVETLRA-LEdaLL-----EFAGTVMVISHD 499
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSiLD--LLkdinrELGLTIVLITHE 200
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
324-511 |
1.41e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 88.23 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGE-VVIGQTVKMAFVDQA---RDA--- 396
Cdd:PRK09493 3 EFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlIVDGLKVNDPKVDERlirQEAgmv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 397 -----LADQKTVWEDISGGldIINVgkfQMASRAYAGRFnfnGADQQKKVG----------TLSGGERGRLHLAKTLIAG 461
Cdd:PRK09493 83 fqqfyLFPHLTALENVMFG--PLRV---RGASKEEAEKQ---ARELLAKVGlaerahhypsELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518484691 462 GNVLLLDEPSNDLDV----ETLRALEDaLLEFAGTVMVISHDRWFLDRIATHIL 511
Cdd:PRK09493 155 PKLMLFDEPTSALDPelrhEVLKVMQD-LAEEGMTMVIVTHEIGFAEKVASRLI 207
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-189 |
1.45e-19 |
|
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: 87.49 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLT--------IGYLEQEPKLNPEHTVR 87
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfdgrDITGLPpheraragIGYVPEGRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 88 ESVEesMGAVN----AAKKRLEEVYELyaaedadFDALAAeqaeleaiiatagtdsehqleiaadalRlpaWDAKIGVLS 163
Cdd:cd03224 94 ENLL--LGAYArrraKRKARLERVYEL-------FPRLKE---------------------------R---RKQLAGTLS 134
|
170 180
....*....|....*....|....*.
gi 518484691 164 GGEKRRVALCRLLLSKPDMLLLDEPT 189
Cdd:cd03224 135 GGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
10-217 |
1.59e-19 |
|
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: 91.65 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 10 RVSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE---------ALPMPGL--TIGYLEQEP 78
Cdd:TIGR02868 339 DLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEvtldgvpvsSLDQDEVrrRVSVCAQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 79 KLNpEHTVRESVeesmgavnaakkrleevyeLYAAEDADFDAL--AAEQAELEAIIAtaGTDSEHQLEIAADALRLpawd 156
Cdd:TIGR02868 419 HLF-DTTVRENL-------------------RLARPDATDEELwaALERVGLADWLR--ALPDGLDTVLGEGGARL---- 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 157 akigvlSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAE-SVEWLEVFLQRFPG-TVVAITHD 217
Cdd:TIGR02868 473 ------SGGERQRLALARALLADAPILLLDEPTEHLDAEtADELLEDLLAALSGrTVVLITHH 529
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
324-498 |
2.01e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 86.64 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQA---------R 394
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPhenilylghL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 395 DALADQKTVWE------DISGGLDiinvgkfQMASRAYAgRFNFNGAdQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLD 468
Cdd:TIGR01189 82 PGLKPELSALEnlhfwaAIHGGAQ-------RTIEDALA-AVGLTGF-EDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|...
gi 518484691 469 EPSNDLD---VETLRALEDALLEFAGTVMVISH 498
Cdd:TIGR01189 153 EPTTALDkagVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-241 |
2.12e-19 |
|
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: 87.56 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEalPMPGLT----------IGYLEQEPKL-- 80
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRpdsgevLIDGE--DISGLSeaelyrlrrrMGMLFQSGALfd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 81 -----------------NPEHTVRESVEESMGAVNaakkrLEEVYELYAAEdadfdalaaeqaeleaiiatagtdsehql 143
Cdd:cd03261 91 sltvfenvafplrehtrLSEEEIREIVLEKLEAVG-----LRGAEDLYPAE----------------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 144 eiaadalrlpawdakigvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD---AESVEWLEVFLQRFPG-TVVAITHDRY 219
Cdd:cd03261 137 ------------------LSGGMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKKELGlTSIMVTHDLD 198
|
250 260
....*....|....*....|..
gi 518484691 220 FLDNAAEWILELDRGRgIPWKG 241
Cdd:cd03261 199 TAFAIADRIAVLYDGK-IVAEG 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
10-241 |
2.46e-19 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 86.48 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 10 RVSKTVPpKRQILKDISLSFFPGAkIGVLGLNGSGKSTLLKIMAGVDKEIEG-------EALPMPGL---TIGYLEQEPK 79
Cdd:cd03264 5 NLTKRYG-KKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGtiridgqDVLKQPQKlrrRIGYLPQEFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 80 LNPEHTVRESVEESmgavnAAKKRLeevyelyaaEDADFDALAAEQAELEAIiatagTDSEHQleiaadalrlpawdaKI 159
Cdd:cd03264 83 VYPNFTVREFLDYI-----AWLKGI---------PSKEVKARVDEVLELVNL-----GDRAKK---------------KI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 160 GVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPGTVVAI--THDRYFLDNAAEWILELDRGRgI 237
Cdd:cd03264 129 GSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGK-L 207
|
....
gi 518484691 238 PWKG 241
Cdd:cd03264 208 VFEG 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
341-498 |
2.93e-19 |
|
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: 86.39 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 341 LSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQtVKMAFVDQAR---------DALADQKTVWEDI---- 407
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-VDVTAAPPADrpvsmlfqeNNLFAHLTVEQNVglgl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 408 SGGLDIINVGkfQMASRAYAGRFNFNGADqQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDvETLRALEDALL 487
Cdd:cd03298 96 SPGLKLTAED--RQAIEVALARVGLAGLE-KRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD-PALRAEMLDLV 171
|
170
....*....|....*.
gi 518484691 488 -----EFAGTVMVISH 498
Cdd:cd03298 172 ldlhaETKMTVLMVTH 187
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
324-510 |
3.05e-19 |
|
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: 86.97 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGD-RLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV----------KMAFVD 391
Cdd:cd03295 2 EFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdGEDIreqdpvelrrKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 392 QaRDALADQKTVWEDISGGLDIINVGKFQMASRA-------------YAGRFNfngadqqkkvGTLSGGERGRLHLAKTL 458
Cdd:cd03295 82 Q-QIGLFPHMTVEENIALVPKLLKWPKEKIRERAdellalvgldpaeFADRYP----------HELSGGQQQRVGVARAL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 459 IAGGNVLLLDEPSNDLDVETLRALEDALL----EFAGTVMVISHDRWFLDRIATHI 510
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKrlqqELGKTIVFVTHDIDEAFRLADRI 206
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
322-498 |
3.34e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 87.06 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI--GQTV----------KMAF 389
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfGERRggedvwelrkRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 390 VDQardALADQ----KTVWEDI-SGGLDIInvGKFQ-----MASRAYA--GRFNFnGADQQKKVGTLSGGERGRLHLAKT 457
Cdd:COG1119 83 VSP---ALQLRfprdETVLDVVlSGFFDSI--GLYReptdeQRERAREllELLGL-AHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518484691 458 LIAGGNVLLLDEPSNDLDV---ETLRALEDALLEFAGTVMV-ISH 498
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLgarELLLALLDKLAAEGAPTLVlVTH 201
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-216 |
3.56e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.08 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG--------VDKEIEGEALPMPGLTIGYLEQEPKLNPEHTVRESv 90
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGllppaagtIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAEN- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 91 eesmgavnaakkrLEEVYELYAAEDADFDAlAAEQAELeaiiatagtdsehqleiaADALRLPAwdakiGVLSGGEKRRV 170
Cdd:PRK13539 94 -------------LEFWAAFLGGEELDIAA-ALEAVGL------------------APLAHLPF-----GYLSAGQKRRV 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518484691 171 ALCRLLLSKPDMLLLDEPTNHLDAESVE-WLEVFLQRFP--GTVVAITH 216
Cdd:PRK13539 137 ALARLLVSNRPIWILDEPTAALDAAAVAlFAELIRAHLAqgGIVIAATH 185
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
324-498 |
4.72e-19 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 86.52 E-value: 4.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGD--RLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV----------KMAFV 390
Cdd:cd03251 2 EFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVrdytlaslrrQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 391 DQarDALADQKTVWEDISGGLDIINVGKFQMASR-AYAGRFNFNGADQ-QKKVG----TLSGGERGRLHLAKTLIAGGNV 464
Cdd:cd03251 82 SQ--DVFLFNDTVAENIAYGRPGATREEVEEAARaANAHEFIMELPEGyDTVIGergvKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 518484691 465 LLLDEPSNDLDVETLRALEDALLEFAG--TVMVISH 498
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKnrTTFVIAH 195
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
8-235 |
6.08e-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: 6.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 8 MNRVSKTVPpKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE-------------ALPMPGLTIGYL 74
Cdd:cd03229 3 LKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSilidgedltdledELPPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 75 EQEPKLNPEHTVRESVEESmgavnaakkrleevyelyaaedadfdalaaeqaeleaiiatagtdsehqleiaadalrlpa 154
Cdd:cd03229 82 FQDFALFPHLTVLENIALG------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 155 wdakigvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFL----QRFPGTVVAITHDRYFLDNAAEWILE 230
Cdd:cd03229 101 -------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLkslqAQLGITVVLVTHDLDEAARLADRVVV 173
|
....*
gi 518484691 231 LDRGR 235
Cdd:cd03229 174 LRDGK 178
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
322-510 |
8.21e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 8.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI---GQTVKMAFVDQA----R 394
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdggDIDDPDVAEACHylghR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 395 DALADQKTV------WEDISGGLDIinvgkfqMASRAYAgRFNFNGAdQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLD 468
Cdd:PRK13539 82 NAMKPALTVaenlefWAAFLGGEEL-------DIAAALE-AVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 518484691 469 EPSNDLDVETLRALEDALLE-FAGTVMVIshdrwfldrIATHI 510
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAhLAQGGIVI---------AATHI 186
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
313-500 |
9.60e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 88.35 E-value: 9.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 313 PVAERLGSQVFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQT------- 384
Cdd:PRK11607 10 AKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLdGVDlshvppy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 385 ---VKMAFvdQARdALADQKTVWEDISGGLDIINVGKFQMASRA-----------YAGRfnfngadqqkKVGTLSGGERG 450
Cdd:PRK11607 90 qrpINMMF--QSY-ALFPHMTVEQNIAFGLKQDKLPKAEIASRVnemlglvhmqeFAKR----------KPHQLSGGQRQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 451 RLHLAKTLIAGGNVLLLDEPSNDLDvETLR---ALE--DALLEFAGTVMVISHDR 500
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALD-KKLRdrmQLEvvDILERVGVTCVMVTHDQ 210
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-251 |
1.03e-18 |
|
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: 85.36 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 16 PPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIM-------------AGVD-KEIEGEALPMpglTIGYLEQEPKLN 81
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvssgsiliDGQDiREVTLDSLRR---AIGVVPQDTVLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 82 PEhTVRESVEesMGAVNAAKkrlEEVYElyaaedadfdalAAEQAELEAIIatagtdsehqleiaadaLRLP-AWDAKIG 160
Cdd:cd03253 88 ND-TIGYNIR--YGRPDATD---EEVIE------------AAKAAQIHDKI-----------------MRFPdGYDTIVG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 161 ----VLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES-VEWLEVFLQRFPG-TVVAITHDRYFLDNAAEwILELDRG 234
Cdd:cd03253 133 erglKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTeREIQAALRDVSKGrTTIVIAHRLSTIVNADK-IIVLKDG 211
|
250
....*....|....*..
gi 518484691 235 RgIPWKGNYSTWLEQKG 251
Cdd:cd03253 212 R-IVERGTHEELLAKGG 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
320-498 |
1.05e-18 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 84.14 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 320 SQVFEFKNVSK------SFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGK--EKPDSGEV-VIGQTVK---- 386
Cdd:cd03213 1 GVTLSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVlINGRPLDkrsf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 387 ---MAFVDQaRDALADQKTVWEDISggldiinvgkFQMASRAyagrfnfngadqqkkvgtLSGGERGRLHLAKTLIAGGN 463
Cdd:cd03213 81 rkiIGYVPQ-DDILHPTLTVRETLM----------FAAKLRG------------------LSGGERKRVSIALELVSNPS 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518484691 464 VLLLDEPSNDLD-------VETLRALEDAllefAGTVMVISH 498
Cdd:cd03213 132 LLFLDEPTSGLDsssalqvMSLLRRLADT----GRTIICSIH 169
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
323-515 |
1.05e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.99 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 323 FEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTV-----------KMAFVD 391
Cdd:PRK10575 12 FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 392 QARDAlADQKTVWEDIS-------GGLdiinvGKFQMASR-------AYAGRFNFngadQQKKVGTLSGGERGRLHLAKT 457
Cdd:PRK10575 92 QQLPA-AEGMTVRELVAigrypwhGAL-----GRFGAADRekveeaiSLVGLKPL----AHRLVDSLSGGERQRAWIAML 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 458 LIAGGNVLLLDEPSNDLD----VETLrALEDALLEFAG-TVMVISHDRWFLDRIATHILAAEG 515
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDiahqVDVL-ALVHRLSQERGlTVIAVLHDINMAARYCDYLVALRG 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-239 |
1.14e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 85.98 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGvdkEIE---------GEALP-MPG----LTIGYLEQEPKLNPE 83
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG---ELSpdsgevrlnGRPLAdWSPaelaRRRAVLPQHSSLSFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 84 HTVRESVEesMGAVnaakkrleevyelyaaedadfdALAAEQAELEAIIATAgtdsEHQLEIAADALRL-PAwdakigvL 162
Cdd:PRK13548 91 FTVEEVVA--MGRA----------------------PHGLSRAEDDALVAAA----LAQVDLAHLAGRDyPQ-------L 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 163 SGGEKRRVALCRLL--LSKPDM----LLLDEPTNHLD-AESVEWLEV---FLQRFPGTVVAITHDryfLDNAAEW---IL 229
Cdd:PRK13548 136 SGGEQQRVQLARVLaqLWEPDGpprwLLLDEPTSALDlAHQHHVLRLarqLAHERGLAVIVVLHD---LNLAARYadrIV 212
|
250
....*....|....
gi 518484691 230 ELDRGR----GIPW 239
Cdd:PRK13548 213 LLHQGRlvadGTPA 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-217 |
1.32e-18 |
|
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: 85.31 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 9 NRVSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG-----------VDKEI---EGEALPMPGLTIGYL 74
Cdd:cd03256 4 ENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlveptsgsvliDGTDInklKGKALRQLRRQIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 75 EQEPKLNPEHTVRESVeesmgavnaakkrleevyelyaaedadfdaLAAEQAELEAIIATAGTDSEHQLEIAADALR--- 151
Cdd:cd03256 84 FQQFNLIERLSVLENV------------------------------LSGRLGRRSTWRSLFGLFPKEEKQRALAALErvg 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 152 -LPAWDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD---AESVewLEVFL---QRFPGTVVAITHD 217
Cdd:cd03256 134 lLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDpasSRQV--MDLLKrinREEGITVIVSLHQ 204
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-235 |
1.40e-18 |
|
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: 84.83 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 17 PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLTIGYLE-------QEPKLNpEHT 85
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgkPISQYEHKYLHskvslvgQEPVLF-ARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 86 VRESVEESMGAVNaakkrLEEVYElyaaedadfdalAAEQAELEAIIatagtdSEHQLEIAADAlrlpawDAKIGVLSGG 165
Cdd:cd03248 104 LQDNIAYGLQSCS-----FECVKE------------AAQKAHAHSFI------SELASGYDTEV------GEKGSQLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 166 EKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG--TVVAITHdRYFLDNAAEWILELDRGR 235
Cdd:cd03248 155 QKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH-RLSTVERADQILVLDGGR 225
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
37-370 |
1.89e-18 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 88.15 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 37 VLGLNGSGKSTLLKIMAGvdkeiegEALPMPGltigyleqEPKLNPEHTVRESVEEsmgavnaAKKRLEEVYE------L 110
Cdd:PRK10938 34 FVGANGSGKSALARALAG-------ELPLLSG--------ERQSQFSHITRLSFEQ-------LQKLVSDEWQrnntdmL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 111 YAAEDaDFDALAAEqaeleaIIATAGTDSEHQLEIAADALRLPAWDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTN 190
Cdd:PRK10938 92 SPGED-DTGRTTAE------IIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 191 HLDAESVEWLEVFLQRFPGTVVAIthdryfldnaaewILELDRGRGIPWKGNYSTWLEQKgeRLAQEQKSEEAHAKALkk 270
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQSGITL-------------VLVLNRFDEIPDFVQFAGVLADC--TLAETGEREEILQQAL-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 271 elewsrqnpkarqaksKSRLARFEELSDVEYQkrnETQEIFIPVAERLGSQVFEFKNVSKSFGDRLLIDNLSFNVPAGAI 350
Cdd:PRK10938 228 ----------------VAQLAHSEQLEGVQLP---EPDEPSARHALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEH 288
|
330 340
....*....|....*....|
gi 518484691 351 VGIIGPNGAGKSTLFKLLAG 370
Cdd:PRK10938 289 WQIVGPNGAGKSTLLSLITG 308
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-216 |
2.92e-18 |
|
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: 84.37 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGvdkeiegEALPMPGLTIGYLEQEpklnpehTVRESVEE---SMG 95
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG-------DLPPTYGNDVRLFGER-------RGGEDVWElrkRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 96 AVNAAkkrLEEVYELYA-AEDadfdalaaeqaeleaIIATAGTDS--------EHQLEIAADALRLpaW------DAKIG 160
Cdd:COG1119 82 LVSPA---LQLRFPRDEtVLD---------------VVLSGFFDSiglyreptDEQRERARELLEL--LglahlaDRPFG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 161 VLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES----VEWLEVFLQRFPGTVVAITH 216
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
325-475 |
2.94e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 86.62 E-value: 2.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 325 FKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQT-----------VKMAFvdQA 393
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvppaergVGMVF--QS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 394 RdALADQKTVWEDISGGLDIINVGKFQMASRA-YAGRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSN 472
Cdd:PRK11000 84 Y-ALYPHLSVAENMSFGLKLAGAKKEEINQRVnQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
...
gi 518484691 473 DLD 475
Cdd:PRK11000 163 NLD 165
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-217 |
3.72e-18 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 83.67 E-value: 3.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKE------IEGEALPMPGLTIGYLEQEPKLNPEHTVRESVEEsmg 95
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPtsggviLEGKQITEPGPDRMVVFQNYSLLPWLTVRENIAL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 96 AVNAAKKRLEEvyelyaaedadfdalaaeqAELEAIIatagtdsEHQLEIAAdaLRLPAwDAKIGVLSGGEKRRVALCRL 175
Cdd:TIGR01184 78 AVDRVLPDLSK-------------------SERRAIV-------EEHIALVG--LTEAA-DKRPGQLSGGMKQRVAIARA 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518484691 176 LLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG----TVVAITHD 217
Cdd:TIGR01184 129 LSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEehrvTVLMVTHD 174
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-216 |
4.14e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 82.79 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpMPGltigyleqepklNPEHTVRESVEESM---G 95
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVR-WNG------------TPLAEQRDEPHENIlylG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 96 AVNAAKKrleevyELYAAEDADF--DALAAEQAELEAIIATAG-TDSEHqleiaadalrLPAwdakiGVLSGGEKRRVAL 172
Cdd:TIGR01189 80 HLPGLKP------ELSALENLHFwaAIHGGAQRTIEDALAAVGlTGFED----------LPA-----AQLSAGQQRRLAL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518484691 173 CRLLLSKPDMLLLDEPTNHLDAESVEWL----EVFLQRfPGTVVAITH 216
Cdd:TIGR01189 139 ARLWLSRRPLWILDEPTTALDKAGVALLagllRAHLAR-GGIVLLTTH 185
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
18-235 |
4.27e-18 |
|
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: 82.96 E-value: 4.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEalpmpgLTIGYLEQEPKLNPEHTVRESVeeSMgav 97
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGT------IIIDGLKLTDDKKNINELRQKV--GM--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 98 naakkrleeVYELYAAedadFDALAAEQAELEAIIATAGTDSEHQLEIAADALR----LPAWDAKIGVLSGGEKRRVALC 173
Cdd:cd03262 81 ---------VFQQFNL----FPHLTVLENITLAPIKVKGMSKAEAEERALELLEkvglADKADAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 174 RLLLSKPDMLLLDEPTNHLDAESV-EWLEVFLQ--RFPGTVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVgEVLDVMKDlaEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
324-510 |
4.71e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 83.63 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQT--VKMAFVDQAR------- 394
Cdd:COG4674 12 YVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTdlTGLDEHEIARlgigrkf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 395 ------DALadqkTVWEDIsggldiinvgkfQMASRAYAG-----RFNFNGADQQK----------------KVGTLSGG 447
Cdd:COG4674 92 qkptvfEEL----TVFENL------------ELALKGDRGvfaslFARLTAEERDRieevletigltdkadrLAGLLSHG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 448 ERGRLHLAKTLIAGGNVLLLDEPSNDL-DVETLRALEdALLEFAG--TVMVISHDRWFLDRIATHI 510
Cdd:COG4674 156 QKQWLEIGMLLAQDPKLLLLDEPVAGMtDAETERTAE-LLKSLAGkhSVVVVEHDMEFVRQIARKV 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
18-188 |
5.75e-18 |
|
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: 82.98 E-value: 5.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE---------ALPM---PGLTIGYLEQEP----KLn 81
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKilldgqditKLPMhkrARLGIGYLPQEAsifrKL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 82 pehtvreSVEESMGAVnaakkrLEEVYELYAAEDADFDALAAEqAELEAIiatagtdsEHQLEIAadalrlpawdakigv 161
Cdd:cd03218 91 -------TVEENILAV------LEIRGLSKKEREEKLEELLEE-FHITHL--------RKSKASS--------------- 133
|
170 180
....*....|....*....|....*..
gi 518484691 162 LSGGEKRRVALCRLLLSKPDMLLLDEP 188
Cdd:cd03218 134 LSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
16-240 |
6.23e-18 |
|
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: 83.23 E-value: 6.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 16 PPKRQILKDISL-----SFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAlPMPGLTIGYLEQEPKLNPEHTVResv 90
Cdd:cd03237 4 PTMKKTLGEFTLeveggSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-EIELDTVSYKPQYIKADYEGTVR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 91 eesmgavnaakkrleevyelyaaedaDFdalaaeqaeLEAIIATAGTDSEHQLEIAaDALRL-PAWDAKIGVLSGGEKRR 169
Cdd:cd03237 80 --------------------------DL---------LSSITKDFYTHPYFKTEIA-KPLQIeQILDREVPELSGGELQR 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 170 VALCrLLLSKP-DMLLLDEPTNHLDAESVEWLEVFLQRF----PGTVVAITHDRYFLDNAAEWILELDrgrGIPWK 240
Cdd:cd03237 124 VAIA-ACLSKDaDIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMIDYLADRLIVFE---GEPSV 195
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
19-256 |
6.30e-18 |
|
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: 83.11 E-value: 6.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEalPMPGLT----------IGYLEQEPKL-- 80
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRpdsgeiLVDGQ--DITGLSekelyelrrrIGMLFQGGALfd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 81 ------N---P--EHT------VRESVEESMGAVNaakkrLEEVYELYAAEdadfdalaaeqaeleaiiatagtdsehql 143
Cdd:COG1127 96 sltvfeNvafPlrEHTdlseaeIRELVLEKLELVG-----LPGAADKMPSE----------------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 144 eiaadalrlpawdakigvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVewlEVFLQ-------RFPGTVVAITH 216
Cdd:COG1127 142 ------------------LSGGMRKRVALARALALDPEILLYDEPTAGLDPITS---AVIDElirelrdELGLTSVVVTH 200
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 518484691 217 DRYFLDNAAEWILELDRGRgIPWKGNYSTWLEQKGERLAQ 256
Cdd:COG1127 201 DLDSAFAIADRVAVLADGK-IIAEGTPEELLASDDPWVRQ 239
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
324-498 |
7.62e-18 |
|
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: 86.69 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFG--DRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVK----------MAFV 390
Cdd:TIGR02203 332 EFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLdGHDLAdytlaslrrqVALV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 391 DQarDALADQKTVWEDIS-GGLDIINVGKFQMASR-AYAGRF---NFNGADQQ--KKVGTLSGGERGRLHLAKTLIAGGN 463
Cdd:TIGR02203 412 SQ--DVVLFNDTIANNIAyGRTEQADRAEIERALAaAYAQDFvdkLPLGLDTPigENGVLLSGGQRQRLAIARALLKDAP 489
|
170 180 190
....*....|....*....|....*....|....*..
gi 518484691 464 VLLLDEPSNDLDVETLRALEDAL--LEFAGTVMVISH 498
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAALerLMQGRTTLVIAH 526
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
322-475 |
7.74e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 85.38 E-value: 7.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQaRD----- 395
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLdGQDITHVPAEN-RHvntvf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 396 ---ALADQKTVWEDISGGLDIINVGKFQMASR-----------AYAGRfnfngadqqkKVGTLSGGERGRLHLAKTLIAG 461
Cdd:PRK09452 93 qsyALFPHMTVFENVAFGLRMQKTPAAEITPRvmealrmvqleEFAQR----------KPHQLSGGQQQRVAIARAVVNK 162
|
170
....*....|....
gi 518484691 462 GNVLLLDEPSNDLD 475
Cdd:PRK09452 163 PKVLLLDESLSALD 176
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
324-528 |
8.15e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.55 E-value: 8.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSF-GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDALAdqk 401
Cdd:PRK13657 336 EFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDIRTVTRASLRRNIA--- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 402 TVWEDisGGL------DIINVGK--------FQMASRAYAGRF---NFNGADQQkkVG----TLSGGERGRLHLAKTLIA 460
Cdd:PRK13657 413 VVFQD--AGLfnrsieDNIRVGRpdatdeemRAAAERAQAHDFierKPDGYDTV--VGergrQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 461 GGNVLLLDEPSNDLDVETLRALEDALLEFAG--TVMVISHdRWFLDRIATHILaaegdsqwtFFD-------GNYQE 528
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMKgrTTFIIAH-RLSTVRNADRIL---------VFDngrvvesGSFDE 555
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
323-519 |
1.09e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 80.66 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 323 FEFKNVS-KSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQA-------- 393
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRpylplgtl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 394 RDALAdqkTVWEDIsggldiinvgkfqmasrayagrfnfngadqqkkvgtLSGGERGRLHLAKTLIAGGNVLLLDEPSND 473
Cdd:cd03223 81 REQLI---YPWDDV------------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518484691 474 LDVETLRALEDALLEFAGTVMVISHdRWFLDRIATHILAAEGDSQW 519
Cdd:cd03223 122 LDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGEGGW 166
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
328-507 |
1.30e-17 |
|
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: 83.08 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 328 VSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV--------------KMAFVDQ 392
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIdGQDIaamsrkelrelrrkKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 393 ARdALADQKTVWEDISGGLDIINVGKFQMASRAYAGRFNFN-GADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPS 471
Cdd:cd03294 110 SF-ALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGlEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518484691 472 NDLDVETLRALEDALL----EFAGTVMVISHDrwfL-------DRIA 507
Cdd:cd03294 189 SALDPLIRREMQDELLrlqaELQKTIVFITHD---LdealrlgDRIA 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
324-500 |
1.35e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 84.37 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV--------KMAFVDQAR 394
Cdd:PRK10851 4 EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhGTDVsrlhardrKVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 395 dALADQKTVWEDISGGLdiinvgkfQMASRayagRFNFNGADQQKKV-----------------GTLSGGERGRLHLAKT 457
Cdd:PRK10851 84 -ALFRHMTVFDNIAFGL--------TVLPR----RERPNAAAIKAKVtqllemvqlahladrypAQLSGGQKQRVALARA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518484691 458 LIAGGNVLLLDEPSNDLDVET-------LRALEDallEFAGTVMVISHDR 500
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVrkelrrwLRQLHE---ELKFTSVFVTHDQ 197
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
326-499 |
1.76e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.08 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQ------------A 393
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQklyldttlpltvN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 394 RDALADQKTVWEDISGGLDIINVGKFQMASrayagrfnfngadQQKkvgtLSGGERGRLHLAKTLIAGGNVLLLDEPSND 473
Cdd:PRK09544 88 RFLRLRPGTKKEDILPALKRVQAGHLIDAP-------------MQK----LSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190
....*....|....*....|....*....|
gi 518484691 474 LDVETLRALEDAL----LEFAGTVMVISHD 499
Cdd:PRK09544 151 VDVNGQVALYDLIdqlrRELDCAVLMVSHD 180
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-235 |
1.87e-17 |
|
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: 80.98 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 7 SMNRVSKTVPPKRQ----ILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpMPGlTIGYLEQEPKLNP 82
Cdd:cd03250 2 SVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS-VPG-SIAYVSQEPWIQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 83 EhTVRESV-------EEsmgavnaakkRLEEVYELyAAEDADFDALAAeqaeleaiiataGTDSEhqleiaadalrlpaw 155
Cdd:cd03250 80 G-TIRENIlfgkpfdEE----------RYEKVIKA-CALEPDLEILPD------------GDLTE--------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 156 dakIGV----LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWL--EVFLQ--RFPGTVVAITHDRYFLDNaAEW 227
Cdd:cd03250 121 ---IGEkginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfeNCILGllLNNKTRILVTHQLQLLPH-ADQ 196
|
....*...
gi 518484691 228 ILELDRGR 235
Cdd:cd03250 197 IVVLDNGR 204
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
322-517 |
2.25e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.54 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSF---GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV----------KM 387
Cdd:TIGR00958 478 LIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLdGVPLvqydhhylhrQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 388 AFVDQarDALADQKTVWEDISGGLDIINVGKFQMASRAyAGRFNFNGADQQ-------KKVGTLSGGERGRLHLAKTLIA 460
Cdd:TIGR00958 558 ALVGQ--EPVLFSGSVRENIAYGLTDTPDEEIMAAAKA-ANAHDFIMEFPNgydtevgEKGSQLSGGQKQRIAIARALVR 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 461 GGNVLLLDEPSNDLDVETLRALEDaLLEFAG-TVMVISHdRWFLDRIATHILAAEGDS 517
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQLLQE-SRSRASrTVLLIAH-RLSTVERADQILVLKKGS 690
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
324-515 |
2.30e-17 |
|
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: 81.38 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFG--DRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIgQTVKMAFVDQA-------- 393
Cdd:cd03252 2 TFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLV-DGHDLALADPAwlrrqvgv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 394 --RDALADQKTVWEDISGGLDIINVGKFQMASRaYAGRFNF-----NGADQ---QKKVGtLSGGERGRLHLAKTLIAGGN 463
Cdd:cd03252 81 vlQENVLFNRSIRDNIALADPGMSMERVIEAAK-LAGAHDFiselpEGYDTivgEQGAG-LSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518484691 464 VLLLDEPSNDLDVETLRALEDALLEF-AG-TVMVISHdRWFLDRIATHILAAEG 515
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDIcAGrTVIIIAH-RLSTVKNADRIIVMEK 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-235 |
2.60e-17 |
|
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: 83.62 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 31 PGAKI-GVLGLNGSGKSTLLKIMAGVDKEIEGEA---------------LPMPGLTIGYLEQEPKLNPEHTVRESVEESM 94
Cdd:TIGR02142 21 PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlfdsrkgifLPPEKRRIGYVFQEARLFPHLSVRGNLRYGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 95 GAVNAAKKRLEEvyelyaaedadfdalaaeqaelEAIIATAGTdsEHQLEiaadalRLPawdakiGVLSGGEKRRVALCR 174
Cdd:TIGR02142 101 KRARPSERRISF----------------------ERVIELLGI--GHLLG------RLP------GRLSGGEKQRVAIGR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 175 LLLSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:TIGR02142 145 ALLSSPRLLLMDEPLAALDdprkYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGR 209
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
324-498 |
3.08e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.58 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSF-GDRLLiDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAfvdQARDALAD-- 399
Cdd:PRK11288 6 SFDGIGKTFpGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEMRFA---STTAALAAgv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 400 -----------QKTVWEDI-------SGGldIINVGKFQMASRAYAGRFNFNgADQQKKVGTLSGGERGRLHLAKTLIAG 461
Cdd:PRK11288 82 aiiyqelhlvpEMTVAENLylgqlphKGG--IVNRRLLNYEAREQLEHLGVD-IDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518484691 462 GNVLLLDEPSNDL---DVETLRALEDALLEFAGTVMVISH 498
Cdd:PRK11288 159 ARVIAFDEPTSSLsarEIEQLFRVIRELRAEGRVILYVSH 198
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
324-515 |
3.54e-17 |
|
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: 80.59 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSF---GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV----------KMAF 389
Cdd:cd03248 13 KFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdGKPIsqyehkylhsKVSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 390 VDQARDALAdqKTVWEDISGGLDIINVGKF-QMASRAYAGRF-------NFNGADQqkKVGTLSGGERGRLHLAKTLIAG 461
Cdd:cd03248 93 VGQEPVLFA--RSLQDNIAYGLQSCSFECVkEAAQKAHAHSFiselasgYDTEVGE--KGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 462 GNVLLLDEPSNDLDVETLRALEDALLEF--AGTVMVISHDRWFLDRiATHILAAEG 515
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVER-ADQILVLDG 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
324-471 |
4.26e-17 |
|
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: 80.17 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG----------QTVKM--AFVD 391
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditglpphERARAgiGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 392 QARDALADQkTVWEDISGGLDIINVGKFQMA-SRAYAgRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEP 470
Cdd:cd03224 82 EGRRIFPEL-TVEENLLLGAYARRRAKRKARlERVYE-LFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
.
gi 518484691 471 S 471
Cdd:cd03224 160 S 160
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-476 |
5.15e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.95 E-value: 5.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 21 ILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAL----PMPGLTIG-YL-EQEPKLNPEHTVRE 88
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPpdsgtlEIGGNPCarltPAKAHQLGiYLvPQEPLLFPNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 89 SVEESMGAVNAAKKRLEEVyelyaaedadfdaLAAEQAELEaIIATAGTdsehqLEIAadalrlpawdakigvlsggEKR 168
Cdd:PRK15439 106 NILFGLPKRQASMQKMKQL-------------LAALGCQLD-LDSSAGS-----LEVA-------------------DRQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 169 RVALCRLLLSKPDMLLLDEPTNHLDAESVEWL----EVFLQRFPGtVVAITHDRYFLDNAAEWILELdRGRGIPWKGNYS 244
Cdd:PRK15439 148 IVEILRGLMRDSRILILDEPTASLTPAETERLfsriRELLAQGVG-IVFISHKLPEIRQLADRISVM-RDGTIALSGKTA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 245 TWL----------EQKGERLAQEQKseeahakaLKKELEWSRQnpkaRQAKSKSRLaRFEELsdveyqkrneTQEIFIpv 314
Cdd:PRK15439 226 DLStddiiqaitpAAREKSLSASQK--------LWLELPGNRR----QQAAGAPVL-TVEDL----------TGEGFR-- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 315 aerlgsqvfefknvsksfgdrllidNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMafvDQA 393
Cdd:PRK15439 281 -------------------------NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLnGKEINA---LST 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 394 RDALaDQKTVW--ED--ISG------------GLDIINVGKFQMASR--AYAGRF------NFNGADQQkkVGTLSGGER 449
Cdd:PRK15439 333 AQRL-ARGLVYlpEDrqSSGlyldaplawnvcALTHNRRGFWIKPARenAVLERYrralniKFNHAEQA--ARTLSGGNQ 409
|
490 500
....*....|....*....|....*..
gi 518484691 450 GRLHLAKTLIAGGNVLLLDEPSNDLDV 476
Cdd:PRK15439 410 QKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
333-499 |
5.20e-17 |
|
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: 84.03 E-value: 5.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 333 GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGqtvkMAFVDQ-ARDALAD------QK---- 401
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD----GADLSQwDREELGRhigylpQDvelf 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 402 --TVWEDISgGLDIINVGKFQMASRAyAG------RFNfNGADQQkkVG----TLSGGERGRLHLAKTLIagGN--VLLL 467
Cdd:COG4618 419 dgTIAENIA-RFGDADPEKVVAAAKL-AGvhemilRLP-DGYDTR--IGeggaRLSGGQRQRIGLARALY--GDprLVVL 491
|
170 180 190
....*....|....*....|....*....|....*
gi 518484691 468 DEPSNDLDVETLRALEDALLEFA---GTVMVISHD 499
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRALKargATVVVITHR 526
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
13-227 |
5.50e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 81.67 E-value: 5.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 13 KTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMagvdkeiegEALPMPGL-TIGYLEQEPKLNPEHTVRESVE 91
Cdd:PRK13651 14 KKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHL---------NALLLPDTgTIEWIFKDEKNKKKTKEKEKVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 92 ESMGAVNAAKKRLEEVYELYA--------AEDADFdalaaEQAELEAIIATA---GTDSEHQLEIAADALRLpawdakIG 160
Cdd:PRK13651 85 EKLVIQKTRFKKIKKIKEIRRrvgvvfqfAEYQLF-----EQTIEKDIIFGPvsmGVSKEEAKKRAAKYIEL------VG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 161 V-----------LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESV-EWLEVF--LQRFPGTVVAITHDryfLDNAAE 226
Cdd:PRK13651 154 LdesylqrspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVkEILEIFdnLNKQGKTIILVTHD---LDNVLE 230
|
.
gi 518484691 227 W 227
Cdd:PRK13651 231 W 231
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
323-481 |
5.70e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 79.83 E-value: 5.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 323 FEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPD---SGEVVIGQT-----------VKMA 388
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRrltalpaeqrrIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 389 FVDqarDALADQKTVWEDISGGLDIiNVGKFQMASRAY--------AGRFNfngadqqKKVGTLSGGERGRLHLAKTLIA 460
Cdd:COG4136 82 FQD---DLLFPHLSVGENLAFALPP-TIGRAQRRARVEqaleeaglAGFAD-------RDPATLSGGQRARVALLRALLA 150
|
170 180
....*....|....*....|.
gi 518484691 461 GGNVLLLDEPSNDLDVeTLRA 481
Cdd:COG4136 151 EPRALLLDEPFSKLDA-ALRA 170
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-235 |
6.48e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.89 E-value: 6.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 17 PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE----ALPMPGL----------TIGYLEQEP--KL 80
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNvswrGEPLAKLnraqrkafrrDIQMVFQDSisAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 81 NPEHTVRESVEESMgavnaakKRLEEVYElyaaedadfdalAAEQAELEAIIATAGTDSEHqleiaadALRLPawdakiG 160
Cdd:PRK10419 103 NPRKTVREIIREPL-------RHLLSLDK------------AERLARASEMLRAVDLDDSV-------LDKRP------P 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518484691 161 VLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:PRK10419 151 QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQ 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
20-235 |
7.69e-17 |
|
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: 80.62 E-value: 7.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaLPMPGLTIGYLEQEPKLNPEHTVRESVEESMGAVNA 99
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGT-VSFRGQDLYQLDRKQRRAFRRDVQLVFQDSPSAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 100 ---AKKRLEEVYELYAAEDAdfdalAAEQAELEAIIATAGTDSEHqleiaadALRLPAWdakigvLSGGEKRRVALCRLL 176
Cdd:TIGR02769 104 rmtVRQIIGEPLRHLTSLDE-----SEQKARIAELLDMVGLRSED-------ADKLPRQ------LSGGQLQRINIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 177 LSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLDmvlqAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-218 |
8.21e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 82.05 E-value: 8.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 8 MNRVSKTVPpKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEiegealpmpglTIGYLeqepKLNPEHTVR 87
Cdd:PRK10851 5 IANIKKSFG-RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ-----------TSGHI----RFHGTDVSR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 88 esveesmgaVNAAKKRLEEVYELYA-------AEDADF--DALAAEQAELEAIIATAGTDSEHQLEIAADALRLPAWdak 158
Cdd:PRK10851 69 ---------LHARDRKVGFVFQHYAlfrhmtvFDNIAFglTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQ--- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518484691 159 igvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVEWLEVFLQRFPGTVVAITHDR 218
Cdd:PRK10851 137 ---LSGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQ 197
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
322-499 |
8.36e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 80.81 E-value: 8.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGD--RLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDALA 398
Cdd:PRK13632 7 MIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 399 ------DQK----TVWEDISGGLDIINVGKFQMASRAYagrfnfngaDQQKKVGT----------LSGGERGRLHLAKTL 458
Cdd:PRK13632 87 iifqnpDNQfigaTVEDDIAFGLENKKVPPKKMKDIID---------DLAKKVGMedyldkepqnLSGGQKQRVAIASVL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518484691 459 IAGGNVLLLDEPSNDLDVETLRALEDALLEFAG----TVMVISHD 499
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrkkTLISITHD 202
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
320-381 |
8.41e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.13 E-value: 8.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 320 SQVFEFKNVSKSF------GDRLL----------------IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSG 377
Cdd:COG1134 2 SSMIEVENVSKSYrlyhepSRSLKelllrrrrtrreefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
....
gi 518484691 378 EVVI 381
Cdd:COG1134 82 RVEV 85
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-217 |
8.55e-17 |
|
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: 79.69 E-value: 8.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE---------ALPMPGLTIGYLEQEPKLNPEHTVRESVEE 92
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKillngkditNLPPEKRDISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 93 SMgavnaaKKRLEEVYELyaaedadfDALAAEQAELEAIiatagtdsEHQLeiaadalrlpawDAKIGVLSGGEKRRVAL 172
Cdd:cd03299 95 GL------KKRKVDKKEI--------ERKVLEIAEMLGI--------DHLL------------NRKPETLSGGEQQRVAI 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518484691 173 CRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQR----FPGTVVAITHD 217
Cdd:cd03299 141 ARALVVNPKILLLDEPFSALDVRTKEKLREELKKirkeFGVTVLHVTHD 189
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
22-235 |
1.08e-16 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 79.40 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL-------PMP-----GLTIGYLEQEPKLNPEHTVRES 89
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgeditGLPpheiaRLGIGRTFQIPRLFPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 90 VeesMGAVNAAKKRleevyelYAAEDADFDALAAEQAELEAIIATAGTDsehqleiaadalrlPAWDAKIGVLSGGEKRR 169
Cdd:cd03219 96 V---MVAAQARTGS-------GLLLARARREEREARERAEELLERVGLA--------------DLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518484691 170 VALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG---TVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRErgiTVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
18-188 |
1.25e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 79.30 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG---VDK---EIEGE---ALPMPG---LTIGYLEQEP----KLn 81
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGlvkPDSgriFLDGEditHLPMHKrarLGIGYLPQEAsifrKL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 82 pehtvreSVEESMGAVnaakkrLeEVYELYAAEDadfdalaaeQAELEAIIAtagtdsEHQLEiaadALRlpawDAKIGV 161
Cdd:COG1137 94 -------TVEDNILAV------L-ELRKLSKKER---------EERLEELLE------EFGIT----HLR----KSKAYS 136
|
170 180
....*....|....*....|....*..
gi 518484691 162 LSGGEKRRVALCRLLLSKPDMLLLDEP 188
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEP 163
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
9-237 |
1.68e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 77.19 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 9 NRVSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaLPMPGLT-IGYLEQEPKLnPEHTVR 87
Cdd:cd03223 4 ENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGR-IGMPEGEdLLFLPQRPYL-PLGTLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 88 EsveesmgavnaakkrleevyelyaaedadfdalaaeqaeleaiiatagtdsehqleiaadALRLPaWDAkigVLSGGEK 167
Cdd:cd03223 82 E------------------------------------------------------------QLIYP-WDD---VLSGGEQ 97
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPGTVVAITHdRYFLDNAAEWILELDRGRGI 237
Cdd:cd03223 98 QRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGEGGW 166
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
326-499 |
1.69e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.58 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI----GQTVKMA------------- 388
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdGQLRDLYalseaerrrllrt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 389 ---FVDQ-ARDALADQktvwedISGGldiINVGKFQMAS--RAYaGRFNFNGADQQKKV-----------GTLSGGERGR 451
Cdd:PRK11701 90 ewgFVHQhPRDGLRMQ------VSAG---GNIGERLMAVgaRHY-GDIRATAGDWLERVeidaariddlpTTFSGGMQQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 452 LHLAKTLIAGGNVLLLDEPSNDLDV-------ETLRALedaLLEFAGTVMVISHD 499
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVsvqarllDLLRGL---VRELGLAVVIVTHD 211
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-223 |
2.21e-16 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 76.97 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 7 SMNRVSKTVPPKRQ-ILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpmpgltigyleqepkLN--PE 83
Cdd:cd03247 2 SINNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT---------------LDgvPV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 84 HTVRESVEESMGAVNaakkrlEEVYeLYAAedadfdalaaeqaeleAIIATAGTDsehqleiaadalrlpawdakigvLS 163
Cdd:cd03247 67 SDLEKALSSLISVLN------QRPY-LFDT----------------TLRNNLGRR-----------------------FS 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518484691 164 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES-VEWLEVFLQRFPG-TVVAITH--------DR-YFLDN 223
Cdd:cd03247 101 GGERQRLALARILLQDAPIVLLDEPTVGLDPITeRQLLSLIFEVLKDkTLIWITHhltgiehmDKiLFLEN 171
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
333-499 |
2.50e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.73 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 333 GDRLLidNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGkEKPDSGEVVIGQT----VKMAFVDQARDALADQKT------ 402
Cdd:COG4138 9 AGRLG--PISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRplsdWSAAELARHRAYLSQQQSppfamp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 403 VWEDISGGL-DIINVGKFQMASRAYAGRFNFngADQ-QKKVGTLSGGERGRLHLAKTLI-------AGGNVLLLDEPSND 473
Cdd:COG4138 86 VFQYLALHQpAGASSEAVEQLLAQLAEALGL--EDKlSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNS 163
|
170 180
....*....|....*....|....*....
gi 518484691 474 LDVETLRALEDALLEFA---GTVMVISHD 499
Cdd:COG4138 164 LDVAQQAALDRLLRELCqqgITVVMSSHD 192
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
342-528 |
2.66e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.47 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 342 SFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQT----------VKMAFVDqarDALADQKTVWEDISGG 410
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLnGQDhtttppsrrpVSMLFQE---NNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 411 LDiinvgkfqmasrayAG-RFNfngADQQKKV-----------------GTLSGGERGRLHLAKTLIAGGNVLLLDEPSN 472
Cdd:PRK10771 96 LN--------------PGlKLN---AAQREKLhaiarqmgiedllarlpGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518484691 473 DLD----VETLRALEDALLEFAGTVMVISHDrwfLD---RIATH-ILAAEGDSQWtffDGNYQE 528
Cdd:PRK10771 159 ALDpalrQEMLTLVSQVCQERQLTLLMVSHS---LEdaaRIAPRsLVVADGRIAW---DGPTDE 216
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
324-498 |
2.83e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 77.53 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVkmafVDQARDALAdQKTV 403
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP----LDFQRDSIA-RGLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 404 W----EDISGGLDIINVGKFQMASRAYAG------RFNFNGAdQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSND 473
Cdd:cd03231 77 YlghaPGIKTTLSVLENLRFWHADHSDEQveealaRVGLNGF-EDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180
....*....|....*....|....*...
gi 518484691 474 LDVETLRALEDAL---LEFAGTVMVISH 498
Cdd:cd03231 156 LDKAGVARFAEAMaghCARGGMVVLTTH 183
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
18-188 |
2.93e-16 |
|
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: 78.47 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEA---------LPMPG---LTIGYLEQEPKLNPEHT 85
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIlidgqdithLPMHErarLGIGYLPQEASIFRKLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 86 VRESVEesmgAVnaakkrLEEVYELYAAEdadfdalaaEQAELEAIIAtagtdsehQLEIAAdaLRlpawDAKIGVLSGG 165
Cdd:TIGR04406 93 VEENIM----AV------LEIRKDLDRAE---------REERLEALLE--------EFQISH--LR----DNKAMSLSGG 139
|
170 180
....*....|....*....|...
gi 518484691 166 EKRRVALCRLLLSKPDMLLLDEP 188
Cdd:TIGR04406 140 ERRRVEIARALATNPKFILLDEP 162
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
324-471 |
3.40e-16 |
|
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: 78.10 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVK-----------MAFVD 391
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdGEDITglpphriarlgIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 392 QARDALADQkTVWEDIsggldiinvgkfQMAsrAYAGRFNFNGADQQKKV---------------GTLSGGERGRLHLAK 456
Cdd:COG0410 85 EGRRIFPSL-TVEENL------------LLG--AYARRDRAEVRADLERVyelfprlkerrrqraGTLSGGEQQMLAIGR 149
|
170
....*....|....*
gi 518484691 457 TLIAGGNVLLLDEPS 471
Cdd:COG0410 150 ALMSRPKLLLLDEPS 164
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
327-499 |
3.45e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.59 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 327 NVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEV------VIGQTVKMAFVDQaRDALADQ 400
Cdd:PRK11248 6 HLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSItldgkpVEGPGAERGVVFQ-NEGLLPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 401 KTVWEDISGGLDIINVGKFQMASRAYA--GRFNFNGADqQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVET 478
Cdd:PRK11248 85 RNVQDNVAFGLQLAGVEKMQRLEIAHQmlKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180
....*....|....*....|....*
gi 518484691 479 LRALEDALL----EFAGTVMVISHD 499
Cdd:PRK11248 164 REQMQTLLLklwqETGKQVLLITHD 188
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
8-217 |
3.46e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 78.57 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 8 MNRVSKTVPpKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLT--IGYLEQEPKLN 81
Cdd:PRK11247 15 LNAVSKRYG-ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLagtaPLAEARedTRLMFQDARLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 82 PEHTVRESVeeSMGAVNAAKKrleevyelyaaedadfdalAAEQAeleaiiatagtdsehqLEIAADALRLPAWDAkigV 161
Cdd:PRK11247 94 PWKKVIDNV--GLGLKGQWRD-------------------AALQA----------------LAAVGLADRANEWPA---A 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 162 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVEWLEVFLQRFPGTVVAITHD 217
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDAltriEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
275-499 |
3.61e-16 |
|
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: 81.25 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 275 SRQNPKARQAksksrLARFEELSDVEyqkrNETQEIFIPVAERLGSQVF--EFKNVSKSF-GDRLLIDNLSFNVPAGAIV 351
Cdd:TIGR02868 294 AQQLTRVRAA-----AERIVEVLDAA----GPVAEGSAPAAGAVGLGKPtlELRDLSAGYpGAPPVLDGVSLDLPPGERV 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 352 GIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGqTVKMAFVDQ----ARDALADQK------TVWEDIS-GGLDIINVGKFQ 420
Cdd:TIGR02868 365 AILGPSGSGKSTLLATLAGLLDPLQGEVTLD-GVPVSSLDQdevrRRVSVCAQDahlfdtTVRENLRlARPDATDEELWA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 421 MASRAYAG---RFNFNGADQqkKVG----TLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETlralEDALLE--FAG 491
Cdd:TIGR02868 444 ALERVGLAdwlRALPDGLDT--VLGeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAET----ADELLEdlLAA 517
|
250
....*....|..
gi 518484691 492 ----TVMVISHD 499
Cdd:TIGR02868 518 lsgrTVVLITHH 529
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
11-235 |
3.69e-16 |
|
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: 77.86 E-value: 3.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 11 VSKTVPPKR---QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEALpmPGLT----------- 70
Cdd:COG4181 14 LTKTVGTGAgelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRptsgtvRLAGQDL--FALDedararlrarh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 71 IGYLEQEPKLNPEHTVRESVeesmgAVNAakkrleevyELyaAEDADFDALAAeqAELEAIiatagtdsehqleiaadAL 150
Cdd:COG4181 92 VGFVFQSFQLLPTLTALENV-----MLPL---------EL--AGRRDARARAR--ALLERV-----------------GL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 151 --RLpawDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDA---ESVEWLEVFLQRFPG-TVVAITHDRYfLDNA 224
Cdd:COG4181 137 ghRL---DHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAatgEQIIDLLFELNRERGtTLVLVTHDPA-LAAR 212
|
250
....*....|.
gi 518484691 225 AEWILELDRGR 235
Cdd:COG4181 213 CDRVLRLRAGR 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-194 |
3.80e-16 |
|
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: 77.70 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 3 QYVYSMNRVSKTVP---PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKE---IEGEAL----PM-PGLT- 70
Cdd:cd03234 1 QRVLPWWDVGLKAKnwnKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILfngqPRkPDQFq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 71 --IGYLEQEPKLNPEHTVRESVeesmgavnaakkrleevyeLYAAedadfdalaaeqaeleaIIATAGTDSEHQLEIAAD 148
Cdd:cd03234 81 kcVAYVRQDDILLPGLTVRETL-------------------TYTA-----------------ILRLPRKSSDAIRKKRVE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518484691 149 ALRL------PAWDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDA 194
Cdd:cd03234 125 DVLLrdlaltRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
326-499 |
4.53e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.05 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKsfGDRLLidNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKeKPDSGEVVIGQTV--KMAFVDQA--RDALADQK 401
Cdd:PRK03695 4 NDVAV--STRLG--PLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPleAWSAAELArhRAYLSQQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 402 T------VWE--DISGGlDIINVGKFQMASRAYAGRFNFngadqQKK----VGTLSGGERGRLHLA-------KTLIAGG 462
Cdd:PRK03695 79 TppfampVFQylTLHQP-DKTRTEAVASALNEVAEALGL-----DDKlgrsVNQLSGGEWQRVRLAavvlqvwPDINPAG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518484691 463 NVLLLDEPSNDLDVETLRALEDALLEFA---GTVMVISHD 499
Cdd:PRK03695 153 QLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-476 |
4.56e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.13 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 1 MAQYVYSMNRVSKTVPPKRQiLKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV------DKEI--EGEALPMPGLT-- 70
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKA-LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyEGEIifEGEELQASNIRdt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 71 ----IGYLEQEPKLNPEHTVRESVeeSMGAvnaakkrleevyELYAAEDADFDALAAEQAELEAiiatagtdsehQLEIA 146
Cdd:PRK13549 80 eragIAIIHQELALVKELSVLENI--FLGN------------EITPGGIMDYDAMYLRAQKLLA-----------QLKLD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 147 ADAlrlpawDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHL-DAESVEWLEVF--LQRFPGTVVAITHDryfLDN 223
Cdd:PRK13549 135 INP------ATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLtESETAVLLDIIrdLKAHGIACIYISHK---LNE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 224 AAE---WILELDRGRGIpwkgnystwleqkGERLAQEQKSEEAHAKALKKELewsrqnpkarqaksksrlarfeelsdve 300
Cdd:PRK13549 206 VKAisdTICVIRDGRHI-------------GTRPAAGMTEDDIITMMVGREL---------------------------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 301 yqkrnetQEIFIPVAERLGSQVFEFKNVS---KSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDS- 376
Cdd:PRK13549 245 -------TALYPREPHTIGEVILEVRNLTawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWe 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 377 GEVVI-GQTVK-----------MAFV--DQARDALADQKTVWEDIS-------GGLDIINVGKFQMASRAYAGRFNFNGA 435
Cdd:PRK13549 318 GEIFIdGKPVKirnpqqaiaqgIAMVpeDRKRDGIVPVMGVGKNITlaaldrfTGGSRIDDAAELKTILESIQRLKVKTA 397
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 518484691 436 DQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV 476
Cdd:PRK13549 398 SPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-499 |
4.92e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.73 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 7 SMNRVSKTVPPKRQiLKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEALPMP--------GLTIG 72
Cdd:PRK11288 6 SFDGIGKTFPGVKA-LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQpdagsiLIDGQEMRFAsttaalaaGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 73 YleQEPKLNPEHTVRESV-----EESMGAVNaaKKRL-EEVYELYAAEDADFDAlaaeqaeleaiiatagtdsehqleia 146
Cdd:PRK11288 85 Y--QELHLVPEMTVAENLylgqlPHKGGIVN--RRLLnYEAREQLEHLGVDIDP-------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 147 adalrlpawDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQ--RFPGTVVA-ITHdryfldn 223
Cdd:PRK11288 135 ---------DTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRelRAEGRVILyVSH------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 224 AAEWILEL-DR------GRGIpwkGNYSTWLEQKGERLAQEQkseeahakalkkelewsrqnpkarqaksksrLARfeEL 296
Cdd:PRK11288 199 RMEEIFALcDAitvfkdGRYV---ATFDDMAQVDRDQLVQAM-------------------------------VGR--EI 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 297 SDV-EYQKRNetqeifipvaerLGSQVFEFKNVSksfGDRLLIDnLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPD 375
Cdd:PRK11288 243 GDIyGYRPRP------------LGEVRLRLDGLK---GPGLREP-ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRT 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 376 SGEVVI-GQTVKmafVDQARDALA--------DQK--------TVWEDIS---------GGLdIINVGKFQMASRAYAGR 429
Cdd:PRK11288 307 AGQVYLdGKPID---IRSPRDAIRagimlcpeDRKaegiipvhSVADNINisarrhhlrAGC-LINNRWEAENADRFIRS 382
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 430 FNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAG---TVMVISHD 499
Cdd:PRK11288 383 LNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAqgvAVLFVSSD 455
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-216 |
5.12e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 76.76 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpMPGltigyleqepklNPEHTVRESVEESM---G 95
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVL-LNG------------GPLDFQRDSIARGLlylG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 96 AVNAAKKRL--EEVYELYAAEDAD---FDALAaeQAELEAiiatagtdsehqLEiaadalrlpawDAKIGVLSGGEKRRV 170
Cdd:cd03231 80 HAPGIKTTLsvLENLRFWHADHSDeqvEEALA--RVGLNG------------FE-----------DRPVAQLSAGQQRRV 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518484691 171 ALCRLLLSKPDMLLLDEPTNHLDAESVEWLEvflQRFP------GTVVAITH 216
Cdd:cd03231 135 ALARLLLSGRPLWILDEPTTALDKAGVARFA---EAMAghcargGMVVLTTH 183
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
324-498 |
6.32e-16 |
|
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: 80.63 E-value: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSksFG---DRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMafVDQA--RDAL 397
Cdd:COG5265 359 RFENVS--FGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIdGQDIRD--VTQAslRAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 398 A--DQKTVwedisggL--DII--NVgkfqmasrAYaGRfnfNGADQ-----------------------QKKVG----TL 444
Cdd:COG5265 435 GivPQDTV-------LfnDTIayNI--------AY-GR---PDASEeeveaaaraaqihdfieslpdgyDTRVGerglKL 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 445 SGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAG--TVMVISH 498
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARgrTTLVIAH 551
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
18-217 |
6.63e-16 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 76.84 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEalPMPG--------------------LTIGYLEQE 77
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGA--PDEGevlldgkdiydldvdvlelrRRVGMVFQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 78 PklNPEH-TVRESVeesmgavnAAKKRLEEVyelyaaedadfdalaAEQAELEAIIATAgtdsehqLEIAAdalrlpAWD 156
Cdd:cd03260 90 P--NPFPgSIYDNV--------AYGLRLHGI---------------KLKEELDERVEEA-------LRKAA------LWD 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 157 -----AKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRF--PGTVVAITHD 217
Cdd:cd03260 132 evkdrLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
324-524 |
7.23e-16 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 77.34 E-value: 7.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV------------KMAFV 390
Cdd:COG1126 3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVdGEDLtdskkdinklrrKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 391 DQaRDALADQKTVWEDISGGLdiINVGKfqmASRAYAGRfnfNGADQQKKVG----------TLSGGERGRLHLAKTLIA 460
Cdd:COG1126 83 FQ-QFNLFPHLTVLENVTLAP--IKVKK---MSKAEAEE---RAMELLERVGladkadaypaQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 461 GGNVLLLDEPSNDLDVETLRALEDALLEFA--GTVMVI-SHDRWFLDRIATHILaaegdsqwtFFDG 524
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVGEVLDVMRDLAkeGMTMVVvTHEMGFAREVADRVV---------FMDG 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-251 |
8.13e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.25 E-value: 8.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 2 AQYVYSMNRVSKTVPPKRQ-ILKDISLSFFPGAKIGVLGLNGSGKSTLLKImagvdkeiegealpmpgLTIGYLEQ--EP 78
Cdd:PRK11160 335 DQVSLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQL-----------------LTRAWDPQqgEI 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 79 KLN--PEHTVRES-VEESMGAVNaakkrlEEVYeLYAAEDADFDALAAEQA---ELEAIIATAGTdsEHQLEiaaDALRL 152
Cdd:PRK11160 398 LLNgqPIADYSEAaLRQAISVVS------QRVH-LFSATLRDNLLLAAPNAsdeALIEVLQQVGL--EKLLE---DDKGL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 153 PAWdakIG----VLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES-VEWLEVFLQRFPG-TVVAITHDRYFLDNAAE 226
Cdd:PRK11160 466 NAW---LGeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETeRQILELLAEHAQNkTVLMITHRLTGLEQFDR 542
|
250 260
....*....|....*....|....*
gi 518484691 227 WILeLDRGRGIPwKGNYSTWLEQKG 251
Cdd:PRK11160 543 ICV-MDNGQIIE-QGTHQELLAQQG 565
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-235 |
8.57e-16 |
|
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: 76.99 E-value: 8.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKE------IEGE---ALPMPGLTIGYLEQEPKLNPEHTVRESVee 92
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdsgtilFGGEdatDVPVQERNVGFVFQHYALFRHMTVFDNV-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 93 SMGAvnAAKKRleevyelyaAEDADFDALAAEQAELEAIIatagtdsehQLEIAADalRLPAWdakigvLSGGEKRRVAL 172
Cdd:cd03296 96 AFGL--RVKPR---------SERPPEAEIRAKVHELLKLV---------QLDWLAD--RYPAQ------LSGGQRQRVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 173 CRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG----TVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelhvTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-507 |
9.82e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.83 E-value: 9.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 1 MAQYVYSMNRVSKTVPPKrQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGealpmpglTIGYLEQE-PK 79
Cdd:PRK09700 1 MATPYISMAGIGKSFGPV-HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKG--------TITINNINyNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 80 LNPehtvRESVEESMGAVnaaKKRLEEVYELYAAEDADFDALAAEQAELEAIIATAGTDSEHQLEIAADALRLPAwDAKI 159
Cdd:PRK09700 72 LDH----KLAAQLGIGII---YQELSVIDELTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDL-DEKV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 160 GVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG---TVVAITHDRYFLDNAAEWILELDRGRG 236
Cdd:PRK09700 144 ANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKegtAIVYISHKLAEIRRICDRYTVMKDGSS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 237 IpwkgnystwleqkGERLAQEQKSEEAHAKALKKELEwsrqnpkarqaksksrlARFEELSDVEYQKRNETqeifipvae 316
Cdd:PRK09700 224 V-------------CSGMVSDVSNDDIVRLMVGRELQ-----------------NRFNAMKENVSNLAHET--------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 317 rlgsqVFEFKNVSKSfgDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVK--------- 386
Cdd:PRK09700 265 -----VFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLnGKDISprspldavk 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 387 --MAFVDQAR--DALADQKTVWEDIS-----------GGLDIINVGKFQMASRAYAGRFNFNGADQQKKVGTLSGGERGR 451
Cdd:PRK09700 338 kgMAYITESRrdNGFFPNFSIAQNMAisrslkdggykGAMGLFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQK 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 452 LHLAKTLIAGGNVLLLDEPSNDLDVET-------LRALEDallEFAGTVMVISHDRWFL---DRIA 507
Cdd:PRK09700 418 VLISKWLCCCPEVIIFDEPTRGIDVGAkaeiykvMRQLAD---DGKVILMVSSELPEIItvcDRIA 480
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
322-499 |
9.98e-16 |
|
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: 76.70 E-value: 9.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGD---RLLI-DNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV----------- 385
Cdd:COG4181 8 IIELRGLTKTVGTgagELTIlKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLaGQDLfaldedararl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 386 ---KMAFVDQARDALADQkTVWEdisggldiiNV-------GKFQMASRAyagrfnfngADQQKKVG----------TLS 445
Cdd:COG4181 88 rarHVGFVFQSFQLLPTL-TALE---------NVmlplelaGRRDARARA---------RALLERVGlghrldhypaQLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 446 GGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEF---AGTVMVI-SHD 499
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnreRGTTLVLvTHD 206
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
18-193 |
1.04e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.08 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALPMPGLTIGYLEQEPKLNPehTVRESVEESMGAV 97
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDT--TLPLTVNRFLRLR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 98 NAAKKrleevyelyaaedAD-FDALAAEQAeleaiiatagtdsEHQLeiaadalrlpawDAKIGVLSGGEKRRVALCRLL 176
Cdd:PRK09544 94 PGTKK-------------EDiLPALKRVQA-------------GHLI------------DAPMQKLSGGETQRVLLARAL 135
|
170
....*....|....*..
gi 518484691 177 LSKPDMLLLDEPTNHLD 193
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVD 152
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-196 |
1.05e-15 |
|
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: 78.60 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 24 DISLSFfPGAKIGVL-GLNGSGKSTLLKIMAGVDKEIEGE---------------ALPMPGLTIGYLEQEPKLNPEHTVR 87
Cdd:COG4148 17 DVDFTL-PGRGVTALfGPSGSGKTTLLRAIAGLERPDSGRirlggevlqdsargiFLPPHRRRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 88 ESVeesmgavnaakkrleevyeLYAAEDAdfdALAAEQAELEAIIATagtdsehqLEIAAdaL--RLPAWdakigvLSGG 165
Cdd:COG4148 96 GNL-------------------LYGRKRA---PRAERRISFDEVVEL--------LGIGH--LldRRPAT------LSGG 137
|
170 180 190
....*....|....*....|....*....|.
gi 518484691 166 EKRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
Cdd:COG4148 138 ERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-216 |
1.11e-15 |
|
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: 76.47 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 7 SMNRVSKTVPPKRQ---ILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE---------ALPMPGLT---- 70
Cdd:cd03258 3 ELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSvlvdgtdltLLSGKELRkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 71 -IGYLEQEPKLNPEHTVRESVEESMGAVNAAKKRLEE-VYELYaaedaDFDALAAEQaeleaiiatagtdsehqleiaad 148
Cdd:cd03258 83 rIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEErVLELL-----ELVGLEDKA----------------------- 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 149 alrlpawDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES----VEWLEVFLQRFPGTVVAITH 216
Cdd:cd03258 135 -------DAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsiLALLRDINRELGLTIVLITH 199
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
333-498 |
1.13e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.61 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 333 GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKmafvdQARDALADQ----------K 401
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIR-----RQRDEYHQDllylghqpgiK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 402 ---TVWEDIsggldiinvgKFQMASRAYAGRFNFNGADQQkkVG----------TLSGGERGRLHLAKTLIAGGNVLLLD 468
Cdd:PRK13538 87 telTALENL----------RFYQRLHGPGDDEALWEALAQ--VGlagfedvpvrQLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190
....*....|....*....|....*....|...
gi 518484691 469 EPSNDLD---VETLRALEDALLEFAGTVMVISH 498
Cdd:PRK13538 155 EPFTAIDkqgVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
330-511 |
1.15e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.93 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 330 KSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDALADQK------- 401
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVnGQTINLVRDKDGQLKVADKNqlrllrt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 402 ---------------TVWEDI-SGGLDIINVGKFQMASRA--YAGRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGN 463
Cdd:PRK10619 93 rltmvfqhfnlwshmTVLENVmEAPIQVLGLSKQEARERAvkYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518484691 464 VLLLDEPSNDLDV----ETLRALEDaLLEFAGTVMVISHDRWFLDRIATHIL 511
Cdd:PRK10619 173 VLLFDEPTSALDPelvgEVLRIMQQ-LAEEGKTMVVVTHEMGFARHVSSHVI 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
323-499 |
1.57e-15 |
|
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: 76.03 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 323 FEFKNVSKSF----------------------GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVV 380
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 381 IGQTVKMAFvdqardaladqktvweDISGGLD--------IINVGKFQMASRAYAGRF-----NFN--GADQQKKVGTLS 445
Cdd:cd03220 81 VRGRVSSLL----------------GLGGGFNpeltgrenIYLNGRLLGLSRKEIDEKideiiEFSelGDFIDLPVKTYS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 446 GGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEF---AGTVMVISHD 499
Cdd:cd03220 145 SGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELlkqGKTVILVSHD 201
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-189 |
1.78e-15 |
|
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: 75.79 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEAL-PMP-----GLTIGYLEQEPKLNPEHTVR 87
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPprsgsiRFDGEDItGLPphriaRLGIGYVPEGRRIFPSLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 88 ESVEesMGA-----VNAAKKRLEEVYELyaaedadFDALAaeqaELeaiiatagtdsehqleiaadaLRLPAwdakiGVL 162
Cdd:COG0410 97 ENLL--LGAyarrdRAEVRADLERVYEL-------FPRLK----ER---------------------RRQRA-----GTL 137
|
170 180
....*....|....*....|....*..
gi 518484691 163 SGGEKRRVALCRLLLSKPDMLLLDEPT 189
Cdd:COG0410 138 SGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
20-235 |
1.85e-15 |
|
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: 76.23 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGE---ALPMPGLT---IGYLEQEPKLNPEHTVR 87
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRptsgriLFDGRditGLPPHRIArlgIARTFQNPRLFPELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 88 ESVEesMGAVNAAKKRLEEVYE---LYAAEDADFDALAAEQAEleaiiatagtdsehQLEIAADAlrlpawDAKIGVLSG 164
Cdd:COG0411 98 ENVL--VAAHARLGRGLLAALLrlpRARREEREARERAEELLE--------------RVGLADRA------DEPAGNLSY 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 165 GEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG----TVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDergiTILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
324-499 |
2.67e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 76.05 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFG----DRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQA----R 394
Cdd:COG4525 5 TVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdGVPVTGPGADRGvvfqK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 395 DALADQKTVWEDISGGLDIINVGKFQMASRA--YAGRFNFNGAdQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSN 472
Cdd:COG4525 85 DALLPWLNVLDNVAFGLRLRGVPKAERRARAeeLLALVGLADF-ARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFG 163
|
170 180 190
....*....|....*....|....*....|.
gi 518484691 473 DLDVETLRALEDALLEFAG----TVMVISHD 499
Cdd:COG4525 164 ALDALTREQMQELLLDVWQrtgkGVFLITHS 194
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
324-514 |
2.74e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 75.43 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG-------------------QT 384
Cdd:COG4161 4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAghqfdfsqkpsekairllrQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 385 VKMAFvdQARDaLADQKTVWED-ISGGLDIINVGKFQMASRA-----------YAGRFNFNgadqqkkvgtLSGGERGRL 452
Cdd:COG4161 84 VGMVF--QQYN-LWPHLTVMENlIEAPCKVLGLSKEQAREKAmkllarlrltdKADRFPLH----------LSGGQQQRV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 453 HLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAG---TVMVISHDRWFLDRIATHILAAE 514
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIVTHEVEFARKVASQVVYME 215
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-258 |
3.09e-15 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 75.27 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 17 PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE---------ALPMPGL--TIGYLEQEPKLNpEHT 85
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEilldgvdirDLNLRWLrsQIGLVSQEPVLF-DGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 86 VRESVeeSMGAVNAAkkrLEEVYElyaaedadfdalAAEQAELEAIIATagtdsehqleiaadalrLP-AWDAKIG---- 160
Cdd:cd03249 93 IAENI--RYGKPDAT---DEEVEE------------AAKKANIHDFIMS-----------------LPdGYDTLVGergs 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 161 VLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG--TVVAITHdRYFLDNAAEWILELDRGRgIP 238
Cdd:cd03249 139 QLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKgrTTIVIAH-RLSTIRNADLIAVLQNGQ-VV 216
|
250 260
....*....|....*....|..
gi 518484691 239 WKGNYSTWLEQKGE--RLAQEQ 258
Cdd:cd03249 217 EQGTHDELMAQKGVyaKLVKAQ 238
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
289-521 |
3.34e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.31 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 289 RLARFEELSDveyqkRNETQEIFIPVAERLGSQVFEFKNVSKSFGD-RLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKL 367
Cdd:COG4178 334 RLAGFEEALE-----AADALPEAASRIETSEDGALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 368 LAGKEKPDSGEVVIGQTVKMAFVDQA--------RDALA--DQKTVWED--ISGGLDIINVGKFqmasrayAGRFNfNGA 435
Cdd:COG4178 409 IAGLWPYGSGRIARPAGARVLFLPQRpylplgtlREALLypATAEAFSDaeLREALEAVGLGHL-------AERLD-EEA 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 436 DQQKkvgTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLE--FAGTVMVISHdRWFLDRIATHILAA 513
Cdd:COG4178 481 DWDQ---VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLEL 556
|
....*...
gi 518484691 514 EGDSQWTF 521
Cdd:COG4178 557 TGDGSWQL 564
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-251 |
3.37e-15 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 75.95 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 4 YVYSMNrvsktVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEalpmpgLTIG--YLEQEPKLN 81
Cdd:TIGR04521 8 YIYQPG-----TPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGT------VTIDgrDITAKKKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 82 --------------PEH-----TVRESVeeSMGAVNaakkrleevyelyaaedadfdaLAAEQAELEaiiatagtdsehq 142
Cdd:TIGR04521 77 lkdlrkkvglvfqfPEHqlfeeTVYKDI--AFGPKN----------------------LGLSEEEAE------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 143 lEIAADALRLPAWDAKIGV-----LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES-VEWLEVF--LQRFPG-TVVA 213
Cdd:TIGR04521 120 -ERVKEALELVGLDEEYLErspfeLSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGrKEILDLFkrLHKEKGlTVIL 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 518484691 214 ITHDryfLDNAAEW---ILELDRGR----GIPWK-GNYSTWLEQKG 251
Cdd:TIGR04521 199 VTHS---MEDVAEYadrVIVMHKGKivldGTPREvFSDVDELEKIG 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
324-498 |
3.51e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 76.76 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSF--GDRLLI--DNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDA-- 396
Cdd:PRK11153 3 ELKNISKVFpqGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVdGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 397 ----------LADQKTVWEDISGGLDIINVGKFQMASR-----------AYAGRFNFNgadqqkkvgtLSGGERGRLHLA 455
Cdd:PRK11153 83 qigmifqhfnLLSSRTVFDNVALPLELAGTPKAEIKARvtellelvglsDKADRYPAQ----------LSGGQKQRVAIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518484691 456 KTLIAGGNVLLLDEPSNDLDVETLRALEDaLL-----EFAGTVMVISH 498
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILE-LLkdinrELGLTIVLITH 199
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-217 |
3.82e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 74.44 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV---DKEIEGE---------ALPMPGLTIGYLEQEPKLNPEHTV 86
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlspAFSASGEvllngrrltALPAEQRRIGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 87 RESVEESM-GAVNAAKKRLeevyelyaaedadfdalAAEQAeLEaiiatagtdsehQLEIAADALRLPAwdakigVLSGG 165
Cdd:COG4136 94 GENLAFALpPTIGRAQRRA-----------------RVEQA-LE------------EAGLAGFADRDPA------TLSGG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 166 EKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLE--VF--LQRFPGTVVAITHD 217
Cdd:COG4136 138 QRARVALLRALLAEPRALLLDEPFSKLDAALRAQFRefVFeqIRQRGIPALLVTHD 193
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
322-482 |
4.79e-15 |
|
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: 74.61 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSF----GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPD---SGEVVI-GQTVK------- 386
Cdd:cd03234 3 VLPWWDVGLKAknwnKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFnGQPRKpdqfqkc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 387 MAFVDQArDALADQKTVWEDISggLDIINVGKFQMASRAYAGRFNFNG----ADQQ---KKVGTLSGGERGRLHLAKTLI 459
Cdd:cd03234 83 VAYVRQD-DILLPGLTVRETLT--YTAILRLPRKSSDAIRKKRVEDVLlrdlALTRiggNLVKGISGGERRRVSIAVQLL 159
|
170 180 190
....*....|....*....|....*....|
gi 518484691 460 AGGNVLLLDEPSNDLD-------VETLRAL 482
Cdd:cd03234 160 WDPKVLILDEPTSGLDsftalnlVSTLSQL 189
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
321-514 |
5.50e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.03 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 321 QVFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG------------------ 382
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRgqhieglpghqiarmgvv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 383 ---QTVKM------------------------------AFVDQARDALaDQKTVWEDisggldiiNVGKFQMASRAyagr 429
Cdd:PRK11300 84 rtfQHVRLfremtvienllvaqhqqlktglfsgllktpAFRRAESEAL-DRAATWLE--------RVGLLEHANRQ---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 430 fnfngadqqkkVGTLSGGERGRLHLAKTLIAGGNVLLLDEPS---NDLDVETLRALEDALL-EFAGTVMVISHDRWFLDR 505
Cdd:PRK11300 151 -----------AGNLAYGQQRRLEIARCMVTQPEILMLDEPAaglNPKETKELDELIAELRnEHNVTVLLIEHDMKLVMG 219
|
....*....
gi 518484691 506 IATHILAAE 514
Cdd:PRK11300 220 ISDRIYVVN 228
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
229-304 |
6.30e-15 |
|
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: 69.91 E-value: 6.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 229 LELDRGRGIPWKGNYSTWLEQKGERLAQEQKSEEAHAKALKKELEWSRQNP----KARQAKSK-SRLARFEELSDVEYQK 303
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRakasKAKQAQSRiKALEKMERIEKPERDK 80
|
.
gi 518484691 304 R 304
Cdd:pfam12848 81 P 81
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
326-475 |
6.69e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.54 E-value: 6.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQ--TVKMAFVDQARDALA----- 398
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedISLLPLHARARRGIGylpqe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 399 ----DQKTVWEDISGGLDI-INVGKFQMASRAYAGRFNFNGADQQKKVG-TLSGGERGRLHLAKTLIAGGNVLLLDEPSN 472
Cdd:PRK10895 87 asifRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGqSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
...
gi 518484691 473 DLD 475
Cdd:PRK10895 167 GVD 169
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
7-235 |
6.93e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 74.35 E-value: 6.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 7 SMNRVSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEALPMPGLTIGyleqepkL 80
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEptsgrvEVNGRVSALLELGAG-------F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 81 NPEHTVRESVEesmgaVNAA---------KKRLEEVyelyaaedADFdalaaeqAELEAIIatagtdsehqleiaadalr 151
Cdd:COG1134 100 HPELTGRENIY-----LNGRllglsrkeiDEKFDEI--------VEF-------AELGDFI------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 152 lpawDAKIGVLSGGEKRR----VALCRlllsKPDMLLLDEPTNHLDAE----SVEWLEVFLQRfPGTVVAITHDRYFL-- 221
Cdd:COG1134 141 ----DQPVKTYSSGMRARlafaVATAV----DPDILLVDEVLAVGDAAfqkkCLARIRELRES-GRTVIFVSHSMGAVrr 211
|
250
....*....|....*.
gi 518484691 222 --DNAAeWileLDRGR 235
Cdd:COG1134 212 lcDRAI-W---LEKGR 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-216 |
7.21e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.30 E-value: 7.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEalpmpgltIGYLEQepklnPEHTVRESVEESM---G 95
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGE--------VLWQGE-----PIRRQRDEYHQDLlylG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 96 AVNAAKKRL--EEVYELYAA------EDADFDALAAeqaeleaiIATAGTdsEHqleiaadalrLPAwdakiGVLSGGEK 167
Cdd:PRK13538 81 HQPGIKTELtaLENLRFYQRlhgpgdDEALWEALAQ--------VGLAGF--ED----------VPV-----RQLSAGQQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518484691 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFP---GTVVAITH 216
Cdd:PRK13538 136 RRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAeqgGMVILTTH 187
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
328-498 |
7.46e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.84 E-value: 7.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 328 VSKSFGDRL------LIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAG--KEKPDSGEVVIgqtVKMAFVDQArdALAD 399
Cdd:COG2401 30 VLEAFGVELrvveryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDV---PDNQFGREA--SLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 400 QKTVWEDISGGLDIIN-VGkfqmASRAYAGRfnfngadqqKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVET 478
Cdd:COG2401 105 AIGRKGDFKDAVELLNaVG----LSDAVLWL---------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180
....*....|....*....|....
gi 518484691 479 LRALEDALLEFA----GTVMVISH 498
Cdd:COG2401 172 AKRVARNLQKLArragITLVVATH 195
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
324-516 |
7.67e-15 |
|
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: 73.33 E-value: 7.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKE--KPDSGEVVI-GQTVK-MAFVDQARDA--L 397
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFkGEDITdLPPEERARLGifL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 398 ADQKTVweDISGgldiINVGKFQmasrayagRFNFNGadqqkkvgtLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVE 477
Cdd:cd03217 82 AFQYPP--EIPG----VKNADFL--------RYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518484691 478 TLRALEDA---LLEFAGTVMVISHDRWFLDRIAT---HIL-----AAEGD 516
Cdd:cd03217 139 ALRLVAEVinkLREEGKSVLIITHYQRLLDYIKPdrvHVLydgriVKSGD 188
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-235 |
7.97e-15 |
|
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: 72.63 E-value: 7.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE-----------ALPMPGLTIGYLEQEPKLnpehtv 86
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRvrldgadisqwDPNELGDHVGYLPQDDEL------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 87 resveesmgavnaakkrleevyelyaaedadFDalaaeqaeleaiiataGTDSEHqleiaadalrlpawdakigVLSGGE 166
Cdd:cd03246 88 -------------------------------FS----------------GSIAEN-------------------ILSGGQ 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 167 KRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFP---GTVVAITHdRYFLDNAAEWILELDRGR 235
Cdd:cd03246 102 RQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaagATRIVIAH-RPETLASADRILVLEDGR 172
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
334-499 |
8.81e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 74.67 E-value: 8.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 334 DRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG------QTV-----KMAFVDQARDALADQKT 402
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlseETVwdvrrQVGMVFQNPDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 403 VWEDISGGLDIINVGKFQMASRAYA-----GRFNFngADQQKKvgTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD-- 475
Cdd:PRK13635 99 VQDDVAFGLENIGVPREEMVERVDQalrqvGMEDF--LNREPH--RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDpr 174
|
170 180
....*....|....*....|....*....
gi 518484691 476 -----VETLRALEDallEFAGTVMVISHD 499
Cdd:PRK13635 175 grrevLETVRQLKE---QKGITVLSITHD 200
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
319-499 |
9.18e-15 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 72.46 E-value: 9.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 319 GSQVFEFKNVSksFGDRLliDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVK----------- 386
Cdd:cd03215 1 GEPVLEVRGLS--VKGAV--RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdGKPVTrrsprdairag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 387 MAFV--DQARDALADQKTVWEDISggldiinvgkfqmasrayAGRFnfngadqqkkvgtLSGGERGRLHLAKTLIAGGNV 464
Cdd:cd03215 77 IAYVpeDRKREGLVLDLSVAENIA------------------LSSL-------------LSGGNQQKVVLARWLARDPRV 125
|
170 180 190
....*....|....*....|....*....|....*...
gi 518484691 465 LLLDEPSNDLDVETLRALEDALLEFA---GTVMVISHD 499
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELAdagKAVLLISSE 163
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
338-499 |
9.70e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.51 E-value: 9.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 338 IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTV----KMAFVDQ----------------ARDAL 397
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfkrRKEFARRigvvfgqrsqlwwdlpAIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 398 ADQKTVWEdISGGL---------DIINVGKFqmasrayagrfnfngADQQkkVGTLSGGERGRLHLAKTLIAGGNVLLLD 468
Cdd:COG4586 118 RLLKAIYR-IPDAEykkrldelvELLDLGEL---------------LDTP--VRQLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190
....*....|....*....|....*....|....*
gi 518484691 469 EPSNDLDVETLRALEDALLE----FAGTVMVISHD 499
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEynreRGTTILLTSHD 214
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
343-510 |
1.00e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 77.13 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 343 FNVPA---GAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEV------------------------VIGQTVKMA----FVD 391
Cdd:COG1245 91 YGLPVpkkGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkrfrgtelqdyfkkLANGEIKVAhkpqYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 392 QA--------RDAL--ADQKTVWEDISGGLDIINVGKfqmasrayagrfnfngadqqKKVGTLSGGERGRLHLAKTLIAG 461
Cdd:COG1245 171 LIpkvfkgtvRELLekVDERGKLDELAEKLGLENILD--------------------RDISELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518484691 462 GNVLLLDEPSNDLDV-ETLRALEdALLEFAG---TVMVISHDRWFLDRIATHI 510
Cdd:COG1245 231 ADFYFFDEPSSYLDIyQRLNVAR-LIRELAEegkYVLVVEHDLAILDYLADYV 282
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
322-533 |
1.10e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.28 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFK----LLAGKEKPDSGEVVIGQTVKMAFvDQARDA- 396
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRTVQREG-RLARDIr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 397 --------------LADQKTVWEDISGG-----------LDIINVGKFQMASRAYA--GRFNFngadQQKKVGTLSGGER 449
Cdd:PRK09984 83 ksrantgyifqqfnLVNRLSVLENVLIGalgstpfwrtcFSWFTREQKQRALQALTrvGMVHF----AHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 450 GRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAG----TVMVISHDRWFLDRIATHILAAEGDSqwTFFDGN 525
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYALRYCERIVALRQGH--VFYDGS 236
|
....*...
gi 518484691 526 YQEYEADK 533
Cdd:PRK09984 237 SQQFDNER 244
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
327-511 |
1.14e-14 |
|
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: 75.52 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 327 NVSKSFGDRLLidNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVkmafvdqardaladqktvWED 406
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV------------------LQD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 407 ISGGLDII----NVGK-FQMAS-------RA---YAGRFNFNGADQ----------------QKKVGTLSGGERGRLHLA 455
Cdd:COG4148 66 SARGIFLPphrrRIGYvFQEARlfphlsvRGnllYGRKRAPRAERRisfdevvellgighllDRRPATLSGGERQRVAIG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 456 KTLIAGGNVLLLDEPSNDLDVET-------LRALEDallEFAGTVMVISHDRWFLDRIATHIL 511
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALDLARkaeilpyLERLRD---ELDIPILYVSHSLDEVARLADHVV 205
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-217 |
1.21e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.05 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 6 YSMNRVSKTVPpKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLT-------IGYL 74
Cdd:PRK10575 12 FALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILldaqPLESWSskafarkVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 75 EQEPKLNPEHTVRESVEESMGAVNAAKKRleevyelYAAEDadfdalaAEQAElEAIIATAGTDSEHQLeiaadalrlpa 154
Cdd:PRK10575 91 PQQLPAAEGMTVRELVAIGRYPWHGALGR-------FGAAD-------REKVE-EAISLVGLKPLAHRL----------- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 155 wdakIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD-AESVEWLEVF--LQRFPG-TVVAITHD 217
Cdd:PRK10575 145 ----VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQVDVLALVhrLSQERGlTVIAVLHD 207
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-216 |
1.42e-14 |
|
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: 71.31 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 7 SMNRVSKTVPPKRqILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEalpmpgLTIGyleqepklnpehtv 86
Cdd:cd03216 2 ELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE------ILVD-------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 87 resveesmgavnaakkrlEEVYELYAAEDAdfdalaaeqaeLEAIIATAgtdseHQLeiaadalrlpawdakigvlSGGE 166
Cdd:cd03216 61 ------------------GKEVSFASPRDA-----------RRAGIAMV-----YQL-------------------SVGE 87
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518484691 167 KRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG---TVVAITH 216
Cdd:cd03216 88 RQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
5-206 |
1.46e-14 |
|
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: 72.28 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 5 VYSMNRVSKTVPPK---RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG--VDKEIEGEALpMPGL--------TI 71
Cdd:cd03232 3 VLTWKNLNYTVPVKggkRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEIL-INGRpldknfqrST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 72 GYLEQEPKLNPEHTVRESVEESmgavnaakkrleevyelyaaedadfdalaaeqaeleaiiatagtdsehqleiaadalr 151
Cdd:cd03232 82 GYVEQQDVHSPNLTVREALRFS---------------------------------------------------------- 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 152 lpawdAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQR 206
Cdd:cd03232 104 -----ALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKK 153
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
340-497 |
1.49e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.15 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 340 NLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEV-VIGQTVK-------MAFVDQARDALADQKTVWEDI---- 407
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsILGQPTRqalqknlVAYVPQSEEVDWSFPVLVEDVvmmg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 408 ----SGGLDIINVGKFQMASRAYA--GRFNFngadQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVET--- 478
Cdd:PRK15056 105 ryghMGWLRRAKKRDRQIVTAALArvDMVEF----RHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTear 180
|
170 180
....*....|....*....|...
gi 518484691 479 ----LRALEDallefAGTVMVIS 497
Cdd:PRK15056 181 iislLRELRD-----EGKTMLVS 198
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
20-218 |
1.68e-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: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEalPMPGLT-----IGYLEQEPKLNPEHTVRE 88
Cdd:COG3842 19 TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETpdsgriLLDGR--DVTGLPpekrnVGMVFQDYALFPHLTVAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 89 SVEE--SMGAVNAA--KKRLEEVYELyaaedadfdalaaeqaeleaiiatagtdsehqLEIAADALRLPAwdakigVLSG 164
Cdd:COG3842 97 NVAFglRMRGVPKAeiRARVAELLEL--------------------------------VGLEGLADRYPH------QLSG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 165 GEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFL----QRFPGTVVAITHDR 218
Cdd:COG3842 139 GQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELrrlqRELGITFIYVTHDQ 196
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
326-512 |
2.02e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.48 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG--QTVKMAFVDQAR--DALADQK 401
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDgeHIQHYASKEVARriGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 402 TVWEDISGGlDIINVGKF---QMASR-------AYAGRFNFNG----ADQQkkVGTLSGGERGRLHLAKTLIAGGNVLLL 467
Cdd:PRK10253 91 TTPGDITVQ-ELVARGRYphqPLFTRwrkedeeAVTKAMQATGithlADQS--VDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518484691 468 DEPSNDLD----VETLRALEDALLEFAGTVMVISHDRWFLDRIATHILA 512
Cdd:PRK10253 168 DEPTTWLDishqIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIA 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
324-498 |
2.06e-14 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 72.96 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDR---LLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARD--AL 397
Cdd:cd03249 2 EFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIRDLNLRWLRSqiGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 398 ADQK------TVWEDISGGLDIINVGKFQMASRAyAGRFNF-----NGADQQkkVG----TLSGGERGRLHLAKTLIAGG 462
Cdd:cd03249 82 VSQEpvlfdgTIAENIRYGKPDATDEEVEEAAKK-ANIHDFimslpDGYDTL--VGergsQLSGGQKQRIAIARALLRNP 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 518484691 463 NVLLLDEPSNDLDVETLRALEDALLEFAG--TVMVISH 498
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKgrTTIVIAH 196
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-217 |
2.62e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 72.97 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 7 SMNRVSKTVPPKRQ---ILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV------DKEIEGEALPMPGLTIGYLEQE 77
Cdd:COG4525 5 TVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFlapssgEITLDGVPVTGPGADRGVVFQK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 78 PKLNPEHTVRESVEESMgavnaakkRLEEVyelyaaedadfdALAAEQAELEAIIATAGtdsehqLEIAADAlrlPAWDa 157
Cdd:COG4525 85 DALLPWLNVLDNVAFGL--------RLRGV------------PKAERRARAEELLALVG------LADFARR---RIWQ- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518484691 158 kigvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFL----QRFPGTVVAITHD 217
Cdd:COG4525 135 ----LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLldvwQRTGKGVFLITHS 194
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-235 |
2.79e-14 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 73.23 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALPMpGL-------------TIGYLEQepklNPEH 84
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD-GLdtldeenlweirkKVGMVFQ----NPDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 85 -----TVRESVE---ESMGaVNAA--KKRLEEvyelyaaedadfdalAAEQAELEAIIatagtDSEHQLeiaadalrlpa 154
Cdd:TIGR04520 89 qfvgaTVEDDVAfglENLG-VPREemRKRVDE---------------ALKLVGMEDFR-----DREPHL----------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 155 wdakigvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEwlEVF-----LQRFPG-TVVAITHDryfLDNA--AE 226
Cdd:TIGR04520 137 -------LSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRK--EVLetirkLNKEEGiTVISITHD---MEEAvlAD 204
|
....*....
gi 518484691 227 WILELDRGR 235
Cdd:TIGR04520 205 RVIVMNKGK 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-499 |
3.12e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.13 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKS-TLLKIM----------AGVDKEIEGEAL---------PMPGLTIGYLEQEP 78
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpsppvvyPSGDIRFHGESLlhaseqtlrGVRGNKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 79 --KLNPEHTVresveesmgavnaaKKRLEEVYELYAAedadfdaLAAEQAELEAIiatagtDSEHQLEIAADALRLPAWD 156
Cdd:PRK15134 102 mvSLNPLHTL--------------EKQLYEVLSLHRG-------MRREAARGEIL------NCLDRVGIRQAAKRLTDYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 157 AKigvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFPGTVVAITHD----RYFLDNAAewi 228
Cdd:PRK15134 155 HQ---LSGGERQRVMIAMALLTRPELLIADEPTTALDvsvqAQILQLLRELQQELNMGLLFITHNlsivRKLADRVA--- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 229 lELDRGRGIpwkgnystwlEQkgeRLAQEQKSEEAHA---KALKKELEwSRQNPKARQAkskSRLARFEELSdveyqkrn 305
Cdd:PRK15134 229 -VMQNGRCV----------EQ---NRAATLFSAPTHPytqKLLNSEPS-GDPVPLPEPA---SPLLDVEQLQ-------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 306 etqeIFIPVAERLGSQVFEFKNVSKsfgdrllidNLSFNVPAGAIVGIIGPNGAGKST----LFKLLAGKekpdsGEVVI 381
Cdd:PRK15134 283 ----VAFPIRKGILKRTVDHNVVVK---------NISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWF 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 382 -GQTV-------------KMAFVDQ-ARDALADQKTVWEDISGGLDI----INVGKFQMASRAYAGRFNFNGADQQKKVG 442
Cdd:PRK15134 345 dGQPLhnlnrrqllpvrhRIQVVFQdPNSSLNPRLNVLQIIEEGLRVhqptLSAAQREQQVIAVMEEVGLDPETRHRYPA 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 443 TLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDvETLRALEDALL-----EFAGTVMVISHD 499
Cdd:PRK15134 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLD-KTVQAQILALLkslqqKHQLAYLFISHD 485
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
326-514 |
3.72e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 72.35 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG-------------------QTVK 386
Cdd:PRK11124 6 NGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAgnhfdfsktpsdkairelrRNVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 387 MAFvdQARDaLADQKTVWED-ISGGLDIINVGKFQMASRA-----------YAGRFNFNgadqqkkvgtLSGGERGRLHL 454
Cdd:PRK11124 86 MVF--QQYN-LWPHLTVQQNlIEAPCRVLGLSKDQALARAekllerlrlkpYADRFPLH----------LSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 455 AKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAGT---VMVISHDRWFLDRIATHILAAE 514
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgitQVIVTHEVEVARKTASRVVYME 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
20-235 |
4.36e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.05 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDkEIEGEALPMPGLTIgyleqepkLNPEHTVRESVEESmGAVna 99
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLE-EITSGDLIVDGLKV--------NDPKVDERLIRQEA-GMV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 100 akkrLEEVY---ELYAAEDADFDAlaaeqaeleaiIATAGTDSEHQLEIAADALrlpawdAKIGV----------LSGGE 166
Cdd:PRK09493 83 ----FQQFYlfpHLTALENVMFGP-----------LRVRGASKEEAEKQARELL------AKVGLaerahhypseLSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 167 KRRVALCRLLLSKPDMLLLDEPTNHLDAE-SVEWLEVF--LQRFPGTVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDPElRHEVLKVMqdLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-216 |
4.95e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 73.33 E-value: 4.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 11 VSKTVPPKrQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE----ALPMPG------LTIGYLEQEPKL 80
Cdd:PRK13536 47 VSKSYGDK-AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKitvlGVPVPArarlarARIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 81 NPEHTVRESVEesmgavnaakkrleeVYELYAAEDAdfdalaaeqAELEAIIATAgtdsehqLEIAadalRLPA-WDAKI 159
Cdd:PRK13536 126 DLEFTVRENLL---------------VFGRYFGMST---------REIEAVIPSL-------LEFA----RLESkADARV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518484691 160 GVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD--AESVEW--LEVFLQRfPGTVVAITH 216
Cdd:PRK13536 171 SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDphARHLIWerLRSLLAR-GKTILLTTH 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
295-498 |
5.61e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 74.67 E-value: 5.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 295 ELSDVEYQKRNETQEIfipvaERLGSQVfEFKNVSKSF--GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKE 372
Cdd:PRK11176 320 AILDLEQEKDEGKRVI-----ERAKGDI-EFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 373 KPDSGEVVI-GQTVKMAFVDQARD--ALADQK------TVWEDISGGL-------DIINVGKFqmasrAYAGRF------ 430
Cdd:PRK11176 394 DIDEGEILLdGHDLRDYTLASLRNqvALVSQNvhlfndTIANNIAYARteqysreQIEEAARM-----AYAMDFinkmdn 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 431 ------NFNGAdqqkkvgTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAG--TVMVISH 498
Cdd:PRK11176 469 gldtviGENGV-------LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH 537
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
324-498 |
6.33e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.48 E-value: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDR--LLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQArdaLADQK 401
Cdd:PRK11160 340 TLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA---LRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 402 TVwedISGGLDIINV---GKFQMAsrayagrfNFNGADQQ-----KKVG--------------------TLSGGERGRLH 453
Cdd:PRK11160 417 SV---VSQRVHLFSAtlrDNLLLA--------APNASDEAlievlQQVGleklleddkglnawlgeggrQLSGGEQRRLG 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518484691 454 LAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAG--TVMVISH 498
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQnkTVLMITH 532
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-235 |
6.36e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 71.32 E-value: 6.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 25 ISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLTIG-----YLEQEPKLNPEHTVRESVeesmg 95
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILwngqDLTALPPAerpvsMLFQENNLFPHLTVAQNI----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 96 avnaakkrleevyelyaaedadfdAL---------AAEQAELEAIIAtagtdsehQLEIAADALRLPawdakiGVLSGGE 166
Cdd:COG3840 93 ------------------------GLglrpglkltAEQRAQVEQALE--------RVGLAGLLDRLP------GQLSGGQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 167 KRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFPGTVVAITHDryfLDNA---AEWILELDRGR 235
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD---PEDAariADRVLLVADGR 207
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-237 |
7.19e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.53 E-value: 7.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 21 ILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPG------LTIGYLEQEPKLNPEHTVRESV 90
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgePVPSrarharQRVGVVPQFDNLDPDFTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 91 EesmgavnaakkrleeVYELYaaedadFDALAAEQAELEAIIatagtdsehqLEIAadalRLPA-WDAKIGVLSGGEKRR 169
Cdd:PRK13537 102 L---------------VFGRY------FGLSAAAARALVPPL----------LEFA----KLENkADAKVGELSGGMKRR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 170 VALCRLLLSKPDMLLLDEPTNHLD--AESVEW--LEVFLQRfPGTVVAITHdryFLDNAAEWILEL---DRGRGI 237
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDpqARHLMWerLRSLLAR-GKTILLTTH---FMEEAERLCDRLcviEEGRKI 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-217 |
7.55e-14 |
|
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: 71.11 E-value: 7.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpmpgltigyLEQEPKLNpehtvresveesmgaVNA 99
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIL---------LDGKDITN---------------LPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 100 AKKRLEEVYELYAAedadFDALAAEQAeleaiIA----TAGTDSEHQLEIAADALRLPAWDA----KIGVLSGGEKRRVA 171
Cdd:cd03300 70 HKRPVNTVFQNYAL----FPHLTVFEN-----IAfglrLKKLPKAEIKERVAEALDLVQLEGyanrKPSQLSGGQQQRVA 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518484691 172 LCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFL---QRFPG-TVVAITHD 217
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQLELkrlQKELGiTFVFVTHD 190
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
327-505 |
8.77e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.36 E-value: 8.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 327 NVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVK---------MAFVDQaRDA 396
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKkdlctyqkqLCFVGH-RSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 397 LADQKTVWEDI-------SGGLDIINVGK-FQMasrayagrfnfnGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLD 468
Cdd:PRK13540 85 INPYLTLRENClydihfsPGAVGITELCRlFSL------------EHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518484691 469 EPSNDLD---VETLRALEDALLEFAGTVMVISHDRWFLDR 505
Cdd:PRK13540 153 EPLVALDelsLLTIITKIQEHRAKGGAVLLTSHQDLPLNK 192
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
340-518 |
9.18e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.00 E-value: 9.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 340 NLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV--------------KMAFVDQARDALADqKTVW 404
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFnGQPMsklssaakaelrnqKLGFIYQFHHLLPD-FTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 405 EDISGGLDIINVGKFQMASRAYAgRFNFNGADQ--QKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRAL 482
Cdd:PRK11629 106 ENVAMPLLIGKKKPAEINSRALE-MLAAVGLEHraNHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518484691 483 EDALLEF---AGTV-MVISHDRWFLDRIATHILAAEGDSQ 518
Cdd:PRK11629 185 FQLLGELnrlQGTAfLVVTHDLQLAKRMSRQLEMRDGRLT 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
24-235 |
9.91e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.95 E-value: 9.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 24 DISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL---------PMPGLTIGYLEQEPKLNPEHTVRESVeesm 94
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMldgvdlshvPPYQRPINMMFQSYALFPHMTVEQNI---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 95 gAVNAAKKRLEEvyelyaaedadfDALAAEQAELEAIIatagtdseHQLEIAAdalRLPAWdakigvLSGGEKRRVALCR 174
Cdd:PRK11607 113 -AFGLKQDKLPK------------AEIASRVNEMLGLV--------HMQEFAK---RKPHQ------LSGGQRQRVALAR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 175 LLLSKPDMLLLDEPTNHLDAESVE--WLEV--FLQRFPGTVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKLRDrmQLEVvdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
324-475 |
1.00e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 71.27 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFG-----DRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV-KMAFVDQARD- 395
Cdd:COG1101 3 ELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIdGKDVtKLPEYKRAKYi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 396 ---------------------ALADQKTVWEDISGGLDIINVGKFqmasRAYAGRFNFNGADQQK-KVGTLSGGERGRLH 453
Cdd:COG1101 83 grvfqdpmmgtapsmtieenlALAYRRGKRRGLRRGLTKKRRELF----RELLATLGLGLENRLDtKVGLLSGGQRQALS 158
|
170 180
....*....|....*....|..
gi 518484691 454 LAKTLIAGGNVLLLDEPSNDLD 475
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALD 180
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
322-510 |
1.02e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 71.76 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSF-GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDALA- 398
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIREVRKFVGl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 399 ------DQ---KTVWEDISGGLDIINVGKFQMASRAYAGRFNFNGADQQKKV-GTLSGGERGRLHLAKTLIAGGNVLLLD 468
Cdd:PRK13652 83 vfqnpdDQifsPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVpHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518484691 469 EPSNDLD----VETLRALEDALLEFAGTVMVISHDRWFLDRIATHI 510
Cdd:PRK13652 163 EPTAGLDpqgvKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYI 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-235 |
1.19e-13 |
|
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: 70.54 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKImagvdkeIEGEALPMPGlTIGYLEQEPKLN----PEHTVRESVEESMGAV 97
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKC-------IYGNYLPDSG-SILVRHDGGWVDlaqaSPREILALRRRTIGYV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 98 NAAKKRLEEVyelyAAEDadfdaLAAEqaeleAIIAtAGTDSEHQLEIAADALR---LPA--WDAKIGVLSGGEKRRVAL 172
Cdd:COG4778 99 SQFLRVIPRV----SALD-----VVAE-----PLLE-RGVDREEARARARELLArlnLPErlWDLPPATFSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 173 CRLLLSKPDMLLLDEPTNHLDAES----VEWLEVFLQRfpGT-VVAITHDRYFLDNAAEWILELDRGR 235
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANravvVELIEEAKAR--GTaIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-217 |
1.26e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.58 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 2 AQYVYSMNRVSKTVPPKRQ---ILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaLPMPGLTIGYL--EQ 76
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEHelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGE-VSLVGQPLHQMdeEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 77 EPKLNPEHtvresveesmgaVNAAKKRLEEVYELYAAEDADFDALAAEQAELEAiiATAGTDSEHQLEIAADALRLPAWd 156
Cdd:PRK10584 82 RAKLRAKH------------VGFVFQSFMLIPTLNALENVELPALLRGESSRQS--RNGAKALLEQLGLGKRLDHLPAQ- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 157 akigvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFL----QRFPGTVVAITHD 217
Cdd:PRK10584 147 -----LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
322-471 |
1.28e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.68 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG-------QTVKM-----AF 389
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgkditdwQTAKImreavAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 390 VDQARDALAdQKTVWEDISGGLDIINVGKFQMASRAYAGRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDE 469
Cdd:PRK11614 85 VPEGRRVFS-RMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
..
gi 518484691 470 PS 471
Cdd:PRK11614 164 PS 165
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
22-237 |
1.39e-13 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 70.09 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpMPGL-----------TIGYLEQEPKLNPEHTVRESV 90
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT-VAGHdvvreprevrrRIGIVFQDLSVDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 91 eESMGAV-----NAAKKRLEEVYELYAAEDadfdalaaeqaeleaiiatagtdsehqleiAADALrlpawdakIGVLSGG 165
Cdd:cd03265 95 -YIHARLygvpgAERRERIDELLDFVGLLE------------------------------AADRL--------VKTYSGG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 166 EKRRVALCRLLLSKPDMLLLDEPTNHLDAESV----EWLEVFLQRFPGTVVAITHDRYFLDNAAEWILELDRGRGI 237
Cdd:cd03265 136 MRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRahvwEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-235 |
1.45e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 70.25 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 16 PPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEALPMPGLTIGyleqepkLNPEHTVRES 89
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPpdsgtvTVRGRVSSLLGLGGG-------FNPELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 90 VEESMGAVNAAKKRLEEVYElyaaEDADFdalaaeqAELEAIIatagtdsehqleiaadalrlpawDAKIGVLSGGEKRR 169
Cdd:cd03220 105 IYLNGRLLGLSRKEIDEKID----EIIEF-------SELGDFI-----------------------DLPVKTYSSGMKAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518484691 170 VALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRF---PGTVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELlkqGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
11-196 |
1.50e-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: 69.84 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 11 VSKTVPPKRQI-LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpMPGLTIgyleqepklnpeHTVRES 89
Cdd:cd03263 6 LTKTYKKGTKPaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAY-INGYSI------------RTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 90 VEESMGavnaakkrleevyelYAAE-DADFDALAAEQ-----AELEAIiatAGTDSEHQLEIAADALRL-PAWDAKIGVL 162
Cdd:cd03263 73 ARQSLG---------------YCPQfDALFDELTVREhlrfyARLKGL---PKSEIKEEVELLLRVLGLtDKANKRARTL 134
|
170 180 190
....*....|....*....|....*....|....
gi 518484691 163 SGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
Cdd:cd03263 135 SGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
327-514 |
1.52e-13 |
|
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: 72.07 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 327 NVSKSFGDRLLidNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIgqtvkmafvdqardaladQKTVWED 406
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVL------------------NGRTLFD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 407 ISGGLDII----NVGK-FQMAS------------------RAYAGRFNFNGADQ--------QKKVGTLSGGERGRLHLA 455
Cdd:TIGR02142 64 SRKGIFLPpekrRIGYvFQEARlfphlsvrgnlrygmkraRPSERRISFERVIEllgighllGRLPGRLSGGEKQRVAIG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 456 KTLIAGGNVLLLDEPSNDLDV----ETLRALEDALLEFAGTVMVISHDRWFLDRIATHILAAE 514
Cdd:TIGR02142 144 RALLSSPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLE 206
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
11-251 |
1.76e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 73.22 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 11 VSKTVP--PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLTIGYLE-------QE 77
Cdd:TIGR00958 484 VSFSYPnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldgvPLVQYDHHYLHrqvalvgQE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 78 PKLnpehtVRESVEESMGavnaakkrleevYELYAAEDADFDAlAAEQAELEAIIA--TAGTDSEhqleiaadalrlpaW 155
Cdd:TIGR00958 564 PVL-----FSGSVRENIA------------YGLTDTPDEEIMA-AAKAANAHDFIMefPNGYDTE--------------V 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 156 DAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEwILELDRGR 235
Cdd:TIGR00958 612 GEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQ-ILVLKKGS 690
|
250
....*....|....*.
gi 518484691 236 gIPWKGNYSTWLEQKG 251
Cdd:TIGR00958 691 -VVEMGTHKQLMEDQG 705
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
326-516 |
1.83e-13 |
|
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: 70.37 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPD--SGEVVI-GQTV-KMAFVDQARDA--LAD 399
Cdd:TIGR01978 4 KDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEvtSGTILFkGQDLlELEPDERARAGlfLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 400 QKTvwEDISG------------------GLDIINVGKFQMASRAYAGRFNFNGADQQKKVGT-LSGGERGRLHLAKTLIA 460
Cdd:TIGR01978 84 QYP--EEIPGvsnleflrsalnarrsarGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEgFSGGEKKRNEILQMALL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 461 GGNVLLLDEPSNDLDVETLRALEDALLEFAG---TVMVISHDRWFLDRIA---THIL-----AAEGD 516
Cdd:TIGR01978 162 EPKLAILDEIDSGLDIDALKIVAEGINRLREpdrSFLIITHYQRLLNYIKpdyVHVLldgriVKSGD 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
338-499 |
1.93e-13 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 69.80 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 338 IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQ----ARDALADQKTVWEDISGGLD 412
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQITEPGPDRmvvfQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 413 IIN----VGKFQMASRAYAGRFNFNGAdQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLE 488
Cdd:TIGR01184 81 RVLpdlsKSERRAIVEEHIALVGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170
....*....|....*
gi 518484691 489 FAG----TVMVISHD 499
Cdd:TIGR01184 160 IWEehrvTVLMVTHD 174
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-258 |
2.26e-13 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 69.82 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 16 PPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpMPGLTIGYLEqepklnpehtvRESVEESMG 95
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVL-VDGHDLALAD-----------PAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 96 AVnaakkrLEEVYeLYAAEDADFDALAAEQAELEAIIATAGTDSEHQLeiaadALRLP-AWDAKIGV----LSGGEKRRV 170
Cdd:cd03252 80 VV------LQENV-LFNRSIRDNIALADPGMSMERVIEAAKLAGAHDF-----ISELPeGYDTIVGEqgagLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 171 ALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG--TVVAITHdRYFLDNAAEWILELDRGRgIPWKGNYSTWLE 248
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAgrTVIIIAH-RLSTVKNADRIIVMEKGR-IVEQGSHDELLA 225
|
250
....*....|..
gi 518484691 249 QKG--ERLAQEQ 258
Cdd:cd03252 226 ENGlyAYLYQLQ 237
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-217 |
2.31e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.84 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 21 ILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLT-----------IGYLEQEPKLNPEHT 85
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIfngqPMSKLSsaakaelrnqkLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 86 VRESVeeSMGAVNAAKKRLEevyelyaAEDADFDALAAEQAEleaiiatagTDSEHQleiaadalrlPAwdakigVLSGG 165
Cdd:PRK11629 104 ALENV--AMPLLIGKKKPAE-------INSRALEMLAAVGLE---------HRANHR----------PS------ELSGG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 166 EKRRVALCRLLLSKPDMLLLDEPTNHLD---AESVEWLEVFLQRFPGTV-VAITHD 217
Cdd:PRK11629 150 ERQRVAIARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGTAfLVVTHD 205
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-231 |
3.35e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.41 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 21 ILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV-----------DKEIEGEALPMPGLTIGYLEQEPKLNPEHTVRES 89
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTltptagtvlvaGDDVEALSARAASRRVASVPQDTSLSFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 90 VEesMGavnaakkRLEEVYELYAAEDADfdalaaEQAELEAIIATagtdsehqlEIAADAlrlpawDAKIGVLSGGEKRR 169
Cdd:PRK09536 98 VE--MG-------RTPHRSRFDTWTETD------RAAVERAMERT---------GVAQFA------DRPVTSLSGGERQR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 170 VALCRLLLSKPDMLLLDEPTNHLDA-ESVEWLEVF--LQRFPGTVVAITHDryfLDNAAEWILEL 231
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDInHQVRTLELVrrLVDDGKTAVAAIHD---LDLAARYCDEL 209
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-219 |
3.67e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.66 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLT-------IGYLEQEPkLNPEH-T 85
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFlgdkPISMLSsrqlarrLALLPQHH-LTPEGiT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 86 VRESVEESMGAVNAAKKRLeevyelyAAEDadfdalaaeqaelEAIIATAgtdsEHQLEIAADAlrlpawDAKIGVLSGG 165
Cdd:PRK11231 93 VRELVAYGRSPWLSLWGRL-------SAED-------------NARVNQA----MEQTRINHLA------DRRLTDLSGG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 166 EKRRVALCRLLLSKPDMLLLDEPTNHLD-AESVEWLEVF--LQRFPGTVVAITHD-----RY 219
Cdd:PRK11231 143 QRQRAFLAMVLAQDTPVVLLDEPTTYLDiNHQVELMRLMreLNTQGKTVVTVLHDlnqasRY 204
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-251 |
3.71e-13 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 69.18 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMA-------------GVDkeIEGEALPMPGLTIGYLEQEPKLNPEh 84
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPrfydvdsgrilidGHD--VRDYTLASLRRQIGLVSQDVFLFND- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 85 TVRESVeeSMGAVNAAKKRLEEvyelyaaedadfdalAAEQAELEAIIatagtdsehqleiaadaLRLP-AWDAKIGV-- 161
Cdd:cd03251 91 TVAENI--AYGRPGATREEVEE---------------AARAANAHEFI-----------------MELPeGYDTVIGErg 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 162 --LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG--TVVAITHDRYFLDNAAEwILELDRGRgI 237
Cdd:cd03251 137 vkLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKnrTTFVIAHRLSTIENADR-IVVLEDGK-I 214
|
250
....*....|....
gi 518484691 238 PWKGNYSTWLEQKG 251
Cdd:cd03251 215 VERGTHEELLAQGG 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
21-235 |
3.79e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.83 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 21 ILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEalpmpgLTIGyleqepklnpehtvresvEESMGAVNAA 100
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD------LFIG------------------EKRMNDVPPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 101 KKRLEEVYELYA-------AEDADFD-ALA-AEQAELEaiiatagtdseHQLEIAADALRLPAW-DAKIGVLSGGEKRRV 170
Cdd:PRK11000 74 ERGVGMVFQSYAlyphlsvAENMSFGlKLAgAKKEEIN-----------QRVNQVAEVLQLAHLlDRKPKALSGGQRQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 171 ALCRLLLSKPDMLLLDEPTNHLDAEsvewLEVFL--------QRFPGTVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:PRK11000 143 AIGRTLVAEPSVFLLDEPLSNLDAA----LRVQMrieisrlhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
325-505 |
3.98e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.75 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 325 FKNVSKSF-GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG----------------QTVKM 387
Cdd:PRK10908 4 FEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghditrlknrevpflrRQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 388 AFVDQardALADQKTVWEDISGGLDIINVGKFQMASRAYAGRFNFNGADQQKKVGT-LSGGERGRLHLAKTLIAGGNVLL 466
Cdd:PRK10908 84 IFQDH---HLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIqLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518484691 467 LDEPSNDLDVETLRALEDALLEF---AGTVMVISHDRWFLDR 505
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFnrvGVTVLMATHDIGLISR 202
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-251 |
4.39e-13 |
|
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: 68.79 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 17 PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL--PMPGLTIgyleqepklnPEHTVRESVeesm 94
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidGIDIRDI----------SRKSLRSMI---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 95 GAVnaakkrLEEVYeLYA---AEDADFDALAAEQAELEAIIATAGTDSEhqleiaadALRLP-AWDAKIG----VLSGGE 166
Cdd:cd03254 80 GVV------LQDTF-LFSgtiMENIRLGRPNATDEEVIEAAKEAGAHDF--------IMKLPnGYDTVLGenggNLSQGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 167 KRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQR-FPG-TVVAITHDRYFLDNAAEwILELDRGRgIPWKGNYS 244
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKlMKGrTSIIIAHRLSTIKNADK-ILVLDDGK-IIEEGTHD 222
|
....*..
gi 518484691 245 TWLEQKG 251
Cdd:cd03254 223 ELLAKKG 229
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
20-202 |
4.67e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 68.87 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEALPMPGLTI-------GYLEQEPKLNPEHTV 86
Cdd:COG1126 15 EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtiTVDGEDLTDSKKDInklrrkvGMVFQQFNLFPHLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 87 RESVEESMGAVnaaKKRleevyelyaaedadfdalAAEQAELEAiiatagtdsEHQLE---IAADAlrlpawDAKIGVLS 163
Cdd:COG1126 95 LENVTLAPIKV---KKM------------------SKAEAEERA---------MELLErvgLADKA------DAYPAQLS 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518484691 164 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESV-EWLEV 202
Cdd:COG1126 139 GGQQQRVAIARALAMEPKVMLFDEPTSALDPELVgEVLDV 178
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-216 |
5.39e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 68.08 E-value: 5.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 9 NRVSKTVPPKrQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL-------PMPGLTIGYLEQEPKLN 81
Cdd:cd03269 4 ENVTKRFGRV-TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldIAARNRIGYLPEERGLY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 82 PEHTVRESveesmgAVNAAkkRLEEVYELYAAEDADFdalaaeqaELEaiiatagtdsehQLEIAadalrlPAWDAKIGV 161
Cdd:cd03269 83 PKMKVIDQ------LVYLA--QLKGLKKEEARRRIDE--------WLE------------RLELS------EYANKRVEE 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 162 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWL--EVFLQRFPG-TVVAITH 216
Cdd:cd03269 129 LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLkdVIRELARAGkTVILSTH 186
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-476 |
5.98e-13 |
|
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: 71.01 E-value: 5.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV------DKEI--EGEALPMPGLT------IGYLEQEPKLNPEHTVR 87
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwDGEIywSGSPLKASNIRdteragIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 88 ESVeeSMGAVNAAKKRLeevyelyaaedADFDALAAEQAELEAiiatagtdsehQLEIAADALRLPawdakIGVLSGGEK 167
Cdd:TIGR02633 97 ENI--FLGNEITLPGGR-----------MAYNAMYLRAKNLLR-----------ELQLDADNVTRP-----VGDYGGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVF---LQRFPGTVVAITHDRYFLDNAAEWILELDRGRGIpwkgnys 244
Cdd:TIGR02633 148 QLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIirdLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 245 twleqkGERLAQEQKSEEAHAKALKKELewSRQNPkarqaksksrlarfeelsdveyqkrNETQEIfipvaerlGSQVFE 324
Cdd:TIGR02633 221 ------ATKDMSTMSEDDIITMMVGREI--TSLYP-------------------------HEPHEI--------GDVILE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 325 FKNVSKSFGD---RLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGK-EKPDSGEV--------------VIGQTVK 386
Cdd:TIGR02633 260 ARNLTCWDVInphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVfingkpvdirnpaqAIRAGIA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 387 MAFVDQARDALADQKTVWEDIS-------GGLDIINVGKFQMASRAYAGRFNFNGADQQKKVGTLSGGERGRLHLAKTLI 459
Cdd:TIGR02633 340 MVPEDRKRHGIVPILGVGKNITlsvlksfCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLL 419
|
490
....*....|....*..
gi 518484691 460 AGGNVLLLDEPSNDLDV 476
Cdd:TIGR02633 420 TNPRVLILDEPTRGVDV 436
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-194 |
6.15e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.23 E-value: 6.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 17 PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMA-----GVDKE----IEGEALPMPGLTI--GYLEQEPKLNPEHT 85
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrspkGVKGSgsvlLNGMPIDAKEMRAisAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 86 VRE----SVEESMGAVNAAKKRLEEVYELYaaedadfdalaaeqaeleaiiatagtdsehqleiaaDALRL-PAWDAKIG 160
Cdd:TIGR00955 116 VREhlmfQAHLRMPRRVTKKEKRERVDEVL------------------------------------QALGLrKCANTRIG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518484691 161 V------LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDA 194
Cdd:TIGR00955 160 VpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-193 |
6.76e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.90 E-value: 6.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 37 VLGLNGSGKSTLLKIMAG----------------VDKEiEGEALPMPGLTIGYLEQEPKLNPEHTVRESVEESMGAVNAA 100
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGltrpqkgrivlngrvlFDAE-KGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 101 KkrleevyelyaaedadFDALAaeqaELEAIiatagtdsEHQLEiaadalRLPAwdakigVLSGGEKRRVALCRLLLSKP 180
Cdd:PRK11144 108 Q----------------FDKIV----ALLGI--------EPLLD------RYPG------SLSGGEKQRVAIGRALLTAP 147
|
170
....*....|...
gi 518484691 181 DMLLLDEPTNHLD 193
Cdd:PRK11144 148 ELLLMDEPLASLD 160
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
324-518 |
6.80e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 69.02 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV-------------KMAF 389
Cdd:PRK11831 9 DMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENIpamsrsrlytvrkRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 390 VDQArDALADQKTVWEDISGGL-------DIINVGKFQMASRAYAGRfnfnGADQQKKvGTLSGGERGRLHLAKTLIAGG 462
Cdd:PRK11831 89 LFQS-GALFTDMNVFDNVAYPLrehtqlpAPLLHSTVMMKLEAVGLR----GAAKLMP-SELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 463 NVLLLDEP---SNDLDVETLRALEDALLEFAG-TVMVISHDRWFLDRIATH--ILA-----AEGDSQ 518
Cdd:PRK11831 163 DLIMFDEPfvgQDPITMGVLVKLISELNSALGvTCVVVSHDVPEVLSIADHayIVAdkkivAHGSAQ 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-235 |
7.57e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 68.89 E-value: 7.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 1 MAQYVYSMNRVSKTVP-PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV----DKEIEGEALPMPGLT----- 70
Cdd:PRK13635 1 MKEEIIRVEHISFRYPdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLllpeAGTITVGGMVLSEETvwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 71 --IGYLEQepklNPEH-----TVRESVeeSMGAVNAAKKRLEEVYELYAAEdadfdalaaeqaeleaiiatagtdseHQL 143
Cdd:PRK13635 81 rqVGMVFQ----NPDNqfvgaTVQDDV--AFGLENIGVPREEMVERVDQAL--------------------------RQV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 144 EIAADALRLPAwdakigVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFPGTVVAITHDry 219
Cdd:PRK13635 129 GMEDFLNREPH------RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITHD-- 200
|
250
....*....|....*...
gi 518484691 220 fLDNAAEW--ILELDRGR 235
Cdd:PRK13635 201 -LDEAAQAdrVIVMNKGE 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-193 |
9.69e-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: 70.60 E-value: 9.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 1 MAQYVYSMNR-VSKTVppkrqilKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEA----------LPMPGL 69
Cdd:TIGR03269 285 VSKRYISVDRgVVKAV-------DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 70 T--------IGYLEQEPKLNPEHTVRESVEESMGavnaakkrLEevyelyaaedadfdaLAAEQAELEAIIA--TAGTDS 139
Cdd:TIGR03269 358 DgrgrakryIGILHQEYDLYPHRTVLDNLTEAIG--------LE---------------LPDELARMKAVITlkMVGFDE 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518484691 140 EHQLEIAAdalRLPAwdakigVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD 193
Cdd:TIGR03269 415 EKAEEILD---KYPD------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-235 |
1.07e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 68.68 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpMPGltigylEQEPKLNpehtVREsVEESMGAVn 98
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVL-IRG------EPITKEN----IRE-VRKFVGLV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 99 aAKKRLEEVYELYAAEDADFDALaaEQAELEAIIATAGTDSEHQLEIAADALRLPAWdakigvLSGGEKRRVALCRLLLS 178
Cdd:PRK13652 84 -FQNPDDQIFSPTVEQDIAFGPI--NLGLDEETVAHRVSSALHMLGLEELRDRVPHH------LSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518484691 179 KPDMLLLDEPTNHLDAESVEWLEVFLQRFPG----TVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMDKGR 215
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-267 |
1.16e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 70.62 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 17 PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG---VDkeiEGEALpMPGLTIGYLEQEpklnpehtvreSVEES 93
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRfydVT---SGRIL-IDGQDIRDVTQA-----------SLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 94 MGAV-------------NAAkkrleevyelYAAEDADFDAL--AAEQAELEAIIAtagtdsehqleiaadalRLP-AWDA 157
Cdd:COG5265 434 IGIVpqdtvlfndtiayNIA----------YGRPDASEEEVeaAARAAQIHDFIE-----------------SLPdGYDT 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 158 KIG----VLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES-----VEWLEVFLQRfpgTVVAITH------Dryfld 222
Cdd:COG5265 487 RVGerglKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTeraiqAALREVARGR---TTLVIAHrlstivD----- 558
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 518484691 223 naAEWILELDRGRgIPWKGNYSTWLEQKGE-----RLAQEQKSEEAHAKA 267
Cdd:COG5265 559 --ADEILVLEAGR-IVERGTHAELLAQGGLyaqmwARQQEEEEAEEALAA 605
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
322-499 |
1.49e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.85 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSF-GDR-LLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTV-----------KMA 388
Cdd:PRK13648 7 IIVFKNVSFQYqSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAitddnfeklrkHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 389 FVDQARDALADQKTVWEDISGGLDIINVGKFQMASR---AYAGRFNFNGADQQKKvgTLSGGERGRLHLAKTLIAGGNVL 465
Cdd:PRK13648 87 IVFQNPDNQFVGSIVKYDVAFGLENHAVPYDEMHRRvseALKQVDMLERADYEPN--ALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 518484691 466 LLDEPSNDLDVETLRALEDALLEFAG----TVMVISHD 499
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSehniTIISITHD 202
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-241 |
1.56e-12 |
|
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: 66.75 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 24 DISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE---------ALPMPGLTIGYLEQEPKLNPEHTVresvEESM 94
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRvlingvdvtAAPPADRPVSMLFQENNLFAHLTV----EQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 95 GAVNAAKKRLEEVyelyaaedadfdalaaEQAELEAIIATAGtdsehqleIAADALRLPawdakiGVLSGGEKRRVALCR 174
Cdd:cd03298 92 GLGLSPGLKLTAE----------------DRQAIEVALARVG--------LAGLEKRLP------GELSGGERQRVALAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518484691 175 LLLSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEWILELDRGRgIPWKG 241
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR-IAAQG 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
338-534 |
1.80e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 67.95 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 338 IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG---------------QTVKMAFvdQARDALADQKT 402
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkpidysrkglmklrESVGMVF--QDPDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 403 VWEDISGGLDIINVGKFQMASRAYAGrFNFNGADQQKKVGT--LSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD----V 476
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNA-LKRTGIEHLKDKPThcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDpmgvS 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 477 ETLRALEDALLEFAGTVMVISHDrwfLDRIATH----ILAAEGDsqwTFFDGNYQEYEADKK 534
Cdd:PRK13636 179 EIMKLLVEMQKELGLTIIIATHD---IDIVPLYcdnvFVMKEGR---VILQGNPKEVFAEKE 234
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
320-507 |
1.92e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.83 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 320 SQVFEFKNVS---KSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV---------- 385
Cdd:PRK13650 2 SNIIEVKNLTfkyKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLteenvwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 386 KMAFVDQARDALADQKTVWEDISGGLDIINVGKFQMASR-----AYAGRFNFngadQQKKVGTLSGGERGRLHLAKTLIA 460
Cdd:PRK13650 82 KIGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERvnealELVGMQDF----KEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518484691 461 GGNVLLLDEPSNDLD----VETLRALEDALLEFAGTVMVISHDrwfLDRIA 507
Cdd:PRK13650 158 RPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD---LDEVA 205
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
324-512 |
1.95e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.01 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEK--PDSGEVVI-GQTVKMAFVDQ-ARD--AL 397
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLdGEDILELSPDErARAgiFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 398 ADQKTVweDISG--------------GLDIINVGKFQMASRAYAGRFNFNGADQQKKV-GTLSGGERGRLHLAKTLIAGG 462
Cdd:COG0396 82 AFQYPV--EIPGvsvsnflrtalnarRGEELSAREFLKLLKEKMKELGLDEDFLDRYVnEGFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 463 NVLLLDEPSNDLDVETLRALEDALLEFAG---TVMVISHDRWFLDRIA---THILA 512
Cdd:COG0396 160 KLAILDETDSGLDIDALRIVAEGVNKLRSpdrGILIITHYQRILDYIKpdfVHVLV 215
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-256 |
1.96e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 67.35 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEalpmpgLTIGyleqepklnpEHTVRESVEESMGAVNA 99
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQ------LNIA----------GHQFDFSQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 100 AKKRLEEVYELYAAedadFDALAAEQAELEAIIATAGTDSEH----------QLEIAADALRLPAwdakigVLSGGEKRR 169
Cdd:COG4161 80 LRQKVGMVFQQYNL----WPHLTVMENLIEAPCKVLGLSKEQarekamkllaRLRLTDKADRFPL------HLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 170 VALCRLLLSKPDMLLLDEPTNHLDAE-SVEWLEVF--LQRFPGTVVAITHDRYFLDNAAEWILELDRGRGIPwKGNYSTW 246
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIreLSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIE-QGDASHF 228
|
250
....*....|
gi 518484691 247 LEQKGERLAQ 256
Cdd:COG4161 229 TQPQTEAFAH 238
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-235 |
2.45e-12 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 66.59 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 16 PPKRQI--LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALPMpgltiGYLEQEPKlnPEHTVResvees 93
Cdd:cd03267 29 RKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA-----GLVPWKRR--KKFLRR------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 94 MGAVNAAKKRL------EEVYEL----YAAEDADFDALAAEQAELeaiiatagTDSEHQLEIAADALRLpawdakigvls 163
Cdd:cd03267 96 IGVVFGQKTQLwwdlpvIDSFYLlaaiYDLPPARFKKRLDELSEL--------LDLEELLDTPVRQLSL----------- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 164 gGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRF----PGTVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:cd03267 157 -GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-235 |
2.46e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 67.30 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 7 SMNRVSKTVPPKR----QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGealpmpglTIGYLEQEPKLnp 82
Cdd:PRK10619 2 SENKLNVIDLHKRygehEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEG--------SIVVNGQTINL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 83 ehtvresVEESMGAVNAAKK--------RLEEVYELYAAedadFDALAAEQAELEAIIATAGTDSEHQLEIAADALrlpa 154
Cdd:PRK10619 72 -------VRDKDGQLKVADKnqlrllrtRLTMVFQHFNL----WSHMTVLENVMEAPIQVLGLSKQEARERAVKYL---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 155 wdAKIGV-----------LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFP---GTVVAITHDRYF 220
Cdd:PRK10619 137 --AKVGIderaqgkypvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeegKTMVVVTHEMGF 214
|
250
....*....|....*
gi 518484691 221 LDNAAEWILELDRGR 235
Cdd:PRK10619 215 ARHVSSHVIFLHQGK 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
322-498 |
2.58e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 66.86 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAG-----KEKPDSGEVVI-GQTV-KMAFVD-QA 393
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLdGQDIfKMDVIElRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 394 RDALADQ-------KTVWEDISGGLDI--INVGKFQMASRAyagRFNFNGADQQKKV--------GTLSGGERGRLHLAK 456
Cdd:PRK14247 83 RVQMVFQipnpipnLSIFENVALGLKLnrLVKSKKELQERV---RWALEKAQLWDEVkdrldapaGKLSGGQQQRLCIAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518484691 457 TLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAG--TVMVISH 498
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
345-515 |
2.80e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 67.01 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 345 VPA-GAIVGIIGPNGAGKSTLFKLLAGKEKPDSG---------EVV-------------------IGQTVKMAFVDQ--- 392
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILdefrgselqnyftkllegdVKVIVKPQYVDLipk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 393 -----ARDAL--ADQKTVWEDISGGLDIINVgkfqmasrayagrfnfngadQQKKVGTLSGGERGRLHLAKTLIAGGNVL 465
Cdd:cd03236 102 avkgkVGELLkkKDERGKLDELVDQLELRHV--------------------LDRNIDQLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518484691 466 LLDEPSNDLDVE---TLRALEDALLEFAGTVMVISHDRWFLDRIATHILAAEG 515
Cdd:cd03236 162 FFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYG 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-217 |
3.04e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 68.18 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEalPMPGLT-----IGYLEQEPKLNPEHTV 86
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDptsgeiLIGGR--DVTDLPpkdrnIAMVFQSYALYPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 87 RESVEESMGAVNAAKKRLEE-VYElyaaedadfdalAAEQAELEaiiatagtdseHQLEiaadalRLPAwdakigVLSGG 165
Cdd:COG3839 93 YENIAFPLKLRKVPKAEIDRrVRE------------AAELLGLE-----------DLLD------RKPK------QLSGG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 166 EKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFL----QRFPGTVVAITHD 217
Cdd:COG3839 138 QRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIkrlhRRLGTTTIYVTHD 193
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
20-206 |
3.05e-12 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 66.24 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpMPGLTIGYLEQEPKLNpehtvresveesMGAVNA 99
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT-VDGFDVVKEPAEARRR------------LGFVSD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 100 AkkrlEEVYE-LYAAEDADFDAlaaeqaeleAIIATAGTDSEHQLEIAADALRLPAW-DAKIGVLSGGEKRRVALCRLLL 177
Cdd:cd03266 86 S----TGLYDrLTARENLEYFA---------GLYGLKGDELTARLEELADRLGMEELlDRRVGGFSTGMRQKVAIARALV 152
|
170 180
....*....|....*....|....*....
gi 518484691 178 SKPDMLLLDEPTNHLDAESVEWLEVFLQR 206
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQ 181
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
325-511 |
3.12e-12 |
|
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: 65.57 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 325 FKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVkmAFVDQA---RDAladqk 401
Cdd:cd03250 8 FTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--AYVSQEpwiQNG----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 402 TVWEDISGGLDiINVGKFQMASRAYAGRF---NFNGADqQKKVG----TLSGGERGRLHLAKTLIAGGNVLLLDEPSNDL 474
Cdd:cd03250 81 TIRENILFGKP-FDEERYEKVIKACALEPdleILPDGD-LTEIGekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518484691 475 DVETLRAL-EDAL---LEFAGTVMVISHDRWFLDRiATHIL 511
Cdd:cd03250 159 DAHVGRHIfENCIlglLLNNKTRILVTHQLQLLPH-ADQIV 198
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
324-499 |
3.18e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 67.13 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGD--RLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAG----KEKPDSGEVVIGQTV----------KM 387
Cdd:PRK13640 7 EFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpDDNPNSKITVDGITLtaktvwdireKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 388 AFVDQARDALADQKTVWEDISGGLDIINVGKFQMAS-----RAYAGRFNFNGADQQkkvgTLSGGERGRLHLAKTLIAGG 462
Cdd:PRK13640 87 GIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKivrdvLADVGMLDYIDSEPA----NLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518484691 463 NVLLLDEPSNDLDVE----TLRALEDALLEFAGTVMVISHD 499
Cdd:PRK13640 163 KIIILDESTSMLDPAgkeqILKLIRKLKKKNNLTVISITHD 203
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-217 |
3.56e-12 |
|
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: 66.56 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 10 RVSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLK-------------IMAGVD-KEIEGEALPMpglTIGYLE 75
Cdd:cd03295 5 NVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKminrlieptsgeiFIDGEDiREQDPVELRR---KIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 76 QEPKLNPEHTVRESVeesmGAVNAAKKRLEEVYELYAAEdadfdalaaeqaeleaIIATAGTDSEHQLEiaadalRLPaw 155
Cdd:cd03295 82 QQIGLFPHMTVEENI----ALVPKLLKWPKEKIRERADE----------------LLALVGLDPAEFAD------RYP-- 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 156 dakiGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWL--EVF-LQRFPG-TVVAITHD 217
Cdd:cd03295 134 ----HELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLqeEFKrLQQELGkTIVFVTHD 195
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-507 |
4.13e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.73 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 17 PKRQILKDISLSFFPGAKIGVLGLNGSGKS-TLLKIMAGVDK---EIEGEALPMP---------------------GLTI 71
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQaggLVQCDKMLLRrrsrqvielseqsaaqmrhvrGADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 72 GYLEQEP--KLNPEHTVRESVEESMgavnaakkRLEEvyelyaaedadfdALAAEQAELEAiiatagtdsehqlEIAADA 149
Cdd:PRK10261 107 AMIFQEPmtSLNPVFTVGEQIAESI--------RLHQ-------------GASREEAMVEA-------------KRMLDQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 150 LRLPAWDAKIG----VLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFPGTVVAITHDRYFL 221
Cdd:PRK10261 153 VRIPEAQTILSryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiqAQILQLIKVLQKEMSMGVIFITHDMGVV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 222 DNAAEWILELDRGRGIpwkgnystwleqkgERLAQEQ---KSEEAHAKALKKELewsrqnPKARQAKSKSRLARFEELSD 298
Cdd:PRK10261 233 AEIADRVLVMYQGEAV--------------ETGSVEQifhAPQHPYTRALLAAV------PQLGAMKGLDYPRRFPLISL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 299 VEYQKRNETQEIFIPVAerlGSQVFEFKNVSKSFGDR--LL---------IDNLSFNVPAGAIVGIIGPNGAGKSTLFKL 367
Cdd:PRK10261 293 EHPAKQEPPIEQDTVVD---GEPILQVRNLVTRFPLRsgLLnrvtrevhaVEKVSFDLWPGETLSLVGESGSGKSTTGRA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 368 LAGKEKPDSGEVVI-GQTVKMAFVDQARDALADQKTVWEDISGGLDI-INVGKFQMASRAYAGRFNFNGADQQ-----KK 440
Cdd:PRK10261 370 LLRLVESQGGEIIFnGQRIDTLSPGKLQALRRDIQFIFQDPYASLDPrQTVGDSIMEPLRVHGLLPGKAAAARvawllER 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 441 VGTL-----------SGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVeTLRA-----LEDALLEFAGTVMVISHDRWFLD 504
Cdd:PRK10261 450 VGLLpehawryphefSGGQRQRICIARALALNPKVIIADEAVSALDV-SIRGqiinlLLDLQRDFGIAYLFISHDMAVVE 528
|
...
gi 518484691 505 RIA 507
Cdd:PRK10261 529 RIS 531
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-260 |
4.14e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 68.72 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG---------VDKeIEGEALPMPGL--TIGYLEQEPKLnPEHTVRE 88
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslkING-IELRELDPESWrkHLSWVGQNPQL-PHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 89 SVeeSMGAVNAAKKRLEEVYELyaAEDADFdalaaeqaeleaiiatagtdsehqLEIAADALRLPAWDAKIGvLSGGEKR 168
Cdd:PRK11174 442 NV--LLGNPDASDEQLQQALEN--AWVSEF------------------------LPLLPQGLDTPIGDQAAG-LSVGQAQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 169 RVALCRLLLSKPDMLLLDEPTNHLDAES----VEWLEVFLQRfpGTVVAITHDryfLDNAAEW--ILELDRGRgIPWKGN 242
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHSeqlvMQALNAASRR--QTTLMVTHQ---LEDLAQWdqIWVMQDGQ-IVQQGD 566
|
250 260
....*....|....*....|.
gi 518484691 243 YSTWLEQKG---ERLAQEQKS 260
Cdd:PRK11174 567 YAELSQAGGlfaTLLAHRQEE 587
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
338-499 |
4.59e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 66.68 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 338 IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEV-VIGQTV----------KMAFVDQARDALADQKTVWED 406
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGREVnaenekwvrsKVGLVFQDPDDQVFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 407 ISGGLDIINVGKFQMASRAYAGRFNFNGAD-QQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD---VETLRAL 482
Cdd:PRK13647 101 VAFGPVNMGLDKDEVERRVEEALKAVRMWDfRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDprgQETLMEI 180
|
170
....*....|....*..
gi 518484691 483 EDALLEFAGTVMVISHD 499
Cdd:PRK13647 181 LDRLHNQGKTVIVATHD 197
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
17-235 |
5.15e-12 |
|
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: 65.35 E-value: 5.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 17 PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEA---------LPMPGLTIGYLEQEPKLNPEHTVR 87
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtdLPPKDRDIAMVFQNYALYPHMTVY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 88 ESVEESMgavnaakkrleevyELYAAEDADFDALAAEQAELEAIiatagtdsEHQLEiaadalRLPAwdakigVLSGGEK 167
Cdd:cd03301 91 DNIAFGL--------------KLRKVPKDEIDERVREVAELLQI--------EHLLD------RKPK------QLSGGQR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 168 RRVALCRLLLSKPDMLLLDEPTNHLDA----ESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:cd03301 137 QRVALGRAIVREPKVFLMDEPLSNLDAklrvQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
320-498 |
5.27e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 5.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 320 SQVFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKeKPD---SGEVVI-GQTVKMAFVdqaRD 395
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFeGEELQASNI---RD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 396 -------------ALADQKTVWEDISGGLDIINVGKF---QMASRAYA--GRFNFNgADQQKKVGTLSGGERGRLHLAKT 457
Cdd:PRK13549 79 teragiaiihqelALVKELSVLENIFLGNEITPGGIMdydAMYLRAQKllAQLKLD-INPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518484691 458 LIAGGNVLLLDEPSNDL---DVETLRALEDALLEFAGTVMVISH 498
Cdd:PRK13549 158 LNKQARLLILDEPTASLtesETAVLLDIIRDLKAHGIACIYISH 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-476 |
5.45e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 17 PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEALPMPG------LTIGYLEQEPKLNPEH 84
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTrdagsiLYLGKEVTFNGpkssqeAGIGIIHQELNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 85 TVRESV------EESMGAVNAAKkrleevyeLYAAEDADFDALAAEQaeleaiiatagtdSEHQLeiaadalrlpawdak 158
Cdd:PRK10762 95 TIAENIflgrefVNRFGRIDWKK--------MYAEADKLLARLNLRF-------------SSDKL--------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 159 IGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHL-DAESVEWLEVflqrfpgtvvaithdryfldnaaewILEL-DRGRG 236
Cdd:PRK10762 139 VGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFRV-------------------------IRELkSQGRG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 237 IPWKgnystwleqkgerlaqeqkseeAHAkaLKKELEWSRQNPKARQAK--SKSRLARFEELSDVEYQKRNETQEIFIPV 314
Cdd:PRK10762 194 IVYI----------------------SHR--LKEIFEICDDVTVFRDGQfiAEREVADLTEDSLIEMMVGRKLEDQYPRL 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 315 AERLGSQVFEFKNVSKSfGdrllIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVK------- 386
Cdd:PRK10762 250 DKAPGEVRLKVDNLSGP-G----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdGHEVVtrspqdg 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 387 ----MAFV--DQARDALADQKTVWEDIS----------GGldIINVGKFQMASRAYAGRFNFNGADQQKKVGTLSGGERG 450
Cdd:PRK10762 325 langIVYIseDRKRDGLVLGMSVKENMSltalryfsraGG--SLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQ 402
|
490 500
....*....|....*....|....*.
gi 518484691 451 RLHLAKTLIAGGNVLLLDEPSNDLDV 476
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVDV 428
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
322-478 |
5.60e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 5.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVV-IGQTVKMAFVDQARDA---- 396
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNGPKSSQEAgigi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 397 ------LADQKTVWEDISGGLDIIN-VGKF---QMASRAYA--GRFNFNGADQQkKVGTLSGGERGRLHLAKTLIAGGNV 464
Cdd:PRK10762 84 ihqelnLIPQLTIAENIFLGREFVNrFGRIdwkKMYAEADKllARLNLRFSSDK-LVGELSIGEQQMVEIAKVLSFESKV 162
|
170
....*....|....*
gi 518484691 465 LLLDEPSNDL-DVET 478
Cdd:PRK10762 163 IIMDEPTDALtDTET 177
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
324-498 |
6.15e-12 |
|
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: 65.13 E-value: 6.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRL--LIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDALA-- 398
Cdd:cd03369 8 EVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdGIDISTIPLEDLRSSLTii 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 399 --DQKTVWEDISGGLDIINV---GKFQMASRAYAGRFNfngadqqkkvgtLSGGERGRLHLAKTLIAGGNVLLLDEPSND 473
Cdd:cd03369 88 pqDPTLFSGTIRSNLDPFDEysdEEIYGALRVSEGGLN------------LSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180 190
....*....|....*....|....*....|..
gi 518484691 474 LDVETlraleDALL------EFAG-TVMVISH 498
Cdd:cd03369 156 IDYAT-----DALIqktireEFTNsTILTIAH 182
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
324-499 |
6.26e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.21 E-value: 6.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSF--GDRLL--IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEV-VIGQTVkmafVDQARDALA 398
Cdd:PRK10535 6 ELKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYrVAGQDV----ATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 399 DQK-----------------TVWEDISGGLDIINVGKFQMASRAYA--GRFNFnGADQQKKVGTLSGGERGRLHLAKTLI 459
Cdd:PRK10535 82 QLRrehfgfifqryhllshlTAAQNVEVPAVYAGLERKQRLLRAQEllQRLGL-EDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 518484691 460 AGGNVLLLDEPSNDLDV---ETLRALEDALLEFAGTVMVISHD 499
Cdd:PRK10535 161 NGGQVILADEPTGALDShsgEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-385 |
6.41e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.61 E-value: 6.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE----------------ALP----MP-GLtiGyleq 76
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRvevlggdmadarhrraVCPriayMPqGL--G---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 77 epK-LNPEHTVRESVeesmgavnaakkrleevyelyaaedaDFDA----LAAeqAELEAIIA--TAGTDsehqLEIAADa 149
Cdd:NF033858 87 --KnLYPTLSVFENL--------------------------DFFGrlfgQDA--AERRRRIDelLRATG----LAPFAD- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 150 lRlPAwdakiGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESV----EWLEVFLQRFPG-TVVAITHdryFLDNA 224
Cdd:NF033858 132 -R-PA-----GKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRrqfwELIDRIRAERPGmSVLVATA---YMEEA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 225 A--EWILELDRGR----GIPwkgnystwleqkGERLAQEQKS--EEAHAKALKKElewsrqnpkarqaksksrlarfeel 296
Cdd:NF033858 202 ErfDWLVAMDAGRvlatGTP------------AELLARTGADtlEAAFIALLPEE------------------------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 297 sdveyqKRNETQEIFIP--VAERLGSQVFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKP 374
Cdd:NF033858 245 ------KRRGHQPVVIPprPADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPA 318
|
410
....*....|..
gi 518484691 375 DSGEV-VIGQTV 385
Cdd:NF033858 319 SEGEAwLFGQPV 330
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
324-498 |
7.22e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.91 E-value: 7.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKE--KPDSGEV---------------------- 379
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpskvgep 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 380 --VIGQTVKMAFVD--------------------QARDALADQKTVWEDISGGLDIINVGKFQMASRAyagrfnfngADQ 437
Cdd:TIGR03269 82 cpVCGGTLEPEEVDfwnlsdklrrrirkriaimlQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRA---------VDL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 438 QKKVG----------TLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFA---GTVMVI-SH 498
Cdd:TIGR03269 153 IEMVQlshrithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkasGISMVLtSH 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-237 |
9.09e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.91 E-value: 9.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 4 YVYSMNRvsktvPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGeALPMPGLTIGYLEQEPKLNPe 83
Cdd:PRK13643 9 YTYQPNS-----PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEG-KVTVGDIVVSSTSKQKEIKP- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 84 htvresVEESMGAVNAAKKrlEEVYELYAAEDADFDAlaaeqaeleaiiATAGTDSEHQLEIAADALRLPA-----WDAK 158
Cdd:PRK13643 82 ------VRKKVGVVFQFPE--SQLFEETVLKDVAFGP------------QNFGIPKEKAEKIAAEKLEMVGladefWEKS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 159 IGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES-VEWLEVF--LQRFPGTVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:PRK13643 142 PFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKArIEMMQLFesIHQSGQTVVLVTHLMDDVADYADYVYLLEKGH 221
|
..
gi 518484691 236 GI 237
Cdd:PRK13643 222 II 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
17-217 |
9.17e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.49 E-value: 9.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 17 PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEALPMPGLTIGYLEQEPKLNPEHTVRESV 90
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPyqhgsiTLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 91 EESMgavnaakkrleevyelyaaedadfdalaaeqaELeaiiatAGTDSEHQLEIAADALR---LPAWDAK-IGVLSGGE 166
Cdd:PRK11248 92 AFGL--------------------------------QL------AGVEKMQRLEIAHQMLKkvgLEGAEKRyIWQLSGGQ 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 167 KRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFL----QRFPGTVVAITHD 217
Cdd:PRK11248 134 RQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlklwQETGKQVLLITHD 188
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-235 |
9.28e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.53 E-value: 9.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDkeiegeaLPMPGlTIGYLEQEPKLNPEHTVRESVeesmGAVNA 99
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY-------LPQRG-RVKVMGREVNAENEKWVRSKV----GLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 100 AKKrlEEVYELYAAEDADFDALAAEQAELEAiiatagtdsEHQLEIAADALRLpaWDAKIGV---LSGGEKRRVALCRLL 176
Cdd:PRK13647 87 DPD--DQVFSSTVWDDVAFGPVNMGLDKDEV---------ERRVEEALKAVRM--WDFRDKPpyhLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 177 LSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG---TVVAITHDryfLDNAAEW---ILELDRGR 235
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNqgkTVIVATHD---VDLAAEWadqVIVLKEGR 215
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
318-498 |
1.08e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.44 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 318 LGSQVFEFKNVSKSF-GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEV-------------VIGQ 383
Cdd:PRK10790 336 LQSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldgrplsslshsVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 384 TVKMafVDQARDALADqkTVWEDISGGLDIIN------VGKFQMAS--RAYAGRFNFNGADQQKkvgTLSGGERGRLHLA 455
Cdd:PRK10790 416 GVAM--VQQDPVVLAD--TFLANVTLGRDISEeqvwqaLETVQLAElaRSLPDGLYTPLGEQGN---NLSVGQKQLLALA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518484691 456 KTLIAGGNVLLLDEPSNDLDVETLRALEDALLEF--AGTVMVISH 498
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAH 533
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
338-499 |
1.12e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.48 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 338 IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVV-----IGQ-----------TVKMAFVDqARDALADQK 401
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwrgepLAKlnraqrkafrrDIQMVFQD-SISAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 402 TVWEDISGGL-DIINVGKFQMASRAYA--GRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV-- 476
Cdd:PRK10419 107 TVREIIREPLrHLLSLDKAERLARASEmlRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvl 186
|
170 180
....*....|....*....|....*
gi 518484691 477 --ETLRALEDALLEFAGTVMVISHD 499
Cdd:PRK10419 187 qaGVIRLLKKLQQQFGTACLFITHD 211
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
279-498 |
1.13e-11 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 67.46 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 279 PKARQAKSKSRlaRFEE--LSDVEYQKRNETQEIFIPvaerLGSQVFEFKNVSKSFGDRLLiDNLSFNVPAGAIVGIIGP 356
Cdd:TIGR01193 436 PKLQAARVANN--RLNEvyLVDSEFINKKKRTELNNL----NGDIVINDVSYSYGYGSNIL-SDISLTIKMNSKTTIVGM 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 357 NGAGKSTLFKLLAGKEKPDSGEVVIGQTvkmAFVDQARDAL-------------------------ADQKTVWEDISGGL 411
Cdd:TIGR01193 509 SGSGKSTLAKLLVGFFQARSGEILLNGF---SLKDIDRHTLrqfinylpqepyifsgsilenlllgAKENVSQDEIWAAC 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 412 DII----NVGKFQMAsraYAGRFNFNGadqqkkvGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALL 487
Cdd:TIGR01193 586 EIAeikdDIENMPLG---YQTELSEEG-------SSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLL 655
|
250
....*....|..
gi 518484691 488 EFA-GTVMVISH 498
Cdd:TIGR01193 656 NLQdKTIIFVAH 667
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
320-475 |
1.21e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.35 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 320 SQVFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV----------KMA 388
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDIstlkpeiyrqQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 389 FVDQARDALADqkTVWEDISGGLDIINVGKFQMASRAYAGRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLD 468
Cdd:PRK10247 85 YCAQTPTLFGD--TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
....*..
gi 518484691 469 EPSNDLD 475
Cdd:PRK10247 163 EITSALD 169
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
322-499 |
1.32e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 65.10 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGD-RLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVK------------M 387
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPIKydkksllevrktV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 388 AFVDQARDALADQKTVWEDISGGLDIINVGKFQMASRAyagrfnfngADQQKKVGT----------LSGGERGRLHLAKT 457
Cdd:PRK13639 81 GIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRV---------KEALKAVGMegfenkpphhLSGGQKKRVAIAGI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518484691 458 LIAGGNVLLLDEPSNDLD----VETLRALEDalLEFAGTVMVIS-HD 499
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDpmgaSQIMKLLYD--LNKEGITIIIStHD 196
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-235 |
1.36e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.51 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 10 RVSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE--------------ALPMPGLTIGYLE 75
Cdd:PRK10908 6 HVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKiwfsghditrlknrEVPFLRRQIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 76 QEPKLNPEHTVRESVEesmgavnaakkrleevyelyaaedadfdalaaeqaeLEAIIATA-GTDSEHQLEIAADALRL-- 152
Cdd:PRK10908 86 QDHHLLMDRTVYDNVA------------------------------------IPLIIAGAsGDDIRRRVSAALDKVGLld 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 153 PAWDAKIGvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD-AESVEWLEVF--LQRFPGTVVAITHDRYFLDNAAEWIL 229
Cdd:PRK10908 130 KAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdALSEGILRLFeeFNRVGVTVLMATHDIGLISRRSYRML 208
|
....*.
gi 518484691 230 ELDRGR 235
Cdd:PRK10908 209 TLSDGH 214
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
337-515 |
1.72e-11 |
|
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: 64.83 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 337 LIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQ---------------TVKMAFVDqARDALADQ 400
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFrGQdlyqldrkqrrafrrDVQLVFQD-SPSAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 401 KTVWEDISGGL-DIINVGKFQMASRAYA--GRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV- 476
Cdd:TIGR02769 105 MTVRQIIGEPLrHLTSLDESEQKARIAEllDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMv 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518484691 477 ---ETLRALEDALLEFAGTVMVISHDRWFLDRIATHILAAEG 515
Cdd:TIGR02769 185 lqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK 226
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
325-516 |
1.74e-11 |
|
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: 62.97 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 325 FKNVSKSFGDRLLIDNLSfNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDsgevvigqtvkmafvdqardalaDQKTVW 404
Cdd:cd03222 3 YPDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPN-----------------------GDNDEW 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 405 EDISggldiiNVGKFQMASrayagrfnfngadqqkkvgtLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVE----TLR 480
Cdd:cd03222 59 DGIT------PVYKPQYID--------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAAR 112
|
170 180 190
....*....|....*....|....*....|....*.
gi 518484691 481 ALEDALLEFAGTVMVISHDRWFLDRIATHILAAEGD 516
Cdd:cd03222 113 AIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-193 |
2.03e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.85 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGvdkeiegeALPMPGLTIGYleqepklnpehTVRESVE---ESMG 95
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--------DLTGGGAPRGA-----------RVTGDVTlngEPLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 96 AVNAAK-KRLEEVyeLYAAEDADFDALAAEQAELEAI--IATAGTDSEHQLEIAADALRLPAWDAKIG----VLSGGEKR 168
Cdd:PRK13547 75 AIDAPRlARLRAV--LPQAAQPAFAFSAREIVLLGRYphARRAGALTHRDGEIAWQALALAGATALVGrdvtTLSGGELA 152
|
170 180 190
....*....|....*....|....*....|....
gi 518484691 169 RVALCRLL---------LSKPDMLLLDEPTNHLD 193
Cdd:PRK13547 153 RVQFARVLaqlwpphdaAQPPRYLLLDEPTAALD 186
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
322-382 |
2.11e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.69 E-value: 2.11e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 322 VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEV-VIG 382
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLG 62
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
338-511 |
2.14e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 64.68 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 338 IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI------GQTVKMAFVdQARDALADQ--------KTV 403
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditDKKVKLSDI-RKKVGLVFQypeyqlfeETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 404 WEDISGGLDIINVGKFQMASRAYAGrFNFNGAD----QQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD---- 475
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRA-MNIVGLDyedyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgr 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 518484691 476 ---VETLRALEDallEFAGTVMVISHDRWFLDRIATHIL 511
Cdd:PRK13637 181 deiLNKIKELHK---EYNMTIILVSHSMEDVAKLADRII 216
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
338-505 |
2.45e-11 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 62.34 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 338 IDNLSFNVPAGAIVGIIGPNGAGKSTLFKllagkekpdsgevVIGQTVKMAFVDQARDALADQKTVWED-----ISGGLD 412
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-------------EGLYASGKARLISFLPKFSRNKLIFIDqlqflIDVGLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 413 IINVGKfqmasrayagrfnfngadqqkKVGTLSGGERGRLHLAKTLIAG--GNVLLLDEPSNDLDVETLRALEDA---LL 487
Cdd:cd03238 78 YLTLGQ---------------------KLSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLHQQDINQLLEVikgLI 136
|
170
....*....|....*...
gi 518484691 488 EFAGTVMVISHDRWFLDR 505
Cdd:cd03238 137 DLGNTVILIEHNLDVLSS 154
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
8-251 |
3.27e-11 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 65.92 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 8 MNRVSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALPMPGL-----------TIGYLEQ 76
Cdd:TIGR01193 476 INDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqFINYLPQ 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 77 EPklnpeHTVRESVEESMGAVNAAKKRLEEVYElyaaedadfdalAAEQAELEAIIATAGTDseHQLEIAADAlrlpawd 156
Cdd:TIGR01193 556 EP-----YIFSGSILENLLLGAKENVSQDEIWA------------ACEIAEIKDDIENMPLG--YQTELSEEG------- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 157 akiGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVEWLeVFLQRfpGTVVAITHdRYFLDNAAEWILELD 232
Cdd:TIGR01193 610 ---SSISGGQKQRIALARALLTDSKVLILDESTSNLDTitekKIVNNL-LNLQD--KTIIFVAH-RLSVAKQSDKIIVLD 682
|
250
....*....|....*....
gi 518484691 233 RGrGIPWKGNYSTWLEQKG 251
Cdd:TIGR01193 683 HG-KIIEQGSHDELLDRNG 700
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-224 |
3.50e-11 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 63.82 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 17 PKRQILK---------DISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEalPMPGLT----------- 70
Cdd:cd03294 26 SKEEILKktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEptsgkvLIDGQ--DIAAMSrkelrelrrkk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 71 IGYLEQEPKLNPEHTVRESVEESMgavnaakkrleEVyelyaaedadfdalaaeqaeleaiiatAGTDSEHQLEIAADAL 150
Cdd:cd03294 104 ISMVFQSFALLPHRTVLENVAFGL-----------EV---------------------------QGVPRAEREERAAEAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 151 R---LPAW-DAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDA-ESVEWLEVFLQ---RFPGTVVAITHDryfLD 222
Cdd:cd03294 146 ElvgLEGWeHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPlIRREMQDELLRlqaELQKTIVFITHD---LD 222
|
..
gi 518484691 223 NA 224
Cdd:cd03294 223 EA 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-227 |
4.09e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 63.89 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 4 YVYSMNrvsktVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEalpmpgLTIGYLEQEPKLN-- 81
Cdd:PRK13634 10 HRYQYK-----TPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGT------VTIGERVITAGKKnk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 82 ---------------PEHTV-RESVEE--SMGAVNaakkrleevyelYAAEDADFDALAAEQAELEAIiatagtdSEHQL 143
Cdd:PRK13634 79 klkplrkkvgivfqfPEHQLfEETVEKdiCFGPMN------------FGVSEEDAKQKAREMIELVGL-------PEELL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 144 EiaadalRLPaWDakigvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES-VEWLEVF--LQRFPG-TVVAITHDry 219
Cdd:PRK13634 140 A------RSP-FE-----LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGrKEMMEMFykLHKEKGlTTVLVTHS-- 205
|
....*...
gi 518484691 220 fLDNAAEW 227
Cdd:PRK13634 206 -MEDAARY 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-235 |
4.09e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.52 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaLPMPGLTIGYLEQE--PKLNPEHtvresveesMGAV 97
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGT-YRVAGQDVATLDADalAQLRREH---------FGFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 98 NaakkrleEVYELYAAedadfdaLAAEQ-AELEAIIAtaGTDSEHQLEIAADALRLPAWDAKI----GVLSGGEKRRVAL 172
Cdd:PRK10535 92 F-------QRYHLLSH-------LTAAQnVEVPAVYA--GLERKQRLLRAQELLQRLGLEDRVeyqpSQLSGGQQQRVSI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 173 CRLLLSKPDMLLLDEPTNHLDAESVEwlEVF-----LQRFPGTVVAITHDRYfLDNAAEWILELDRGR 235
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGE--EVMailhqLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGE 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-193 |
4.60e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.57 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 7 SMNRVSKTVPP----KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG---VDK---EIEGEAL-PMP----GLTI 71
Cdd:COG1101 3 ELKNLSKTFNPgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGslpPDSgsiLIDGKDVtKLPeykrAKYI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 72 GYLEQEPKLN--PEHTvresVEESMG-AVNAAKKRleevyelyaaedadfdAL-----AAEQAELEAIIATAGTDSEHQL 143
Cdd:COG1101 83 GRVFQDPMMGtaPSMT----IEENLAlAYRRGKRR----------------GLrrgltKKRRELFRELLATLGLGLENRL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518484691 144 eiaadalrlpawDAKIGVLSGGEkrRVALCrLL---LSKPDMLLLDEPTNHLD 193
Cdd:COG1101 143 ------------DTKVGLLSGGQ--RQALS-LLmatLTKPKLLLLDEHTAALD 180
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-217 |
5.02e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 13 KTVPPKrQILKDISLSFFPGAKIGVLGLNGSGKST----LLKIMAGvDKEIEGEALPMPGLT----------IGYLEQEP 78
Cdd:PRK15134 294 RTVDHN-VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-QGEIWFDGQPLHNLNrrqllpvrhrIQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 79 --KLNPEHTVRESVEESMgavnaakkrleEVYElyaaedadfDALAAEQAELEAIIATAgtdsehqlEIAADAL---RLP 153
Cdd:PRK15134 372 nsSLNPRLNVLQIIEEGL-----------RVHQ---------PTLSAAQREQQVIAVME--------EVGLDPEtrhRYP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 154 AwdakigVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFPGTVVAITHD 217
Cdd:PRK15134 424 A------EFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFISHD 485
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-248 |
5.17e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.96 E-value: 5.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 17 PKrQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALPMPglTIGYLEQEP-KLNPehTVRESVeesmg 95
Cdd:PTZ00243 672 PK-VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER--SIAYVPQQAwIMNA--TVRGNI----- 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 96 avnaakkrleevyELYAAEDADFDALAAEQAELEAIIATAGTDSEhqLEIaadalrlpawdAKIGV-LSGGEKRRVALCR 174
Cdd:PTZ00243 742 -------------LFFDEEDAARLADAVRVSQLEADLAQLGGGLE--TEI-----------GEKGVnLSGGQKARVSLAR 795
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 175 LLLSKPDMLLLDEPTNHLDAESVEWL--EVFLQRFPG-TVVAITHDRYFLDNaAEWILELDRGRgIPWKGNYSTWLE 248
Cdd:PTZ00243 796 AVYANRDVYLLDDPLSALDAHVGERVveECFLGALAGkTRVLATHQVHVVPR-ADYVVALGDGR-VEFSGSSADFMR 870
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
324-507 |
5.40e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.23 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTV------------------ 385
Cdd:PRK11264 5 EVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITidtarslsqqkglirqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 386 -KMAFVDQARDaLADQKTVWEDISGGLDIINVGKFQMA---SRAYAGRFNFNGADQQKKvGTLSGGERGRLHLAKTLIAG 461
Cdd:PRK11264 85 qHVGFVFQNFN-LFPHRTVLENIIEGPVIVKGEPKEEAtarARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518484691 462 GNVLLLDEPSNDLDVE-------TLRALEdallEFAGTVMVISHDRWFLDRIA 507
Cdd:PRK11264 163 PEVILFDEPTSALDPElvgevlnTIRQLA----QEKRTMVIVTHEMSFARDVA 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
322-498 |
6.10e-11 |
|
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: 64.85 E-value: 6.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAG--KEKPDSGEVVI-GQTVKMAFVDQARDA-- 396
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWsGSPLKASNIRDTERAgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 397 --------LADQKTVWEDISGGLDIINVGKF----QMASRAYA--GRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGG 462
Cdd:TIGR02633 81 viihqeltLVPELSVAENIFLGNEITLPGGRmaynAMYLRAKNllRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 518484691 463 NVLLLDEPSNDLDVETLRALEDAL--LEFAGTVMV-ISH 498
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIrdLKAHGVACVyISH 199
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
339-507 |
6.62e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 63.60 E-value: 6.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 339 DNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG----------------QTVKMAFVD-QArdALADQK 401
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqditglsgrelrplrRRMQMVFQDpYA--SLNPRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 402 TVWEDISGGLDIINVGKfqmasrayagrfnfnGADQQKKVGTL------------------SGGERGRLHLAKTLIAGGN 463
Cdd:COG4608 113 TVGDIIAEPLRIHGLAS---------------KAERRERVAELlelvglrpehadryphefSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518484691 464 VLLLDEPSNDLDVeTLRA-----LEDALLEFAGTVMVISHD----RWFLDRIA 507
Cdd:COG4608 178 LIVCDEPVSALDV-SIQAqvlnlLEDLQDELGLTYLFISHDlsvvRHISDRVA 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
327-541 |
8.84e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.81 E-value: 8.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 327 NVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKP-----DSGEVVIGQTVKMAFvdqaRDALADQK 401
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNY----RDVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 402 TVwedisgGLDIINVGKFQMA--SRAYAG--------RFNFNGADQQK--KVG--------------TLSGGERGRLHLA 455
Cdd:PRK14271 102 RV------GMLFQRPNPFPMSimDNVLAGvrahklvpRKEFRGVAQARltEVGlwdavkdrlsdspfRLSGGQQQLLCLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 456 KTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAG--TVMVISHDRWFLDRIAthilaaegDSQWTFFDGnyqeyeadk 533
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARIS--------DRAALFFDG--------- 238
|
....*...
gi 518484691 534 kkRLGEEG 541
Cdd:PRK14271 239 --RLVEEG 244
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-222 |
9.25e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 61.39 E-value: 9.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVD--KEIEGE---------ALPMP-----GLTIGYleQEPKLN 81
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEilfkgeditDLPPEerarlGIFLAF--QYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 82 PEHTVRESVEEsmgaVNAAkkrleevyelyaaedadfdalaaeqaeleaiiatagtdsehqleiaadalrlpawdakigv 161
Cdd:cd03217 90 PGVKNADFLRY----VNEG------------------------------------------------------------- 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518484691 162 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRF--PGT-VVAITHDRYFLD 222
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreEGKsVLIITHYQRLLD 168
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-201 |
1.04e-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: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLT---IGYLEQEPKLNPEHTVRESV 90
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgePLDPEDrrrIGYLPEERGLYPKMKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 91 E-----ESMGAvNAAKKRLEEVYElyaaedadfdalaaeqaeleaiiatagtdsehQLEIAAdalrlpAWDAKIGVLSGG 165
Cdd:COG4152 93 VylarlKGLSK-AEAKRRADEWLE--------------------------------RLGLGD------RANKKVEELSKG 133
|
170 180 190
....*....|....*....|....*....|....*.
gi 518484691 166 EKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLE 201
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLK 169
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
317-476 |
1.05e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.04 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 317 RLGSQVFEFKNVS---KSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKE--KPDSGEVVI-GQTVKMAFV 390
Cdd:NF040905 252 KIGEVVFEVKNWTvyhPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKdGKEVDVSTV 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 391 DQARDA-LA----DQKT----VWEDISGGLDIINVGK------------FQMASRaYAGRFNFNGADQQKKVGTLSGGER 449
Cdd:NF040905 332 SDAIDAgLAyvteDRKGyglnLIDDIKRNITLANLGKvsrrgvideneeIKVAEE-YRKKMNIKTPSVFQKVGNLSGGNQ 410
|
170 180
....*....|....*....|....*..
gi 518484691 450 GRLHLAKTLIAGGNVLLLDEPSNDLDV 476
Cdd:NF040905 411 QKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
320-497 |
1.43e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 60.74 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 320 SQVFEFKNVS----KSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAG----KEKPdSGEVVI-GQTVKMAFV 390
Cdd:cd03233 1 ASTLSWRNISfttgKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtegNVSV-EGDIHYnGIPYKEFAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 391 DQARDALADQK--------TVWEDIsggldiinvgKFqmASRAYAGRFnfngadqqkkVGTLSGGERGRLHLAKTLIAGG 462
Cdd:cd03233 80 KYPGEIIYVSEedvhfptlTVRETL----------DF--ALRCKGNEF----------VRGISGGERKRVSIAEALVSRA 137
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518484691 463 NVLLLDEPSNDLD-------VETLRALEDALlefaGTVMVIS 497
Cdd:cd03233 138 SVLCWDNSTRGLDsstaleiLKCIRTMADVL----KTTTFVS 175
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
19-235 |
1.53e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 61.69 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLK------------IMAGvDKEIEGeALPM---PGLT------IGYLEQE 77
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRcinlleqpeagtIRVG-DITIDT-ARSLsqqKGLIrqlrqhVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 78 PKLNPEHTVRESVEEsmGAVNAAKKRLEEVyelyaaedadfdalAAEQAELEAIIATAGTDsehqleiaadalrlpawDA 157
Cdd:PRK11264 94 FNLFPHRTVLENIIE--GPVIVKGEPKEEA--------------TARARELLAKVGLAGKE-----------------TS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 158 KIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESV-EWLEVF--LQRFPGTVVAITHDRYFLDNAAEWILELDRG 234
Cdd:PRK11264 141 YPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVgEVLNTIrqLAQEKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
.
gi 518484691 235 R 235
Cdd:PRK11264 221 R 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-234 |
1.61e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.08 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE------ALPMPGLT-----IGYLEQepklNPEH-----T 85
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEifynnqAITDDNFEklrkhIGIVFQ----NPDNqfvgsI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 86 VRESVeeSMGAVNAA---KKRLEEVYElyAAEDADFDALAaeqaeleaiiatagtDSEHQleiaadalrlpawdakigVL 162
Cdd:PRK13648 101 VKYDV--AFGLENHAvpyDEMHRRVSE--ALKQVDMLERA---------------DYEPN------------------AL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 163 SGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG----TVVAITHDryfLDNAAE--WILELDRG 234
Cdd:PRK13648 144 SGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehniTIISITHD---LSEAMEadHVIVMNKG 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
324-507 |
2.42e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 61.77 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFG-----DRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV------------ 385
Cdd:PRK13641 4 KFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHItpetgnknlkkl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 386 --KMAFVDQARDALADQKTVWEDIsggldiinvgKFqmasrayaGRFNFNGADQQ---------KKVG-----------T 443
Cdd:PRK13641 84 rkKVSLVFQFPEAQLFENTVLKDV----------EF--------GPKNFGFSEDEakekalkwlKKVGlsedliskspfE 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 444 LSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEF--AG-TVMVISHDrwfLDRIA 507
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqkAGhTVILVTHN---MDDVA 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-499 |
2.52e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 62.78 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKS-TLLKIM-------AGVDKEI--EGE---ALPMPGLT------IGYLEQEP- 78
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpdpaAHPSGSIlfDGQdllGLSERELRrirgnrIAMIFQEPm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 79 -KLNPEHTVRESVEESMgavnaakkRLEEvyelyaaedadfdALAAEQAELEAIiatagtdsE--HQLEIAADALRLPAW 155
Cdd:COG4172 103 tSLNPLHTIGKQIAEVL--------RLHR-------------GLSGAAARARAL--------EllERVGIPDPERRLDAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 156 DAKigvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFPGTVVAITHD----RYFLDNAAew 227
Cdd:COG4172 154 PHQ---LSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqAQILDLLKDLQRELGMALLLITHDlgvvRRFADRVA-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 228 ileldrgrgipwkgnystwLEQKGERLaqeqksEEAHAKAL---------KKELEWSRQNPKARQAKSKSRLARFEELSd 298
Cdd:COG4172 229 -------------------VMRQGEIV------EQGPTAELfaapqhpytRKLLAAEPRGDPRPVPPDAPPLLEARDLK- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 299 VEYqkrnetqeifiPVAER-LGSQVFEFKNVsksfgdrlliDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEkPDSG 377
Cdd:COG4172 283 VWF-----------PIKRGlFRRTVGHVKAV----------DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 378 EVVI-GQTVkmafvdQARDALADQK--------------------TVWEDISGGLDIINVGKfqmasrayagrfnfNGAD 436
Cdd:COG4172 341 EIRFdGQDL------DGLSRRALRPlrrrmqvvfqdpfgslsprmTVGQIIAEGLRVHGPGL--------------SAAE 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 437 QQKKVGTL------------------SGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV-------ETLRALEDallEFAG 491
Cdd:COG4172 401 RRARVAEAleevgldpaarhryphefSGGQRQRIAIARALILEPKLLVLDEPTSALDVsvqaqilDLLRDLQR---EHGL 477
|
....*...
gi 518484691 492 TVMVISHD 499
Cdd:COG4172 478 AYLFISHD 485
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
11-251 |
2.64e-10 |
|
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: 62.81 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 11 VSKTVPPK-RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLTIGYLEQEPKLNPEHT 85
Cdd:TIGR02203 336 VTFRYPGRdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILldghDLADYTLASLRRQVALVSQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 86 V--RESVeesmgAVNAAKKRLEEVyelyaaEDADFDAlAAEQAELEAIIatagtdsehqleiaaDALRLpAWDAKIGV-- 161
Cdd:TIGR02203 416 VlfNDTI-----ANNIAYGRTEQA------DRAEIER-ALAAAYAQDFV---------------DKLPL-GLDTPIGEng 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 162 --LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRF-PG-TVVAITHDRYFLDNAAEwILELDRGRgI 237
Cdd:TIGR02203 468 vlLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLmQGrTTLVIAHRLSTIEKADR-IVVMDDGR-I 545
|
250
....*....|....
gi 518484691 238 PWKGNYSTWLEQKG 251
Cdd:TIGR02203 546 VERGTHNELLARNG 559
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-195 |
2.75e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 60.80 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIM-------------AGVDKEIEGEALPMPGLT----IGYLEQEPKLNP 82
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprsgtlniAGNHFDFSKTPSDKAIRElrrnVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 83 EHTVRESVEEsmgavnAAKKRLeevyelyaaedadfdALAAEQAELEA--IIATAgtdsehQLEIAADALRLPawdakig 160
Cdd:PRK11124 96 HLTVQQNLIE------APCRVL---------------GLSKDQALARAekLLERL------RLKPYADRFPLH------- 141
|
170 180 190
....*....|....*....|....*....|....*
gi 518484691 161 vLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAE 195
Cdd:PRK11124 142 -LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-237 |
2.78e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 61.38 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 4 YVYSmnrvsKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEalpmpgLTI-GYleqepKLNP 82
Cdd:PRK13641 10 YIYS-----PGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGT------ITIaGY-----HITP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 83 EhTVRESVEESMGAVNAAKKRLE-EVYELYAAEDADFDALAAEQAELEAIIAtagtdsehqleiaadALRlpaWDAKIGV 161
Cdd:PRK13641 74 E-TGNKNLKKLRKKVSLVFQFPEaQLFENTVLKDVEFGPKNFGFSEDEAKEK---------------ALK---WLKKVGL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 162 -----------LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES-VEWLEVFL--QRFPGTVVAITHDryfLDNAAEW 227
Cdd:PRK13641 135 sedliskspfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKdyQKAGHTVILVTHN---MDDVAEY 211
|
250
....*....|...
gi 518484691 228 ---ILELDRGRGI 237
Cdd:PRK13641 212 addVLVLEHGKLI 224
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
18-222 |
2.83e-10 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 60.74 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK-EIEGEalpmpglTIGYLEQE-PKLNPEHTVRESVEESMG 95
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyEVTSG-------TILFKGQDlLELEPDERARAGLFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 96 AVnaakkrlEEVYELYAAEDADFDALAAEQAELEAIIATAgtDSEHQLEIAADALRLPAWDAKIGV---LSGGEKRRVAL 172
Cdd:TIGR01978 85 YP-------EEIPGVSNLEFLRSALNARRSARGEEPLDLL--DFEKLLKEKLALLDMDEEFLNRSVnegFSGGEKKRNEI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518484691 173 CRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRF--PGT-VVAITHDRYFLD 222
Cdd:TIGR01978 156 LQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLrePDRsFLIITHYQRLLN 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-239 |
3.76e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.70 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV-----DKEIEGEALpmpgltigyleqepkLNPEHTVRESVEEsm 94
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVY---------------LDGQDIFKMDVIE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 95 gavnaAKKRLEEVYEL-----------YAAEDADFDALAAEQAELEAIIATAGTDSEHQLEIAaDALRLPAwdakiGVLS 163
Cdd:PRK14247 80 -----LRRRVQMVFQIpnpipnlsifeNVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVK-DRLDAPA-----GKLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 164 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLE-VFLQ-RFPGTVVAITHdryFLDNAA---EWILELDRGRGIP 238
Cdd:PRK14247 149 GGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIEsLFLElKKDMTIVLVTH---FPQQAArisDYVAFLYKGQIVE 225
|
.
gi 518484691 239 W 239
Cdd:PRK14247 226 W 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
332-509 |
4.48e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.90 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 332 FGDRLLIDnLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTV---------------KMAFVDQARDA 396
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsstskqkeikpvrkKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 397 LADQKTVWEDISGGLDIINVGKfQMASRAYAGRFNFNGADQ---QKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSND 473
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNFGIPK-EKAEKIAAEKLEMVGLADefwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518484691 474 LD----VETLRALEdALLEFAGTVMVISHdrwFLDRIATH 509
Cdd:PRK13643 175 LDpkarIEMMQLFE-SIHQSGQTVVLVTH---LMDDVADY 210
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
324-475 |
4.79e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.40 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSF-GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVkmafVDQA----RD--- 395
Cdd:PRK11650 5 KLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV----VNELepadRDiam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 396 -----ALADQKTVWEDISGGLDIINVGKFQMASR-AYAGRFNFNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDE 469
Cdd:PRK11650 81 vfqnyALYPHMSVRENMAYGLKIRGMPKAEIEERvAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
....*.
gi 518484691 470 PSNDLD 475
Cdd:PRK11650 161 PLSNLD 166
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
16-237 |
5.29e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 60.39 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 16 PPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEALPMPGLT-----IGYLEQepklNPEH 84
Cdd:PRK13632 19 NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKpqsgeiKIDGITISKENLKeirkkIGIIFQ----NPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 85 T-VRESVEESMgAVNAAKKRLeevyelyaaedadfdalaaEQAELEAII--ATAGTDSEHQLEiaadalRLPAWdakigv 161
Cdd:PRK13632 95 QfIGATVEDDI-AFGLENKKV-------------------PPKKMKDIIddLAKKVGMEDYLD------KEPQN------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 162 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVEWLEVFLQRFPGTVVAITHDryfLDNA--AEWILELDRGR 235
Cdd:PRK13632 143 LSGGQKQRVAIASVLALNPEIIIFDESTSMLDPkgkrEIKKIMVDLRKTRKKTLISITHD---MDEAilADKVIVFSEGK 219
|
..
gi 518484691 236 GI 237
Cdd:PRK13632 220 LI 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
332-475 |
5.68e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.41 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 332 FGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVV---------------IGQTVKMAFVDqarda 396
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwqgkpldyskrgllaLRQQVATVFQD----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 397 lADQKTVWEDISG----GLDIINVGKFQMASR-------AYAGRFnfngadQQKKVGTLSGGERGRLHLAKTLIAGGNVL 465
Cdd:PRK13638 86 -PEQQIFYTDIDSdiafSLRNLGVPEAEITRRvdealtlVDAQHF------RHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170
....*....|
gi 518484691 466 LLDEPSNDLD 475
Cdd:PRK13638 159 LLDEPTAGLD 168
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-218 |
5.95e-10 |
|
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: 62.24 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKI---MAGVDKEIEGEALPMPGLTIGYLEQEPKLNPEHTVRESveesmg 95
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAllrLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFS------ 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 96 avNAAKKRLEEvYELYAAEDAdfdALAAEQAELEAIIatagtdsehqlEIAADALRLPAWDAKIgVLSGGEKRRVALCRL 175
Cdd:TIGR01271 1306 --GTFRKNLDP-YEQWSDEEI---WKVAEEVGLKSVI-----------EQFPDKLDFVLVDGGY-VLSNGHKQLMCLARS 1367
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518484691 176 LLSKPDMLLLDEPTNHLDAESVEWLEVFL-QRFPGTVVAITHDR 218
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIRKTLkQSFSNCTVILSEHR 1411
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-235 |
6.12e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.20 E-value: 6.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 1 MAQYVYSMNRVSKTVP-PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV--DKEIEGEALPMPGLTIGyleqe 77
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllPDDNPNSKITVDGITLT----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 78 pklnpEHTVREsVEESMGAVnaakkrleevyelYAAEDADFdalaaeqaeleaIIATAGTDSEHQLE-----------IA 146
Cdd:PRK13640 76 -----AKTVWD-IREKVGIV-------------FQNPDNQF------------VGATVGDDVAFGLEnravprpemikIV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 147 ADALR----LPAWDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG----TVVAITHDr 218
Cdd:PRK13640 125 RDVLAdvgmLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknnlTVISITHD- 203
|
250
....*....|....*....
gi 518484691 219 yfLDNA--AEWILELDRGR 235
Cdd:PRK13640 204 --IDEAnmADQVLVLDDGK 220
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-196 |
6.39e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.82 E-value: 6.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGvdkEIEGEALPMPGLT------------IGYLEQEPKLNPEHT 85
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG---RIQGNNFTGTILAnnrkptkqilkrTGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 86 VRESVeesmgaVNAAKKRLEEvyelyaAEDADFDALAAEqaeleAIIATAGTDSEHQLEIAADALRlpawdakiGVlSGG 165
Cdd:PLN03211 157 VRETL------VFCSLLRLPK------SLTKQEKILVAE-----SVISELGLTKCENTIIGNSFIR--------GI-SGG 210
|
170 180 190
....*....|....*....|....*....|.
gi 518484691 166 EKRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
Cdd:PLN03211 211 ERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-217 |
6.89e-10 |
|
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: 60.45 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 11 VSKTVPPKRQILK---DISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKE---IEGEA-------LPMP--------GL 69
Cdd:COG0444 7 LKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEIlfdgedlLKLSekelrkirGR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 70 TIGYLEQEPK--LNPEHTVRESVEESMgavnaakkrleEVYELYAAEDADfdalaaeqaeleaiiatagtdsehqlEIAA 147
Cdd:COG0444 87 EIQMIFQDPMtsLNPVMTVGDQIAEPL-----------RIHGGLSKAEAR--------------------------ERAI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 148 DALR---LPAWDAKIGV----LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAeSVEW--LEVF--LQR-FPGTVVAIT 215
Cdd:COG0444 130 ELLErvgLPDPERRLDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDV-TIQAqiLNLLkdLQReLGLAILFIT 208
|
..
gi 518484691 216 HD 217
Cdd:COG0444 209 HD 210
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
315-510 |
6.96e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.68 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 315 AERLGSQVFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLA-------GKEKPDSGEVVIGQTV-- 385
Cdd:PRK14246 3 AGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFGKDIfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 386 --------KMAFVDQARDALAdQKTVWEDIS------GGLDIINVGKFQMASRAYAGRFNFNGADQQKKVGTLSGGERGR 451
Cdd:PRK14246 83 idaiklrkEVGMVFQQPNPFP-HLSIYDNIAyplkshGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518484691 452 LHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAG--TVMVISHDRWFLDRIATHI 510
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYV 222
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-217 |
7.58e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 59.47 E-value: 7.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVdkeIEGEalpmpgltigyleqepklnpehtvresveesmGAVNAAK 101
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL---LPGQ--------------------------------GEILLNG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 102 KRLEevyELYAAEDADFDALAAEQAELEAIIAT---------AGTDSEHQ---LEIAADALRLpawDAK----IGVLSGG 165
Cdd:COG4138 57 RPLS---DWSAAELARHRAYLSQQQSPPFAMPVfqylalhqpAGASSEAVeqlLAQLAEALGL---EDKlsrpLTQLSGG 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 166 EKRRVALCRLLL-----SKPD--MLLLDEPTNHLDAESVEWLEVFLQRFP---GTVVAITHD 217
Cdd:COG4138 131 EWQRVRLAAVLLqvwptINPEgqLLLLDEPMNSLDVAQQAALDRLLRELCqqgITVVMSSHD 192
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-224 |
8.10e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 8.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 21 ILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaLPMPGLTI-----GYLEQ------EPKLNPEHTVRES 89
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGE-ILFERQSIkkdlcTYQKQlcfvghRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 90 VeesmgavnaakkrleevyeLYaaeDADFDALAAEQAELEAIIATagtdsEHQLeiaadalrlpawDAKIGVLSGGEKRR 169
Cdd:PRK13540 95 C-------------------LY---DIHFSPGAVGITELCRLFSL-----EHLI------------DYPCGLLSSGQKRQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 170 VALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFP---GTVVAITHDRYFLDNA 224
Cdd:PRK13540 136 VALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRakgGAVLLTSHQDLPLNKA 193
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
319-510 |
9.07e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 9.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 319 GSQVFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG------------QTVK 386
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGgnpcarltpakaHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 387 MAFVDQARDALADQkTVWEDISGGLdiinvGKFQMASRAYAGRFNFNGA--DQQKKVGTLSGGERGRLHLAKTLIAGGNV 464
Cdd:PRK15439 88 IYLVPQEPLLFPNL-SVKENILFGL-----PKRQASMQKMKQLLAALGCqlDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518484691 465 LLLDEPSNDL---DVETLRALEDALLEFAGTVMVISHDRWFLDRIATHI 510
Cdd:PRK15439 162 LILDEPTASLtpaETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRI 210
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
324-508 |
9.51e-10 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 58.66 E-value: 9.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGD--RLLIDNLSFNVPAGAIVGIIGPNGAGKST----LFKLLagkeKPDSGEVVIG----QTV-------K 386
Cdd:cd03244 4 EFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDgvdiSKIglhdlrsR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 387 MAFVDQ-----------------------ARDALADQ--KTVWEDISGGLD--IINVGKFqmasrayagrfnfngadqqk 439
Cdd:cd03244 80 ISIIPQdpvlfsgtirsnldpfgeysdeeLWQALERVglKEFVESLPGGLDtvVEEGGEN-------------------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518484691 440 kvgtLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDAL-LEFAG-TVMVISHdrwfldRIAT 508
Cdd:cd03244 140 ----LSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIrEAFKDcTVLTIAH------RLDT 200
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-222 |
9.67e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 9.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKimagvdkEIEGEALPMPGLTIGYLEQEPkLNPEHTVRESVeesmgav 97
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLR-------LLAGALKGTPVAGCVDVPDNQ-FGREASLIDAI------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 98 naakkrleevyelyaAEDADFDAlAAEqaeleaIIATAGTdsehqleiaADAlrlPAWDAKIGVLSGGEKRRVALCRLLL 177
Cdd:COG2401 107 ---------------GRKGDFKD-AVE------LLNAVGL---------SDA---VLWLRRFKELSTGQKFRFRLALLLA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518484691 178 SKPDMLLLDEPTNHLDAE-----SVEWLEvFLQRFPGTVVAITHDRYFLD 222
Cdd:COG2401 153 ERPKLLVIDEFCSHLDRQtakrvARNLQK-LARRAGITLVVATHHYDVID 201
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-216 |
9.92e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.40 E-value: 9.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKI---MAGVDKEI--------EGEALPMPGL-------TIGYLEQEPk 79
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSinrMNDLNPEVtitgsivyNGHNIYSPRTdtvdlrkEIGMVFQQP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 80 lNP-EHTVRESVeesmgavnaakkrleeVYELYAAEDADFDAL--AAEQAELEAIIATAGTDSEHqleiaadalrlpawD 156
Cdd:PRK14239 96 -NPfPMSIYENV----------------VYGLRLKGIKDKQVLdeAVEKSLKGASIWDEVKDRLH--------------D 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 157 AKIGvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLE--VFLQRFPGTVVAITH 216
Cdd:PRK14239 145 SALG-LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEetLLGLKDDYTMLLVTR 205
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-235 |
1.06e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 59.62 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 8 MNRVSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpMPGLTIGYLEQEPKL------- 80
Cdd:PRK13644 4 LENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVL-VSGIDTGDFSKLQGIrklvgiv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 81 --NPE-HTVRESVEESMGavnaakkrleevyelYAAEDadfdaLAAEQAELEAIIATAgtdsehQLEIAADALRLPAWDA 157
Cdd:PRK13644 83 fqNPEtQFVGRTVEEDLA---------------FGPEN-----LCLPPIEIRKRVDRA------LAEIGLEKYRHRSPKT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 158 kigvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEW-LEVF--LQRFPGTVVAITHDRYFLdNAAEWILELDRG 234
Cdd:PRK13644 137 ----LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAvLERIkkLHEKGKTIVYITHNLEEL-HDADRIIVMDRG 211
|
.
gi 518484691 235 R 235
Cdd:PRK13644 212 K 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-216 |
1.24e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 59.81 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 9 NRVSKTVP-PKRQI--LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE---------ALPMPGLT-----I 71
Cdd:PRK11153 5 KNISKVFPqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRvlvdgqdltALSEKELRkarrqI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 72 GYLEQEPKLNPEHTVRESVEESMGAVNAAK----KRLEEVYELyaaedadfdalaaeqaeleaiiatagtdsehqLEIAA 147
Cdd:PRK11153 85 GMIFQHFNLLSSRTVFDNVALPLELAGTPKaeikARVTELLEL--------------------------------VGLSD 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 148 DALRLPAwdakigVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVewLEVF--LQRFPG-TVVAITH 216
Cdd:PRK11153 133 KADRYPA------QLSGGQKQRVAIARALASNPKVLLCDEATSALDPAttrSI--LELLkdINRELGlTIVLITH 199
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-193 |
1.25e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.83 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 26 SLSFFPGAKIGVLGLNGSGKSTLLKIMAGV------DKEIEGE---ALPMPGLTIGYLEQEPKLNPEHTVRESVeeSMGA 96
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFltpasgSLTLNGQdhtTTPPSRRPVSMLFQENNLFSHLTVAQNI--GLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 97 VNAAKkrleevyelyaaedadfdaLAAEQAELEAIIAtagtdseHQLEIAADALRLPawdakiGVLSGGEKRRVALCRLL 176
Cdd:PRK10771 97 NPGLK-------------------LNAAQREKLHAIA-------RQMGIEDLLARLP------GQLSGGQRQRVALARCL 144
|
170
....*....|....*..
gi 518484691 177 LSKPDMLLLDEPTNHLD 193
Cdd:PRK10771 145 VREQPILLLDEPFSALD 161
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
330-511 |
1.59e-09 |
|
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: 58.00 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 330 KSFGDRLLIDnlsFNVPagaIVGIIGPNGAGKSTLFKLL-------------AGKEKPD---SGEVvIGQtVKMAFvdqa 393
Cdd:cd03240 10 RSFHERSEIE---FFSP---LTLIVGQNGAGKTTIIEALkyaltgelppnskGGAHDPKlirEGEV-RAQ-VKLAF---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 394 RDALADQKTVWEDISGGLDIINVGKFQMASRAYAGRfnfngadqqkkvGTLSGGERG------RLHLAKTLIAGGNVLLL 467
Cdd:cd03240 78 ENANGKKYTITRSLAILENVIFCHQGESNWPLLDMR------------GRCSGGEKVlasliiRLALAETFGSNCGILAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518484691 468 DEPSNDLDVETLR-ALEDALLEFAGT----VMVISHDRWFLDRiATHIL 511
Cdd:cd03240 146 DEPTTNLDEENIEeSLAEIIEERKSQknfqLIVITHDEELVDA-ADHIY 193
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
335-515 |
1.90e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.68 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 335 RLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGkEKPDS----GEVVIGQTV----KMAFVDQARdaLADQKTVWED 406
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprGARVTGDVTlngePLAAIDAPR--LARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 407 IS------GGLDIINVGKFQMASRAYAGR----------FNFNGADQ--QKKVGTLSGGERGRLHLAKTL---------I 459
Cdd:PRK13547 91 AAqpafafSAREIVLLGRYPHARRAGALThrdgeiawqaLALAGATAlvGRDVTTLSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518484691 460 AGGNVLLLDEPSNDLD-------VETLRALEDallEFAGTVMVISHDRWFLDRIATHI-LAAEG 515
Cdd:PRK13547 171 QPPRYLLLDEPTAALDlahqhrlLDTVRRLAR---DWNLGVLAIVHDPNLAARHADRIaMLADG 231
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
324-488 |
2.00e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 58.65 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRL---------LIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI------------- 381
Cdd:PRK15112 6 EVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIddhplhfgdysyr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 382 GQTVKMAFVDQARDALADQKtvwedISGGLDIINVGKFQMASRAYAGRFNfngaDQQKKVG-----------TLSGGERG 450
Cdd:PRK15112 86 SQRIRMIFQDPSTSLNPRQR-----ISQILDFPLRLNTDLEPEQREKQII----ETLRQVGllpdhasyyphMLAPGQKQ 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 518484691 451 RLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLE 488
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLE 194
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-286 |
2.27e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 59.97 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 11 VSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIM-------AGVDKeIEGE---ALPMPGL--TIGYLEQEP 78
Cdd:PRK13657 340 VSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRIL-IDGTdirTVTRASLrrNIAVVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 79 KL-NpeHTVRESVeeSMGAVNAAkkrLEEVYElyaaedadfdalAAEQAELEAIIATagtdsehqleiaadalRLPAWDA 157
Cdd:PRK13657 419 GLfN--RSIEDNI--RVGRPDAT---DEEMRA------------AAERAQAHDFIER----------------KPDGYDT 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 158 KIG----VLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWL-----EVFLQRfpgTVVAITHDRYFLDNAAEwI 228
Cdd:PRK13657 464 VVGergrQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVkaaldELMKGR---TTFIIAHRLSTVRNADR-I 539
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 229 LELDRGRGIPwKGNYSTwLEQKGERLAqeqksEEAHAKALKKELEwsRQNPKARQAKS 286
Cdd:PRK13657 540 LVFDNGRVVE-SGSFDE-LVARGGRFA-----ALLRAQGMLQEDE--RRKQPAAEGAN 588
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
322-499 |
2.51e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 58.25 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFK------------------LLAGKE--KPDSGEVVI 381
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndlipgfrvegkvTFHGKNlyAPDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 382 GQTVKMAFvdQARDALAdqKTVWEDISGGLDI----INVGKFQMASRAYAGRFNfNGADQQKKVG-TLSGGERGRLHLAK 456
Cdd:PRK14243 90 RRRIGMVF--QKPNPFP--KSIYDNIAYGARIngykGDMDELVERSLRQAALWD-EVKDKLKQSGlSLSGGQQQRLCIAR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518484691 457 TLIAGGNVLLLDEPSNDLD-VETLRaLEDALLEFAG--TVMVISHD 499
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDpISTLR-IEELMHELKEqyTIIIVTHN 209
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-217 |
2.75e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.02 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 25 ISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVdkeiegeaLPMPGltigyleqepklnpEHTVRESVEESMGAVNAAKKRL 104
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL--------LPGSG--------------SIQFAGQPLEAWSAAELARHRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 105 eevyelYAAEDAD-------FDALAAEQAELeaiiaTAGTDSEHQLEIAADALRLpawDAK----IGVLSGGEKRRVALC 173
Cdd:PRK03695 73 ------YLSQQQTppfampvFQYLTLHQPDK-----TRTEAVASALNEVAEALGL---DDKlgrsVNQLSGGEWQRVRLA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518484691 174 RLLL-----SKPD--MLLLDEPTNHLDAESVEWLEVFLQRFP---GTVVAITHD 217
Cdd:PRK03695 139 AVVLqvwpdINPAgqLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-222 |
3.28e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 57.77 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK-EI-EGEA-------LPMP-----GLTIGYLEQEPKLNPEH 84
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyEVtSGSIlldgediLELSpderaRAGIFLAFQYPVEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 85 TVRESVEESMGAVnaakkRLEEVyelyaaEDADFDALAAEQAELeaiiatagtdsehqLEIAADALRLPawdakIGV-LS 163
Cdd:COG0396 93 SVSNFLRTALNAR-----RGEEL------SAREFLKLLKEKMKE--------------LGLDEDFLDRY-----VNEgFS 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 164 GGEKRRVALCRLLLSKPDMLLLDEPTNHLD-------AESVEWLevflqRFPGT-VVAITHDRYFLD 222
Cdd:COG0396 143 GGEKKRNEILQMLLLEPKLAILDETDSGLDidalrivAEGVNKL-----RSPDRgILIITHYQRILD 204
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-194 |
3.58e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.86 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 15 VPPKR-QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG------VDKEIEGEALPMPGLTI----GYLEQEPKLNPE 83
Cdd:PLN03140 888 VTEDRlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGrktggyIEGDIRISGFPKKQETFarisGYCEQNDIHSPQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 84 HTVRESVeesmgavnaakkrleevyeLYAAedadFDALAAEQAELEAIIATagtDSEHQLeIAADALRlpawDAKIGV-- 161
Cdd:PLN03140 968 VTVRESL-------------------IYSA----FLRLPKEVSKEEKMMFV---DEVMEL-VELDNLK----DAIVGLpg 1016
|
170 180 190
....*....|....*....|....*....|....*.
gi 518484691 162 ---LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDA 194
Cdd:PLN03140 1017 vtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-235 |
3.69e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 57.79 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMagvdkeiegEALPMPGLTIGYLEQEPKLNPEHTVreSVEESMGAV--NA 99
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHM---------NALLIPSEGKVYVDGLDTSDEENLW--DIRNKAGMVfqNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 100 AKKRLEEVYElyaaEDADF--DALAAEQAELEAIIatagtdsEHQLEiaadalRLPAWDAK---IGVLSGGEKRRVALCR 174
Cdd:PRK13633 95 DNQIVATIVE----EDVAFgpENLGIPPEEIRERV-------DESLK------KVGMYEYRrhaPHLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 175 LLLSKPDMLLLDEPTNHLDA----ESVEWLEVFLQRFPGTVVAITHdryFLDNAAEW--ILELDRGR 235
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPsgrrEVVNTIKELNKKYGITIILITH---YMEEAVEAdrIIVMDSGK 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-197 |
4.82e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.21 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEA---------LPMPGLT---IGYLEQEPKLnpehTV 86
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedislLPLHARArrgIGYLPQEASI----FR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 87 RESVEESMGAVnaakkrleevyeLYAAEDadfdaLAAEQAELEAiiatagtdSEHQLEIAADALRlpawDAKIGVLSGGE 166
Cdd:PRK10895 92 RLSVYDNLMAV------------LQIRDD-----LSAEQREDRA--------NELMEEFHIEHLR----DSMGQSLSGGE 142
|
170 180 190
....*....|....*....|....*....|.
gi 518484691 167 KRRVALCRLLLSKPDMLLLDEPTNHLDAESV 197
Cdd:PRK10895 143 RRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-218 |
4.84e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 58.42 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 1 MAQYVYSMNRVSKTVPPKrQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpMPGLTIGYL--EQEP 78
Cdd:PRK09452 10 SLSPLVELRGISKSFDGK-EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM-LDGQDITHVpaENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 79 --------KLNPEHTVRESVeesmgavnAAKKRLEEVYELYAAEDAdFDALAAEQAEleaiiatagtdsehqlEIAadal 150
Cdd:PRK09452 88 vntvfqsyALFPHMTVFENV--------AFGLRMQKTPAAEITPRV-MEALRMVQLE----------------EFA---- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 151 rlpawDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEV---FLQRFPG-TVVAITHDR 218
Cdd:PRK09452 139 -----QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNelkALQRKLGiTFVFVTHDQ 205
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-251 |
5.12e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.88 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKST---LLKIMAGVDkeiEGEALpMPGLTIgyleQEPKLNpehTVRESVeesmgavn 98
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTianLLTRFYDID---EGEIL-LDGHDL----RDYTLA---SLRNQV-------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 99 aakkrleevyelyaaedadfdALAAEQAEL--EAI---IATAGTD--SEHQLEIAADAL-------RLP-AWDAKIG--- 160
Cdd:PRK11176 420 ---------------------ALVSQNVHLfnDTIannIAYARTEqySREQIEEAARMAyamdfinKMDnGLDTVIGeng 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 161 -VLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG--TVVAITHDRYFLDNAAEwILELDRGRgI 237
Cdd:PRK11176 479 vLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAHRLSTIEKADE-ILVVEDGE-I 556
|
250
....*....|....
gi 518484691 238 PWKGNYSTWLEQKG 251
Cdd:PRK11176 557 VERGTHAELLAQNG 570
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
326-498 |
5.44e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDA-------- 396
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFqGKEIDFKSSKEALENgismvhqe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 397 --LADQKTVWEDI------SGGLdIINVGKFQMASRAYAGRFNFNgADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLD 468
Cdd:PRK10982 82 lnLVLQRSVMDNMwlgrypTKGM-FVDQDKMYRDTKAIFDELDID-IDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190
....*....|....*....|....*....|...
gi 518484691 469 EPSNDL---DVETLRALEDALLEFAGTVMVISH 498
Cdd:PRK10982 160 EPTSSLtekEVNHLFTIIRKLKERGCGIVYISH 192
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-189 |
5.56e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.49 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEALPMP--------GltIGYLEQEPK---LNPEH 84
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPadsgeiRLDGKPVRIRsprdairaG--IAYVPEDRKgegLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 85 TVRESVeeSMGAVNAAKKRLeevyelyaaedadFDALAAEQAELEAIIAtagtdsehQLEIaadalRLPAWDAKIGVLSG 164
Cdd:COG1129 346 SIRENI--TLASLDRLSRGG-------------LLDRRRERALAEEYIK--------RLRI-----KTPSPEQPVGNLSG 397
|
170 180
....*....|....*....|....*
gi 518484691 165 GEKRRVALCRLLLSKPDMLLLDEPT 189
Cdd:COG1129 398 GNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
338-499 |
5.99e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 57.67 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 338 IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAfvDQARDALADQKT--VWEDISGGLD-- 412
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDLLKA--DPEAQKLLRQKIqiVFQNPYGSLNpr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 413 -----------IIN--VGKFQMASRAyagrfnfngADQQKKVG-----------TLSGGERGRLHLAKTLIAGGNVLLLD 468
Cdd:PRK11308 109 kkvgqileeplLINtsLSAAERREKA---------LAMMAKVGlrpehydryphMFSGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190
....*....|....*....|....*....|....*
gi 518484691 469 EPSNDLDV----ETLRALEDALLEFAGTVMVISHD 499
Cdd:PRK11308 180 EPVSALDVsvqaQVLNLMMDLQQELGLSYVFISHD 214
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
341-498 |
6.11e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.40 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 341 LSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAfvDQARDA--LADQKTVWEDISG--GLDIIN 415
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATRG--DRSRFMayLGHLPGLKADLSTleNLHFLC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 416 VGKFQMASRAYAGRFNFNG-AD-QQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALE---DALLEFA 490
Cdd:PRK13543 108 GLHGRRAKQMPGSALAIVGlAGyEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNrmiSAHLRGG 187
|
....*...
gi 518484691 491 GTVMVISH 498
Cdd:PRK13543 188 GAALVTTH 195
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
338-508 |
6.36e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.41 E-value: 6.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 338 IDNLSFNVPAGAIVGIIGPNGAGKST-------LFKLLAGKEKPDsGEVVIGQTV-----KMAFVDQARDALADQKTVWE 405
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTtarlidgLFEEFEGKVKID-GELLTAENVwnlrrKIGMVFQNPDNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 406 DISGGLDIINVGKFQMASRAYAGRFNFNGAD-QQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD----VETLR 480
Cdd:PRK13642 102 DVAFGMENQGIPREEMIKRVDEALLAVNMLDfKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDptgrQEIMR 181
|
170 180
....*....|....*....|....*...
gi 518484691 481 ALEDALLEFAGTVMVISHDrwfLDRIAT 508
Cdd:PRK13642 182 VIHEIKEKYQLTVLSITHD---LDEAAS 206
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
322-485 |
7.31e-09 |
|
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: 55.71 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSF----GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPD--SGEVVI-GQTVKMAF----- 389
Cdd:cd03232 3 VLTWKNLNYTVpvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILInGRPLDKNFqrstg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 390 -VDQArDALADQKTVWEDIsggldiinvgKFQMASRAyagrfnfngadqqkkvgtLSGGERGRLHLAKTLIAGGNVLLLD 468
Cdd:cd03232 83 yVEQQ-DVHSPNLTVREAL----------RFSALLRG------------------LSVEQRKRLTIGVELAAKPSILFLD 133
|
170 180
....*....|....*....|....
gi 518484691 469 EPSNDLD-------VETLRALEDA 485
Cdd:cd03232 134 EPTSGLDsqaayniVRFLKKLADS 157
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-235 |
7.53e-09 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 55.96 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 21 ILKDISLSFFPGAKIGVLGLNGSGKSTLL------------KIMA-GVD-KEIEGEALPMpglTIGYLEQEPKLNpEHTV 86
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLlalfrlvelssgSILIdGVDiSKIGLHDLRS---RISIIPQDPVLF-SGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 87 RESVeesmgavnaakkrleevyelyaaedaDFDALAAEqAELEAIIATAGTDSEhqleIAADALRLpawDAKI----GVL 162
Cdd:cd03244 95 RSNL--------------------------DPFGEYSD-EELWQALERVGLKEF----VESLPGGL---DTVVeeggENL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 163 SGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWL-EVFLQRFPG-TVVAITH--------DRyfldnaaewILELD 232
Cdd:cd03244 141 SVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIqKTIREAFKDcTVLTIAHrldtiidsDR---------ILVLD 211
|
...
gi 518484691 233 RGR 235
Cdd:cd03244 212 KGR 214
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
316-528 |
8.12e-09 |
|
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: 58.80 E-value: 8.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 316 ERLGSQVFEFKNVSKSFGDRLLIDN---------------LSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVV 380
Cdd:TIGR00957 617 EELEPDSIERRTIKPGEGNSITVHNatftwardlpptlngITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVH 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 381 IGQTVkmAFVDQarDALADQKTVWEDISGGLDiINVGKFQMASRAYAGRFNFN---GADQQ---KKVGTLSGGERGRLHL 454
Cdd:TIGR00957 697 MKGSV--AYVPQ--QAWIQNDSLRENILFGKA-LNEKYYQQVLEACALLPDLEilpSGDRTeigEKGVNLSGGQKQRVSL 771
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518484691 455 AKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAG-----TVMVISHDRWFLDRIATHILAAEGDSQWTffdGNYQE 528
Cdd:TIGR00957 772 ARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGvlknkTRILVTHGISYLPQVDVIIVMSGGKISEM---GSYQE 847
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
11-217 |
8.60e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 57.40 E-value: 8.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 11 VSKTVPPKRQ---ILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGE---ALPMPGL-----TIGY 73
Cdd:COG1135 7 LSKTFPTKGGpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERptsgsvLVDGVdltALSERELraarrKIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 74 LEQEPKLNPEHTVRESVE---ESMGAvnAAKKRLEEVYELyaaedadfdalaaeqaeLEAIiataGtdsehqLEIAADAL 150
Cdd:COG1135 87 IFQHFNLLSSRTVAENVAlplEIAGV--PKAEIRKRVAEL-----------------LELV----G------LSDKADAY 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 151 rlPAwdakigVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVewLEVFL---QRFPGTVVAITHD 217
Cdd:COG1135 138 --PS------QLSGGQKQRVGIARALANNPKVLLCDEATSALDPEttrSI--LDLLKdinRELGLTIVLITHE 200
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-252 |
9.03e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.59 E-value: 9.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 2 AQYVYSMNRVSKTVPPKrQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVdKEIEGEALPMPGLT----------- 70
Cdd:PRK14246 7 AEDVFNISRLYLYINDK-AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRL-IEIYDSKIKVDGKVlyfgkdifqid 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 71 -------IGYLEQEPKLNPEHTVRESVEESMGAVNAAKKRleEVYELyaaedadfdalaaeqaeLEAIIATAGTDSEhql 143
Cdd:PRK14246 85 aiklrkeVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKR--EIKKI-----------------VEECLRKVGLWKE--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 144 eiAADALRLPAwdakiGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG--TVVAITHDRYFL 221
Cdd:PRK14246 143 --VYDRLNSPA-----SQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQV 215
|
250 260 270
....*....|....*....|....*....|.
gi 518484691 222 DNAAEWILELDRGRGIPWKGNYSTWLEQKGE 252
Cdd:PRK14246 216 ARVADYVAFLYNGELVEWGSSNEIFTSPKNE 246
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-234 |
9.62e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 56.56 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 3 QYVYSMNRVSKTVPpKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVdkeIEGEALP-----MPGLTIgylEQE 77
Cdd:PRK09984 2 QTIIRVEKLAKTFN-QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSAgshieLLGRTV---QRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 78 PKLnpehtvRESVEESMGAVNAAKKRLEEVYELYAAEDADFDALAA---------------EQAELEAIIATAGTDSEHQ 142
Cdd:PRK09984 75 GRL------ARDIRKSRANTGYIFQQFNLVNRLSVLENVLIGALGStpfwrtcfswftreqKQRALQALTRVGMVHFAHQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 143 leiaadalrlpawdaKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES----VEWLEVFLQRFPGTVVAITHDR 218
Cdd:PRK09984 149 ---------------RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESarivMDTLRDINQNDGITVVVTLHQV 213
|
250
....*....|....*.
gi 518484691 219 YFLDNAAEWILELDRG 234
Cdd:PRK09984 214 DYALRYCERIVALRQG 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-216 |
9.71e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 56.20 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIM-------AGV---------DKEIEGEALPMPGLT--IGYLEQEPk 79
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGArvegeilldGEDIYDPDVDVVELRrrVGMVFQKP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 80 lNP-EHTVRESVeeSMGA-VNAAKKRleevyelyaaedadfdalaaeqAELEAIIatagtdsEHQLEIAA------DALR 151
Cdd:COG1117 102 -NPfPKSIYDNV--AYGLrLHGIKSK----------------------SELDEIV-------EESLRKAAlwdevkDRLK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518484691 152 LPAWDakigvLSGGEKRRvaLC--RLLLSKPDMLLLDEPTNHLDAES---VEWLEVFL-QRFpgTVVAITH 216
Cdd:COG1117 150 KSALG-----LSGGQQQR--LCiaRALAVEPEVLLMDEPTSALDPIStakIEELILELkKDY--TIVIVTH 211
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
337-521 |
1.38e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 57.45 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 337 LIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQ----ARDALADQkTVWEDisggld 412
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQrpymTLGTLRDQ-IIYPD------ 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 413 iinvGKFQMASRAYagrfnfngADQ---------------QKKVG---------TLSGGERGRLHLAKTLIAGGNVLLLD 468
Cdd:TIGR00954 540 ----SSEDMKRRGL--------SDKdleqildnvqlthilEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518484691 469 EPSNDLDVETLRALEDALLEFAGTVMVISHdRWFLDRIATHILAAEGDSQWTF 521
Cdd:TIGR00954 608 ECTSAVSVDVEGYMYRLCREFGITLFSVSH-RKSLWKYHEYLLYMDGRGGYQF 659
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-217 |
1.42e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 56.63 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 16 PPKRQI--LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALPMpGLT-----IGYLE-------QEPKLN 81
Cdd:COG4586 30 REYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL-GYVpfkrrKEFARrigvvfgQRSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 82 PEHTVRESVEesmgaVNAAkkrleeVYELyaaEDADFDALAAEQAELeaiiatagtdsehqLEIaADALRLPawdakigV 161
Cdd:COG4586 109 WDLPAIDSFR-----LLKA------IYRI---PDAEYKKRLDELVEL--------------LDL-GELLDTP-------V 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 162 --LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFL----QRFPGTVVAITHD 217
Cdd:COG4586 153 rqLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLkeynRERGTTILLTSHD 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
19-193 |
1.49e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.49 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpmpgltigyLEQEP--KLNPEhTVRESVEESmga 96
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLL---------FEGEDisTLKPE-IYRQQVSYC--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 97 vnAAKKRL--EEVYElyaaeDADFDALAAEQAELEAIIAtagtDSEHQLEIAADALrlpawDAKIGVLSGGEKRRVALCR 174
Cdd:PRK10247 87 --AQTPTLfgDTVYD-----NLIFPWQIRNQQPDPAIFL----DDLERFALPDTIL-----TKNIAELSGGEKQRISLIR 150
|
170
....*....|....*....
gi 518484691 175 LLLSKPDMLLLDEPTNHLD 193
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALD 169
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-235 |
1.62e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.40 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 21 ILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEalpmpgLTIGYLEQEPKLNPEHTVRESVEESMGAVNAA 100
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGT------IQVGDIYIGDKKNNHELITNPYSKKIKNFKEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 101 KKRLEEV-----YELYA---AEDADFDALAAEQAELEAIIATAgtdseHQLEIAAdaLRLPAWDAKIGVLSGGEKRRVAL 172
Cdd:PRK13631 115 RRRVSMVfqfpeYQLFKdtiEKDIMFGPVALGVKKSEAKKLAK-----FYLNKMG--LDDSYLERSPFGLSGGQKRRVAI 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 173 CRLLLSKPDMLLLDEPTNHLDAE-SVEWLEVFL--QRFPGTVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKgEHEMMQLILdaKANNKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
18-218 |
1.93e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 56.27 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKE------IEGEALPMPGLT---IGYLEQEPKLNPEHTVRE 88
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPtegqifIDGEDVTHRSIQqrdICMVFQSYALFPHMSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 89 SVEES--MGAVNAA--KKRLEEVYELyaaedADFDALAaeqaeleaiiatagtdsehqleiaadalrlpawDAKIGVLSG 164
Cdd:PRK11432 98 NVGYGlkMLGVPKEerKQRVKEALEL-----VDLAGFE---------------------------------DRYVDQISG 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518484691 165 GEKRRVALCRLLLSKPDMLLLDEPTNHLDA-------ESVEWLEvflQRFPGTVVAITHDR 218
Cdd:PRK11432 140 GQQQRVALARALILKPKVLLFDEPLSNLDAnlrrsmrEKIRELQ---QQFNITSLYVTHDQ 197
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-193 |
2.11e-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: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 31 PGAKIGVLGLNGSGKSTLLKIMAGVDKeiegealpmPGLtiGYLEQEPKLnpehtvRESVEESMGavNAAKKRLEEVYE- 109
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLK---------PNL--GKFDDPPDW------DEILDEFRG--SELQNYFTKLLEg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 110 -LYAAEDADFDALAAEQAELEAIIATAGTDSEHQLEIAADALRL-PAWDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDE 187
Cdd:cd03236 86 dVKVIVKPQYVDLIPKAVKGKVGELLKKKDERGKLDELVDQLELrHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDE 165
|
....*.
gi 518484691 188 PTNHLD 193
Cdd:cd03236 166 PSSYLD 171
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-217 |
2.61e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 55.74 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE-------ALPMPGLTIGYLE-------QEP--KLNPE 83
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGElyyqgqdLLKADPEAQKLLRqkiqivfQNPygSLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 84 HTVRESVEESMgAVNAakkrleevyELYAAEdadfdalAAEQAelEAIIATAGTDSEHqleiaadALRLPAwdakigVLS 163
Cdd:PRK11308 109 KKVGQILEEPL-LINT---------SLSAAE-------RREKA--LAMMAKVGLRPEH-------YDRYPH------MFS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518484691 164 GGEKRRVALCRLLLSKPDMLLLDEPTNHLDAeSV--EWLEVF--LQRFPGTV-VAITHD 217
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDV-SVqaQVLNLMmdLQQELGLSyVFISHD 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-217 |
2.76e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 55.24 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 1 MAQYVYSMNRVSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLTIGYLEq 76
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILfdgkPIDYSRKGLMK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 77 epklnpehtvresVEESMGAVNAAKKrleevYELYAA---EDADFDALAAEQAELEAiiataGTDSEHQLEIAADAlrlP 153
Cdd:PRK13636 80 -------------LRESVGMVFQDPD-----NQLFSAsvyQDVSFGAVNLKLPEDEV-----RKRVDNALKRTGIE---H 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 154 AWDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFPGTVVAITHD 217
Cdd:PRK13636 134 LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-236 |
2.80e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 56.68 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 15 VPPKRQIL-KDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVdKEIEGEAL--PMPGlTIGYLEQEPKLNpEHTVRESVe 91
Cdd:TIGR00954 460 VTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGRLtkPAKG-KLFYVPQRPYMT-LGTLRDQI- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 92 esmgavnaakkrleevyeLYAAEDADFDALAAEQAELEAIIATagTDSEHQLEiaadalRLPAWDAK---IGVLSGGEKR 168
Cdd:TIGR00954 536 ------------------IYPDSSEDMKRRGLSDKDLEQILDN--VQLTHILE------REGGWSAVqdwMDVLSGGEKQ 589
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 169 RVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPGTVVAITHdRYFLDNAAEWILELDrGRG 236
Cdd:TIGR00954 590 RIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH-RKSLWKYHEYLLYMD-GRG 655
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
5-196 |
3.05e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.66 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 5 VYSMNRVSKTVPPK---RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG-VDKEI--EGEALP-MPGL------TI 71
Cdd:TIGR00956 759 IFHWRNLTYEVKIKkekRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErVTTGVitGGDRLVnGRPLdssfqrSI 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 72 GYLEQEPKLNPEHTVRESVEESmgavnaakKRLEEVYELYAAEDADFdalaaeqaeLEAIIATAGtdsehqLEIAADALr 151
Cdd:TIGR00956 839 GYVQQQDLHLPTSTVRESLRFS--------AYLRQPKSVSKSEKMEY---------VEEVIKLLE------MESYADAV- 894
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518484691 152 lpawdakIGV----LSGGEKRRVALCRLLLSKPDMLL-LDEPTNHLDAES 196
Cdd:TIGR00956 895 -------VGVpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-217 |
3.21e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.04 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDkEIEGEalpmpgltigyLEQEPKLnpeHTVRESVEESMGAVN 98
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN-ELESE-----------VRVEGRV---EFFNQNIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 99 AAKKRLEEVY---ELYAAEDADFDALAAE------QAELEAIIATAGTDSEHQLEIAaDALRLPAWDakigvLSGGEKRR 169
Cdd:PRK14258 85 RLRRQVSMVHpkpNLFPMSVYDNVAYGVKivgwrpKLEIDDIVESALKDADLWDEIK-HKIHKSALD-----LSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518484691 170 VALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQ----RFPGTVVAITHD 217
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslrlRSELTMVIVSHN 210
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
331-498 |
3.30e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 56.39 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 331 SFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKeKPDSGEVVI-GQTVKMAFVDQARDALA--------DQK 401
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKInGIELRELDPESWRKHLSwvgqnpqlPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 402 TVWEDISGGLDIINVGKFQMA-SRAYAGRF---NFNGADQQ--KKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD 475
Cdd:PRK11174 438 TLRDNVLLGNPDASDEQLQQAlENAWVSEFlplLPQGLDTPigDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180
....*....|....*....|....*
gi 518484691 476 VETLRALEDALLEFAG--TVMVISH 498
Cdd:PRK11174 518 AHSEQLVMQALNAASRrqTTLMVTH 542
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-251 |
4.61e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.87 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG----VDKEIEGEALPMPGLTI-------GYLEQEPKLNPEhTVR 87
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRhfdvSEGDIRFHDIPLTKLQLdswrsrlAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 88 ESVeeSMGAVNAAKKRLEEVYELYAAEDadfdalaaeqaeleaiiatagtdsehqleiaaDALRLP-AWDAKIG----VL 162
Cdd:PRK10789 407 NNI--ALGRPDATQQEIEHVARLASVHD--------------------------------DILRLPqGYDTEVGergvML 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 163 SGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES--------VEWLEvflQRfpgTVVAITHDRYFLDNAAEwILELDRG 234
Cdd:PRK10789 453 SGGQKQRISIARALLLNAEILILDDALSAVDGRTehqilhnlRQWGE---GR---TVIISAHRLSALTEASE-ILVMQHG 525
|
250
....*....|....*..
gi 518484691 235 rGIPWKGNYSTWLEQKG 251
Cdd:PRK10789 526 -HIAQRGNHDQLAQQSG 541
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-217 |
4.89e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 54.74 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 1 MAQYVYSMNRVSKTVPPKRQILK----------DISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PM 66
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGLFGrtvgvvkavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 67 PGLTIGYLE----------QEP--KLNPEHTVRESVEESMGA--VNAAKKRLEEVYELyaaedadfdalaaeqaeleaiI 132
Cdd:COG4608 83 TGLSGRELRplrrrmqmvfQDPyaSLNPRMTVGDIIAEPLRIhgLASKAERRERVAEL---------------------L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 133 ATAGTDSEHqleiaadALRLPawdakiGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFP 208
Cdd:COG4608 142 ELVGLRPEH-------ADRYP------HEFSGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQVLNLLEDLQDELG 208
|
....*....
gi 518484691 209 GTVVAITHD 217
Cdd:COG4608 209 LTYLFISHD 217
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
338-503 |
5.09e-08 |
|
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: 53.87 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 338 IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQARD-------ALADQK------TVW 404
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnrysvAYAAQKpwllnaTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 405 EDISGGlDIINVGKFQMASRAYAGRFNFN--GADQQKKVG----TLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVE- 477
Cdd:cd03290 97 ENITFG-SPFNKQRYKAVTDACSLQPDIDllPFGDQTEIGergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 175
|
170 180 190
....*....|....*....|....*....|
gi 518484691 478 TLRALEDALLEF----AGTVMVISHDRWFL 503
Cdd:cd03290 176 SDHLMQEGILKFlqddKRTLVLVTHKLQYL 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-235 |
5.33e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 54.24 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpMPGLTIGYleqepklnpehtvresveeSMGAVNA 99
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVL-WQGKPLDY-------------------SKRGLLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 100 AKKRLEEVYE------LYAAEDAD----FDALAAEQAELEAIIATAGT--DSEHqleiaadaLRlpawDAKIGVLSGGEK 167
Cdd:PRK13638 75 LRQQVATVFQdpeqqiFYTDIDSDiafsLRNLGVPEAEITRRVDEALTlvDAQH--------FR----HQPIQCLSHGQK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518484691 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPGT---VVAITHDRYFLDNAAEWILELDRGR 235
Cdd:PRK13638 143 KRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYVLRQGQ 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
338-487 |
7.45e-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: 55.79 E-value: 7.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 338 IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGE-VVIGQTV---------KMAFVDQArDALADQKT----- 402
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDaTVAGKSIltnisdvhqNMGYCPQF-DAIDDLLTgrehl 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 403 -VWEDISG--GLDIINVGKFQMAS---RAYAGRFnfngadqqkkVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV 476
Cdd:TIGR01257 2034 yLYARLRGvpAEEIEKVANWSIQSlglSLYADRL----------AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170
....*....|.
gi 518484691 477 ETLRALEDALL 487
Cdd:TIGR01257 2104 QARRMLWNTIV 2114
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
338-381 |
8.33e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.90 E-value: 8.33e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 518484691 338 IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI 381
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI 83
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-197 |
8.76e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 52.65 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 17 PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKE---IEGEalpmpgltIGYLEQEPKLNPEHTVRESVEES 93
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGD--------IHYNGIPYKEFAEKYPGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 94 mgavnaakkrleevyelyaAEDADFDALAAEQAeleaiiatagtdsehqLEIAADALRlpawDAKIGVLSGGEKRRVALC 173
Cdd:cd03233 90 -------------------EEDVHFPTLTVRET----------------LDFALRCKG----NEFVRGISGGERKRVSIA 130
|
170 180
....*....|....*....|....
gi 518484691 174 RLLLSKPDMLLLDEPTNHLDAESV 197
Cdd:cd03233 131 EALVSRASVLCWDNSTRGLDSSTA 154
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
324-499 |
1.05e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.55 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRL-----LIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEV------------------- 379
Cdd:PRK13651 4 KVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 380 ----VIGQTV--KMAFVDQARDAL------AD----QKTVWEDISGGLDIINVGKFQMASRAyAGRFNFNGADQ---QKK 440
Cdd:PRK13651 84 leklVIQKTRfkKIKKIKEIRRRVgvvfqfAEyqlfEQTIEKDIIFGPVSMGVSKEEAKKRA-AKYIELVGLDEsylQRS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 441 VGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLD---VETLRALEDALLEFAGTVMVISHD 499
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
338-515 |
1.10e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.98 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 338 IDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKP-DSGEVVIGQTVkmAFVDQArdALADQKTVWEDISGGLDI--- 413
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRGSV--AYVPQV--SWIFNATVRENILFGSDFese 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 414 -----INVGKFQMASRAYAGRfnfNGADQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALL- 487
Cdd:PLN03232 709 rywraIDVTALQHDLDLLPGR---DLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMk 785
|
170 180 190
....*....|....*....|....*....|
gi 518484691 488 -EFAG-TVMVISHDRWFLDRIATHILAAEG 515
Cdd:PLN03232 786 dELKGkTRVLVTNQLHFLPLMDRIILVSEG 815
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-189 |
1.14e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.96 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 1 MAQYVYSMNRVSKTVPpKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGeALPMPGLTIG------YL 74
Cdd:PRK11614 1 MEKVMLSFDKVSAHYG-KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSG-RIVFDGKDITdwqtakIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 75 EQEPKLNPEHT---VRESVEE--SMGAVNAAKK----RLEEVYELyaaedadFDALAAEQAEleaiiatagtdsehqlei 145
Cdd:PRK11614 79 REAVAIVPEGRrvfSRMTVEEnlAMGGFFAERDqfqeRIKWVYEL-------FPRLHERRIQ------------------ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518484691 146 aadalrlpawdaKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPT 189
Cdd:PRK11614 134 ------------RAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
326-525 |
1.23e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.12 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLaGKEKPDSGEVVI-------GQTVKMAFVDQARdaLA 398
Cdd:PRK14258 11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVegrveffNQNIYERRVNLNR--LR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 399 DQ------------KTVWEDISGGLDIINV-------GKFQMASRAyAGRFNFNGADQQKKVGTLSGGERGRLHLAKTLI 459
Cdd:PRK14258 88 RQvsmvhpkpnlfpMSVYDNVAYGVKIVGWrpkleidDIVESALKD-ADLWDEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 460 AGGNVLLLDEPSNDLD------VETLraLEDALLEFAGTVMVISHDRWFLDRIathilaaegdSQWT-FFDGN 525
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDpiasmkVESL--IQSLRLRSELTMVIVSHNLHQVSRL----------SDFTaFFKGN 227
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-218 |
1.41e-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: 52.93 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 21 ILKDISLSFFPGAKIGVLGLNGSGKSTLLKI---MAGVDKEIEGEALPMPGLTIGYLEQEPKLNPEHTVRESVEESMGAV 97
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAflrLLNTEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 98 NAAKKRLEEVYELyaaedadfdalaAEQAELEAIIATAGTDSEHQLEIAAdalrlpawdakiGVLSGGEKRRVALCRLLL 177
Cdd:cd03289 99 PYGKWSDEEIWKV------------AEEVGLKSVIEQFPGQLDFVLVDGG------------CVLSHGHKQLMCLARSVL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518484691 178 SKPDMLLLDEPTNHLDAESVEWLEVFL-QRFPGTVVAITHDR 218
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLkQAFADCTVILSEHR 196
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
326-497 |
1.43e-07 |
|
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: 54.63 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 326 KNVSKSF--GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVKMAFVDQARDALA---DQ 400
Cdd:TIGR01257 932 KNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGmcpQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 401 KTVWEDISGGLDIINVGKFQMASRAYA-----GRFNFNGADQQK--KVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSND 473
Cdd:TIGR01257 1012 NILFHHLTVAEHILFYAQLKGRSWEEAqlemeAMLEDTGLHHKRneEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180
....*....|....*....|....*
gi 518484691 474 LDVETLRALEDALLEF-AGTVMVIS 497
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYrSGRTIIMS 1116
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
332-475 |
1.55e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.10 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 332 FGDRLLID-NLSFnvPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTV---------------KMAFVDQARD 395
Cdd:PRK13634 18 FERRALYDvNVSI--PSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklkplrkKVGIVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 396 ALADQKTVWEDISGGldIINVGkfqmASRAYAGRfnfNGADQQKKVG-----------TLSGGERGRLHLAKTLIAGGNV 464
Cdd:PRK13634 96 HQLFEETVEKDICFG--PMNFG----VSEEDAKQ---KAREMIELVGlpeellarspfELSGGQMRRVAIAGVLAMEPEV 166
|
170
....*....|.
gi 518484691 465 LLLDEPSNDLD 475
Cdd:PRK13634 167 LVLDEPTAGLD 177
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-193 |
1.70e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGealpmpglTIGYLEQEPKlnpEHTVRESVEESMGAVNAAK 101
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAG--------TITLHGKKIN---NHNANEAINHGFALVTEER 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 102 KRLeevyELYAAEDADFDALAAEQAELE---AIIATAGTDSEHQLEIAADALRLPAWDAKIGVLSGGEKRRVALCRLLLS 178
Cdd:PRK10982 333 RST----GIYAYLDIGFNSLISNIRNYKnkvGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLT 408
|
170
....*....|....*
gi 518484691 179 KPDMLLLDEPTNHLD 193
Cdd:PRK10982 409 QPEILMLDEPTRGID 423
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
141-228 |
1.75e-07 |
|
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: 51.84 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 141 HQLEIAADALRLpawdakIGVLSGGEKR------RVALCRLLLSKPDMLLLDEPTNHLDAESVEW-----LEVFLQRFPG 209
Cdd:cd03240 101 HQGESNWPLLDM------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNF 174
|
90
....*....|....*....
gi 518484691 210 TVVAITHDRYFLDNAAEWI 228
Cdd:cd03240 175 QLIVITHDEELVDAADHIY 193
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-193 |
2.10e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 53.68 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 17 PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVdkeiegealpMPGLTIG--YLEQEPkLNPEhTVRESVEESM 94
Cdd:TIGR02633 271 PHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGA----------YPGKFEGnvFINGKP-VDIR-NPAQAIRAGI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 95 GAVNAAKKRLEEVYELYAAEDADFDALAA--------EQAELEAIIAtagtdSEHQLEIAADALRLPawdakIGVLSGGE 166
Cdd:TIGR02633 339 AMVPEDRKRHGIVPILGVGKNITLSVLKSfcfkmridAAAELQIIGS-----AIQRLKVKTASPFLP-----IGRLSGGN 408
|
170 180
....*....|....*....|....*..
gi 518484691 167 KRRVALCRLLLSKPDMLLLDEPTNHLD 193
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
323-475 |
2.22e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 52.70 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 323 FEFKnvsksfgdrlLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG-----------QTVK----- 386
Cdd:PRK13645 22 FEFK----------ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipanlkkiKEVKrlrke 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 387 MAFVDQARDALADQKTVWEDISGGldIINVG--------------KFQMASRAYAGRFNFNgadqqkkvgtLSGGERGRL 452
Cdd:PRK13645 92 IGLVFQFPEYQLFQETIEKDIAFG--PVNLGenkqeaykkvpellKLVQLPEDYVKRSPFE----------LSGGQKRRV 159
|
170 180
....*....|....*....|...
gi 518484691 453 HLAKTLIAGGNVLLLDEPSNDLD 475
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLD 182
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-217 |
2.32e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.30 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE-----------ALPMPGLTIGYLEQEPKLNPEHTV 86
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHvwldgehiqhyASKEVARRIGLLAQNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 87 RESVeesmgavnaAKKRL--EEVYELYAAEDADfdalaaeqAELEAIIATAGTDSEHQleiaadalrlpawdaKIGVLSG 164
Cdd:PRK10253 99 QELV---------ARGRYphQPLFTRWRKEDEE--------AVTKAMQATGITHLADQ---------------SVDTLSG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 165 GEKRRVALCRLLLSKPDMLLLDEPTNHLD-AESVEWLEVF--LQRFPG-TVVAITHD 217
Cdd:PRK10253 147 GQRQRAWIAMVLAQETAIMLLDEPTTWLDiSHQIDLLELLseLNREKGyTLAAVLHD 203
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
19-273 |
2.54e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 53.57 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAlpmpgltigYLEQEPKLNPEHTV-RESVeesmgav 97
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI---------RLDGRPLSSLSHSVlRQGV------- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 98 naakkrleevyelyAAEDADFDALAaeqaelEAIIA--TAGTD-SEHQLEIAADALRLPAW--------DAKIG----VL 162
Cdd:PRK10790 418 --------------AMVQQDPVVLA------DTFLAnvTLGRDiSEEQVWQALETVQLAELarslpdglYTPLGeqgnNL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 163 SGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQ--RFPGTVVAITHdRYFLDNAAEWILELDRGRGIPwK 240
Cdd:PRK10790 478 SVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAavREHTTLVVIAH-RLSTIVEADTILVLHRGQAVE-Q 555
|
250 260 270
....*....|....*....|....*....|....*..
gi 518484691 241 GNYSTWLEQKGeRLAQ----EQKSEEAHAKALKKELE 273
Cdd:PRK10790 556 GTHQQLLAAQG-RYWQmyqlQLAGEELAASVREEESL 591
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
11-217 |
2.89e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 52.01 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 11 VSKTVPPKrQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMA---GVDK---EIEGEAL-PMPG------LTIgyLEQE 77
Cdd:COG4604 7 VSKRYGGK-VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISrllPPDSgevLVDGLDVaTTPSrelakrLAI--LRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 78 PKLNPEHTVRESVeeSMGAVNAAKKRLEevyelyaAEDadfdalaaeqaelEAIIATAgtdsEHQLEIaaDALRlpawDA 157
Cdd:COG4604 84 NHINSRLTVRELV--AFGRFPYSKGRLT-------AED-------------REIIDEA----IAYLDL--EDLA----DR 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518484691 158 KIGVLSGGEKRR--VA--LCRlllsKPDMLLLDEPTNHLD-AESVEWLEVfLQR----FPGTVVAITHD 217
Cdd:COG4604 132 YLDELSGGQRQRafIAmvLAQ----DTDYVLLDEPLNNLDmKHSVQMMKL-LRRladeLGKTVVIVLHD 195
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-217 |
3.44e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.54 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 11 VSKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEalpmpgLTIGYL---EQEPK-------- 79
Cdd:PRK11650 9 VRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE------IWIGGRvvnELEPAdrdiamvf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 80 ----LNPEHTVRESveesMGavnaakkrleevyelYAAEDADFDalaaeQAELEAIIATAgtdsehqleiaADALRL-PA 154
Cdd:PRK11650 83 qnyaLYPHMSVREN----MA---------------YGLKIRGMP-----KAEIEERVAEA-----------ARILELePL 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518484691 155 WDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAE-----SVEWLEvfLQRFPGTV-VAITHD 217
Cdd:PRK11650 128 LDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKlrvqmRLEIQR--LHRRLKTTsLYVTHD 194
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-510 |
3.47e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.77 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKL------------------LAGKE--KPDSGEVVIGQ 383
Cdd:PRK14267 6 ETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllelneearvegevrLFGRNiySPDVDPIEVRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 384 TVKMAFvdQARDALAdQKTVWEDISGGLDIINV--GKFQMASRAYAGRFNFNGADQQK-----KVGTLSGGERGRLHLAK 456
Cdd:PRK14267 86 EVGMVF--QYPNPFP-HLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKdrlndYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 457 TLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAG--TVMVISHDRWFLDRIATHI 510
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTHSPAQAARVSDYV 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-217 |
4.24e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 51.70 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 4 YVYSmnrvsKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGeALPMPGLTIGYLEQEPKLN-- 81
Cdd:PRK13646 10 YTYQ-----KGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTG-TVTVDDITITHKTKDKYIRpv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 82 ----------PEHTVRE-SVEESM--GAVNAaKKRLEEVyelyaaEDADFDALAaeqaeleaiiatagtdsehQLEIAAD 148
Cdd:PRK13646 84 rkrigmvfqfPESQLFEdTVEREIifGPKNF-KMNLDEV------KNYAHRLLM-------------------DLGFSRD 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 149 ALRLPAWDakigvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFP----GTVVAITHD 217
Cdd:PRK13646 138 VMSQSPFQ-----MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHD 205
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-225 |
4.65e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 51.63 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKE------IEGEALPMPGL-----TIGYLEQEPKlnpEHTVRESV 90
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEfegkvkIDGELLTAENVwnlrrKIGMVFQNPD---NQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 91 EE--SMGAVNAAKKRLEEVYELYaaedadfdalaaeqaelEAIIATAGTDSEhqleiaadaLRLPAwdakigVLSGGEKR 168
Cdd:PRK13642 100 EDdvAFGMENQGIPREEMIKRVD-----------------EALLAVNMLDFK---------TREPA------RLSGGQKQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518484691 169 RVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFPGTVVAITHDryfLDNAA 225
Cdd:PRK13642 148 RVAVAGIIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD---LDEAA 205
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
31-219 |
4.71e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.62 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 31 PGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAlpmpgltigyleqepKLNPEHtvresveesmgAVNAAKKRleevyel 110
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI---------------QIDGKT-----------ATRGDRSR------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 111 YAAEDADFDALAAEQAELEAIIATAGTDSEHQLEIAADALRLPAW----DAKIGVLSGGEKRRVALCRLLLSKPDMLLLD 186
Cdd:PRK13543 83 FMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQMPGSALAIVGLagyeDTLVRQLSAGQKKRLALARLWLSPAPLWLLD 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 518484691 187 EPTNHLDAESVEWLEVFLQ---RFPGTVVAITHDRY 219
Cdd:PRK13543 163 EPYANLDLEGITLVNRMISahlRGGGAALVTTHGAY 198
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
320-370 |
4.78e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 4.78e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 518484691 320 SQVFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAG 370
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
325-499 |
5.18e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 51.96 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 325 FKNVSKSFGDRLLID---------NLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG------------- 382
Cdd:PRK10070 22 FKYIEQGLSKEQILEktglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiakisdaelr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 383 --QTVKMAFVDQARdALADQKTVWEDISGGLDIINVGKFQMASRAYagrfnfngaDQQKKVG----------TLSGGERG 450
Cdd:PRK10070 102 evRRKKIAMVFQSF-ALMPHMTVLDNTAFGMELAGINAEERREKAL---------DALRQVGlenyahsypdELSGGMRQ 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518484691 451 RLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAG----TVMVISHD 499
Cdd:PRK10070 172 RVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAkhqrTIVFISHD 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
14-217 |
5.33e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 51.23 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 14 TVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpMPGLTIGY-----LEQEPKL-----NPE 83
Cdd:PRK13639 10 SYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL-IKGEPIKYdkkslLEVRKTVgivfqNPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 84 H-----TVRESVeeSMGAVNAAKKRlEEVyelyaaEDADFDALAAeqaeleaiIATAGTDSE--HQLeiaadalrlpawd 156
Cdd:PRK13639 89 DqlfapTVEEDV--AFGPLNLGLSK-EEV------EKRVKEALKA--------VGMEGFENKppHHL------------- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518484691 157 akigvlSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD---AESVEWLEVFLQRFPGTVVAITHD 217
Cdd:PRK13639 139 ------SGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmgASQIMKLLYDLNKEGITIIISTHD 196
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
348-508 |
5.85e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 49.29 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 348 GAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVigqtvkmafvdqardaladqktvwedisggldIINVGKFQMASRAYA 427
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI--------------------------------YIDGEDILEEVLDQL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 428 GRFNFNGadqqkKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVET---------LRALEDALLEFAGTVMVISH 498
Cdd:smart00382 50 LLIIVGG-----KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllleeLRLLLLLKSEKNLTVILTTN 124
|
170
....*....|
gi 518484691 499 DRWFLDRIAT 508
Cdd:smart00382 125 DEKDLGPALL 134
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-235 |
5.88e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 51.28 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 16 PPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEalpmpgLTIGylEQEPKLNPEHTVRESVEESMG 95
Cdd:PRK13649 17 PFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGS------VRVD--DTLITSTSKNKDIKQIRKKVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 96 AVNAAKKrlEEVYELYAAEDADFD----ALAAEQAEleaiiatagtdsehqlEIAADALRLpawdakIGV---------- 161
Cdd:PRK13649 89 LVFQFPE--SQLFEETVLKDVAFGpqnfGVSQEEAE----------------ALAREKLAL------VGIseslfeknpf 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 162 -LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES-VEWLEVF--LQRFPGTVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:PRK13649 145 eLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGrKELMTLFkkLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-196 |
6.29e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.04 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 1 MAQYVYSMNRVSKTVPPKRQILKDISLSFfPGAKIGVL-GLNGSGKSTLLKIMAGVDKEIEGEalpmpgltIGYLEQepk 79
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALRDASFTV-PGGSIAALvGVNGSGKSTLFKALMGFVRLASGK--------ISILGQ--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 80 lnpehTVRESVEESMGAVNAAKkrlEEVyelyaaeDADFDALAaEQAELEAIIATAG---TDSEHQLEIAADAL-RLPAW 155
Cdd:PRK15056 70 -----PTRQALQKNLVAYVPQS---EEV-------DWSFPVLV-EDVVMMGRYGHMGwlrRAKKRDRQIVTAALaRVDMV 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518484691 156 DAK---IGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
Cdd:PRK15056 134 EFRhrqIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-235 |
6.74e-07 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 50.10 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTL-LKIMAGVDKE-----IEGEALPMPGLT-----IGYLEQEPKLNpEHTVRE 88
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLiLALFRFLEAEegkieIDGIDISTIPLEdlrssLTIIPQDPTLF-SGTIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 89 SVEesmgavnaakkrleeVYELYAAEDAdFDALAaeqaeleaiIATAGTDsehqleiaadalrlpawdakigvLSGGEKR 168
Cdd:cd03369 101 NLD---------------PFDEYSDEEI-YGALR---------VSEGGLN-----------------------LSQGQRQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 169 RVALCRLLLSKPDMLLLDEPTNHLDAES-VEWLEVFLQRFPG-TVVAITHD-RYFLDNAAewILELDRGR 235
Cdd:cd03369 133 LLCLARALLKRPRVLVLDEATASIDYATdALIQKTIREEFTNsTILTIAHRlRTIIDYDK--ILVMDAGE 200
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
331-543 |
7.29e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.43 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 331 SFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDS-GEVVIGQTVkmAFVDQArdALADQKTVWEDISG 409
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTV--AYVPQV--SWIFNATVRDNILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 410 GLDiINVGKFQMASRAYAGRFNFN---GADqQKKVG----TLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRAL 482
Cdd:PLN03130 702 GSP-FDPERYERAIDVTALQHDLDllpGGD-LTEIGergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQV 779
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 483 EDALL--EFAGTVMV-ISHDRWFLDRIATHILAAEGDSQWtffDGNYQEYEADKK--KRLGEEGAK 543
Cdd:PLN03130 780 FDKCIkdELRGKTRVlVTNQLHFLSQVDRIILVHEGMIKE---EGTYEELSNNGPlfQKLMENAGK 842
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
325-499 |
7.57e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 50.76 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 325 FKNVSKSFGDRL-LIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG----------QTVK--MAFVD 391
Cdd:PRK13644 4 LENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgidtgdfsklQGIRklVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 392 QARDALADQKTVWEDISGG-----LDIINVGKFQMASRAYAGRFNFngadQQKKVGTLSGGERGRLHLAKTLIAGGNVLL 466
Cdd:PRK13644 84 QNPETQFVGRTVEEDLAFGpenlcLPPIEIRKRVDRALAEIGLEKY----RHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 518484691 467 LDEPSNDLDVETLRA-LEDA--LLEFAGTVMVISHD 499
Cdd:PRK13644 160 FDEVTSMLDPDSGIAvLERIkkLHEKGKTIVYITHN 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
333-500 |
8.47e-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: 52.22 E-value: 8.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 333 GDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDsGEVVIG---------QTVKMAF--VDQA-------- 393
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDgvswnsvtlQTWRKAFgvIPQKvfifsgtf 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 394 RDALaDQKTVWEDISGGLDIINVGKFQMASRaYAGRFNFNGADQQKkvgTLSGGERGRLHLAKTLIAGGNVLLLDEPSND 473
Cdd:TIGR01271 1309 RKNL-DPYEQWSDEEIWKVAEEVGLKSVIEQ-FPDKLDFVLVDGGY---VLSNGHKQLMCLARSILSKAKILLLDEPSAH 1383
|
170 180
....*....|....*....|....*...
gi 518484691 474 LDVETLRALEDALLE-FAGTVMVISHDR 500
Cdd:TIGR01271 1384 LDPVTLQIIRKTLKQsFSNCTVILSEHR 1411
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
324-475 |
8.52e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 50.90 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKS------FGDRLLIDnLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTV------------ 385
Cdd:PRK13649 4 NLQNVSYTyqagtpFEGRALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 386 ---KMAFVDQARDALADQKTVWEDISGGLDIINVGKFQMASRAYAgRFNFNGADQQ---KKVGTLSGGERGRLHLAKTLI 459
Cdd:PRK13649 83 irkKVGLVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALARE-KLALVGISESlfeKNPFELSGGQMRRVAIAGILA 161
|
170
....*....|....*.
gi 518484691 460 AGGNVLLLDEPSNDLD 475
Cdd:PRK13649 162 MEPKILVLDEPTAGLD 177
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
324-498 |
9.88e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.89 E-value: 9.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTlFKLLAGKEKPDSGEVVIGQTVKMAFVDQARDALADQKTV 403
Cdd:NF000106 15 EVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 404 W----EDISGGLDIINVGKFQMASRAYA--------GRFNFNGAdQQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPS 471
Cdd:NF000106 94 R*grrESFSGRENLYMIGR*LDLSRKDAraradellERFSLTEA-AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190
....*....|....*....|....*....|
gi 518484691 472 NDLDVETLRALED---ALLEFAGTVMVISH 498
Cdd:NF000106 173 TGLDPRTRNEVWDevrSMVRDGATVLLTTQ 202
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-225 |
1.18e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 50.12 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 21 ILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV------DKEIEGEALPMPGL-----TIGYLEQepklNPEH----- 84
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLleaesgQIIIDGDLLTEENVwdirhKIGMVFQ----NPDNqfvga 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 85 TVRESVE---ESMG-AVNAAKKRLEEVYELYAAEDAdfdalaaeqaeleaiiatagtdsehqleiaadALRLPAwdakig 160
Cdd:PRK13650 98 TVEDDVAfglENKGiPHEEMKERVNEALELVGMQDF--------------------------------KEREPA------ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518484691 161 VLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES----VEWLEVFLQRFPGTVVAITHDryfLDNAA 225
Cdd:PRK13650 140 RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGrlelIKTIKGIRDDYQMTVISITHD---LDEVA 205
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
322-498 |
1.24e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 50.04 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFK------------------LLAGKE--KPDSGEVVI 381
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndlipgarvegeiLLDGEDiyDPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 382 GQTVKMAFvdqardaladQK------TVWEDISGGLDIINV-GKFQMASRA-YAGRfnfnGA-------DQQKKVGT-LS 445
Cdd:COG1117 91 RRRVGMVF----------QKpnpfpkSIYDNVAYGLRLHGIkSKSELDEIVeESLR----KAalwdevkDRLKKSALgLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 446 GGERGRLHLAKTLIAGGNVLLLDEPSNDLD-VETLRaLEDALLEFAG--TVMVISH 498
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILELKKdyTIVIVTH 211
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
327-476 |
1.56e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 50.26 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 327 NVSKSFGDRLLIDNLSfnVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQTVkmaFVDQARD-ALADQKT--- 402
Cdd:PRK11144 5 NFKQQLGDLCLTVNLT--LPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRV---LFDAEKGiCLPPEKRrig 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 403 -VWED--------ISGGLdiinvgKFQMAsRAYAGRFNfngadqqKKVG-------------TLSGGERGRLHLAKTLIA 460
Cdd:PRK11144 80 yVFQDarlfphykVRGNL------RYGMA-KSMVAQFD-------KIVAllgieplldrypgSLSGGEKQRVAIGRALLT 145
|
170
....*....|....*.
gi 518484691 461 GGNVLLLDEPSNDLDV 476
Cdd:PRK11144 146 APELLLMDEPLASLDL 161
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
345-528 |
1.57e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.39 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 345 VPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEV-VIGQTVKmAFVDQARDALADQK--------------TVWEDISg 409
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVsLVGQPLH-QMDEEARAKLRAKHvgfvfqsfmliptlNALENVE- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 410 gLDIINVGKFQMASRAYAgrfnfngADQQKKVG----------TLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETL 479
Cdd:PRK10584 111 -LPALLRGESSRQSRNGA-------KALLEQLGlgkrldhlpaQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518484691 480 RALEDALL----EFAGTVMVISHDRWfldriathiLAAEGDSQWTFFDGNYQE 528
Cdd:PRK10584 183 DKIADLLFslnrEHGTTLILVTHDLQ---------LAARCDRRLRLVNGQLQE 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
320-534 |
1.60e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 49.77 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 320 SQVFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLL------------------AGKE--KPDSGEV 379
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtitgsivyNGHNiySPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 380 VIGQTVKMAFvdQARDALAdqKTVWEDISGGLDIINVGKFQMASRAYAGrfNFNGA---DQQKK------VGtLSGGERG 450
Cdd:PRK14239 83 DLRKEIGMVF--QQPNPFP--MSIYENVVYGLRLKGIKDKQVLDEAVEK--SLKGAsiwDEVKDrlhdsaLG-LSGGQQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 451 RLHLAKTLIAGGNVLLLDEPSNDLDVETLRALEDALLEFAG--TVMVISHDRWFLDRIAthilaaegDSQWTFFDGNYQE 528
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRSMQQASRIS--------DRTGFFLDGDLIE 227
|
....*.
gi 518484691 529 YEADKK 534
Cdd:PRK14239 228 YNDTKQ 233
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-194 |
1.92e-06 |
|
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: 51.10 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 12 SKTVPPKrqiLKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEaLPMPGlTIGYLEQEPKLNPEhTVRESVe 91
Cdd:TIGR00957 647 ARDLPPT---LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGH-VHMKG-SVAYVPQQAWIQND-SLRENI- 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 92 esmgavnAAKKRLEEVYElyaaedadfdalaaeQAELEAIIATAgtdsehQLEIaadalrLPAWD-AKIGV----LSGGE 166
Cdd:TIGR00957 720 -------LFGKALNEKYY---------------QQVLEACALLP------DLEI------LPSGDrTEIGEkgvnLSGGQ 765
|
170 180
....*....|....*....|....*...
gi 518484691 167 KRRVALCRLLLSKPDMLLLDEPTNHLDA 194
Cdd:TIGR00957 766 KQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
321-506 |
1.96e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.36 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 321 QVFEFKNVSKSFGDR-LLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTVKMAFVDQARDALA 398
Cdd:PRK10522 321 QTLELRNVTFAYQDNgFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 399 dqkTVWEDISGGLDIINVGKFQMASRAYAGRFNFngADQQKKVG---------TLSGGERGRLHLAKTLIAGGNVLLLDE 469
Cdd:PRK10522 401 ---AVFTDFHLFDQLLGPEGKPANPALVEKWLER--LKMAHKLEledgrisnlKLSKGQKKRLALLLALAEERDILLLDE 475
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518484691 470 PSNDLDVETLRALEDALL----EFAGTVMVISH-DRWFL--DRI 506
Cdd:PRK10522 476 WAADQDPHFRREFYQVLLpllqEMGKTIFAISHdDHYFIhaDRL 519
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-193 |
1.96e-06 |
|
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: 50.45 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 13 KTVPPKRqILKDISLSFFPGAKIGVLGLNGSGKSTL-LKIMAGVDKEieGEALpMPGLTIGYLE---------------Q 76
Cdd:COG4172 294 RTVGHVK-AVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLIPSE--GEIR-FDGQDLDGLSrralrplrrrmqvvfQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 77 EP--KLNPEHTVRESVEESMGAVNAAKKRleevyelyaaedADFDALAAEqaeleaIIATAGTDsehqleiAADALRLPA 154
Cdd:COG4172 370 DPfgSLSPRMTVGQIIAEGLRVHGPGLSA------------AERRARVAE------ALEEVGLD-------PAARHRYPH 424
|
170 180 190
....*....|....*....|....*....|....*....
gi 518484691 155 wdakigVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD 193
Cdd:COG4172 425 ------EFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
337-533 |
2.17e-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: 50.68 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 337 LIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEvvIGQTVKMAFVDQARDALADqkTVWEDISGGLdiiNV 416
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK--IKHSGRISFSPQTSWIMPG--TIKDNIIFGL---SY 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 417 GKFQMASRAYAGRFNFNGA---DQQKKV-----GTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDVETLRAL-EDAL- 486
Cdd:TIGR01271 514 DEYRYTSVIKACQLEEDIAlfpEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLc 593
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518484691 487 -LEFAGTVMVISHDRWFLDRIATHILAAEGDSqwtFFDGNYQEYEADK 533
Cdd:TIGR01271 594 kLMSNKTRILVTSKLEHLKKADKILLLHEGVC---YFYGTFSELQAKR 638
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-217 |
2.34e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 50.03 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpMPGLTIGYLEqepklnpEHTVREsveesmgavnAAK 101
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVL-IDGVDIAKIS-------DAELRE----------VRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 102 KRLEEVYELYaaedadfdALAAEQAELEAI---IATAGTDSEHQLEIAADALRlpawdaKIGV----------LSGGEKR 168
Cdd:PRK10070 106 KKIAMVFQSF--------ALMPHMTVLDNTafgMELAGINAEERREKALDALR------QVGLenyahsypdeLSGGMRQ 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518484691 169 RVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFPGTVVAITHD 217
Cdd:PRK10070 172 RVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-200 |
2.39e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEA------------LPMPGLTIGYLEQEPKLNpEHTVR 87
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindshnlkdinLKWWRSKIGVVSQDPLLF-SNSIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 88 ESVEESMGAVN---AAKKRLEE-VYELYAAEDADFDALAAEQAELEAIIATagTDSEHQLEIAAD--------------- 148
Cdd:PTZ00265 478 NNIKYSLYSLKdleALSNYYNEdGNDSQENKNKRNSCRAKCAGDLNDMSNT--TDSNELIEMRKNyqtikdsevvdvskk 555
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 149 ------ALRLP-AWDAKIGV----LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESvEWL 200
Cdd:PTZ00265 556 vlihdfVSALPdKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-EYL 617
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-193 |
2.47e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 49.28 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 16 PPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpMPGLTIgyLEQEPKLN------------PE 83
Cdd:PRK13637 17 PFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKII-IDGVDI--TDKKVKLSdirkkvglvfqyPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 84 HTV-RESVEE--SMGAVNAA------KKRLEEVYELYAAEDADFdalaAEQAELEaiiatagtdsehqleiaadalrlpa 154
Cdd:PRK13637 94 YQLfEETIEKdiAFGPINLGlseeeiENRVKRAMNIVGLDYEDY----KDKSPFE------------------------- 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 518484691 155 wdakigvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD 193
Cdd:PRK13637 145 -------LSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
324-499 |
2.56e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.47 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 324 EFKNVsKSFGDRLLIDnlsFNvpaGAIVGIIGPNGAGKSTLFK----LLAGK----EKPDSGEVVIGQT---VKMAFV-- 390
Cdd:COG0419 6 RLENF-RSYRDTETID---FD---DGLNLIVGPNGAGKSTILEairyALYGKarsrSKLRSDLINVGSEeasVELEFEhg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 391 -----------DQARDALADQKTVWEDISG--GLDIINVGKFQMASRAYAGRFNFNGADQQKK--------------VGT 443
Cdd:COG0419 79 gkryrierrqgEFAEFLEAKPSERKEALKRllGLEIYEELKERLKELEEALESALEELAELQKlkqeilaqlsgldpIET 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 444 LSGGERGRLHLAKTLiaggnVLLLDEPSndLDVETLRALEDALLEFAgtvmVISHD 499
Cdd:COG0419 159 LSGGERLRLALADLL-----SLILDFGS--LDEERLERLLDALEELA----IITHV 203
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
322-498 |
3.31e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 48.93 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNvSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVV--------------IGQTVKM 387
Cdd:PRK13633 11 SYKYES-NEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYvdgldtsdeenlwdIRNKAGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 388 AFvdQARDALADQKTVWEDISGGLDIINVGKFQMASRAyagrfnfngADQQKKVGT----------LSGGERGRLHLAKT 457
Cdd:PRK13633 90 VF--QNPDNQIVATIVEEDVAFGPENLGIPPEEIRERV---------DESLKKVGMyeyrrhaphlLSGGQKQRVAIAGI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518484691 458 LIAGGNVLLLDEPSNDLD----VETLRALEDALLEFAGTVMVISH 498
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
155-216 |
3.48e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 3.48e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 155 WDAKIG----VLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFL----QRFPGTVVAITH 216
Cdd:PTZ00265 1348 YDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKADKTIITIAH 1417
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
340-385 |
3.65e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 49.80 E-value: 3.65e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 518484691 340 NLSFNvpAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI-GQTV 385
Cdd:COG4615 352 DLTIR--RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLdGQPV 396
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
162-217 |
3.65e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.94 E-value: 3.65e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 162 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG--TVVAITHD 217
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-222 |
3.67e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.48 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG--VDKEIEGEALpMPGLTIGYLEQEPKLNpehtvresveesMGA 96
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDIL-FKGESILDLEPEERAH------------LGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 97 VNAAKKRLeevyELYAAEDADFDALA-------AEQAELEAIiatagtdseHQLEIAADALRLPAWDAKI-------GvL 162
Cdd:CHL00131 87 FLAFQYPI----EIPGVSNADFLRLAynskrkfQGLPELDPL---------EFLEIINEKLKLVGMDPSFlsrnvneG-F 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 163 SGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPGT---VVAITHDRYFLD 222
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSensIILITHYQRLLD 215
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
324-370 |
4.22e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 4.22e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 518484691 324 EFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAG 370
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
22-196 |
5.10e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEA---------LPMPGLTigYLEQEPKLNPEHTVRESVee 92
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyykncninnIAKPYCT--YIGHNLGLKLEMTVFENL-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 93 smgavnaakKRLEEVYelyaaedadfdalaaeqaeleaiiatagtDSEHQLEIAADALRLPAW-DAKIGVLSGGEKRRVA 171
Cdd:PRK13541 92 ---------KFWSEIY-----------------------------NSAETLYAAIHYFKLHDLlDEKCYSLSSGMQKIVA 133
|
170 180
....*....|....*....|....*
gi 518484691 172 LCRLLLSKPDMLLLDEPTNHLDAES 196
Cdd:PRK13541 134 IARLIACQSDLWLLDEVETNLSKEN 158
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-217 |
6.73e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.18 E-value: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 24 DISLSFFPGAKIGVLGLNGSGKS-TLLKIMAGVDK--EIEGEA---------LPMPGLT------IGYLEQEP--KLNPE 83
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAAngRIGGSAtfngreilnLPEKELNklraeqISMIFQDPmtSLNPY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 84 HTVREsveesmgavnaakkRLEEVYELYAAEDAdfdalaaeqaeleaiiATAGTDSEHQLeiaaDALRLPAWDAKIGV-- 161
Cdd:PRK09473 114 MRVGE--------------QLMEVLMLHKGMSK----------------AEAFEESVRML----DAVKMPEARKRMKMyp 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518484691 162 --LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFPGTVVAITHD 217
Cdd:PRK09473 160 heFSGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD 221
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
335-499 |
8.58e-06 |
|
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: 46.20 E-value: 8.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 335 RLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFK------LLAGKEKPDSGEVVIGQTVkmAFVDqardaladqktvwedis 408
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaiglalGGAQSATRRRSGVKAGCIV--AAVS----------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 409 ggldiinvgkfqmASRAYAgrfnfngadqqkkVGTLSGGERGRLHLAKTL----IAGGNVLLLDEPSNDLDVETLRALED 484
Cdd:cd03227 69 -------------AELIFT-------------RLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAE 122
|
170
....*....|....*...
gi 518484691 485 ALLEFAG---TVMVISHD 499
Cdd:cd03227 123 AILEHLVkgaQVIVITHL 140
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
19-217 |
1.16e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 47.23 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 19 RQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE--------------ALPMPGLTI------GYLEQep 78
Cdd:PRK11701 19 RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEvhyrmrdgqlrdlyALSEAERRRllrtewGFVHQ-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 79 klNPEHTVRESVeeSMGAvNAAkKRLeevyelyaaedadfdaLAAEQAELEAIIATAGtDSEHQLEIAADalRLpawDAK 158
Cdd:PRK11701 97 --HPRDGLRMQV--SAGG-NIG-ERL----------------MAVGARHYGDIRATAG-DWLERVEIDAA--RI---DDL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 159 IGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFPGTVVAITHD 217
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARLLDLLRGLVRELGLAVVIVTHD 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-216 |
1.18e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.14 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 20 QILKDISLSFFPGAKIGVLGLNGSGKSTLLK-----IMAGVDKEIEGEaLPMPGLTIgyleQEPKLNPEHTVREsveesM 94
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGE-VRLFGRNI----YSPDVDPIEVRRE-----V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 95 GAVNAAKKRLEE--VYElYAAEDADFDALAAEQAELEAIIatagtdsEHQLEIAAdalrlpAWDA-------KIGVLSGG 165
Cdd:PRK14267 88 GMVFQYPNPFPHltIYD-NVAIGVKLNGLVKSKKELDERV-------EWALKKAA------LWDEvkdrlndYPSNLSGG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518484691 166 EKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG--TVVAITH 216
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
12-237 |
1.20e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.31 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 12 SKTVPPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGV-----DKEIEGEALPMPGLT----IGYLEQEPKLN- 81
Cdd:PRK13645 17 AKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetGQTIVGDYAIPANLKkikeVKRLRKEIGLVf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 82 --PEHTV-RESVEE--SMGAVNAAKKRlEEVYElYAAEDADFDALAAEQAEleaiiatagtdsehqleiaadalRLPAwd 156
Cdd:PRK13645 97 qfPEYQLfQETIEKdiAFGPVNLGENK-QEAYK-KVPELLKLVQLPEDYVK-----------------------RSPF-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 157 akigVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVE-WLEVFL---QRFPGTVVAITHDRYFLDNAAEWILELD 232
Cdd:PRK13645 150 ----ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdFINLFErlnKEYKKRIIMVTHNMDQVLRIADEVIVMH 225
|
....*
gi 518484691 233 RGRGI 237
Cdd:PRK13645 226 EGKVI 230
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
443-511 |
1.25e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.84 E-value: 1.25e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 443 TLSGGERGRLHLAKTL--IAGGNVL-LLDEPSNDL---DVETLRALEDALLEFAGTVMVISHDrwfLD--RIATHIL 511
Cdd:cd03271 169 TLSGGEAQRIKLAKELskRSTGKTLyILDEPTTGLhfhDVKKLLEVLQRLVDKGNTVVVIEHN---LDviKCADWII 242
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
14-217 |
1.53e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 46.62 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 14 TVPPKRQILKDISLSFFPGAKIGVLGLNGSGKS----TLLKIM-AGVDKE-----IEGEAL---PMPGLTIGYLEQEPK- 79
Cdd:PRK10418 11 ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQTagrvlLDGKPVapcALRGRKIATIMQNPRs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 80 -LNPEHTVRESVEESMGAVnaakkrleevyelyaaedadfdALAAEQAELEAIIATAGtdsehqLEIAADALRLPAWDak 158
Cdd:PRK10418 91 aFNPLHTMHTHARETCLAL----------------------GKPADDATLTAALEAVG------LENAARVLKLYPFE-- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518484691 159 igvLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES----VEWLE-VFLQRFPGtVVAITHD 217
Cdd:PRK10418 141 ---MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAqariLDLLEsIVQKRALG-MLLVTHD 200
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
158-237 |
2.01e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.39 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 158 KIGVLSGGEKRRVALCRLLLS--KPDMLLLDEPTNHLDAESVE-WLEVF--LQRFPGTVVAITHDRYFLDnAAEWILELD 232
Cdd:cd03238 84 KLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINqLLEVIkgLIDLGNTVILIEHNLDVLS-SADWIIDFG 162
|
....*
gi 518484691 233 RGRGI 237
Cdd:cd03238 163 PGSGK 167
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
322-506 |
2.17e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.32 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 322 VFEFKNVSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKE--KPDSGEVVIGQTVKMAFVDQARDA--- 396
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGegi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 397 -LADQKTVweDISGGLDIINVGKFQMASRAYAG-----RFNFNGADQQK---------------KVGtLSGGERGRLHLA 455
Cdd:PRK09580 81 fMAFQYPV--EIPGVSNQFFLQTALNAVRSYRGqepldRFDFQDLMEEKiallkmpedlltrsvNVG-FSGGEKKRNDIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518484691 456 KTLIAGGNVLLLDEPSNDLDVETLRALE---DALLEFAGTVMVISHDRWFLDRI 506
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDALKIVAdgvNSLRDGKRSFIIVTHYQRILDYI 211
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-193 |
2.25e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 46.32 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEAL----PMPGLTIGYLEQEpklnpehtVRESVEESMGAV 97
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiddhPLHFGDYSYRSQR--------IRMIFQDPSTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 98 NaAKKRLEEVYELYAAEDADFDALAAEQaeleAIIAT---AGTDSEHqleiaadALRLPAwdakigVLSGGEKRRVALCR 174
Cdd:PRK15112 101 N-PRQRISQILDFPLRLNTDLEPEQREK----QIIETlrqVGLLPDH-------ASYYPH------MLAPGQKQRLGLAR 162
|
170
....*....|....*....
gi 518484691 175 LLLSKPDMLLLDEPTNHLD 193
Cdd:PRK15112 163 ALILRPKVIIADEALASLD 181
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
128-225 |
2.30e-05 |
|
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: 44.67 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 128 LEAIIATAGTDSEHQLEIAADALRLPAWDAKIGV--------LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES--- 196
Cdd:smart00382 19 ARALARELGPPGGGVIYIDGEDILEEVLDQLLLIivggkkasGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeal 98
|
90 100 110
....*....|....*....|....*....|....*
gi 518484691 197 ------VEWLEVFLQRFPGTVVAITHDRYFLDNAA 225
Cdd:smart00382 99 lllleeLRLLLLLKSEKNLTVILTTNDEKDLGPAL 133
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
162-231 |
2.36e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.07 E-value: 2.36e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518484691 162 LSGGEKRRVALCRLLlSKPD----MLLLDEPTNHLDAESVEWLEVFLQRFP---GTVVAITHDryfLD--NAAEWILEL 231
Cdd:cd03271 170 LSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVdkgNTVVVIEHN---LDviKCADWIIDL 244
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-235 |
2.63e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.89 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpmpgltigyLEQEPklnpehtvresveesmgaVNAAK 101
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIL---------LDGKP------------------VTAEQ 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 102 krLEEVYELYAAEDAD---FDAL------AAEQAELEAIIATAGTdsEHQLEIAADALRLPAwdakigvLSGGEKRRVAL 172
Cdd:PRK10522 392 --PEDYRKLFSAVFTDfhlFDQLlgpegkPANPALVEKWLERLKM--AHKLELEDGRISNLK-------LSKGQKKRLAL 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518484691 173 CRLLLSKPDMLLLDE------PtnHLDAESVEWLEVFLQRFPGTVVAITHDRYFLDNaAEWILELDRGR 235
Cdd:PRK10522 461 LLALAEERDILLLDEwaadqdP--HFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQ 526
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
247-371 |
3.59e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.03 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 247 LEQKGERLAQEQKSEEAHAKALKKElEWSRQNPKARQAKSKSRLarFEELSDVEYQKRNETQEifipvaerlGSQVFEFK 326
Cdd:TIGR00956 696 AKQKGEILVFRRGSLKRAKKAGETS-ASNKNDIEAGEVLGSTDL--TDESDDVNDEKDMEKES---------GEDIFHWR 763
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 518484691 327 N----VSKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGK 371
Cdd:TIGR00956 764 NltyeVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAER 812
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-194 |
4.11e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.64 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 17 PKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMA--------GVDKEIEGEALP-------MPGLTIGYLEQEPKLn 81
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdgfhiGVEGVITYDGITpeeikkhYRGDVVYNAETDVHF- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 82 PEHTVRESVEESmGAVNAAKKRLEEVYEL-YAAEDADFdalaaeqaeleaIIATAGTDSEHQLEIAADALRlpawdakiG 160
Cdd:TIGR00956 151 PHLTVGETLDFA-ARCKTPQNRPDGVSREeYAKHIADV------------YMATYGLSHTRNTKVGNDFVR--------G 209
|
170 180 190
....*....|....*....|....*....|....
gi 518484691 161 VlSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDA 194
Cdd:TIGR00956 210 V-SGGERKRVSIAEASLGGAKIQCWDNATRGLDS 242
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
337-500 |
4.22e-05 |
|
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: 45.62 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 337 LIDNLSFNVPAGAIVGIIGPNGAGKSTLF----KLLAGKekpdsGEV--------------------VIGQTVkMAFVDQ 392
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLNTE-----GDIqidgvswnsvplqkwrkafgVIPQKV-FIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 393 ARDALaDQKTVWEDisggLDIINVGK---FQMASRAYAGRFNFNGADQQKkvgTLSGGERGRLHLAKTLIAGGNVLLLDE 469
Cdd:cd03289 93 FRKNL-DPYGKWSD----EEIWKVAEevgLKSVIEQFPGQLDFVLVDGGC---VLSHGHKQLMCLARSVLSKAKILLLDE 164
|
170 180 190
....*....|....*....|....*....|..
gi 518484691 470 PSNDLDVETLRALEDALLE-FAGTVMVISHDR 500
Cdd:cd03289 165 PSAHLDPITYQVIRKTLKQaFADCTVILSEHR 196
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
442-499 |
6.21e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 6.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 442 GTLSGGERGRLHLAKTLIAG--GNVLLLDEPS-------NDLDVETLRALEDalleFAGTVMVISHD 499
Cdd:TIGR00630 487 GTLSGGEAQRIRLATQIGSGltGVLYVLDEPSiglhqrdNRRLINTLKRLRD----LGNTLIVVEHD 549
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
441-499 |
6.56e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 44.56 E-value: 6.56e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 441 VGTLSGGERGRLHLAKTLIAG--GNVLLLDEPS-------NDLDVETLRALEDAllefAGTVMVISHD 499
Cdd:cd03270 135 APTLSGGEAQRIRLATQIGSGltGVLYVLDEPSiglhprdNDRLIETLKRLRDL----GNTVLVVEHD 198
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
337-482 |
7.40e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 45.42 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 337 LIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPD---SGEVVIG--------QTVKMAFVDQ---------ARDA 396
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNgmpidakeMRAISAYVQQddlfiptltVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 397 L-------------ADQKTvwEDISGGLDIINVGKFQMASRAYAGRfnfngadqqkkVGTLSGGERGRLHLAKTLIAGGN 463
Cdd:TIGR00955 120 LmfqahlrmprrvtKKEKR--ERVDEVLQALGLRKCANTRIGVPGR-----------VKGLSGGERKRLAFASELLTDPP 186
|
170 180
....*....|....*....|....*.
gi 518484691 464 VLLLDEPSNDLD-------VETLRAL 482
Cdd:TIGR00955 187 LLFCDEPTSGLDsfmaysvVQVLKGL 212
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
330-510 |
9.10e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.80 E-value: 9.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 330 KSFGDRLLIDNLSFN-VPAGAIVGIIGPNGAGKSTLFKLL--------AGKEKPDSGEVVIG---QTVKMAFVDQARdal 397
Cdd:cd03279 9 KNFGPFREEQVIDFTgLDNNGLFLICGPTGAGKSTILDAItyalygktPRYGRQENLRSVFApgeDTAEVSFTFQLG--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 398 adQKTVWEDISGGLDI---INV-----GKF-QMASRAYAgrfnfngadqqkkvgTLSGGERG------RLHLAKTLIAGG 462
Cdd:cd03279 86 --GKKYRVERSRGLDYdqfTRIvllpqGEFdRFLARPVS---------------TLSGGETFlaslslALALSEVLQNRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518484691 463 NV----LLLDEPSNDLDVETLRALEDALLEFAGT---VMVISHDRWFLDRIATHI 510
Cdd:cd03279 149 GArleaLFIDEGFGTLDPEALEAVATALELIRTEnrmVGVISHVEELKERIPQRL 203
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-234 |
9.55e-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: 43.86 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEalpmpgltigyLEQEPKLNPEHTVRESVEESMGAVNAAK 101
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGK-----------VHWSNKNESEPSFEATRSRNRYSVAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 102 KR---LEEVYElyaaEDADFDALAAEQAELEAIIATAgtdsehqleIAADALRLPAWD-AKIGV----LSGGEKRRVALC 173
Cdd:cd03290 86 QKpwlLNATVE----ENITFGSPFNKQRYKAVTDACS---------LQPDIDLLPFGDqTEIGErginLSGGQRQRICVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 174 RLLLSKPDMLLLDEPTNHLDAESVEWLEV-----FLQRFPGTVVAITHDRYFLDNaAEWILELDRG 234
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIHLSDHLMQegilkFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-198 |
9.91e-05 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 43.19 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDK------EIEGEALPMPgltigyleqepklnpehTVRESVEESMG 95
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPpasgeiTLDGKPVTRR-----------------SPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 96 avnaakkrleevyelYAAEDADFDALAAEQAELEAIIATAgtdsehqleiaadalrlpawdakigVLSGGEKRRVALCRL 175
Cdd:cd03215 79 ---------------YVPEDRKREGLVLDLSVAENIALSS-------------------------LLSGGNQQKVVLARW 118
|
170 180
....*....|....*....|...
gi 518484691 176 LLSKPDMLLLDEPTNHLDAESVE 198
Cdd:cd03215 119 LARDPRVLILDEPTRGVDVGAKA 141
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
162-231 |
1.15e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.00 E-value: 1.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 162 LSGGEKRRVALCRLLLSK---PDMLLLDEPTNHLDAESVEWLEVFLQRFPG---TVVAITHDryfLD--NAAEWILEL 231
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDkgnTVVVIEHN---LDviKTADYIIDL 904
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
325-498 |
1.38e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 325 FKNVSKSFGDRLLIDnLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIG--QTVKMA-----FVDQARdAL 397
Cdd:PRK13541 4 LHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKncNINNIAkpyctYIGHNL-GL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 398 ADQKTVWEDISGGLDIINvgkfqMASRAYAGRFNFNGAD-QQKKVGTLSGGERGRLHLAKTLIAGGNVLLLDEPSNDLDV 476
Cdd:PRK13541 82 KLEMTVFENLKFWSEIYN-----SAETLYAAIHYFKLHDlLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK 156
|
170 180
....*....|....*....|....*.
gi 518484691 477 ETlRALEDALLEF----AGTVMVISH 498
Cdd:PRK13541 157 EN-RDLLNNLIVMkansGGIVLLSSH 181
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
443-508 |
1.76e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.63 E-value: 1.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 443 TLSGGERGRLHLAKTL--IAGGNVL-LLDEPSNDL---DVETL-RALeDALLEFAGTVMVISHDrwfLDRIAT 508
Cdd:COG0178 826 TLSGGEAQRVKLASELskRSTGKTLyILDEPTTGLhfhDIRKLlEVL-HRLVDKGNTVVVIEHN---LDVIKT 894
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-235 |
1.89e-04 |
|
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: 44.62 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 16 PPKRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEALpmpgltIGYLEQEPKLnpehtvrESVEESMG 95
Cdd:TIGR01257 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVL------VGGKDIETNL-------DAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 96 AVNAAKKRLeevYELYAAEDADFDA------LAAEQAELEAIIATAGTDSEHQLEiAADalrlpawdakigvLSGGEKRR 169
Cdd:TIGR01257 1007 MCPQHNILF---HHLTVAEHILFYAqlkgrsWEEAQLEMEAMLEDTGLHHKRNEE-AQD-------------LSGGMQRK 1069
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 170 VALCRLLLSKPDMLLLDEPTNHLDAESVE--WLEVFLQRFPGTVVAITHDRYFLDNAAEWILELDRGR 235
Cdd:TIGR01257 1070 LSVAIAFVGDAKVVVLDEPTSGVDPYSRRsiWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
159-222 |
2.22e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 43.53 E-value: 2.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 159 IGVLSGGEKR---RVALCRLLLSKPDMLLLDEPTNHLDAESVEWL-EVF--LQRFPGTVVAITHDRYFLD 222
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLlELLkeLSRNGAQLILTTHSPLLLD 303
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-81 |
2.31e-04 |
|
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: 42.17 E-value: 2.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 518484691 32 GAKIGVLGLNGSGKSTLLKIMAGVDKEiEGEALPMPGLTIGYLEQEPKLN 81
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIP-NGDNDEWDGITPVYKPQYIDLS 73
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
323-369 |
3.21e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 43.11 E-value: 3.21e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 518484691 323 FEFKNVsKSFGDRLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLA 369
Cdd:COG1106 5 FSIENF-RSFKDELTLSMVASGLRLLRVNLIYGANASGKSNLLEALY 50
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-235 |
3.31e-04 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 43.25 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 25 ISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGEalpmpgltIgYLEQEPkLNPEHtvRESVEESMGAVnaakkrL 104
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGE--------I-LLDGQP-VTADN--REAYRQLFSAV------F 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 105 EEVY---ELYAAEDADFDALAA---EQAELeaiiatagtdsEHQLEIAADALRLPAwdakigvLSGGEKRRVALCRLLLS 178
Cdd:COG4615 413 SDFHlfdRLLGLDGEADPARARellERLEL-----------DHKVSVEDGRFSTTD-------LSQGQRKRLALLVALLE 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518484691 179 KPDMLLLDeptnhldaesvEWL--------EVF-------LQRFPGTVVAITHD-RYFldNAAEWILELDRGR 235
Cdd:COG4615 475 DRPILVFD-----------EWAadqdpefrRVFytellpeLKARGKTVIAISHDdRYF--DLADRVLKMDYGK 534
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
22-292 |
5.76e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLK--IMAGVDKEIEGEALPMPGLTIGYLEQEPKLNPEHTVRESVEESMGAVNA 99
Cdd:PRK00635 611 LKDLTISLPLGRLTVVTGVSGSGKSSLINdtLVPAVEEFIEQGFCSNLSIQWGAISRLVHITRDLPGRSQRSIPLTYIKA 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 100 akkrLEEVYELYAAEDA-----------DFDALAAEQAELEAIIATAGTDSEHQ---------------LEI------AA 147
Cdd:PRK00635 691 ----FDDLRELFAEQPRskrlgltkshfSFNTPLGACAECQGLGSITTTDNRTSipcpsclgkrflpqvLEVrykgknIA 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 148 DALRLPAWDAK-----------------------------IGVLSGGEKRRVALCRLLLS---KPDMLLLDEPTNHLDAE 195
Cdd:PRK00635 767 DILEMTAYEAEkffldepsihekihalcslgldylplgrpLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTH 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 196 SVEWLEVFLQRFP---GTVVAITHDRYFLdNAAEWILELDrgrgiPWKGNYSTWLeqkgerLAQEQKSEEAH-----AKA 267
Cdd:PRK00635 847 DIKALIYVLQSLThqgHTVVIIEHNMHVV-KVADYVLELG-----PEGGNLGGYL------LASCSPEELIHlhtptAKA 914
|
330 340
....*....|....*....|....*
gi 518484691 268 LKKELEWSRQNPKARQAKSKSRLAR 292
Cdd:PRK00635 915 LRPYLSSPQELPYLPDPSPKPPVPA 939
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
442-500 |
7.55e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 7.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 442 GTLSGGERGRLHLAkTLIAGG--NVL-LLDEPS-------NDLDVETLRALEDallefAG-TVMVISHDR 500
Cdd:COG0178 484 GTLSGGEAQRIRLA-TQIGSGlvGVLyVLDEPSiglhqrdNDRLIETLKRLRD-----LGnTVIVVEHDE 547
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
25-229 |
7.89e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 41.65 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 25 ISLSFFPGAKIGVLGLNGSGKS-TLLKIMAGVD------------------KEIEGEALPMPGLTIGYLEQEP--KLNPE 83
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDypgrvmaeklefngqdlqRISEKERRNLVGAEVAMIFQDPmtSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 84 HTVRESVEESMGAVNAAKKRleevyelyaaedadfdalAAEQAELEAIIatagtdsehQLEIAADALRLPAWDAKigvLS 163
Cdd:PRK11022 106 YTVGFQIMEAIKVHQGGNKK------------------TRRQRAIDLLN---------QVGIPDPASRLDVYPHQ---LS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 164 GGEKRRVALCRLLLSKPDMLLLDEPTNHLD----AESVEWLEVFLQRFPGTVVAITHDRYFLDNAAEWIL 229
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDvtiqAQIIELLLELQQKENMALVLITHDLALVAEAAHKII 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
162-217 |
8.86e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 41.31 E-value: 8.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 162 LSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVEWLEVFLQRFPG--TVVAITHD 217
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTHN 209
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-62 |
1.07e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 1.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 518484691 22 LKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAGVDKEIEGE 62
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
3-61 |
1.10e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.80 E-value: 1.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 518484691 3 QYVYSMNRVSKTVPPkrqilkdislsffpGAKIGVLGLNGSGKSTLLKIMAGVDKEIEG 61
Cdd:PRK13545 35 EYHYALNNISFEVPE--------------GEIVGIIGLNGSGKSTLSNLIAGVTMPNKG 79
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
326-379 |
1.29e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 1.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 518484691 326 KNVSKSFgdrLLIDNLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEV 379
Cdd:PRK13546 31 KHKNKTF---FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
443-515 |
1.38e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 443 TLSGGERGRLHLAKTLIA---GGNVLLLDEPSNDLDVETLRALEDAL--LEFAG-TVMVISHDrwfLDRI--ATHI--LA 512
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLqrLVDKGnTVVVIEHN---LDVIktADYIidLG 905
|
...
gi 518484691 513 AEG 515
Cdd:TIGR00630 906 PEG 908
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
330-362 |
1.57e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 39.76 E-value: 1.57e-03
10 20 30
....*....|....*....|....*....|...
gi 518484691 330 KSFGDRLLIdnlsfNVPAGaIVGIIGPNGAGKS 362
Cdd:cd03278 10 KSFADKTTI-----PFPPG-LTAIVGPNGSGKS 36
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
151-193 |
1.66e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 1.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 518484691 151 RLPAWDAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD 193
Cdd:NF040905 394 KTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
163-237 |
1.88e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.87 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 163 SGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAESVE--WLEVFLQRFPGTVVAITHDryFLDNAAEWILEL---DRGRGI 237
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNevWDEVRSMVRDGATVLLTTQ--YMEEAEQLAHELtviDRGRVI 223
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-193 |
2.01e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 40.23 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 21 ILKDISLSFFPGAKIGVLGLNGSGKSTLLKImagvdkeIEGEALPMPGLT-----IGYLEQEPKLNPeHTVRESVeesmg 95
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLML-------ILGELEPSEGKIkhsgrISFSSQFSWIMP-GTIKENI----- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 96 avnaakkrleevyelyaaedadFDALAAEQAELEAIIATAgtdsehQLEiaADALRLPAWDAKI----GV-LSGGEKRRV 170
Cdd:cd03291 119 ----------------------IFGVSYDEYRYKSVVKAC------QLE--EDITKFPEKDNTVlgegGItLSGGQRARI 168
|
170 180
....*....|....*....|...
gi 518484691 171 ALCRLLLSKPDMLLLDEPTNHLD 193
Cdd:cd03291 169 SLARAVYKDADLYLLDSPFGYLD 191
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-193 |
2.05e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.99 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 8 MNRVSKTVppkrQILKDISLSFFPGAKIGVLGLNGSGKST----LLKIMAGVDKEI--EGE---ALPMPGLT-----IGY 73
Cdd:PRK10261 330 LNRVTREV----HAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVESQGGEIifNGQridTLSPGKLQalrrdIQF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 74 LEQEP--KLNPEHTVRESVEESMgavnaakkrleEVYELYAAEDAdfdalaaeQAELEAIIATAGTDSEHqleiaadALR 151
Cdd:PRK10261 406 IFQDPyaSLDPRQTVGDSIMEPL-----------RVHGLLPGKAA--------AARVAWLLERVGLLPEH-------AWR 459
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518484691 152 LPAwdakigVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLD 193
Cdd:PRK10261 460 YPH------EFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
438-506 |
2.48e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 2.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518484691 438 QKKVGTLSGGERGRLHLAKTLIA--GGNVLLLDEPSNDL---DVETLRALEDALLEFAGTVMVISHDRW---FLDRI 506
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAelIGITYILDEPSIGLhpqDTHKLINVIKKLRDQGNTVLLVEHDEQmisLADRI 547
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
35-217 |
2.49e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 35 IGVLGLNGSGKSTLLkimagvdkeiegEALpMPGLTiGYLEQEPKLNPEHTVRESVE-------ESMGAVNAAKKRLEEV 107
Cdd:COG0419 26 NLIVGPNGAGKSTIL------------EAI-RYALY-GKARSRSKLRSDLINVGSEEasvelefEHGGKRYRIERRQGEF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 108 YELYAAEDAD-------------FDALAAEQAELEAIIATAGTDSEHQLEIAADALRLPAWDAKIGVLSGGEKRRVALCR 174
Cdd:COG0419 92 AEFLEAKPSErkealkrllgleiYEELKERLKELEEALESALEELAELQKLKQEILAQLSGLDPIETLSGGERLRLALAD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 518484691 175 LLlskpdMLLLDepTNHLDAESVEWLEVFLQRfpgtVVAITHD 217
Cdd:COG0419 172 LL-----SLILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
162-273 |
4.22e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 162 LSGGEKRRVALCRLLlSKPD----MLLLDEPT--------NHLdaesvewLEVfLQRF--PG-TVVAITHDryfLD--NA 224
Cdd:COG0178 827 LSGGEAQRVKLASEL-SKRStgktLYILDEPTtglhfhdiRKL-------LEV-LHRLvdKGnTVVVIEHN---LDviKT 894
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 225 AEWILEL-----DRGrgipwkgnystwleqkGERLAQ---EQ--KSEEAH-AKALKKELE 273
Cdd:COG0178 895 ADWIIDLgpeggDGG----------------GEIVAEgtpEEvaKVKASYtGRYLKEYLE 938
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-196 |
4.35e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.21 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 18 KRQILKDISLSFFPGAKIGVLGLNGSGKSTLLKIMAG-VDKEIE--------GEALP--MPGLTIGYLEQEPKLNPEHTV 86
Cdd:PLN03140 177 KLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGkLDPSLKvsgeitynGYRLNefVPRKTSAYISQNDVHVGVMTV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 87 RESVEESmGAVNAAKKRLEEVYELYAAE-------DADFD----ALAAEQAELEAIiaTAGTDSEHQLEIAADALrlpAW 155
Cdd:PLN03140 257 KETLDFS-ARCQGVGTRYDLLSELARREkdagifpEAEVDlfmkATAMEGVKSSLI--TDYTLKILGLDICKDTI---VG 330
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518484691 156 DAKIGVLSGGEKRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
Cdd:PLN03140 331 DEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSST 371
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
442-499 |
4.57e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 4.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518484691 442 GTLSGGERGRLHLAkTLIAGG--NVL-LLDEPS-------NDLDVETLRALEDalleFAGTVMVISHD 499
Cdd:PRK00349 488 GTLSGGEAQRIRLA-TQIGSGltGVLyVLDEPSiglhqrdNDRLIETLKHLRD----LGNTLIVVEHD 550
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
159-224 |
4.61e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 4.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518484691 159 IGVLSGGEK------RRVALCRLLLSKPDMLLLDEPTNHLDAES----VEWLEVFLQRFPgTVVAITHDRYFLDNA 224
Cdd:PRK03918 786 LTFLSGGERialglaFRLALSLYLAGNIPLLILDEPTPFLDEERrrklVDIMERYLRKIP-QVIIVSHDEELKDAA 860
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-362 |
5.03e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 5.03e-03
10 20 30
....*....|....*....|....*....|...
gi 518484691 330 KSFGDRLLIDnlsFNvpaGAIVGIIGPNGAGKS 362
Cdd:TIGR02168 11 KSFADPTTIN---FD---KGITGIVGPNGCGKS 37
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
324-384 |
5.21e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 5.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518484691 324 EFKNVSKSFGDRLLID---NLSFNVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVIGQT 384
Cdd:PTZ00265 384 QFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS 447
|
|
| COG4928 |
COG4928 |
Predicted P-loop ATPase, KAP-like [General function prediction only]; |
323-500 |
6.46e-03 |
|
Predicted P-loop ATPase, KAP-like [General function prediction only];
Pssm-ID: 443956 Cd Length: 386 Bit Score: 39.12 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 323 FEFKNVSKSFGDrlLIDNLSfnVPAGAIVGIIGPNGAGKSTLFKLLAGKEKPDSGEVVI---------GQTVKMAFVDQA 393
Cdd:COG4928 8 LGRKKYAESLAN--LIKSSD--ADEPLVIGLDGEWGSGKTSFLNLIEKELESNEKVIVVyfnawlydgEEDLLAALLSEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518484691 394 RDALADQKTVWEDISGGL-DIINVGKFQMASRAYAGRFNFNGADQQKKV-GTLSGGERGRLH--------LAKTLIAGGN 463
Cdd:COG4928 84 AAELEKKKKKDKKAAKKLkKYAKRLSKLALKAGLLGGPAEAVAEALKALlKKEYKSKKKSIEafreeleeLLKELKGKRL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518484691 464 VLLLDepsnDLD-------VETLRALEdALLEFAGTVMVISHDR 500
Cdd:COG4928 164 VVFID----DLDrcepdeaIEVLELIK-LFFDFPNVVFVLAFDR 202
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
323-369 |
6.57e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.83 E-value: 6.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 518484691 323 FEFKNVsKSFGDRllidNLSFNVPAGAIVgIIGPNGAGKSTLFKLLA 369
Cdd:COG3950 6 LTIENF-RGFEDL----EIDFDNPPRLTV-LVGENGSGKTTLLEAIA 46
|
|
| |
